ID 1431_MAIZE STANDARD; PRT; 261 AA. AC P49106; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 14-3-3-like protein GF14-6. GN GRF1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95148741; PubMed=7846163; RA de Vetten N.C., Ferl R.J.; RT "Two genes encoding GF14 (14-3-3) proteins in Zea mays. Structure, RT expression, and potential regulation by the G-box binding complex."; RL Plant Physiol. 106:1593-1604(1994). CC -!- FUNCTION: Is associated with a DNA binding complex to bind to CC the G box, a well-characterized cis-acting DNA regulatory element CC found in plants genes. CC -!- SIMILARITY: Belongs to the 14-3-3 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S77133; AAB33304.1; -. DR PIR; T01752; T01752. DR HSSP; P29312; 1A38. DR MaizeDB; 65832; -. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 261 AA; 29662 MW; 25EC70725A5F6801 CRC64; MASAELSREE NVYMAKLAEQ AERYEEMVEF MEKVAKTVDS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEEGRG NEDRVTLIKD YRGKIETELT KICDGILKLL ETHLVPSSTA PESKVFYLKM KGDYYRYLAE FKTGAERKDA AENTMVAYKA AQDIALAELA PTHPIRLGLA LNFSVFYYEI LNSPDRACSL AKQAFDEAIS ELDTLSEESY KDSTLIMQLL RDNLTLWTSD ISEDPAEEIR EAPKRDSSEG Q // ID 1432_MAIZE STANDARD; PRT; 261 AA. AC Q01526; DT 01-JUL-1993 (Rel. 26, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 14-3-3-like protein GF14-12. GN GRF2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95148741; PubMed=7846163; RA de Vetten N.C., Ferl R.J.; RT "Two genes encoding GF14 (14-3-3) proteins in Zea mays. Structure, RT expression, and potential regulation by the G-box binding complex."; RL Plant Physiol. 106:1593-1604(1994). RN [2] RP SEQUENCE OF 14-261 FROM N.A. RX MEDLINE=93076113; PubMed=1446170; RA de Vetten N.C., Lu G., Ferl R.J.; RT "A maize protein associated with the G-box binding complex has RT homology to brain regulatory proteins."; RL Plant Cell 4:1295-1307(1992). CC -!- FUNCTION: Is associated with a DNA binding complex to bind to the CC G box, a well-characterized cis-acting DNA regulatory element CC found in plants genes. CC -!- SIMILARITY: Belongs to the 14-3-3 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S77135; -; NOT_ANNOTATED_CDS. DR EMBL; M96856; AAA33505.1; -. DR PIR; JQ1680; JQ1680. DR HSSP; P29312; 1A4O. DR TRANSFAC; T04134; -. DR MaizeDB; 65832; -. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 261 AA; 29636 MW; DE7B707538BA1662 CRC64; MASAELSREE NVYMAKLAEQ AERYEEMVEF MEKVAKTVDS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEEGRG NEDRVTLIKD YRGKIETELT KICDGILKLL ESHLVPSSTA PESKVFYLKM KGDYYRYLAE FKTGAERKDA AENTMVAYKA AQDIALAELA PTHPIRLGLA LNFSVFYYEI LNSPDRACSL AKQAFDEAIS ELDTLSEESY KDSTLIMQLL HDNLTLWTSD ISEDPAEEIR EAPKHDLSEG Q // ID 143X_MAIZE STANDARD; PRT; 61 AA. AC P29306; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE 14-3-3-like protein (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RX MEDLINE=94105294; PubMed=8278499; RA Keith C.S., Hoang D.O., Barrett B.M., Feigelman B., Nelson M.C., RA Thai H., Baysdorfer C.; RT "Partial sequence analysis of 130 randomly selected maize cDNA RT clones."; RL Plant Physiol. 101:329-332(1993). CC -!- SIMILARITY: Belongs to the 14-3-3 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95066; AAA18553.2; -. DR HSSP; P29312; 1A38. DR MaizeDB; 25467; -. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; PARTIAL. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT NON_TER 1 1 FT NON_TER 61 61 SQ SEQUENCE 61 AA; 6758 MW; E999A5A3079D6FCA CRC64; ILNSPDRACN LAKQAFDEAI SELDSLGEES YKDSTLIMQL LXDNLTLWTS DTNEDGGDEI K // ID ABP1_MAIZE STANDARD; PRT; 201 AA. AC P13689; Q41193; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Auxin-binding protein 1 precursor (ABP) (ERABP1). GN ABP1 OR AUX311. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Coleoptile; RX MEDLINE=90060001; PubMed=2555179; RA Hesse T., Feldwisch J., Balshuesemann D., Bauw G., Puype M., RA Vandekerckhove J., Loebler M., Klaembt D., Schell J., Palme K.; RT "Molecular cloning and structural analysis of a gene from Zea mays RT (L.) coding for a putative receptor for the plant hormone auxin."; RL EMBO J. 8:2453-2461(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90060002; PubMed=2555180; RA Tillmann U., Viola G., Kayser B., Siemeister G., Hesse T., RA Palme K., Loebler M., Klaembt D.; RT "cDNA clones of the auxin-binding protein from corn coleoptiles (Zea RT mays L.): isolation and characterization by immunological methods."; RL EMBO J. 8:2463-2467(1989). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=89264464; PubMed=2542939; RA Inohara N., Shimomura S., Fukui T., Futai M.; RT "Auxin-binding protein located in the endoplasmic reticulum of maize RT shoots: molecular cloning and complete primary structure."; RL Proc. Natl. Acad. Sci. U.S.A. 86:3564-3568(1989). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=cv. LG11; TISSUE=Shoot; RX MEDLINE=91316232; PubMed=1650260; RA Yu L.X., Lazarus C.M.; RT "Structure and sequence of an auxin-binding protein gene from maize RT (Zea mays L.)."; RL Plant Mol. Biol. 16:925-930(1991). RN [5] RP SEQUENCE FROM N.A., AND VARIANT GLY-13. RX MEDLINE=93142177; PubMed=1668837; RA Lazarus C.M., Napier R.M., Yu L.X., Lynas C., Venis M.A.; RT "Auxin-binding protein -- antibodies and genes."; RL Symp. Soc. Exp. Biol. 45:129-148(1991). RN [6] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=94035191; PubMed=7693132; RA Schwob E., Choi S.Y., Simmons C., Migliaccio F., Ilag L., Hesse T., RA Palme K., Soell D.; RT "Molecular analysis of three maize 22 kDa auxin-binding protein RT genes -- transient promoter expression and regulatory regions."; RL Plant J. 4:423-432(1993). RN [7] RP REVIEW. RX MEDLINE=91313633; PubMed=1650041; RA Napier R.M., Venis M.A.; RT "From auxin-binding protein to plant hormone receptor?"; RL Trends Biochem. Sci. 16:72-75(1991). RN [8] RP DISULFIDE BOND. RX MEDLINE=21622975; PubMed=11749971; RA Feckler C., Muster G., Feser W., Romer A., Palme K.; RT "Mass spectrometric analysis reveals a cysteine bridge between RT residues 2 and 61 of the auxin-binding protein 1 from Zea mays L."; RL FEBS Lett. 509:446-450(2001). CC -!- FUNCTION: This is probably a receptor for the plant hormone auxin. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16309; CAA34376.1; -. DR EMBL; J04550; AAA33436.1; -. DR EMBL; X56737; CAA40061.1; -. DR EMBL; X16308; CAA34375.1; -. DR EMBL; S53630; AAB25115.1; -. DR EMBL; L08425; AAA33430.1; -. DR PIR; S16262; S16262. DR PDB; 1LR5; 20-NOV-02. DR PDB; 1LRH; 20-NOV-02. DR MaizeDB; 25342; -. DR InterPro; IPR000526; Auxin_BP. DR InterPro; IPR007113; Cupin_sup. DR InterPro; IPR000886; ER_target_S. DR Pfam; PF02041; Auxin_BP; 1. DR PRINTS; PR00655; AUXINBINDNGP. DR ProDom; PD006253; Auxin_BP; 1. DR PROSITE; PS00014; ER_TARGET; 1. KW Receptor; Glycoprotein; Endoplasmic reticulum; Signal; 3D-structure. FT SIGNAL 1 38 FT CHAIN 39 201 Auxin-binding protein 1. FT DISULFID 40 99 FT CARBOHYD 133 133 N-linked (GlcNAc...) (Probable). FT SITE 198 201 Prevent secretion from ER. FT VARIANT 13 13 A -> G. FT VARIANT 141 141 N -> S. SQ SEQUENCE 201 AA; 21977 MW; 1AF11DFEC247D9D0 CRC64; MAPDLSELAA AAAARGAYLA GVGVAVLLAA SFLPVAESSC VRDNSLVRDI SQMPQSSYGI EGLSHITVAG ALNHGMKEVE VWLQTISPGQ RTPIHRHSCE EVFTVLKGKG TLLMGSSSLK YPGQPQEIPF FQNTTFSIPV NDPHQVWNSD EHEDLQVLVI ISRPPAKIFL YDDWSMPHTA AVLKFPFVWD EDCFEAAKDE L // ID ABP4_MAIZE STANDARD; PRT; 204 AA. AC P33488; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Auxin-binding protein 4 precursor (ABP). GN ABP4. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94033297; PubMed=8219056; RA Hesse T., Garbers C., Brzobohaty B., Kreimer G., Soell D., RA Melkonian M., Schell J., Palme K.; RT "Two members of the ERabp gene family are expressed differentially in RT reproductive organs but to similar levels in the coleoptile of RT maize."; RL Plant Mol. Biol. 23:57-66(1993). CC -!- FUNCTION: This is probably a receptor for the plant hormone auxin. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S66813; AAB28589.1; -. DR EMBL; L08426; AAA33431.1; -. DR PIR; B43033; B43033. DR MaizeDB; 65341; -. DR InterPro; IPR000526; Auxin_BP. DR InterPro; IPR007113; Cupin_sup. DR InterPro; IPR000886; ER_target_S. DR Pfam; PF02041; Auxin_BP; 1. DR PRINTS; PR00655; AUXINBINDNGP. DR ProDom; PD006253; Auxin_BP; 1. DR PROSITE; PS00014; ER_TARGET; 1. KW Receptor; Glycoprotein; Endoplasmic reticulum; Signal. FT SIGNAL 1 41 By similarity. FT CHAIN 42 204 Auxin-binding protein 4. FT CARBOHYD 136 136 N-linked (GlcNAc...) (Potential). FT SITE 201 204 Prevent secretion from ER. SQ SEQUENCE 204 AA; 22628 MW; 1C71C94BBCB0D242 CRC64; MVRRRPATGA APRPHLAAVG RGLLLASVLA AAASSLPVAE SSCPRDNSLV RDISRMQQRN YGREGFSHIT VTGALAHGTK EVEVWLQTFG PGQRTPIHRH SCEEVFIVLK GKGTLLLGSS SLKYPGQPQE VPVFQNTTFS IPVNDPHQVW NSNEHEDLQV LVIISRPPVK IFIYDDWSMP HTAAKLKFPY FWDEDCLPAP KDEL // ID ABP5_MAIZE STANDARD; PRT; 150 AA. AC P33489; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Auxin-binding protein 5 precursor (ABP) (ERABP5) (Fragment). GN ABP5. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=94035191; PubMed=7693132; RA Schwob E., Choi S.Y., Simmons C., Migliaccio F., Ilag L., Hesse T., RA Palme K., Soell D.; RT "Molecular analysis of three maize 22 kDa auxin-binding protein RT genes -- transient promoter expression and regulatory regions."; RL Plant J. 4:423-432(1993). CC -!- FUNCTION: This is probably a receptor for the plant hormone auxin. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08427; AAA33432.1; -. DR PIR; C43033; C43033. DR MaizeDB; 78602; -. DR InterPro; IPR000526; Auxin_BP. DR InterPro; IPR007113; Cupin_sup. DR Pfam; PF02041; Auxin_BP; 1. DR PRINTS; PR00655; AUXINBINDNGP. DR ProDom; PD006253; Auxin_BP; 1. KW Receptor; Glycoprotein; Endoplasmic reticulum; Signal. FT SIGNAL 1 41 By similarity. FT CHAIN 42 >150 Auxin-binding protein 5. FT CARBOHYD 136 136 N-linked (GlcNAc...) (Potential). FT NON_TER 150 150 SQ SEQUENCE 150 AA; 16225 MW; 951094769D5D6C19 CRC64; MVRRRPATGA AQRPQLAAVG RGLLLASVLA AAASSLPVAE SSCPRDNSLV RDISRMQQSN YGREGFSHIT VTGALAHGTK EVEVWLQTFG PGQRTPIHRH SCEEVFIVLK GKGTLLLGSS SLKYPGQPQE VPVFQNTTFS IPVNDPHQVW // ID ACT1_MAIZE STANDARD; PRT; 375 AA. AC P02582; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Actin 1. GN ACT1 OR ACT-1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83187987; PubMed=6842118; RA Shah D.M., Hightower R.C., Meagher R.B.; RT "Genes encoding actin in higher plants: intron positions are highly RT conserved but the coding sequences are not."; RL J. Mol. Appl. Genet. 2:111-126(1983). CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- FUNCTION: Essential component of cell cytoskeleton; plays an CC important role in cytoplasmic streaming, cell shape determination, CC cell division, organelle movement and extension growth. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- MISCELLANEOUS: There are at least six actin genes in maize. CC -!- SIMILARITY: Belongs to the actin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01238; AAA33433.1; ALT_SEQ. DR PIR; A03008; ATZM1. DR HSSP; P02570; 2BTF. DR MaizeDB; 13835; -. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR Pfam; PF00022; actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Structural protein; Multigene family. SQ SEQUENCE 375 AA; 41617 MW; B658FE903E1131E5 CRC64; MADEDIQPIV CDNGTGMVKA GFAGDDAPRA VFPSIVGRPR HTGVMVGMGQ KDAYVGDEAQ AKRGILTLKY PIEHGIVNNW DDMENWHHTF YNELRVSPED HPVLLTEAPL NPKANREKMT QIMFETFECP AMYVAIEAVL SLYASGRTTG IVMDSGDGVS HTVPIYEGYT LPHAILRLDL AGRDLTDHLM KILTERGYSL TTSAEREIVR DIKEKLAYVA LDYEQELETA KSSSSVEKSY EMPDGQVITI GSERFRCPEV LFQPSLVGME SPSVHEATYN SIMKCDVDIR KDLYGNVVLS GGFTMFPGIA DRMSKEITSL VPSSMKVKVV APPRRKYSVW IGGSILASLS TFQQMWISKG EYDETGPGIV HMKCF // ID ADF1_MAIZE STANDARD; PRT; 139 AA. AC P46251; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Actin-depolymerizing factor 1 (ADF 1) (ZmABP1) (ZmADF1). GN ADF1 OR ABP1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; TISSUE=Pollen; RX MEDLINE=95232182; PubMed=7716228; RA Rozycka M., Lopez I., Khan S., Greenland A.J., Hussey P.J.; RT "A Zea mays pollen cDNA encoding a putative actin-depolymerizing RT factor."; RL Plant Physiol. 107:1011-1012(1995). CC -!- FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F- CC actin) and binds to actin monomers (By similarity). CC -!- TISSUE SPECIFICITY: Expressed in pollen. CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X80820; CAA56786.1; -. DR PIR; T02882; T02882. DR HSSP; Q39250; 1F7S. DR MaizeDB; 113737; -. DR InterPro; IPR002108; Actbind_cofln. DR Pfam; PF00241; cofilin_ADF; 1. DR ProDom; PD002129; Actbind_cofln; 1. DR SMART; SM00102; ADF; 1. DR PROSITE; PS00325; ACTIN_DEPOLYMERIZING; 1. KW Actin-binding; Multigene family. FT DOMAIN 92 111 Actin-binding (Potential). SQ SEQUENCE 139 AA; 16168 MW; 08675E0A2C92D94D CRC64; MANSSSGLAV NDECKVKFRE LKSRRTFRFI VFRIDDTDME IKVDRLGEPN QGYGDFTDSL PANECRYAIY DLDFTTIENC QKSKIFFFSW SPDTARTRSK MLYASSKDRF RRELDGIQCE IQATDPSEMS LDIVRSRTN // ID ADH1_MAIZE STANDARD; PRT; 379 AA. AC P00333; DT 21-JUL-1986 (Rel. 01, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Alcohol dehydrogenase 1 (EC 1.1.1.1). GN ADH1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=84221411; PubMed=6328449; RA Dennis E.S., Gerlach W.L., Pryor A.J., Bennetzen J.L., Inglis A., RA Llewellyn D.J., Sachs M.M., Ferl R.J., Peacock W.J.; RT "Molecular analysis of the alcohol dehydrogenase (Adh1) gene of RT maize."; RL Nucleic Acids Res. 12:3983-4000(1984). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85215511; PubMed=2987807; RA Dennis E.S., Sachs M.M., Gerlach W.L., Finnegan E.J., Peacock W.J.; RT "Molecular analysis of the alcohol dehydrogenase 2 (Adh2) gene of RT maize."; RL Nucleic Acids Res. 13:727-743(1985). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=84261418; PubMed=6378620; RA Braenden C.-I., Eklund H., Cambillau C., Pryor A.J.; RT "Correlation of exons with structural domains in alcohol RT dehydrogenase."; RL EMBO J. 3:1307-1310(1984). RN [4] RP SEQUENCE FROM N.A. (ADH1-F). RC STRAIN=cv. Berkeley Fast; RA Sachs M.M., Dennis E.S., Gerlach W.L., Peacock W.J.; RT "Two alleles of maize alcohol dehydrogenase 1 have 3'-structural and RT poly(A) addition polymorphisms."; RL Genetics 113:449-467(1986). RN [5] RP SEQUENCE FROM N.A. (ADH1-CM). RX MEDLINE=92003667; PubMed=2577507; RA Osterman J.C., Dennis E.S.; RT "Molecular analysis of the ADH1-Cm allele of maize."; RL Plant Mol. Biol. 13:203-212(1989). RN [6] RP SEQUENCE OF 212-379 FROM N.A. RA Gerlach W.L., Pryor A.J., Dennis E.S., Ferl R.J., Sachs M.M., RA Peacock W.J.; RT "cDNA cloning and induction of the alcohol dehydrogenase gene (Adh1) RT of maize."; RL Proc. Natl. Acad. Sci. U.S.A. 79:2981-2985(1982). CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone + CC NADH. CC -!- COFACTOR: Binds 2 zinc ions per subunit. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- POLYMORPHISM: The sequence shown is that of allele ADH1-F. CC -!- MISCELLANEOUS: In maize there are two isozymes. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04049; CAA27681.1; -. DR EMBL; X00580; CAA25239.1; -. DR EMBL; X04050; CAA27682.1; -. DR EMBL; M32984; AAA33434.1; -. DR PIR; S04571; S04571. DR HSSP; P11766; 1TEH. DR MaizeDB; 13844; -. DR InterPro; IPR002328; ADH_zinc. DR InterPro; IPR002085; Adh_zn_family. DR InterPro; IPR000205; NAD_BS. DR Pfam; PF00107; ADH_zinc_N; 1. DR PROSITE; PS00059; ADH_ZINC; 1. KW Oxidoreductase; Zinc; Metal-binding; NAD; Multigene family; KW Polymorphism. FT METAL 47 47 Zinc 1 (catalytic). FT METAL 69 69 Zinc 1 (catalytic). FT METAL 99 99 Zinc 2. FT METAL 102 102 Zinc 2. FT METAL 105 105 Zinc 2. FT METAL 113 113 Zinc 2. FT METAL 177 177 Zinc 1 (catalytic). FT VARIANT 52 52 Y -> D (in allele ADH1-Cm). FT VARIANT 127 127 A -> G (in allele ADH1-S). FT VARIANT 179 179 Y -> I (in allele ADH1-Cm and allele FT ADH1-S). FT VARIANT 363 363 D -> N (in allele ADH1-S). SQ SEQUENCE 379 AA; 40981 MW; 5E0618F7E1A4B973 CRC64; MATAGKVIKC KAAVAWEAGK PLSIEEVEVA PPQAMEVRVK ILFTSLCHTD VYFWEAKGQT PVFPRIFGHE AGGIIESVGE GVTDVAPGDH VLPVFTGECK ECAHCKSAES NMCDLLRINT DRGVMIADGK SRFSINGKPI YHFVGTSTFS EYTVMHVGCV AKINPQAPLD KVCVLSCGYS TGLGASINVA KPPKGSTVAV FGLGAVGLAA AEGARIAGAS RIIGVDLNPS RFEEARKFGC TEFVNPKDHN KPVQEVLAEM TNGGVDRSVE CTGNINAMIQ AFECVHDGWG VAVLVGVPHK DAEFKTHPMN FLNERTLKGT FFGNYKPRTD LPNVVELYMK KELEVEKFIT HSVPFAEINK AFDLMAKGEG IRCIIRMEN // ID ADH2_MAIZE STANDARD; PRT; 379 AA. AC P04707; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alcohol dehydrogenase 2 (EC 1.1.1.1). GN ADH2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85215511; PubMed=2987807; RA Dennis E.S., Sachs M.M., Gerlach W.L., Finnegan E.J., Peacock W.J.; RT "Molecular analysis of the alcohol dehydrogenase 2 (Adh2) gene of RT maize."; RL Nucleic Acids Res. 13:727-743(1985). CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone + CC NADH. CC -!- COFACTOR: Binds 2 zinc ions per subunit. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- MISCELLANEOUS: In maize there are two isozymes. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X01965; CAA26001.1; -. DR PIR; A23084; A23084. DR HSSP; P11766; 1TEH. DR MaizeDB; 13844; -. DR InterPro; IPR002328; ADH_zinc. DR InterPro; IPR002085; Adh_zn_family. DR InterPro; IPR000205; NAD_BS. DR Pfam; PF00107; ADH_zinc_N; 1. DR PROSITE; PS00059; ADH_ZINC; 1. KW Oxidoreductase; Zinc; Metal-binding; NAD; Multigene family. FT METAL 47 47 Zinc 1 (catalytic). FT METAL 69 69 Zinc 1 (catalytic). FT METAL 99 99 Zinc 2. FT METAL 102 102 Zinc 2. FT METAL 105 105 Zinc 2. FT METAL 113 113 Zinc 2. FT METAL 177 177 Zinc 1 (catalytic). SQ SEQUENCE 379 AA; 41054 MW; BC09E47DD5EA894F CRC64; MATAGKVIKC RAAVTWEAGK PLSIEEVEVA PPQAMEVRIK ILYTALCHTD VYFWEAKGQT PVFPRILGHE AGGIVESVGE GVTDVAPGDH VLPVFTGECK ECAHCKSEES NMCDLLRINV DRGVMIGDGK SRFTISGQPI FHFVGTSTFS EYTVIHVGCL AKINPEAPLD KVCILSCGIS TGLGATLNVA KPAKGSTVAI FGLGAVGLAA MEGARLAGAS RIIGVDINPA KYEQAKKFGC TEFVNPKDHD KPVQEVLIEL TNGGVDRSVE CTGNVNAMIS AFECVHDGWG VAVLVGVPHK DDQFKTHPMN FLSEKTLKGT FFGNYKPRTD LPNVVEMYMK KELELEKFIT HSVPFSEINT AFDLMLKGES LRCIMRMED // ID ADT1_MAIZE STANDARD; PRT; 387 AA. AC P04709; DT 13-AUG-1987 (Rel. 05, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE ADP,ATP carrier protein 1, mitochondrial precursor (ADP/ATP DE translocase 1) (Adenine nucleotide translocator 1) (ANT 1). GN ANT1 OR ANT-G1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. MUTIND-FR7205034; RX MEDLINE=91322533; PubMed=1863785; RA Winning B.M., Day C.D., Sarah C.J., Leaver C.J.; RT "Nucleotide sequence of two cDNAs encoding the adenine nucleotide RT translocator from Zea mays L."; RL Plant Mol. Biol. 17:305-307(1991). RN [2] RP SEQUENCE OF 59-387 FROM N.A. RC STRAIN=cv. B37N; RX MEDLINE=89338399; PubMed=2547608; RA Leaver C.J., Bathgate B., Baker A.; RT "Two genes encode the adenine nucleotide translocator of maize RT mitochondria. Isolation, characterisation and expression of the RT structural genes."; RL Eur. J. Biochem. 183:303-310(1989). RN [3] RP SEQUENCE OF 70-387 FROM N.A. RX MEDLINE=85297781; PubMed=2994015; RA Baker A., Leaver C.J.; RT "Isolation and sequence analysis of a cDNA encoding the ATP/ADP RT translocator of Zea mays L."; RL Nucleic Acids Res. 13:5857-5867(1985). CC -!- FUNCTION: Catalyzes the exchange of ADP and ATP across the CC mitochondrial inner membrane. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Mitochondrial CC inner membrane. CC -!- SIMILARITY: Belongs to the mitochondrial carrier family. CC -!- SIMILARITY: Contains 3 Solcar repeats. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57556; CAA40781.1; -. DR EMBL; X15711; CAA33742.1; -. DR EMBL; X02842; CAA26600.1; -. DR PIR; S14876; S14876. DR MaizeDB; 17145; -. DR InterPro; IPR001993; Mitoch_carrier. DR InterPro; IPR002067; Mit_carrier. DR Pfam; PF00153; mito_carr; 3. DR PRINTS; PR00926; MITOCARRIER. DR PROSITE; PS50920; SOLCAR; 3. KW Mitochondrion; Inner membrane; Repeat; Transmembrane; Transport; KW Transit peptide; Multigene family. FT TRANSIT 1 77 Mitochondrion. FT CHAIN 78 387 ADP,ATP carrier protein 1. FT TRANSMEM 91 108 1 (Potential). FT TRANSMEM 153 171 2 (Potential). FT TRANSMEM 196 213 3 (Potential). FT TRANSMEM 257 276 4 (Potential). FT TRANSMEM 296 313 5 (Potential). FT TRANSMEM 352 370 6 (Potential). FT REPEAT 85 178 Solcar 1. FT REPEAT 190 282 Solcar 2. FT REPEAT 290 376 Solcar 3. FT CONFLICT 102 102 K -> E (in Ref. 2). FT CONFLICT 154 154 N -> Y (in Ref. 3). SQ SEQUENCE 387 AA; 42391 MW; DE73BB0F478BD57D CRC64; MADQANQPTV LHKLGGQFHL RSIISEGVRA RNICPSVSSY ERRFATRNYM TQSLWGPSMS VSGGINVPVM QTPLCANAPA EKGGKNFMID FMMGGVSAAV SKTAAAPIER VKLLIQNQDE MIKSGRLSEP YKGIVDCFKR TIKDEGFSSL WRGNTANVIR YFPTQALNFA FKDYFKRLFN FKKDRDGYWK WFAGNLASGG AAGASSLFFV YSLDYARTRL ANDAKAAKGG GERQFNGLVD VYRKTLKSDG IAGLYRGFNI SCVGIIVYRG LYFGLYDSIK PVVLTGNLQD NFFASFALGW LITNGAGLAS YPIDTVRRRM MMTSGEAVKY KSSLDAFQQI LKKEGPKSLF KGAGANILRA IAGAGVLSGY DQLQILFFGK KYGSGGA // ID ADT2_MAIZE STANDARD; PRT; 387 AA. AC P12857; DT 01-OCT-1989 (Rel. 12, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE ADP,ATP carrier protein 2, mitochondrial precursor (ADP/ATP DE translocase 2) (Adenine nucleotide translocator 2) (ANT 2). GN ANT2 OR ANT-G2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. MUTIND-FR7205034; RX MEDLINE=91322533; PubMed=1863785; RA Winning B.M., Day C.D., Sarah C.J., Leaver C.J.; RT "Nucleotide sequence of two cDNAs encoding the adenine nucleotide RT translocator from Zea mays L."; RL Plant Mol. Biol. 17:305-307(1991). RN [2] RP SEQUENCE OF 59-387 FROM N.A. RC STRAIN=cv. B37N; RX MEDLINE=89338399; PubMed=2547608; RA Leaver C.J., Bathgate B., Baker A.; RT "Two genes encode the adenine nucleotide translocator of maize RT mitochondria. Isolation, characterisation and expression of the RT structural genes."; RL Eur. J. Biochem. 183:303-310(1989). CC -!- FUNCTION: Catalyzes the exchange of ADP and ATP across the CC mitochondrial inner membrane. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Mitochondrial CC inner membrane. CC -!- SIMILARITY: Belongs to the mitochondrial carrier family. CC -!- SIMILARITY: Contains 3 Solcar repeats. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X59086; CAA41812.1; -. DR EMBL; X15712; CAA33743.1; -. DR PIR; S16568; S16568. DR MaizeDB; 17145; -. DR InterPro; IPR001993; Mitoch_carrier. DR InterPro; IPR002067; Mit_carrier. DR Pfam; PF00153; mito_carr; 3. DR PRINTS; PR00926; MITOCARRIER. DR PROSITE; PS50920; SOLCAR; 3. KW Mitochondrion; Inner membrane; Repeat; Transmembrane; Transport; KW Transit peptide; Multigene family. FT TRANSIT 1 77 Mitochondrion. FT CHAIN 78 387 ADP,ATP carrier protein 2. FT TRANSMEM 91 108 1 (Potential). FT TRANSMEM 153 171 2 (Potential). FT TRANSMEM 196 213 3 (Potential). FT TRANSMEM 257 276 4 (Potential). FT TRANSMEM 296 313 5 (Potential). FT TRANSMEM 352 370 6 (Potential). FT REPEAT 85 178 Solcar 1. FT REPEAT 190 282 Solcar 2. FT REPEAT 290 376 Solcar 3. FT CONFLICT 242 242 Y -> I (in Ref. 2). FT CONFLICT 327 327 A -> G (in Ref. 2). SQ SEQUENCE 387 AA; 42332 MW; 020E616DC5EC2664 CRC64; MADQANQPTV LHKLGGQFHL SSSFSEGVRA RNICPSFSPY ERRFATRNYM TQSLWGPSMS VSGGINVPVM PTPLFANAPA EKGGKNFMID FMMGGVSAAV SKTAAAPIER VKLLIQNQDE MIKSGRLSEP YKGIADCFKR TIKDEGFSSL WRGNTANVIR YFPTQALNFA FKDYFKRLFN FKKDRDGYWK WFAGNLASGG AAGASSLFFV YSLDYARTRL ANDAKAAKGG GDRQFNGLVD VYRKTLKSDG IAGLYRGFNI SCVGIIVYRG LYFGLYDSIK PVVLTGSLQD NFFASFALGW LITNGAGLAS YPIDTVRRRM MMTSGEAVKY KSSLDAFQQI LKKEGPKSLF KGAGANILRA IAGAGVLSGY DQLQILFFGK KYGSGGA // ID AKH1_MAIZE STANDARD; PRT; 920 AA. AC P49079; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplast DE precursor (AK-HD 1) (AK-HSDH 1) [Includes: Aspartokinase (EC 2.7.2.4); DE Homoserine dehydrogenase (EC 1.1.1.3)]. GN AKHSDH1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seedling leaf; RX MEDLINE=95148730; PubMed=7846152; RA Muehlbauer G.J., Somers D.A., Matthews B.F., Gengenbach B.G.; RT "Molecular genetics of the maize (Zea mays L.) aspartate kinase- RT homoserine dehydrogenase gene family."; RL Plant Physiol. 106:1303-1312(1994). CC -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4- CC semialdehyde + NAD(P)H. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. CC -!- PATHWAY: Catalyzes 2 nonconsecutive reactions in the common CC biosynthetic pathway leading from Asp to diaminopimelate and Lys, CC to Met, and to Thr and Ile. CC -!- SUBUNIT: Homo- or heterodimer (Potential). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC aspartokinase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine CC dehydrogenase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L33912; AAA74360.1; -. DR PIR; T02953; T02953. DR MaizeDB; 66609; -. DR InterPro; IPR001048; Aa_kinase. DR InterPro; IPR002912; ACT. DR InterPro; IPR001341; Aspartate_kinase. DR InterPro; IPR001342; Homoserine_dh. DR InterPro; IPR005106; NAD_binding_3. DR Pfam; PF00696; aakinase; 1. DR Pfam; PF01842; ACT; 2. DR Pfam; PF00742; Homoserine_dh; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. DR PROSITE; PS01042; HOMOSER_DHGENASE; 1. KW Transferase; Kinase; Oxidoreductase; Methionine biosynthesis; NADP; KW Multifunctional enzyme; Chloroplast; Transit peptide; KW Multigene family. FT TRANSIT 1 92 Chloroplast (Potential). FT CHAIN 93 920 Bifunctional aspartokinase/homoserine FT dehydrogenase 1. FT DOMAIN 93 341 Aspartokinase. FT DOMAIN 342 566 Interface. FT DOMAIN 567 920 Homoserine dehydrogenase. FT NP_BIND 568 573 NADP (Potential). SQ SEQUENCE 920 AA; 100335 MW; 08DCF444BE645529 CRC64; MRSLTVASRH PGAAFSTRRR PLLHPAAAGR DSTFQRCWRW EKTQDSSFGS SLRTSRLPRT VHGDILKNLL APTAGAVSVE QAEAIADLPK GDMWSVHKFG GTCMGTSERI HNVADIVLRD PSERKLVVVS AMSKVTDMMY NLVNKAQSRD DSYIAVLDEV FDKHMTTAKD LLAGEDLARF LSQLHADISN LKAMLRAIYI AGHATESFSD FVVGHGELWS AQMLSYAIQK SGTPCSWMDT REVLVVNPSG ANQVDPDYLE SEKRLEKWFS RCPAETIIAT GFIASTPENI PTTLKRDGSD FSAAIIGSLV KARQVTIWTD VDGVFSADPR KVSEAVILST LSYQEAWEMS YFGANVLHPR TIIPVMKYNI PIVIRNIFNT SAPGTMICQQ PANENGDLEA CVKAFATIDK LALVNVEGTG MAGVPGTANA IFGAVKDVGA NVIMISQASS EHSVCFAVPE KEVALVSAAL HARFREALAA GRLSKVEVIH NCSILATVGL RMASTPGVSA TLFDALAKAN INVRAIAQGC SEYNITIVLK QEDCVRALRA AHSRFFLSKT TLAVGIIGPG LIGRTLLNQL KDQAAVLKEN MNIDLRVMGI AGSRTMLLSD IGVDLTQWKE KLQTEAEPAN LDKFVHHLSE NHFFPNRVLV DCTADTSVAS HYYDWLKKGI HVITPNKKAN SGPLDRYLKL RTLQRASYTH YFYEATVGAG LPIISTLRGL LETGDKILRI EGIFSGTLSY IFNNFEGART FSDVVAEAKK AGYTEPDPRD DLSGTDVARK VIILARESGL GLELSDIPVR SLVPEALKSC TSADEYMQKL PSFDEDWARE RKNAEAAGEV LRYVGVVDVV SKKGQVELRA YKRDHPFAQL SGSDNIIAFT TSRYKDQPLI VRGPGAGAEV TAGGVFCDIL RLSSYLGAPS // ID AKH2_MAIZE STANDARD; PRT; 917 AA. AC P49080; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplast DE precursor (AK-HD 2) (AK-HSDH 2) [Includes: Aspartokinase (EC 2.7.2.4); DE Homoserine dehydrogenase (EC 1.1.1.3)]. GN AKHSDH2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seedling leaf; RX MEDLINE=95148730; PubMed=7846152; RA Muehlbauer G.J., Somers D.A., Matthews B.F., Gengenbach B.G.; RT "Molecular genetics of the maize (Zea mays L.) aspartate kinase- RT homoserine dehydrogenase gene family."; RL Plant Physiol. 106:1303-1312(1994). CC -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4- CC semialdehyde + NAD(P)H. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. CC -!- PATHWAY: Catalyzes 2 nonconsecutive reactions in the common CC biosynthetic pathway leading from Asp to diaminopimelate and Lys, CC to Met, and to Thr and Ile. CC -!- SUBUNIT: Homo- or heterodimer (Potential). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC aspartokinase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the homoserine CC dehydrogenase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L33913; AAA74361.1; -. DR PIR; T02954; T02954. DR MaizeDB; 66609; -. DR InterPro; IPR001048; Aa_kinase. DR InterPro; IPR002912; ACT. DR InterPro; IPR001341; Aspartate_kinase. DR InterPro; IPR001342; Homoserine_dh. DR InterPro; IPR005106; NAD_binding_3. DR Pfam; PF00696; aakinase; 1. DR Pfam; PF01842; ACT; 2. DR Pfam; PF00742; Homoserine_dh; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS00324; ASPARTOKINASE; 1. DR PROSITE; PS01042; HOMOSER_DHGENASE; 1. KW Transferase; Kinase; Oxidoreductase; Methionine biosynthesis; NADP; KW Multifunctional enzyme; Chloroplast; Transit peptide; KW Multigene family. FT TRANSIT 1 89 Chloroplast (Potential). FT CHAIN 90 917 Bifunctional aspartokinase/homoserine FT dehydrogenase 2. FT DOMAIN 90 338 Aspartokinase. FT DOMAIN 339 563 Interface. FT DOMAIN 564 917 Homoserine dehydrogenase. FT NP_BIND 565 570 NADP (Potential). SQ SEQUENCE 917 AA; 99582 MW; 69229EA13CAEA7E9 CRC64; MQGLAVSCQL PPAAAAARWR PRASSSNREA VLQCWKYELS QDHYLGGPLR IGQSQGSLHR HRSTNFLRPA AAAISVEQDE VNTYLPKGDM WSVHKFGGTC MGTPKRIQCV ANIVLGDSSE RKLIIVSAMS KVTDMMYNLV QKAQSRDDSY AIALAEVFEK HMTAAKDLLD GEDLARFLSQ LHSDVSNLRA MLRAIYIAGH ATESFSDFVV GHGELWSAQM LSYAIKKSGA PCSWMDTREV LVVTPSGCNQ VDPDYLECEK RLQKWFSRQP AEIIVATGFI ASTAGNIPTT LKRDGSDFSA AIVGSLVRAR QVTIWTDVDG VFSADPRKVS EAVILSTLSY QEAWEMSYFG ANVLHPRTII PVMKDNIPIV IRNMFNLSAP GTMICKQPAN ENGDLDACVK SFATVDNLAL VNVEGTGMAG VPGTASAIFS AVKDVGANVI MISQASSEHS VCFAVPEKEV AVVSAELHDR FREALAAGRL SKVEVINGCS ILAAVGLRMA STPGVSAILF DALAKANINV RAIAQGCSEY NITVVLKQQD CVRALRAAHS RFFLSKTTLA VGIIGPGLIG GALLNQLKNQ TAVLKENMNI DLRVIGITGS STMLLSDTGI DLTQWKQLLQ KEAEPADIGS FVHHLSDNHV FPNKVLVDCT ADTSVASHYY DWLKKGIHVI TPNKKANSGP LDQYLKLRTM QRASYTHYFY EATVGAGLPI ISTLRGLLET GDKILRIEGI FSGTLSYIFN NFEGTRAFSD VVAEAREAGY TEPDPRDDLS GTDVARKVVV LARESGLRLE LSDIPVKSLV PETLASCSSA DEFMQKLPSF DEDWARQRSD AEAAGEVLRY VGALDAVNRS GQVELRRYRR DHPFAQLSGS DNIIAFTTSR YKEQPLIVRG PGAGAEVTAG GVFCDILRLA SYLGAPS // ID ALB3_MAIZE STANDARD; PRT; 303 AA. AC P10593; DT 01-JUL-1989 (Rel. 11, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Albumin b-32 protein (EC 3.2.2.22) (Opaque-6 protein) (rRNA N- DE glycosidase). GN O6. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91346687; PubMed=2102870; RA Hartings H., Lazzaroni N., Marsan P.A., Aragay A., Thompson R., RA Salamini F., di Fonzo N., Palau J., Motto M.; RT "The b-32 protein from maize endosperm: characterization of genomic RT sequences encoding two alternative central domains."; RL Plant Mol. Biol. 14:1031-1040(1990). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Endosperm; RX MEDLINE=88334499; PubMed=3419419; RA di Fonzo N., Hartings H., Brembilla M., Motto M., Soave C., RA Navarro E., Palau J., Rhode W., Salamini F.; RT "The b-32 protein from maize endosperm, an albumin regulated by the RT O2 locus: nucleic acid (cDNA) and amino acid sequences."; RL Mol. Gen. Genet. 212:481-487(1988). CC -!- FUNCTION: A possible regulatory factor for the synthesis of zeins, CC the major group of storage proteins. CC -!- CATALYTIC ACTIVITY: Endohydrolysis of the N-glycosidic bond at one CC specific adenosine on the 28S rRNA. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- TISSUE SPECIFICITY: Endosperm. CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. CC Type 1 RIP subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54212; CAA38124.1; -. DR EMBL; X07987; CAA30797.1; -. DR PIR; S03172; S03172. DR MaizeDB; 30000; -. DR InterPro; IPR001574; RIP. DR Pfam; PF00161; RIP; 1. DR PRINTS; PR00396; SHIGARICIN. DR PROSITE; PS00275; SHIGA_RICIN; 1. KW Plant defense; Protein synthesis inhibitor; Hydrolase; Toxin. FT DOMAIN 182 188 Poly-Ala. FT DOMAIN 286 294 Poly-Ala. FT CONFLICT 269 269 D -> N (in Ref. 2). SQ SEQUENCE 303 AA; 32428 MW; 24003521CEF91790 CRC64; MAETNPELSD LMAQTNKKIV PKFTEIFPVE DVNYPYSAFI ASVRKDVIKH CTDHKGIFQP VLPPEKKVPE LWFYTELKTR TSSITLAIRM DNLYLVGFRT PGGVWWELAR PATPTSSATT PGGSASAAGT RTSSATRVWR PSPWAARDDQ GRQRPGEEEE DGDTGGGGGA DADADAGGAE LAAAAAAADP QADTKSKLVK LVVMVCEGLR FNTLSRTVDA GFNSQHGVTL TVTQGKQVQK WDRISKAAFE WADHPTAVIP DMQKLGIKDK NEAARIVALV KNQTTAAAAA ATAASADNDD DEA // ID ALF_MAIZE STANDARD; PRT; 355 AA. AC P08440; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Fructose-bisphosphate aldolase, cytoplasmic isozyme (EC 4.1.2.13). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89012000; PubMed=3172237; RA Dennis E.S., Gerlach W.L., Walker J.C., Lavin M., Peacock W.J.; RT "Anaerobically regulated aldolase gene of maize. A chimaeric origin?"; RL J. Mol. Biol. 202:759-767(1988). RN [2] RP SEQUENCE FROM N.A. RA Kelley P.M., Tolan D.R.; RT "The complete amino acid sequence for the anaerobically induced RT aldolase from maize derived from cDNA clones."; RL Plant Physiol. 82:1076-1080(1986). CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone CC phosphate + D-glyceraldehyde 3-phosphate. CC -!- PATHWAY: Glycolysis; sixth step. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X12872; CAA31366.1; -. DR EMBL; M16220; AAA33435.1; -. DR PIR; S07789; ADZM. DR HSSP; P00883; 1ADO. DR MaizeDB; 24903; -. DR InterPro; IPR000741; Aldolase_I. DR Pfam; PF00274; glycolytic_enzy; 1. DR ProDom; PD001128; Aldolase_I; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. KW Lyase; Schiff base; Glycolysis. FT ACT_SITE 183 183 Proton acceptor (By similarity). FT ACT_SITE 225 225 Schiff-base intermediate with FT dihydroxyacetone-P. FT SITE 355 355 Necessary for preference for fructose FT 1,6-bisphosphate over fructose 1- FT phosphate. FT BINDING 52 52 C-1-phosphate group of the substrate. FT BINDING 142 142 C-1-phosphate group of the substrate. SQ SEQUENCE 355 AA; 38604 MW; 54B480978ECD1470 CRC64; MSAYCGKYKD ELIKNAAYIG TPGKGILAAD ESTGTIGKRL SSINVENVEE NRRALRELLF CCPGALQYIS GVILFEETLY QKTKDGKPFV DVLKEGGVLP GIKVDKGTIE VVGTDKETTT QGHDDLGKRC AKYYEAGARF AKWRAVLKIG PNEPSQLAID LNAQGLARYA IICQENGLVP IVEPEILVDG PHDIDRCAYV TETVLAACYK ALNEHHVLLE GTLLKPNMVT PGSDSKKVTP EVIAEYTVRT LQRTVPAAVP AVLFLSGGQS EEEATRNLNA MNKLSTKKPW SLSFSFGRAL QASTLKAWAG KVENLEKARA AFLARCKANS EATLGTYKGD AAADTESLHV KDYKY // ID AMYB_MAIZE STANDARD; PRT; 488 AA. AC P55005; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Beta-amylase (EC 3.2.1.2) (1,4-alpha-D-glucan maltohydrolase). GN BMY1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. TN351; TISSUE=Aleurone; RX MEDLINE=97198548; PubMed=9046591; RA Wang S.M., Lue W.L., Wu S.Y., Huang H.W., Chen J.; RT "Characterization of a maize beta-amylase cDNA clone and its RT expression during seed germination."; RL Plant Physiol. 113:403-409(1997). CC -!- CATALYTIC ACTIVITY: Hydrolysis of 1,4-alpha-glucosidic linkages in CC polysaccharides so as to remove successive maltose units from the CC non-reducing ends of the chains. CC -!- SIMILARITY: Belongs to family 14 of glycosyl hydrolases. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z25871; CAA81091.1; -. DR PIR; S37075; S37075. DR HSSP; P16098; 1B1Y. DR MaizeDB; 30053; -. DR InterPro; IPR001554; Glyco_hydro_14. DR Pfam; PF01373; Glyco_hydro_14; 1. DR PRINTS; PR00750; BETAAMYLASE. DR PROSITE; PS00506; BETA_AMYLASE_1; 1. DR PROSITE; PS00679; BETA_AMYLASE_2; 1. KW Hydrolase; Glycosidase; Polysaccharide degradation. FT ACT_SITE 184 184 By similarity. FT ACT_SITE 378 378 By similarity. SQ SEQUENCE 488 AA; 55180 MW; A04D57F1C73C064E CRC64; MAGNALANYV QVYVMLPLDV ITVDNTFEKE DETRAQLKKL TEAGADGVMI DVWWGLVEGK EPGVYDWSAY RQVFKLVQEA GLKLQAIMSC HQCGGNVGDV VNIPIPQWVR DVGKSNPDIF YTNRSGLTNI EYLTLGVDDQ PLFHGRTAIQ LYADYMKSFR ENMADFLDAG VVVDIEVGLG PAGEMRYPSY PQSQGWVFPG VGEFICYDKY LQADFKAAAE EAGHPEWDLL DDAGTYNDTP EKTQFFADNG TYQTDKGKFF LTWYSNKLIK HGDKILDEAN KVFLGCKVQL AIKVSGIHWW YNVPNHAAEL TAGYYNLDDR DGYRTIAHML TRHRASMNFT CAEMRDSEQS SEAKSAPEEL VQQVLSAGWR EGLNLACENA LNRYDATAYN TILRNARPQG INKNGPPEHK LHGFTYLRVS DELFQEQNYT TFKTFVRRMH ANLDYNPNVD PVAPLERSKA EIPIEEILEV AQPKLEPFPF DKDTDLPV // ID ARF_MAIZE STANDARD; PRT; 180 AA. AC P49076; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE ADP-ribosylation factor. GN ARF1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Black Mexican Sweet; RX MEDLINE=95201256; PubMed=7894026; RA Verwoert I.I.G.S., Brown A., Slabas A.R., Stuitje A.R.; RT "A Zea mays GTP-binding protein of the ARF family complements an RT Escherichia coli mutant with a temperature-sensitive malonyl-coenzyme RT A:acyl carrier protein transacylase."; RL Plant Mol. Biol. 27:629-633(1995). CC -!- FUNCTION: GTP-binding protein that functions as an allosteric CC activator of the cholera toxin catalytic subunit, an ADP- CC ribosyltransferase. Involved in protein trafficking; may modulate CC vesicle budding and uncoating within the Golgi apparatus. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X80042; CAA56351.1; -. DR PIR; S53486; S49325. DR HSSP; P32889; 1RRF. DR MaizeDB; 113878; -. DR InterPro; IPR006688; ARF. DR InterPro; IPR006689; ARF/SAR. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00025; arf; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01019; ARF; 1. KW GTP-binding; Myristate; Protein transport; Golgi stack; Lipoprotein. FT INIT_MET 0 0 By similarity. FT LIPID 1 1 N-myristoyl glycine (Potential). FT NP_BIND 23 30 GTP (By similarity). FT NP_BIND 66 70 GTP (By similarity). FT NP_BIND 125 128 GTP (By similarity). SQ SEQUENCE 180 AA; 20529 MW; 5CD4FE8058398556 CRC64; GLTFTKLFSR LFAKKEMRIL MVGLDAAGKT TILYKLKLGE IVTTIPTIGF NVETVEYKNI SFTVWDVGGQ DKIRPLWRHY FQNTQGLIFV VDSNDRDRVV EARDELHRML NEDELRDAVL LVFANKQDLP NAMNAAEITD KLGLNSLRQR HWYIQSTCAT TGEGLYEGLD WLSSNIATKS // ID ARLC_MAIZE STANDARD; PRT; 610 AA. AC P13526; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Anthocyanin regulatory Lc protein. GN LC. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89386686; PubMed=2674946; RA Ludwig S.R., Habera L.F., Dellaporta S.L., Wessler S.R.; RT "Lc, a member of the maize R gene family responsible for RT tissue-specific anthocyanin production, encodes a protein similar to RT transcriptional activators and contains the myc-homology region."; RL Proc. Natl. Acad. Sci. U.S.A. 86:7092-7096(1989). CC -!- FUNCTION: Putative transcriptional activator. Control tissue- CC specific synthesis of anthocyanin pigments in various parts of CC the maize plant. CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another CC bHLH protein. CC -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M26227; AAA33504.1; -. DR PIR; A41388; A41388. DR TRANSFAC; T00463; -. DR MaizeDB; 65390; -. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Nuclear protein; Transcription regulation; Activator; DNA-binding. FT DNA_BIND 413 425 Basic motif. FT DOMAIN 426 462 Helix-loop-helix motif. SQ SEQUENCE 610 AA; 66272 MW; B691DB48B94AC757 CRC64; MALSASRVQQ AEELLQRPAE RQLMRSQLAA AARSINWSYA LFWSISDTQP GVLTWTDGFY NGEVKTRKIS NSVELTSDQL VMQRSDQLRE LYEALLSGEG DRRAAPARPA GSLSPEDLGD TEWYYVVSMT YAFRPGQGLP GRSFASDEHV WLCNAHLAGS KAFPRALLAK SASIQSILCI PVMGGVLELG TTDTVPEAPD LVSRATAAFW EPQCPSSSPS GRANETGEAA ADDGTFAFEE LDHNNGMDDI EAMTAAGGHG QEEELRLREA EALSDDASLE HITKEIEEFY SLCDEMDLQA LPLPLEDGWT VDASNFEVPC SSPQPAPPPV DRATANVAAD ASRAPVYGSR ATSFMAWTRS SQQSSCSDDA APAAVVPAIE EPQRLLKKVV AGGGAWESCG GATGAAQEMS GTGTKNHVMS ERKRREKLNE MFLVLKSLLP SIHRVNKASI LAETIAYLKE LQRRVQELES SREPASRPSE TTTRLITRPS RGNNESVRKE VCAGSKRKSP ELGRDDVERP PVLTMDAGTS NVTVTVSDKD VLLEVQCRWE ELLMTRVFDA IKSLHLDVLS VQASAPDGFM GLKIRAQFAG SGAVVPWMIS EALRKAIGKR // ID ARRS_MAIZE STANDARD; PRT; 612 AA. AC P13027; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Anthocyanin regulatory R-S protein. GN R-S. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=90016898; PubMed=2798145; RA Perrot G.H., Cone K.C.; RT "Nucleotide sequence of the maize R-S gene."; RL Nucleic Acids Res. 17:8003-8003(1989). CC -!- FUNCTION: Putative transcriptional activator. Control tissue- CC specific synthesis of anthocyanin pigments in various parts of CC the maize plant. CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another CC bHLH protein. CC -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15806; CAA33805.1; -. DR PIR; S06072; S06072. DR MaizeDB; 60508; -. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS50888; HLH; 1. KW Nuclear protein; Transcription regulation; Activator; DNA-binding. FT DNA_BIND 415 427 Basic motif. FT DOMAIN 428 464 Helix-loop-helix motif. SQ SEQUENCE 612 AA; 66620 MW; 79CEDB283043831C CRC64; MAVSASRVQQ AEELLQRPAE RQLMRSQLAA AARSINWSYA LFWSISDTQP GVLTWTDGFY NGEVKTRKIS NSVELTSDQL VMQRSDQLRE LYEALLSGEG DRRAAPARPA GSLSPEDLGD TEWYYVVSMT YAFRPGQGLP GRSFASDEHV WLCNAHLAGS KAFPRALLAK SASIQSILCI PVMGGVLELG TTDTVPEAPD LVSRATAAFW EPQCPTYSEE PSSSPSGRAN ETGEAAADDG TFAFEELDHN NGMDIEAMTA AGGHGQEEEL RLREAEALSD DASLEHITKE IEEFYSLCDE MDLQALPLPL EDGWTVDASN FEVPCSSPQP APPPVDRATA NVAADASRAP VYGSRATSFM AWTRSSQQSS CSDDAAPAVV PAIEEPQRLL KKVVAGGGAW ESCGGATGAA QEMSATKNHV MSERKRREKL NEMFLVLKSL LPSIHRVNKA SILAETIAYL KELQRRVQEL ESSREPASRP SETTTRLITR PSRGNNESVR KEVCAGSKRK SPELGRDDVE RPPVLTMDAG SSNVTVTVSD KDVLLEVQCR WEELLMTRVF DAIKSLHLDV LSVQASAPDG FMGLKIRAQF AGSGAVVPWM ISEALRKAIG KR // ID ASNS_MAIZE STANDARD; PRT; 585 AA. AC P49094; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Asparagine synthetase [glutamine-hydrolyzing] (EC 6.3.5.4) (Glutamine- DE dependent asparagine synthetase). GN ASN1 OR AS. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. DEA; TISSUE=Root meristem; RX MEDLINE=96158342; PubMed=8580967; RA Chevalier C., Bourgeois E., Just D., Raymond P.; RT "Metabolic regulation of asparagine synthetase gene expression in RT maize (Zea mays L.) root tips."; RL Plant J. 9:1-11(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + L-glutamine = AMP + CC diphosphate + L-asparagine + L-glutamate. CC -!- PATHWAY: Asparagine biosynthesis. CC -!- SIMILARITY: Belongs to the asparagine synthetase family. CC -!- SIMILARITY: Contains 1 type-2 glutamine amidotransferase domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X82849; CAA58052.1; -. DR PIR; T02978; T02978. DR HSSP; P22106; 1CT9. DR MaizeDB; 79071; -. DR InterPro; IPR006426; Asn_synth_AEB. DR InterPro; IPR001962; Asn_synthase. DR InterPro; IPR000583; GATase_2. DR Pfam; PF00733; Asn_synthase; 1. DR Pfam; PF00310; GATase_2; 1. DR TIGRFAMs; TIGR01536; asn_synth_AEB; 1. DR PROSITE; PS00443; GATASE_TYPE_II; 1. KW Ligase; Asparagine biosynthesis; Glutamine amidotransferase. FT INIT_MET 0 0 By similarity. FT ACT_SITE 1 1 GATase (By similarity). SQ SEQUENCE 585 AA; 66446 MW; 095CE2F99973797E CRC64; CGILAVLGVV EVSLAKRSRI IELSRRLRHR GPDWSGLHCH EDCYLAHQRL AIIDPTSGDQ PLYNEDKTVV VTVNGEIYNH EELKAKLKTH EFQTGSDCEV IAHLYEEYGE EFVDMLDGMF SFVLLDTRDK SFIAARDAIG ICPLYMGWGL DGSVWFSSEM KALSDDCERF ITFPPGHLYS SKTGGLRRWY NPPWFSETVP STPYNALFLR EMFEKAVIKR LMTDVPFGVL LSGGLDSSLV ASVASRHLNE TKVDRQWGNK LHTFCIGLKG SPDLKAAREV ADYLSTVHHE FHFTVQEGID ALEEVIYHIE TYDVTTIRAS TPMFLMSRKI KSLGVKMVIS GEGSDEIFGG YLYFHKAPNK KEFLEETCRK IKALHLYDCL RANKATSAWG VEARVPFLDK SFISVAMDID PEWNMIKRDL GRIEKWVMRK AFDDDEHPYL PKHILYRQKE QFSDGVGYNW IDGLKSFTEQ QVTDEMMNNA AQMFPYNTPV NKEAYYYRMI FERLFPQDSA RETVPWGPSI ACSTPAAIEW VEQWKASNDP SGRFISSHDS AATDHTAVSR RWPTAAARPA NGTVNGKDVP VPIAV // ID ATP0_MAIZE STANDARD; PRT; 508 AA. AC P05494; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE ATP synthase alpha chain, mitochondrial (EC 3.6.3.14). GN ATPA. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Braun C.J., Levings C.S. III; RT "Nucleotide sequence of the F1-ATPase alpha subunit from maize RT mitochondria."; RL Plant Physiol. 79:571-577(1985). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88311189; PubMed=2900697; RA Isaac P.G., Brennicke A., Dunbar S.M., Leaver C.J.; RT "The mitochondrial genome of fertile maize (Zea mays L.) contains two RT copies of the gene encoding the alpha-subunit of the F1-ATPase."; RL Curr. Genet. 10:321-328(1985). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The alpha chain is a regulatory CC subunit. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Mitochondrial. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M16222; AAA70269.1; -. DR EMBL; Z00026; CAA77319.1; -. DR PIR; A23757; PWZMAM. DR HSSP; P19483; 1BMF. DR MaizeDB; 69198; -. DR InterPro; IPR005294; ATP_synthF1_alph. DR InterPro; IPR000793; ATPase_a/b_C. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR004100; ATPase_a/bN. DR InterPro; IPR000790; ATPase_a_C. DR InterPro; IPR009005; F1_ATPase_a/bN. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR ProDom; PD001099; ATPase_aC; 1. DR TIGRFAMs; TIGR00962; atpA; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. KW ATP synthesis; CF(1); Hydrogen ion transport; KW Hydrolase; ATP-binding; Mitochondrion. FT NP_BIND 171 178 ATP (By similarity). FT SITE 373 373 Required for activity (By similarity). SQ SEQUENCE 508 AA; 55180 MW; FBA3DD33141A0456 CRC64; MEFSPRAAEL TTLLESRMIN FYTNLKVDEI GRVVSVGDGI ARVYGLNEIQ AGEMVEFASG VKGIALNLEN ENVGIVVFGS DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV DALGVPIDGK GALSDHERRR VEVKAPGIIE RKSVHEPMQT GLKAVDSLVP IGRGQRELII GDRQTGKTAI AIDTILNQKQ MNSRGTNESE TLYCVYVAIG QKRSTVAQLV QILSEANALE YSMLVAATAS DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVISITD GQICLETELF YRGIRPAINV GLSVSRVGSA AQLKAMKQVC GSSKLELAQY REVAAFAQFG SDLDAATQAL LNRGARLTEV PKQPQYEPLP IEKQIVVIYA AVNGFCDRMP LDRISQYEKN ILSTINPELL KSFLEKGGLT NERKMEPDAS LKESALNL // ID ATP2_MAIZE STANDARD; PRT; 553 AA. AC P19023; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE ATP synthase beta chain, mitochondrial precursor (EC 3.6.3.14). GN ATPB OR ATP2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. MUTIND-FR7205035; TISSUE=Coleoptile; RX MEDLINE=91016935; PubMed=2145551; RA Winning B.M., Bathgate B., Purdue P.E., Leaver C.J.; RT "Nucleotide sequence of a cDNA encoding the beta subunit of the RT mitochondrial ATP synthase from Zea mays."; RL Nucleic Acids Res. 18:5885-5885(1990). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Kernel; RA Ehrenshaft M., Brambl R.; RT "Respiration and mitochondrial biogenesis in germinating embryos of RT maize."; RL Plant Physiol. 93:295-304(1990). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The beta chain is the catalytic CC subunit. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Mitochondrial. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54233; CAA38140.1; -. DR EMBL; M36087; AAA70268.1; -. DR PIR; S11491; S11491. DR HSSP; P00829; 1BMF. DR MaizeDB; 66952; -. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR005722; ATP_synthF1_beta. DR InterPro; IPR000793; ATPase_a/b_C. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR004100; ATPase_a/bN. DR InterPro; IPR009005; F1_ATPase_a/bN. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR01039; atpD; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. KW ATP synthesis; CF(1); Hydrogen ion transport; KW Hydrolase; ATP-binding; Mitochondrion; Transit peptide. FT TRANSIT 1 47 Mitochondrion (By similarity). FT CHAIN 48 553 ATP synthase beta chain. FT NP_BIND 228 235 ATP (By similarity). SQ SEQUENCE 553 AA; 59103 MW; EABF1BD3DA1E5831 CRC64; MASRRVVSSL LRSASRLRAA SPAAPRPRAP PHRPSPAGYL FNRAAAYASS AAAQAAPATP PPATGKTGGG KITDEFTGAG AIGQVCQVIG AVVDVRFDEG LPPILTALEV LDNNIRLVLE VAQHLGENMV RTIAMDGTEG LVRGQRVLNT GSPITVPVGR ATLGRIINVI GEPIDEKGDI KTNHFLPIHR EAPAFVEQAT EQQILVTGIK VVDLLAPYQR GGKIGLFGGA GVGKTVLIME LINNVAKAHG GFSVFAGVGE RTREGNDLYR EMIESGVIKL DDKQSESKCA LVYGQMNEPP GARARVGLTG LTVAEHFRDA EGQDVLLFID NIFRFTQANS EVSALLGRIP SAVGYQPTLA TDLGGLQERI TTTKKGSITS VQAIYVPADD LTDPAPATTF AHLDATTVLS RQISELGIYP AVDPLDSTSR MLSPHVLGED HYNTARGVQK VLQNYKNLQD IIAILGMDEL SEDDKLTVAR ARKIQRFLSQ PFHVAEVFTG APGKYVELKE SVKSFQGVLD GKYDDLPEQS FYMVGGIEEV IAKAEKIAKE SAS // ID ATP6_MAIZE STANDARD; PRT; 291 AA. AC P07925; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE ATP synthase a chain (EC 3.6.3.14) (ATPase protein 6). GN ATP6. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Dewey R.E., Levings C.S. III, Timothy D.H.; RT "Nucleotide sequence of ATPase subunit 6 gene of maize mitochondria."; RL Plant Physiol. 79:914-919(1985). CC -!- FUNCTION: Key component of the proton channel; it may play a CC direct role in the translocation of protons across the membrane. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Mitochondrial CC inner membrane. CC -!- SIMILARITY: Belongs to the ATPase A chain family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M16223; AAA70270.1; -. DR PIR; JN0042; PWZM6M. DR MaizeDB; 69201; -. DR InterPro; IPR000568; ATPsynt_Asub. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1. DR PROSITE; PS00449; ATPASE_A; 1. KW Hydrogen ion transport; CF(0); Mitochondrion; Transmembrane. SQ SEQUENCE 291 AA; 31758 MW; 97749E9C3AC70477 CRC64; MERNGEIVNN GSIIIPGGGG PVTESPLDQF GIHPILDLNI GKYYVSFTNL SLSMLLTLGL VLLLVFVVTK KGGGKSVPNA FQSLVELIYD FVPNLVNEQI GGLSGNVKHK FFPCISVTFT FSLFRNPQGM IPFSFTVTSH FLITLALSFS IFIGITIVGF QRHGLHFFSF LLPAGVPLPL APFLVLLELI SHCFRALSSG IRLFANMMAG HSSVKILSGF AWTMLFLNNI FYFLGDLGPL FIVLALTGLE LGVAISQAHV STISICIYLN DATNLHQNES FHNCIKTRSQ S // ID ATP9_MAIZE STANDARD; PRT; 74 AA. AC P00840; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE ATP synthase protein 9, mitochondrial (EC 3.6.3.14) (Lipid-binding DE protein). GN ATP9. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Dewey R.E., Schuster A.M., Levings C.S. III, Timothy D.H.; RT "Nucleotide sequence of F0-ATPase proteolipid (subunit 9) gene of RT maize mitochondria."; RL Proc. Natl. Acad. Sci. U.S.A. 82:1015-1019(1985). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RX MEDLINE=86310310; PubMed=2875379; RA Bland M.M., Levings C.S. III, Matzinger D.F.; RT "The tobacco mitochondrial ATPase subunit 9 gene is closely linked to RT an open reading frame for a ribosomal protein."; RL Mol. Gen. Genet. 204:8-16(1986). CC -!- FUNCTION: This protein is one of the chains of the nonenzymatic CC membrane component (F0) of mitochondrial ATPase. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SIMILARITY: Belongs to the ATPase C chain family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M10408; AAA70271.1; -. DR EMBL; M18339; AAA70273.1; -. DR PIR; A01041; LWZMA. DR MaizeDB; 69203; -. DR InterPro; IPR002379; ATPase_Csub. DR InterPro; IPR000454; Eub_ATPase_Csub. DR Pfam; PF00137; ATP-synt_C; 1. DR PRINTS; PR00124; ATPASEC. DR PROSITE; PS00605; ATPASE_C; 1. KW Hydrogen ion transport; Lipid-binding; Mitochondrion; CF(0); KW Transmembrane. FT TRANSMEM 8 28 Potential. FT TRANSMEM 45 72 Potential. SQ SEQUENCE 74 AA; 7377 MW; E42854F14A6C2EA6 CRC64; MLEGAKSIGA GAATIALAGA AVGIGNVLSS SIHSVARNPS LAKQSFGYAI LGFALTEAIA SFAPMMAFLI SFVF // ID ATPA_MAIZE STANDARD; PRT; 507 AA. AC P05022; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE ATP synthase alpha chain (EC 3.6.3.14). GN ATPA. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87248033; PubMed=2885245; RA Rodermel S.R., Bogorao L.; RT "Molecular evolution and nucleotide sequences of the maize plastid RT genes for the alpha subunit of CF1 (atpA) and the proteolipid subunit RT of CF0 (atpH)."; RL Genetics 116:127-139(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The alpha chain is a regulatory CC subunit. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05255; CAA28876.1; -. DR EMBL; M27557; AAA84474.1; -. DR EMBL; X86563; CAA60283.1; -. DR PIR; S06291; PWZMA. DR Gramene; P05022; -. DR MaizeDB; 69206; -. DR InterPro; IPR005294; ATP_synthF1_alph. DR InterPro; IPR000793; ATPase_a/b_C. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR004100; ATPase_a/bN. DR InterPro; IPR000790; ATPase_a_C. DR InterPro; IPR009005; F1_ATPase_a/bN. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR ProDom; PD001099; ATPase_aC; 1. DR TIGRFAMs; TIGR00962; atpA; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. KW ATP synthesis; Chloroplast; Thylakoid; Membrane; CF(1); KW ATP-binding; Hydrolase; Hydrogen ion transport. FT NP_BIND 170 177 ATP (By similarity). FT SITE 363 363 Required for activity (By similarity). SQ SEQUENCE 507 AA; 55706 MW; 44685BF464B6302E CRC64; MATLRVDEIN KILRERIEQY NRKVGIENIG RVVQVGDGIA RIIGLGEIMS GELVEFAEGT RGIALNLESK NVGIVLMGDG LMIQEGSFVK ATGRIAQIPV SEAYLGRVIN ALAKPIDGRG EIVASESRLI ESPAPGIISR RSVYEPLQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA TDTILNQKGQ DVICVYVAIG QRASSVAQVV TTFHEEGAME YTIVVAEMAD SPATLQYLAP YTGAALAEYF MYRERHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYLGD VFYLHSRLLE RAAKLNSLLG EGSMTALPIV ETQSGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV GISVSRVGSA AQIKAMKQVA GKSKLELAQF AELQAFAQFA SALDKTSQNQ LARGRRLREL LKQSQSNPLP VEEQVATIYT GTRGYLDSLE IEQVKKFLDE LRKHLKDTKP QFQEIISSSK TFTEQAETLL KEAIQEQLER FSLQEQT // ID ATPB_MAIZE STANDARD; PRT; 498 AA. AC P00827; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE ATP synthase beta chain (EC 3.6.3.14). GN ATPB. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83038650; PubMed=6290998; RA Krebbers E.T., Larrinua I.M., McIntosh L., Bogorad L.; RT "The maize chloroplast genes for the beta and epsilon subunits of the RT photosynthetic coupling factor CF1 are fused."; RL Nucleic Acids Res. 10:4985-5002(1982). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The beta chain is the catalytic CC subunit. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01421; AAA85356.1; -. DR EMBL; X86563; CAA60293.1; -. DR PIR; A01025; PWZMB. DR HSSP; P00829; 1BMF. DR Gramene; P00827; -. DR MaizeDB; 69208; -. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR005722; ATP_synthF1_beta. DR InterPro; IPR000793; ATPase_a/b_C. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR004100; ATPase_a/bN. DR InterPro; IPR009005; F1_ATPase_a/bN. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR01039; atpD; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. KW ATP synthesis; Chloroplast; Thylakoid; Membrane; CF(1); KW Hydrolase; ATP-binding; Hydrogen ion transport. FT NP_BIND 172 179 ATP (By similarity). SQ SEQUENCE 498 AA; 54041 MW; 97D1E6873108F54A CRC64; MRTNPTTSRP GISTIEEKSV GRIDQIIGPV LDITFPPGKL PYIYNALIVK SRDTADKQIN VTCEVQQLLG NNRVRAVAMS ATEGLMRGME VIDTGTPLSV PVGGATLGRI FNVLGEPIDN LGPVDTSATF PIHRSAPAFI ELDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEKNIEES KVALVYGQMN EPPGARMRVG LTALTMAEYF RDVNKQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP TLSTEMGSLQ ERITSTKKGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLASKG IYPAVDPLDS TSTMLQPRIV GNEHYETAQR VKETLQRYKE LQDIIAILGL DELSEEDRLT VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFQL ILSGELDGLP EQAFYLVGNI DEASTKAINL EEESKLKK // ID ATPE_MAIZE STANDARD; PRT; 137 AA. AC P00835; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE ATP synthase epsilon chain (EC 3.6.3.14) (ATP synthase F1 sector DE epsilon subunit). GN ATPE. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83038650; PubMed=6290998; RA Krebbers E.T., Larrinua I.M., McIntosh L., Bogorad L.; RT "The maize chloroplast genes for the beta and epsilon subunits of the RT photosynthetic coupling factor CF1 are fused."; RL Nucleic Acids Res. 10:4985-5002(1982). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01421; AAA85357.1; -. DR EMBL; X86563; CAA60292.1; -. DR PIR; A01036; PWZME. DR Gramene; P00835; -. DR MaizeDB; 69211; -. DR HAMAP; MF_00530; -; 1. DR InterPro; IPR001469; ATPsynt_DE. DR Pfam; PF00401; ATP-synt_DE; 1. DR Pfam; PF02823; ATP-synt_DE_N; 1. DR ProDom; PD000944; ATPsynt_DE; 1. DR TIGRFAMs; TIGR01216; ATP_synt_epsi; 1. KW Hydrolase; ATP synthesis; CF(1); Hydrogen ion transport; Thylakoid; KW Membrane; Chloroplast. SQ SEQUENCE 137 AA; 15217 MW; D9550B1D0F0778F8 CRC64; MKLNLYVLTP KRIIWDCEVK EIILSTNSGQ IGVLPNHAPI NTAVDMGPLR IRLLNDQWLT AVLWSGFARI VNNEIIILGN DAELGSDIDP EEAQQALEIA EANLSKAEGT KELVEAKLAL RRARIRVEAV NWIPPSN // ID ATPF_MAIZE STANDARD; PRT; 183 AA. AC P48186; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE ATP synthase B chain (EC 3.6.3.14) (Subunit I). GN ATPF. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- SIMILARITY: Belongs to the ATPase B chain family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60282.1; -. DR PIR; S58548; S58548. DR Gramene; P48186; -. DR MaizeDB; 106206; -. DR InterPro; IPR002146; ATPsynt_B/B'sub. DR Pfam; PF00430; ATP-synt_B; 1. KW Hydrogen ion transport; Transmembrane; CF(0); Chloroplast. FT TRANSMEM 27 45 Potential. SQ SEQUENCE 183 AA; 20981 MW; 3748C901295116CA CRC64; MKNVTHSFVF LAHWPFAGSF GLNTDILATN LINLTVVVGV LIFFGKGVLK DLLDNRKQRI LSTIRNSEEL RKGTLEQLEK ARIRLQKVEL EADEYRMNGY SEIEREKENL INATSISLEQ LEKSKNETLY FEKQRAMNQV RQQGFQQAVQ GALGTLNSCL NTELHFRTIR ANIGILGAIE WKR // ID ATPH_SPIOL STANDARD; PRT; 81 AA. AC P00843; Q33180; Q9XPT1; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE ATP synthase C chain (EC 3.6.3.14) (Lipid-binding protein) (Subunit DE III). GN ATPH. OS Spinacia oleracea (Spinach), OS Triticum aestivum (Wheat), OS Zea mays (Maize), and OS Oryza sativa (Rice). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Caryophyllales; Amaranthaceae; Spinacia. OX NCBI_TaxID=3562, 4565, 4577, 4530; RN [1] RP SEQUENCE. RC SPECIES=S.oleracea; RA Sebald W., Wachter E.; RT "Amino acid sequence of the proteolipid subunit of the ATP synthase RT from spinach chloroplasts."; RL FEBS Lett. 122:307-311(1980). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=S.oleracea; RA Hennig J., Herrmann R.G.; RT "Chloroplast ATP synthase of spinach contains nine nonidentical RT subunit species, six of which are encoded by plastid chromosomes in RT two operons in a phylogenetically conserved arrangement."; RL Mol. Gen. Genet. 203:117-128(1986). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=S.oleracea; RX MEDLINE=88011330; PubMed=2443718; RA Hudson G.S., Mason J.G., Holton T.A., Koller B., Cox G.B., RA Whitfeld P.R., Bottomley W.; RT "A gene cluster in the spinach and pea chloroplast genomes encoding RT one CF1 and three CF0 subunits of the H+-ATP synthase complex and the RT ribosomal protein S2."; RL J. Mol. Biol. 196:283-298(1987). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=S.oleracea; RA Alt J., Winter P., Sebald W., Moser J.G., Schedel R., Westhoff P., RA Herrmann R.G.; RT "Localization and nucleotide sequence of the gene for the ATP synthase RT proteolipid subunit on the spinach plastid chromosome."; RL Curr. Genet. 7:129-138(1983). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=S.oleracea; STRAIN=cv. Geant d'hiver, and cv. Monatol; RX MEDLINE=21187424; PubMed=11292076; RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., RA Herrmann R.G., Mache R.; RT "The plastid chromosome of spinach (Spinacia oleracea): complete RT nucleotide sequence and gene organization."; RL Plant Mol. Biol. 45:307-315(2001). RN [6] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC SPECIES=T.aestivum; RA Howe C.J., Auffret A.D., Doherty A., Bowman C.M., Dyer T.A., RA Gray J.C.; RT "Location and nucleotide sequence of the gene for the proton- RT translocating subunit of wheat chloroplast ATP synthase."; RL Proc. Natl. Acad. Sci. U.S.A. 79:6903-6907(1982). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; STRAIN=cv. Chinese Spring; RA Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T., RA Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., RA Gojobori T., Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., RA Tsunewaki K.; RT "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: RT complete sequence and contig clones."; RL Plant Mol. Biol. Rep. 18:243-253(2000). RN [8] RP SEQUENCE OF 62-81 FROM N.A. RC SPECIES=T.aestivum; RA Bird C.R., Koller B., Auffret A.D., Huttly A.K., Howe C.J., RA Dyer T.A., Gray J.C.; RT "The wheat chloroplast gene for CF-0 subunit I of ATP synthase RT contains a large intron."; RL EMBO J. 4:1381-1388(1985). RN [9] RP SEQUENCE OF 1-32 FROM N.A. RC SPECIES=T.aestivum; STRAIN=cv. Chinese Spring; RA Matsuoka Y., Tsunewaki K., Ohnishi Y.; RT "Molecular analysis of a 21.1-kb fragment of wheat chloroplast DNA RT bearing RNA polymerase subunit (rpo) genes."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [10] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=87248033; PubMed=2885245; RA Rodermel S.R., Bogorao L.; RT "Molecular evolution and nucleotide sequences of the maize plastid RT genes for the alpha subunit of CF1 (atpA) and the proteolipid subunit RT of CF0 (atpH)."; RL Genetics 116:127-139(1987). RN [11] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [12] RP SEQUENCE OF 1-3 FROM N.A. RC SPECIES=Maize; STRAIN=cv. FR9cms X FR37; TISSUE=Leaf; RX MEDLINE=90272437; PubMed=2140888; RA Stahl D., Rodermel S., Subramanian A.R., Bogorad L.; RT "Nucleotide sequence of a 3.46 kb region of maize chloroplast DNA RT containing the gene cluster rpoC2-rps2-atpI-atpH."; RL Nucleic Acids Res. 18:3073-3074(1990). RN [13] RP SEQUENCE FROM N.A. RC SPECIES=O.sativa; STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=89364698; PubMed=2770692; RA Hiratsuka J., Shimada H., Whittier R., Ishibashi T., Sakamoto M., RA Mori M., Kondo C., Honji Y., Sun C.-R., Meng B.-Y., Li Y.-Q., RA Kanno A., Nishizawa Y., Hirai A., Shinozaki K., Sugiura M.; RT "The complete sequence of the rice (Oryza sativa) chloroplast genome: RT intermolecular recombination between distinct tRNA genes accounts for RT a major plastid DNA inversion during the evolution of the cereals."; RL Mol. Gen. Genet. 217:185-194(1989). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- MISCELLANEOUS: Dicyclohexylcarbodiimide (DCDD) inhibits ATPase. CC -!- SIMILARITY: Belongs to the ATPase C chain family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03775; CAA27402.1; -. DR EMBL; AJ400848; CAB88712.1; -. DR EMBL; J01458; AAA84724.1; -. DR EMBL; X05254; CAA28875.1; -. DR EMBL; X02595; CAA26440.1; -. DR EMBL; AB042240; BAB47029.1; -. DR EMBL; AB027572; BAA78045.1; -. DR EMBL; X52270; CAA36514.1; -. DR EMBL; M27557; AAA84473.1; -. DR EMBL; X15901; CAA33991.1; -. DR EMBL; X86563; CAA60281.1; -. DR PIR; JQ0218; LWRZA. DR PIR; S07677; LWZMC. DR PIR; S14423; LWSPA. DR MaizeDB; 54734; -. DR InterPro; IPR005953; ATP_synth_C. DR InterPro; IPR002379; ATPase_Csub. DR InterPro; IPR000454; Eub_ATPase_Csub. DR Pfam; PF00137; ATP-synt_C; 1. DR PRINTS; PR00124; ATPASEC. DR TIGRFAMs; TIGR01260; ATP_synt_c; 1. DR PROSITE; PS00605; ATPASE_C; 1. KW Hydrogen ion transport; Lipid-binding; Chloroplast; CF(0); KW Transmembrane; Formylation. FT MOD_RES 1 1 FORMYLATION. FT TRANSMEM 7 33 Potential. FT TRANSMEM 51 77 Potential. FT BINDING 61 61 Dicyclohexylcarbodiimide (By similarity). SQ SEQUENCE 81 AA; 7974 MW; 75F8DBD4F23A896D CRC64; MNPLIAAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM EALTIYGLVV ALALLFANPF V // ID ATPI_MAIZE STANDARD; PRT; 247 AA. AC P17344; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Chloroplast ATP synthase a chain precursor (EC 3.6.3.14) (ATPase DE subunit IV). GN ATPI. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9cms X FR37; TISSUE=Leaf; RX MEDLINE=90272437; PubMed=2140888; RA Stahl D., Rodermel S., Subramanian A.R., Bogorad L.; RT "Nucleotide sequence of a 3.46 kb region of maize chloroplast DNA RT containing the gene cluster rpoC2-rps2-atpI-atpH."; RL Nucleic Acids Res. 18:3073-3074(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Key component of the proton channel; it may play a CC direct role in the translocation of protons across the membrane. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast CC thylakoid membrane. CC -!- SIMILARITY: Belongs to the ATPase A chain family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52270; CAA36513.1; -. DR EMBL; X86563; CAA60280.1; -. DR PIR; S10174; S10174. DR HSSP; P00855; 1C17. DR Gramene; P17344; -. DR MaizeDB; 69212; -. DR InterPro; IPR000568; ATPsynt_Asub. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1. DR PROSITE; PS00449; ATPASE_A; 1. KW Hydrogen ion transport; CF(0); Chloroplast; Transmembrane; Signal. FT SIGNAL 1 18 By similarity. FT CHAIN 19 247 Chloroplast ATP synthase a chain. FT TRANSMEM 39 58 Potential. FT TRANSMEM 97 115 Potential. FT TRANSMEM 134 153 Potential. FT TRANSMEM 221 240 Potential. SQ SEQUENCE 247 AA; 27294 MW; 99B149C63DA4CD8E CRC64; MNITPCSIKT LKGLYDISGV EVGQHFYWQI GGFQIHAQVL ITSWVVITIL LGSVIIAVRN PQTIPTDGQN FFEYVLEFIR DLSKTQIGEE YGPWVPFIGT MFLFIFVSNW SGALLPWKII ELPHGELAAP TNDINTTVAL ALLTSAAYFY AGLSKKGLSY FEKYIKPTPI LLPINILEDF TKPLSLSFRL FGNILADELV VVVLVSLVPL VVPIPVMFLG LFTSGIQALI FATLAAAYIG ESMEGHH // ID BGLC_MAIZE STANDARD; PRT; 566 AA. AC P49235; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Beta-glucosidase, chloroplast precursor (EC 3.2.1.21) (Gentiobiase) DE (Cellobiase) (Beta-D-glucoside glucohydrolase). GN GLU1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Inbred line K55; TISSUE=Shoot; RA Esen A., Shahid M.; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. MUTIN; TISSUE=Coleoptile; RX MEDLINE=94053747; PubMed=8235622; RA Brzobohaty B., Moore I., Kristoffersen P., Bako L., Campos N., RA Schell J., Palme K.; RT "Release of active cytokinin by a beta-glucosidase localized to the RT maize root meristem."; RL Science 262:1051-1054(1993). RN [3] RP SEQUENCE OF 55-74, AND CHARACTERIZATION. RC STRAIN=cv. Inbred line K55; RA Esen A.; RT "Purification and partial characterization of Maize (Zea Mays L.) RT beta-glucosidase."; RL Plant Physiol. 98:174-182(1992). RN [4] RP SEQUENCE OF 55-69; 165-174; 207-213 AND 217-235. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- FUNCTION: Is implicated in many functions such as ABA metabolism, CC hydrolysis of conjugated gibberellins, conversion of storage forms CC of cytokinins to active forms. Also acts in defense of young plant CC parts against pests via the production of hydroxamic acids from CC hydroxamic acid glucosides. Enzymatic activity is highly CC correlated with plant growth. Its optimal pH is 5.8, and optimal CC temperature 50 degrees Celsius. Activity is totally lost when the CC enzyme is heated at 55 degrees Celsius. CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D- CC glucose residues with release of beta-D-glucose. CC -!- ENZYME REGULATION: Reversibly inhibited by micromolar CC concentrations of Hg(2+) or Ag(+), but irreversibly inhibited by CC alkylation in presence of urea. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- TISSUE SPECIFICITY: Most abundant in the coleoptile. CC -!- SIMILARITY: Belongs to family 1 of glycosyl hydrolases. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U25157; AAA65946.1; -. DR EMBL; X74217; CAA52293.1; -. DR PIR; A48860; A48860. DR PDB; 1E1E; 19-FEB-01. DR PDB; 1E1F; 19-FEB-01. DR PDB; 1E4L; 11-DEC-00. DR PDB; 1E4N; 11-DEC-00. DR PDB; 1E55; 11-DEC-00. DR PDB; 1E56; 11-DEC-00. DR PDB; 1H49; 03-JUL-03. DR Maize-2DPAGE; P49235; COLEOPTILE. DR MaizeDB; 13870; -. DR InterPro; IPR001360; Glyco_hydro_1. DR Pfam; PF00232; Glyco_hydro_1; 1. DR PRINTS; PR00131; GLHYDRLASE1. DR ProDom; PD000650; Glyco_hydro_1; 1. DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1. DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1. KW Hydrolase; Glycosidase; Chloroplast; Transit peptide; 3D-structure. FT TRANSIT 1 54 Chloroplast. FT CHAIN 55 566 Beta-glucosidase. FT ACT_SITE 245 245 Proton donor (Potential). FT ACT_SITE 460 460 Nucleophile (By similarity). FT CONFLICT 477 477 A -> D (in Ref. 2). FT CONFLICT 551 551 E -> Q (in Ref. 2). FT CONFLICT 554 554 T -> A (in Ref. 2). FT TURN 69 71 FT HELIX 75 77 FT TURN 80 81 FT STRAND 83 87 FT HELIX 90 93 FT TURN 97 98 FT TURN 100 101 FT STRAND 105 105 FT HELIX 106 113 FT HELIX 115 117 FT TURN 119 120 FT TURN 127 128 FT HELIX 130 143 FT TURN 144 145 FT STRAND 148 152 FT HELIX 155 158 FT TURN 160 161 FT TURN 164 166 FT HELIX 170 185 FT TURN 186 187 FT STRAND 189 195 FT STRAND 200 200 FT HELIX 201 207 FT HELIX 209 211 FT TURN 213 214 FT HELIX 217 233 FT TURN 234 236 FT STRAND 239 244 FT HELIX 246 254 FT TURN 255 255 FT TURN 260 261 FT STRAND 263 263 FT TURN 266 267 FT STRAND 272 272 FT TURN 273 274 FT TURN 277 279 FT HELIX 280 302 FT TURN 303 303 FT TURN 306 307 FT STRAND 309 321 FT HELIX 326 339 FT TURN 340 340 FT HELIX 341 349 FT HELIX 354 360 FT HELIX 361 363 FT HELIX 369 375 FT TURN 376 377 FT STRAND 381 394 FT TURN 399 400 FT HELIX 406 410 FT STRAND 412 415 FT STRAND 417 417 FT TURN 419 420 FT STRAND 423 423 FT STRAND 427 427 FT STRAND 434 434 FT TURN 437 437 FT HELIX 438 449 FT TURN 450 450 FT STRAND 456 460 FT STRAND 465 466 FT HELIX 475 479 FT HELIX 482 500 FT TURN 501 502 FT STRAND 505 511 FT STRAND 514 514 FT HELIX 519 521 FT TURN 522 523 FT STRAND 525 526 FT STRAND 530 533 FT TURN 534 537 FT STRAND 539 542 FT HELIX 544 554 SQ SEQUENCE 566 AA; 64237 MW; 4EA241258AE3641B CRC64; MAPLLAAAMN HAAAHPGLRS HLVGPNNESF SRHHLPSSSP QSSKRRCNLS FTTRSARVGS QNGVQMLSPS EIPQRDWFPS DFTFGAATSA YQIEGAWNED GKGESNWDHF CHNHPERILD GSNSDIGANS YHMYKTDVRL LKEMGMDAYR FSISWPRILP KGTKEGGINP DGIKYYRNLI NLLLENGIEP YVTIFHWDVP QALEEKYGGF LDKSHKSIVE DYTYFAKVCF DNFGDKVKNW LTFNEPQTFT SFSYGTGVFA PGRCSPGLDC AYPTGNSLVE PYTAGHNILL AHAEAVDLYN KHYKRDDTRI GLAFDVMGRV PYGTSFLDKQ AEERSWDINL GWFLEPVVRG DYPFSMRSLA RERLPFFKDE QKEKLAGSYN MLGLNYYTSR FSKNIDISPN YSPVLNTDDA YASQEVNGPD GKPIGPPMGN PWIYMYPEGL KDLLMIMKNK YGNPPIYITE NGIGDVDTKE TPLPMEAALN DYKRLDYIQR HIATLKESID LGSNVQGYFA WSLLDNFEWF AGFTERYGIV YVDRNNNCTR YMKESAKWLK EFNTAKKPSK KILTPA // ID BIP2_MAIZE STANDARD; PRT; 663 AA. AC P24067; DT 01-MAR-1992 (Rel. 21, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Luminal binding protein 2 precursor (BiP2) (Heat shock protein 70 DE homolog 2) (B70) (B-70). GN BIPE2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RC STRAIN=cv. Floury-2; TISSUE=Kernel; RX MEDLINE=98094260; PubMed=9434171; RA Wrobel R.L., Obrian G.R., Boston R.S.; RT "Comparative analysis of BiP gene expression in maize endosperm."; RL Gene 204:105-113(1997). RN [2] RP SEQUENCE OF 197-663 FROM N.A., AND CHARACTERIZATION. RC STRAIN=cv. Floury-2; TISSUE=Kernel; RX MEDLINE=93005712; PubMed=1840923; RA Fontes E.B.P., Shank B.B., Wrobel R.L., Moose S.P., Obrian G.R., RA Wurtzel E.T., Boston R.S.; RT "Characterization of an immunoglobulin binding protein homolog in the RT maize floury-2 endosperm mutant."; RL Plant Cell 3:483-496(1991). CC -!- FUNCTION: Probably plays a role in facilitating the assembly of CC multimeric protein complexes inside the ER. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -!- INDUCTION: By treatment with tunicamycin. Overproduced in fl2, CC defective endosperm-b30, and mucronate mutants. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U58208; AAC49899.1; -. DR EMBL; M59449; AAA92743.1; ALT_TERM. DR PIR; JQ0966; JQ0966. DR PIR; T04078; T04078. DR HSSP; P19120; 3HSC. DR MaizeDB; 66083; -. DR InterPro; IPR000886; ER_target_S. DR InterPro; IPR001023; Hsp70. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR ProDom; PD000089; Hsp70; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. DR PROSITE; PS00014; ER_TARGET; 1. KW ATP-binding; Endoplasmic reticulum; Multigene family; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 663 Luminal binding protein 2. FT CARBOHYD 614 614 N-linked (GlcNAc...) (Potential). FT SITE 660 663 Prevent secretion from ER. SQ SEQUENCE 663 AA; 73084 MW; 6769B7D19A0D918A CRC64; MDRARGSAFL LGVLLAGSLF AFSVAKEETK KLGTVIGIDL GTTYSCVGVY KNGHVEIIAN DQGNRITPSW VAFTDSERLI GEAAKNQAAV NPERTIFDVK RLIGRKFADK EVQRDMKLVP YKIINKDGKP YIQVKIKDGE NKVFSPEEIS AMILGKMKDT AEAYLGKKIN DAVVTVPAYF NDAQRQATKD AGVIAGLNVA RIINEPTAAA IAYGLDKKGG EKNILVFDLG GGTFDVSILT IDNGVFEVLA TNGDTHLGGE DFDQRIMEYF IKLIKKKYSK DISKDNRALG KLRREAERAK RALSNQHQVR VEIESLFDGT DFSEPLTRAR FEELNNDLFR KTMGPVKKAM EDAGLEKSQI HEIVLVGGST RIPKVQQLLR DYFDGKEPNK GVNPDEAVAF GAAVQGSILS GEGGDETKDI LLLDVAPLTL GIETVGGVMT KLIPRNTVIP TKKSQVFTTY QDQQTTVSIQ VFEGERSMTK DCRLLGKFDL NGIAPAPRGT PQIEVTFEVD ANGILNVKAE DKGTGKSEKI TITNEKGRLS QEEIDRMVRE AEEFAEEDKK VKERIDARNQ LETYVYNMKN TVGDKDKLAD KLEAEEKEKV EEALKEALEW LDDNQSAEKE DYEEKLKEVE AVCNPIVSAV YQRSGGAPGG DADGGVDDDH DEL // ID BT1_MAIZE STANDARD; PRT; 436 AA. AC P29518; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Brittle-1 protein, chloroplast precursor. GN BT1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93005685; PubMed=1668652; RA Sullivan T.D., Strelow L.I., Illingworth C.A., Phillips R.L., RA Nelson O.E. Jr.; RT "Analysis of maize brittle-1 alleles and a defective RT Suppressor-mutator-induced mutable allele."; RL Plant Cell 3:1337-1348(1991). CC -!- FUNCTION: Could play a role in amyloplast membrane transport. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast inner CC membrane; amyloplast inner membrane (Potential). CC -!- TISSUE SPECIFICITY: Endosperm of developing kernels. CC -!- SIMILARITY: Belongs to the mitochondrial carrier family. CC -!- SIMILARITY: Contains 3 Solcar repeats. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M79333; AAA33438.1; -. DR PIR; JQ1459; JQ1459. DR MaizeDB; 47578; -. DR InterPro; IPR001993; Mitoch_carrier. DR InterPro; IPR002067; Mit_carrier. DR Pfam; PF00153; mito_carr; 3. DR PRINTS; PR00926; MITOCARRIER. DR PROSITE; PS50920; SOLCAR; 3. KW Transit peptide; Chloroplast; Amyloplast; Inner membrane; Repeat; KW Transmembrane; Transport. FT TRANSIT 1 75 Chloroplast (Potential). FT CHAIN 76 436 Brittle-1 protein. FT TRANSMEM 229 247 Potential. FT TRANSMEM 327 347 Potential. FT REPEAT 132 216 Solcar 1. FT REPEAT 227 311 Solcar 2. FT REPEAT 324 412 Solcar 3. SQ SEQUENCE 436 AA; 46627 MW; 9600C05F603E9DAE CRC64; MAATMAVTTM VTRSKESWSS LQVPAVAFPW KPRGGKTGGL EFPRRAMFAS VGLNVCPGVP AGRDPREPDP KVVRAADNCD IAASLAPPFP GSRPPGRRGR GSEEEEAEGR RHEEAAAAGR SEPEEGQGQD RQPAPARLVS GAIAGAVSRT FVAPLETIRT HLMVGSIGVD SMAGVFQWIM QNEGWTGLFR GNAVNVLRVA PSKAIEHFTY DTAKKFLTPK GDEPPKIPIP TPLVAGALAG FASTLCTYPM ELIKTRVTIE KDVYDNVAHA FVKILRDEGP SELYRGLTPS LIGVVPYAAC NFYAYETLKR LYRRATGRRP GADVGPVATL LIGSAAGAIA SSATFPLEVA RKQMQVGAVG GRQVYQNVLH AIYCILKKEG AGGLYRGLGP SCIKLMPAAG IAFMCYEACK KILVDKEDEE EEDEAGGGED DKKKVE // ID C13_MAIZE STANDARD; PRT; 170 AA. AC P33050; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Pollen specific protein C13 precursor. GN MGS1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92404707; PubMed=2535540; RA Hanson D.D., Hamilton D.A., Travis J.L., Bashe D.M., Mascarenhas J.P.; RT "Characterization of a pollen-specific cDNA clone from Zea mays and RT its expression."; RL Plant Cell 1:173-179(1989). CC -!- TISSUE SPECIFICITY: Pollen. CC -!- SIMILARITY: Belongs to the Ole e I family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S44171; AAB23277.1; -. DR PIR; JQ1107; JQ1107. DR MaizeDB; 25723; -. DR InterPro; IPR006041; Ole_e1_ext. DR InterPro; IPR006040; Pollen_Ole_e_I. DR Pfam; PF01190; Pollen_Ole_e_I; 1. DR PROSITE; PS00925; OLEEI; 1. KW Glycoprotein; Signal. FT SIGNAL 1 27 Potential. FT CHAIN 28 170 Pollen specific protein C13. FT CARBOHYD 53 53 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 170 AA; 18217 MW; ED6A734654AE8E14 CRC64; MASVPAPATT TAAVILCLCV VLSCAAADDP NLPDYVIQGR VYCDTCRAGF VTNVTEYIAG AKVRLECKHF GTGKLERAID GVTDATGTYT IELKDSHEED ICQVVLVASP RKDCDEVQAL RDRAGVLLTR NVGISDSLRP ANPLGYFKDV PLPVCAALLK QLDSDDDDDQ // ID CALM_MAIZE STANDARD; PRT; 148 AA. AC P41040; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Calmodulin. GN CALM1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RX MEDLINE=94286753; PubMed=8016275; RA Griess E.A., Igloi G., Feix G.; RT "Isolation and sequence comparison of a maize calmodulin cDNA."; RL Plant Physiol. 104:1467-1468(1994). CC -!- FUNCTION: Calmodulin mediates the control of a large number of CC enzymes by Ca(2+). Among the enzymes to be stimulated by the CC calmodulin-Ca(2+) complex are a number of protein kinases and CC phosphatases. CC -!- MISCELLANEOUS: This protein has four functional calcium-binding CC sites. CC -!- SIMILARITY: Contains 4 EF-hand calcium-binding domains. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X74490; CAA52602.1; -. DR PIR; S58924; S40086. DR HSSP; P02593; 1AK8. DR MaizeDB; 64086; -. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 4. DR ProDom; PD000012; EF-hand; 2. DR SMART; SM00054; EFh; 4. DR PROSITE; PS00018; EF_HAND; 4. KW Calcium-binding; Repeat; Methylation. FT INIT_MET 0 0 By similarity. FT MOD_RES 115 115 METHYLATION (BY SIMILARITY). FT CA_BIND 20 31 EF-hand 1. FT CA_BIND 56 67 EF-hand 2. FT CA_BIND 93 104 EF-hand 3. FT CA_BIND 129 140 EF-hand 4. SQ SEQUENCE 148 AA; 16680 MW; BE3AB4E9776F7D4D CRC64; ADQLTDEQIA EFKEAFSLFD KDGDGCITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPELLN LMARKMKDTD SEEELKEAFR VFDKDQNGFI SAAELRHVMT NLGEKLTDEE VDEMIREADV DGDGQINYEE FVKVMMAK // ID CAP1_MAIZE STANDARD; PRT; 970 AA. AC P04711; DT 13-AUG-1987 (Rel. 05, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Phosphoenolpyruvate carboxylase 1 (EC 4.1.1.31) (PEPCase 1). GN PEP1 OR PPC. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Leaf; RA Hudspeth R.L., Grula J.W.; RT "Structure and expression of the maize gene encoding the RT phosphoenolpyruvate carboxylase isozyme involved in C4 RT photosynthesis."; RL Plant Mol. Biol. 12:579-589(1989). RN [2] RP SEQUENCE OF 39-970 FROM N.A. RX MEDLINE=86148496; PubMed=3005978; RA Izui K., Ishijima S., Yamaguchi Y., Katagiri F., Murata T., RA Shigesada K., Sugiyama T., Katsuki H.; RT "Cloning and sequence analysis of cDNA encoding active RT phosphoenolpyruvate carboxylase of the C4-pathway from maize."; RL Nucleic Acids Res. 14:1615-1628(1986). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=cv. Golden cross Bantam; RX MEDLINE=89276342; PubMed=2731539; RA Matsuoka M., Minami E.; RT "Complete structure of the gene for phosphoenolpyruvate carboxylase RT from maize."; RL Eur. J. Biochem. 181:593-598(1989). RN [4] RP SEQUENCE OF 1-3 FROM N.A. RC STRAIN=cv. H84; TISSUE=Leaf; RX MEDLINE=90186704; PubMed=2628434; RA Yanagisawa S., Izui K.; RT "Maize phosphoenolpyruvate carboxylase involved in C4 photosynthesis: RT nucleotide sequence analysis of the 5' flanking region of the gene."; RL J. Biochem. 106:982-987(1989). RN [5] RP SEQUENCE OF 1-82 FROM N.A. RX MEDLINE=88152202; PubMed=2894322; RA Yanagisawa S., Izui K., Yamaguchi Y., Shigesada K., Katsuki H.; RT "Further analysis of cDNA clones for maize phosphoenolpyruvate RT carboxylase involved in C4 photosynthesis. Nucleotide sequence of RT entire open reading frame and evidence for polyadenylation of mRNA at RT multiple sites in vivo."; RL FEBS Lett. 229:107-110(1988). RN [6] RP ACTIVE SITE, AND SEQUENCE OF 599-610. RX MEDLINE=91098247; PubMed=2268676; RA Jiao J.-A., Podesta F.E., Chollet R., O'Leary M.H., Andreo C.S.; RT "Isolation and sequence of an active-site peptide from maize leaf RT phosphoenolpyruvate carboxylase inactivated by pyridoxal RT 5'-phosphate."; RL Biochim. Biophys. Acta 1041:291-295(1990). RN [7] RP PHOSPHORYLATION SITE SER-15. RA Jiao J.-A., Vidal J., Echevarria C., Chollet R.; RT "In vivo regulatory phosphorylation site in C4-leaf RT phosphoenolpyruvate carboxylase from maize and sorghum."; RL Plant Physiol. 96:297-301(1991). CC -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) CC it forms oxaloacetate, a four-carbon dicarboxylic acid source for CC the tricarboxylic acid cycle. CC -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O + CC phosphoenolpyruvate + CO(2). CC -!- ENZYME REGULATION: By light-reversible phosphorylation. CC -!- PATHWAY: Tricarboxylic acid cycle. This isozyme is involved in C4 CC photosynthesis. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the PEPCase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15238; CAA33316.1; -. DR EMBL; X03613; CAA27270.1; -. DR EMBL; X14581; CAA32724.1; -. DR EMBL; X14579; CAA32722.1; ALT_INIT. DR EMBL; X14580; CAA32723.1; -. DR EMBL; X15642; CAA33663.1; -. DR EMBL; X07168; CAA30158.1; -. DR PDB; 1JQO; 14-JAN-03. DR MaizeDB; 30066; -. DR InterPro; IPR001449; PEPcase. DR Pfam; PF00311; PEPcase; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR PROSITE; PS00393; PEPCASE_2; 1. DR PROSITE; PS00781; PEPCASE_1; 1. KW Lyase; Carbon dioxide fixation; Allosteric enzyme; Multigene family; KW Tricarboxylic acid cycle; Phosphorylation; Photosynthesis; KW 3D-structure. FT MOD_RES 15 15 PHOSPHORYLATION. FT ACT_SITE 177 177 By similarity. FT ACT_SITE 606 606 FT CONFLICT 239 239 A -> D (in Ref. 2 and 3). FT CONFLICT 338 339 EL -> DV (in Ref. 2). FT CONFLICT 482 482 P -> S (in Ref. 2 and 3). FT CONFLICT 509 509 D -> E (in Ref. 3). FT CONFLICT 557 559 QPL -> PAV (in Ref. 2 and 3). FT CONFLICT 570 570 D -> S (in Ref. 2 and 3). FT CONFLICT 573 574 SA -> LR (in Ref. 2). FT CONFLICT 687 687 C -> S (in Ref. 2). FT CONFLICT 736 736 A -> P (in Ref. 2). FT CONFLICT 963 963 A -> R (in Ref. 2). FT HELIX 36 53 FT HELIX 55 74 FT TURN 77 77 FT HELIX 78 89 FT HELIX 92 122 FT HELIX 143 151 FT TURN 152 153 FT HELIX 158 166 FT TURN 167 167 FT STRAND 169 175 FT TURN 178 179 FT HELIX 184 199 FT TURN 200 201 FT TURN 203 204 FT HELIX 207 226 FT HELIX 237 248 FT TURN 249 255 FT HELIX 256 268 FT TURN 269 271 FT TURN 278 279 FT STRAND 283 287 FT TURN 289 291 FT STRAND 292 292 FT TURN 294 295 FT TURN 297 298 FT HELIX 301 329 FT HELIX 337 350 FT TURN 356 357 FT TURN 367 368 FT HELIX 370 394 FT TURN 403 404 FT HELIX 409 425 FT TURN 426 426 FT TURN 430 434 FT HELIX 435 446 FT TURN 447 448 FT STRAND 452 456 FT HELIX 459 473 FT TURN 474 474 FT TURN 479 480 FT HELIX 483 495 FT TURN 503 504 FT HELIX 509 523 FT TURN 527 528 FT STRAND 529 534 FT TURN 535 536 FT TURN 540 540 FT HELIX 541 552 FT TURN 553 553 FT STRAND 561 565 FT HELIX 568 572 FT TURN 573 573 FT HELIX 574 582 FT TURN 583 583 FT HELIX 585 591 FT TURN 592 592 FT STRAND 594 600 FT TURN 602 603 FT HELIX 604 607 FT HELIX 610 629 FT TURN 630 632 FT STRAND 634 640 FT HELIX 645 647 FT TURN 648 648 FT HELIX 652 657 FT TURN 658 658 FT TURN 661 662 FT TURN 665 666 FT STRAND 667 673 FT HELIX 674 681 FT HELIX 684 703 FT HELIX 711 732 FT TURN 733 734 FT TURN 736 737 FT HELIX 738 745 FT HELIX 749 754 FT TURN 770 771 FT HELIX 775 783 FT TURN 784 785 FT HELIX 788 791 FT TURN 792 793 FT HELIX 794 804 FT TURN 806 807 FT HELIX 808 818 FT HELIX 820 833 FT TURN 834 835 FT HELIX 838 847 FT TURN 848 848 FT TURN 852 853 FT HELIX 854 875 FT TURN 876 876 FT TURN 880 881 FT HELIX 885 913 FT TURN 915 916 FT TURN 937 941 FT TURN 949 950 FT HELIX 951 966 FT TURN 967 967 SQ SEQUENCE 970 AA; 109296 MW; 95B66F96ABCE22F4 CRC64; MASTKAPGPG EKHHSIDAQL RQLVPGKVSE DDKLIEYDAL LVDRFLNILQ DLHGPSLREF VQECYEVSAD YEGKGDTTKL GELGAKLTGL APADAILVAS SILHMLNLAN LAEEVQIAHR RRNSKLKKGG FADEGSATTE SDIEETLKRL VSEVGKSPEE VFEALKNQTV DLVFTAHPTQ SARRSLLQKN ARIRNCLTQL NAKDITDDDK QELDEALQRE IQAAFRTDEI RRAQPTPQAE MRYGMSYIHE TVWKGVPKFL RRVDTALKNI GINERLPYNV SLIRFSSWMG GDRDGNPRVT PEVTRDVCLL ARMMAANLYI DQIEELMFEL SMWRCNDELR VRAEELHSSS GSKVTKYYIE FWKQIPPNEP YRVILGHVRD KLYNTRERAR HLLASGVSEI SAESSFTSIE EFLEPLELCY KSLCDCGDKA IADGSLLDLL RQVFTFGLSL VKLDIRQESE RHTDVIDAIT THLGIGSYRE WPEDKRQEWL LSELRGKRPL LPPDLPQTDE IADVIGAFHV LAELPPDSFG PYIISMATAP SDVLAVELLQ RECGVRQPLP VVPLFERLAD LQSAPASVER LFSVDWYMDR IKGKQQVMVG YSDSGKDAGR LSAAWQLYRA QEEMAQVAKR YGVKLTLFHG RGGTVGRGGG PTHLAILSQP PDTINGSIRV TVQGEVIEFC FGEEHLCFQT LQRFTAATLE HGMHPPVSPK PEWRKLMDEM AVVATEEYRS VVVKEARFVE YFRSATPETE YGRMNIGSRP AKRRPGGGIT TLRAIPWIFS WTQTRFHLPV WLGVGAAFKF AIDKDVRNFQ VLKEMYNEWP FFRVTLDLLE MVFAKGDPGI AGLYDELLVA EELKPFGKQL RDKYVETQQL LLQIAGHKDI LEGDPFLKQG LVLRNPYITT LNVFQAYTLK RIRDPNFKVT PQPPLSKEFA DENKPAGLVK LNPASEYPPG LEDTLILTMK GIAAGMQNTG // ID CAP2_MAIZE STANDARD; PRT; 967 AA. AC P51059; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Phosphoenolpyruvate carboxylase 2 (EC 4.1.1.31) (PEPCase 2). GN PEP4 OR PEP. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. H84; TISSUE=Root; RX MEDLINE=93054411; PubMed=1429504; RA Kawamura T., Shigesada K., Toh H., Okumura S., Yanagisawa S., RA Izui K.; RT "Molecular evolution of phosphoenolpyruvate carboxylase for C4 RT photosynthesis in maize: comparison of its cDNA sequence with a newly RT isolated cDNA encoding an isozyme involved in the anaplerotic RT function."; RL J. Biochem. 112:147-154(1992). CC -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) CC it forms oxaloacetate, a four-carbon dicarboxylic acid source for CC the tricarboxylic acid cycle. CC -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O + CC phosphoenolpyruvate + CO(2). CC -!- ENZYME REGULATION: By light-reversible phosphorylation (By CC similarity). CC -!- PATHWAY: Tricarboxylic acid cycle. This isozyme is involved in C3 CC photosynthesis. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: Belongs to the PEPCase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61489; CAA43709.1; -. DR PIR; JH0667; JH0667. DR HSSP; P00864; 1FIY. DR MaizeDB; 30066; -. DR InterPro; IPR001449; PEPcase. DR Pfam; PF00311; PEPcase; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR PROSITE; PS00393; PEPCASE_2; 1. DR PROSITE; PS00781; PEPCASE_1; 1. KW Lyase; Carbon dioxide fixation; Allosteric enzyme; Multigene family; KW Tricarboxylic acid cycle; Phosphorylation; Photosynthesis. FT MOD_RES 13 13 PHOSPHORYLATION (BY SIMILARITY). FT ACT_SITE 174 174 By similarity. FT ACT_SITE 602 602 By similarity. SQ SEQUENCE 967 AA; 109998 MW; 7034A2AD5521645B CRC64; MAALGPKMER LSSIDAQLRM LVPGKVSEDD KLIEYDALLL DRFLDILQDL HGDDLKEMVQ ECYEVAAEYE TKHDLQKLDE LGKMITSLDP GDSIVIAKSL SHMLNLANLA EEVQIAYRRR IKLKKGDFAD ENSAITESDI EETLKRLVVD LKKSPAEVFD ALKSQTVDLV LTAHPTQSVR RSLLQKHSRI RNCLVQLYSK DITPDDKQEL DEALQREIQA AFRTDEIRRT QPTPQDEMRA GMSYFHETIW KGVPKFLRRV DTALKNIGIN ERVPYNAPLI QFSSWMGGDR DGNPRVTPEV TRDVCLLARM MASNLYCSQI EDLMFELSMW RCSDELRMRA DVLHLSTKKD AKHYIEFWKK VPPNEPYRVI LSDVRDKLYN TRERSRELLS SGHSDIPEEA TLTNVEQLLE PLELCYRSLC ACGDSVIADG TLLDFLRQVS TFGLSLVRLD IRQESDRHTD VLDAITTYLG IGSYREWTEE RRQEWLLSEL NGKRPLFGSD LPKTEEISDV LDTFHVIAEL PSDNFGAYII SMATAPSDVL AVELLQRECH VKTPLRVVPL FEKLADLEAA PAALARLFSI DWYRQRINGK QEVMIGYSDS GKDAGRLSAA WQLYKAQEEL IKVAKDFGVK LTMFHGRGGT VGRGGGPTHL AILSQPPDTI HGSLRVTVQG EVIEQSFGEE HLCFRTLQRF TAATLEHGMH PPNAPKPEWR ALLDEMAVVA TEEYRSIVFK EPRFVEYFRL ATPETEYGRM NIGSRPSKRK PSGGIDSLRA IPWIFAWTQT RFHLPVWLGF GAAFKNVLQK DIRNLHMLQE MYNEWPFFRV TIDLVEMVFA KGNPGIAALY DKLLVSEELH PLGEKLRANY EETQKLLLQV AGHRDLLEGD LYLKQRLRLR DAYITTLNVC QAYTLKRIRD PDYHVALRPH LSKEIMDSTK AAADVVKLNP GSEYAPGLED TLILTMKGIA AGLQNTG // ID CAT1_MAIZE STANDARD; PRT; 492 AA. AC P18122; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Catalase isozyme 1 (EC 1.11.1.6). GN CAT1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. R6-67; TISSUE=Scutellum; RX MEDLINE=89051000; PubMed=2461221; RA Redinbaugh M.G., Wadsworth G.J., Scandalios J.G.; RT "Characterization of catalase transcripts and their differential RT expression in maize."; RL Biochim. Biophys. Acta 951:104-116(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; TISSUE=Leaf; RX MEDLINE=94035156; PubMed=8220459; RA Guan L., Scandalios J.G.; RT "Characterization of the catalase antioxidant defense gene Cat1 of RT maize, and its developmentally regulated expression in transgenic RT tobacco."; RL Plant J. 3:527-536(1993). CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and CC serves to protect cells from the toxic effects of hydrogen CC peroxide. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC -!- COFACTOR: Heme group. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Peroxisomal. CC -!- TISSUE SPECIFICITY: Scutella, milky endosperm of immature CC kernels, leaves and epicotyls. CC -!- SIMILARITY: Belongs to the catalase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X12538; CAA31056.1; -. DR EMBL; X60135; CAA42720.1; -. DR PIR; S48124; S48124. DR HSSP; P21179; 1CF9. DR MaizeDB; 13855; -. DR InterPro; IPR002226; Catalase. DR Pfam; PF00199; catalase; 1. DR PRINTS; PR00067; CATALASE. DR ProDom; PD000510; Catalase; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. KW Oxidoreductase; Peroxidase; Iron; Heme; Hydrogen peroxide; KW Peroxisome; Multigene family. FT ACT_SITE 65 65 By similarity. FT ACT_SITE 138 138 By similarity. FT METAL 348 348 Iron (heme axial ligand) (By similarity). FT VARIANT 157 157 A -> V (in strain W64A). FT VARIANT 211 211 S -> T (in strain W64A). FT VARIANT 329 329 S -> I (in strain W64A). FT VARIANT 483 483 P -> A (in strain W64A). FT CONFLICT 332 332 A -> G (in Ref. 1). FT CONFLICT 415 415 R -> G (in Ref. 1). FT CONFLICT 456 456 H -> D (in Ref. 1). SQ SEQUENCE 492 AA; 56877 MW; CE10C93BEC1D9529 CRC64; MDPYKHRPSS GSNSSFWTTN SGAPVWNNNS ALTVGQRGPI LLEDYHLIEK LAQFDRERIP ERVVHARGAS AKGFFEVTHD VSHLTCADFL RAPGVQTPVI VRFSTVVHER GSPETLRDPR GFAVKFYTRE GNFDLVGNNM PVFFIRDGMK FPDMVHAFKP NPKTNLQENW RIVDFFSHHP ESLHMFTFLF DDVGIPLNYR HMEGFGVNTY SLINRDGKPH LVKFHWKPTC GVKCLLDNEA VTVGGTCHSH ATKDLYDSIA AGNYPEWKLY IQTIDLDHED KFDFDPLDVT KTWPEDIIPL QPVGRMVLNK NVDNFFAENE QIAFCPAISV PAIHYSDDKL LQTRIFSYAD TQRHRLGPNY LMLPVNAPKC AHHNNHHDGF MNFMHRDEEV NYFPSRFDPA RHAEKVPIPP RVLTRCREKC IIQKENNFKQ AGERYRSFDP ARQDRFIQRW VDALTHPRVT HEHRTIWISY WSQCDAALGQ KLPSRLNLKP SM // ID CAT2_MAIZE STANDARD; PRT; 491 AA. AC P12365; DT 01-OCT-1989 (Rel. 12, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Catalase isozyme 2 (EC 1.11.1.6). GN CAT2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; RA Guan L., Ruzsa S., Skadsen R.W., Scandalios J.G.; RT "Comparison of the cat2 complementary DNA sequences of a normal RT catalase activity line (W64A) and a high catalase activity line (R6- RT 67) of maize."; RL Plant Physiol. 96:1379-1381(1991). RN [2] RP PRELIMINARY SEQUENCE FROM N.A. RC STRAIN=cv. R6-67; RX MEDLINE=88016183; PubMed=2821546; RA Bethards L.A., Skadsen R.W., Scandalios J.G.; RT "Isolation and characterization of a cDNA clone for the Cat2 gene in RT maize and its homology with other catalases."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6830-6834(1987). RN [3] RP REVISIONS TO C-TERMINUS. RX MEDLINE=90370897; PubMed=2395887; RA Bethards L.A., Skadsen R.W., Scandalios J.G.; RT "Isolation and characterization of a cDNA clone for the Cat2 gene in RT maize and its homology with other catalases."; RL Proc. Natl. Acad. Sci. U.S.A. 87:6927-6927(1990). CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and CC serves to protect cells from the toxic effects of hydrogen CC peroxide. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC -!- COFACTOR: Heme group. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Peroxisomal or cytoplasmic. CC -!- SIMILARITY: Belongs to the catalase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54819; CAA38588.1; -. DR EMBL; J02976; AAA33440.1; -. DR PIR; S71455; S71455. DR HSSP; P00432; 4BLC. DR MaizeDB; 13855; -. DR InterPro; IPR002226; Catalase. DR Pfam; PF00199; catalase; 1. DR PRINTS; PR00067; CATALASE. DR ProDom; PD000510; Catalase; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. KW Oxidoreductase; Peroxidase; Iron; Heme; Hydrogen peroxide; KW Peroxisome; Multigene family. FT ACT_SITE 64 64 By similarity. FT ACT_SITE 137 137 By similarity. FT METAL 347 347 Iron (heme axial ligand) (By similarity). FT VARIANT 296 296 T -> R. FT CONFLICT 14 14 A -> P (in Ref. 2). FT CONFLICT 124 124 K -> N (in Ref. 2). SQ SEQUENCE 491 AA; 56465 MW; 6B686B6A94EA8598 CRC64; MDPYKHRPSS AFNAPYWTTN SGAPVWNNDS SLTVGARGPI LLEDYHCEKL ANFDRERIPE RVVHARGASA KGFFEVTHDI THLTCADFLR APGVQTPVIV RFSTVIHERG SPETLRDPRG FAVKFYTREG NWDLVGNNFP VFFIRDGIKF PDMVHALKPN PRTHIQDNWR ILDFFSHHPE SLHMFSFLFD DVGIPADYRH MDGSGVHTYT LVSRAGTVTY VKFHWRPTCG VRSLMDDEAV RCGANHSHAT KDLTDAIAAG NFPEWTLYIQ TMDPEMEDRL DDLDPLDVTK TWPEDTFPLQ PVGRLVLNRN IDNFFAENEQ LAFCPGLIVP GIYYSDDKLL QTRIFSYSDT QRHRLGPNYL LLPANAPKCA HHNNHYDGSM NFMHRHEEVD YFPSRYDAVR NAPRYPIPTA HIAGRREKTV ISKENNFKQP GERYRAMDPA RQERFITRWV DALSDPRLTH EIRTIWLSNW SQADRSLGQK LASRLSAKPS M // ID CAT3_MAIZE STANDARD; PRT; 496 AA. AC P18123; DT 01-NOV-1990 (Rel. 16, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Catalase isozyme 3 (EC 1.11.1.6). GN CAT3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; TISSUE=Seedling leaf; RX MEDLINE=94003062; PubMed=8400123; RA Abler M.L., Scandalios J.G.; RT "Isolation and characterization of a genomic sequence encoding the RT maize Cat3 catalase gene."; RL Plant Mol. Biol. 22:1031-1038(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; TISSUE=Epicotyl; RX MEDLINE=89051000; PubMed=2461221; RA Redinbaugh M.G., Wadsworth G.J., Scandalios J.G.; RT "Characterization of catalase transcripts and their differential RT expression in maize."; RL Biochim. Biophys. Acta 951:104-116(1988). CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and CC serves to protect cells from the toxic effects of hydrogen CC peroxide. Its levels are highest in the light period and are CC lowest in the dark period, hence it may be important for CC scavenging hydrogen peroxide at night, rather than during the day. CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O. CC -!- COFACTOR: Heme group. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Mitochondrial. CC -!- TISSUE SPECIFICITY: Leaf mesophyll cells, pericarp, seedling roots CC and the coleoptile. CC -!- SIMILARITY: Belongs to the catalase family. CC -!- CAUTION: There are two EMBL entries that correspond to the Ref.2 CC sequence and they encode slightly different proteins (see the CC feature table). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L05934; AAC37357.1; -. DR EMBL; M33103; AAA33441.1; -. DR EMBL; X12539; CAA31057.1; -. DR PIR; S37379; S37379. DR HSSP; P00432; 4BLC. DR MaizeDB; 13855; -. DR InterPro; IPR002226; Catalase. DR Pfam; PF00199; catalase; 1. DR PRINTS; PR00067; CATALASE. DR ProDom; PD000510; Catalase; 1. DR PROSITE; PS00437; CATALASE_1; 1. DR PROSITE; PS00438; CATALASE_2; 1. KW Oxidoreductase; Peroxidase; Iron; Heme; Hydrogen peroxide; KW Mitochondrion; Multigene family. FT ACT_SITE 67 67 By similarity. FT ACT_SITE 140 140 By similarity. FT METAL 351 351 Iron (heme axial ligand) (By similarity). FT CONFLICT 57 57 A -> D (in Ref. 2). FT CONFLICT 79 79 C -> S (in Ref. 2). FT CONFLICT 107 107 T -> Q (in Ref. 2). FT CONFLICT 110 110 H -> P (in Ref. 2). FT CONFLICT 112 112 R -> P (in Ref. 2). FT CONFLICT 115 116 PE -> GR (in Ref. 2). FT CONFLICT 121 121 P -> A (in Ref. 2). FT CONFLICT 194 194 D -> H (in Ref. 2; AAA33441). FT CONFLICT 234 234 V -> E (in Ref. 2). FT CONFLICT 236 236 C -> S (in Ref. 2; AAA33441). FT CONFLICT 244 245 AL -> R (in Ref. 2). FT CONFLICT 254 254 Missing (in Ref. 2). FT CONFLICT 264 264 A -> AE (in Ref. 2). FT CONFLICT 280 281 DT -> AQ (in Ref. 2). FT CONFLICT 282 282 E -> Q (in Ref. 2; AAA33441). FT CONFLICT 319 319 F -> L (in Ref. 2). FT CONFLICT 374 375 AH -> GT (in Ref. 2). FT CONFLICT 386 386 F -> L (in Ref. 2). FT CONFLICT 402 408 PLRQAAP -> RRCGRAA (in Ref. 2). FT CONFLICT 452 465 RRFADSLGHPKVSQ -> KAIRRLARTPQRQP (in FT Ref. 2). FT CONFLICT 478 478 C -> V (in Ref. 2). SQ SEQUENCE 496 AA; 56796 MW; 566FFD05B3795B49 CRC64; MTMDPTKFRP SSSHDTTVTT TNAGAPVWND NEALTVGPRG PILLEDYHLI EKVAHFARER IPERVVHARG ASAKGFFECT HDVTSLTCAD FLRAPGVRTP VIVRFSTVIH ERGSPETIRD PRGFAVKFYT REGNWDLLGN NFPVFFIRDG IKFPDVIHAF KPNPRSHVQE YWRVFDFLSH LPESLHTFFF LFDDVGVPSD YRHMEGFGVN TYTFVSAAGK AQYVKFHWKP TCGVRCILTD EEAALVGGRN HSHATQDLYD SIAAGSFPEW TLYVQVMDPD TEEQYDFDPL DDTKTWPEDL LPLRPVGRLV LDRNVDNFFN ENEQLAFGPG LVVPGIYYSD DKMLQCRVFA YADTQRYRLG PNYLMLPVNA PRCAHHNNHY DGAMNFMHRD EEVDYYPSRH APLRQAAPPT PLPPRPVAGR REKATIRKPN DFKQPGERYR SWDADRQDRF VRRFADSLGH PKVSQELRSI WIDLLAKCDA SLGMKIATRL NMKANM // ID CB21_MAIZE STANDARD; PRT; 262 AA. AC P12329; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Chlorophyll a-b binding protein 1, chloroplast precursor (LHCII type I DE CAB-1) (LHCP). GN CAB1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B37; RX MEDLINE=89218953; PubMed=2651890; RA Sullivan T.D., Christensen A.H., Quail P.H.; RT "Isolation and characterization of a maize chlorophyll a/b binding RT protein gene that produces high levels of mRNA in the dark."; RL Mol. Gen. Genet. 215:431-440(1989). CC -!- FUNCTION: The light-harvesting complex (LHC) functions as a light CC receptor, it captures and delivers excitation energy to CC photosystems with which it is closely associated. The N-terminus CC of the protein extends into the stroma where it is involved with CC adhesion of granal membranes and photoregulated by reversible CC phosphorylation of its threonine residues; both are believed to CC mediate the distribution of excitation energy between photosystems CC I and II. CC -!- SUBUNIT: The LHC complex consists of chlorophylls (a and b) and CC chlorophyll a-b binding proteins. CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b- CC binding (LHC) protein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14794; CAA32900.1; -. DR PIR; S04453; S04453. DR MaizeDB; 61648; -. DR InterPro; IPR001344; Chloro_ABbind. DR Pfam; PF00504; chloroa_b-bind; 1. DR ProDom; PD000275; Chloro_ABbind; 1. KW Chlorophyll; Photosynthesis; Photosystem I; Photosystem II; KW Thylakoid; Membrane; Chloroplast; Transit peptide; Multigene family; KW Transmembrane; Phosphorylation. FT TRANSIT 1 29 Chloroplast (Probable). FT CHAIN 30 262 Chlorophyll a-b binding protein 1. FT TRANSMEM 96 115 Potential. FT TRANSMEM 148 168 Potential. FT TRANSMEM 216 232 Potential. SQ SEQUENCE 262 AA; 27816 MW; 4165FADFE6727853 CRC64; MAASTMAISS TAMAGTPIKV GSFGEGRITM RKTVGKPKVA ASGSPWYGPD RVKYLGPFSG EPPSYLTGEF PGDYGWDTAG LSADPETFAK NRELEVIHSR WAMLGALGCV FPELLSRNGV KFGEAVWFKA GSQIFSEGGL DYLGNPSLIH AQSILAIWAC QVVLMGAVEG YRIAGGPLGE VVDPLYPGGS FDPLGLADDP EAFAELKVKE LKNGRLAMFS MFGFFVQAIV TGKGPLENLA DHIADPVNNN AWAYATNFVP GN // ID CB22_MAIZE STANDARD; PRT; 265 AA. AC P06671; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Chlorophyll a-b binding protein, chloroplast precursor (LHCII type I DE CAB) (LHCP). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Golden cross Bantam; RX MEDLINE=87316893; PubMed=3306599; RA Matsuoka M., Kano-Murakami Y., Yamamoto N.; RT "Nucleotide sequence of cDNA encoding the light-harvesting RT chlorophyll a/b binding protein from maize."; RL Nucleic Acids Res. 15:6302-6302(1987). CC -!- FUNCTION: The light-harvesting complex (LHC) functions as a light CC receptor, it captures and delivers excitation energy to CC photosystems with which it is closely associated. The N-terminus CC of the protein extends into the stroma where it is involved with CC adhesion of granal membranes and photoregulated by reversible CC phosphorylation of its threonine residues; both are believed to CC mediate the distribution of excitation energy between photosystems CC I and II. CC -!- SUBUNIT: The LHC complex consists of chlorophylls (a and b) and CC chlorophyll a-b binding proteins. CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b- CC binding (LHC) protein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00379; CAA68451.1; -. DR PIR; A29119; A29119. DR MaizeDB; 61648; -. DR InterPro; IPR001344; Chloro_ABbind. DR Pfam; PF00504; chloroa_b-bind; 1. DR ProDom; PD000275; Chloro_ABbind; 1. KW Chlorophyll; Photosynthesis; Photosystem I; Photosystem II; KW Thylakoid; Membrane; Chloroplast; Transit peptide; Multigene family; KW Transmembrane; Phosphorylation. FT TRANSIT 1 31 Chloroplast (Probable). FT CHAIN 32 265 Chlorophyll a-b binding protein. FT TRANSMEM 99 118 Potential. FT TRANSMEM 151 171 Potential. FT TRANSMEM 219 235 Potential. SQ SEQUENCE 265 AA; 27995 MW; 612A831B7432875B CRC64; MASSTMALSS TAFAGKAVNV PSSSFGEARV TMRKTAAKAK PAAASGSPWY GPDRVLYLGP LSGEPPSYLT GEFPGDYGWD TAGLSADPET FAKNRELEVI HCRWAMLGAL GCVFPELLAR NGVKFGEAVW FKAGSQIFSE GGLDYLGNPS LIHAQSILAI WACQVVLMGA VEGYRIAGGP LGEVVDPLYP GGSFDPLGLA DDPEAFGELK VKELKKGRLA MLSMFGFFVQ AIVTGKGPLE NLADHIADPV NNNAWAYATN FVPGK // ID CB29_MAIZE STANDARD; PRT; 265 AA. AC P27497; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Chlorophyll a-b binding protein M9, chloroplast precursor (LHCII type DE I CAB-M9) (LHCP). GN CAB-M9. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=91088340; PubMed=2263499; RA Viret J.F., Schantz M.L., Schantz R.; RT "Nucleotide sequence of a maize cDNA coding for a light-harvesting RT chlorophyll a/b binding protein of photosystem II."; RL Nucleic Acids Res. 18:7179-7179(1990). CC -!- FUNCTION: The light-harvesting complex (LHC) functions as a light CC receptor, it captures and delivers excitation energy to CC photosystems with which it is closely associated. The N-terminus CC of the protein extends into the stroma where it is involved with CC adhesion of granal membranes and photoregulated by reversible CC phosphorylation of its threonine residues; both are believed to CC mediate the distribution of excitation energy between photosystems CC I and II. CC -!- SUBUNIT: The LHC complex consists of chlorophylls (a and b) and CC chlorophyll a-b binding proteins. CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b- CC binding (LHC) protein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55892; CAA39376.1; -. DR PIR; S13098; S13098. DR MaizeDB; 61648; -. DR InterPro; IPR001344; Chloro_ABbind. DR Pfam; PF00504; chloroa_b-bind; 1. DR ProDom; PD000275; Chloro_ABbind; 1. KW Chlorophyll; Photosynthesis; Photosystem I; Photosystem II; KW Thylakoid; Membrane; Chloroplast; Transit peptide; Multigene family; KW Transmembrane; Phosphorylation. FT TRANSIT 1 31 Chloroplast (Probable). FT CHAIN 32 265 Chlorophyll a-b binding protein M9. FT TRANSMEM 99 118 Potential. FT TRANSMEM 151 171 Potential. FT TRANSMEM 219 235 Potential. SQ SEQUENCE 265 AA; 28041 MW; 1CC147D3044AC4A1 CRC64; MASSTMALSS TAFAGKAVNV PSSLFGEARV TMRKTAAKAK PAASSGSPWY GPDRVLYLGP LSGEPPSYLT GEFPGDYGWD TAGLSADPET FAKNRELEVI HSRWAMLGAL GCVFPELLAR NGVKFGEAVW FKAGSQIFSE GGLDYLGNPS LIHAQSILAI WACQVVLMGA IEGYRVAGGP LGEVVDPLYP GGTFDPLGLA DDPEAFADVK VKELKNGRLA MFSMFGFFVQ AIVTGKGPLE NLADHLADPV NNNAWAYATN FVPGK // ID CB48_MAIZE STANDARD; PRT; 264 AA. AC Q00827; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Chlorophyll a-b binding protein 48, chloroplast precursor (LHCII type DE I CAB-48) (LHCP). GN CAB48. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. BE10; RX MEDLINE=92322991; PubMed=1623200; RA Knight M.E., Ray J.A., Schuch W.; RT "Isolation of a gene from maize encoding a chlorophyll a/b-binding RT protein."; RL Plant Mol. Biol. 19:533-536(1992). CC -!- FUNCTION: The light-harvesting complex (LHC) function as a light CC receptor, it captures and delivers excitation energy to CC photosystems with which it is closely associated. The N-terminus CC of the protein extends into the stroma where it is involved with CC adhesion of granal membranes and photoregulated reversible CC phosphorylation of its threonine residues. Both are believed to CC mediate the distribution of excitation energy between photosystems CC I and II. CC -!- SUBUNIT: The LHC complex consists of chlorophylls (a and b) and CC chlorophyll a-b binding proteins. CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b- CC binding (LHC) protein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63205; CAA44888.1; -. DR PIR; S22497; S22497. DR MaizeDB; 61648; -. DR InterPro; IPR001344; Chloro_ABbind. DR Pfam; PF00504; chloroa_b-bind; 1. DR ProDom; PD000275; Chloro_ABbind; 1. KW Chlorophyll; Photosynthesis; Photosystem I; Photosystem II; KW Thylakoid; Membrane; Chloroplast; Transit peptide; Multigene family; KW Transmembrane; Phosphorylation. FT TRANSIT 1 31 Chloroplast (Probable). FT CHAIN 32 264 Chlorophyll a-b binding protein 48. FT TRANSMEM 98 117 By similarity. FT TRANSMEM 159 170 By similarity. FT TRANSMEM 218 234 By similarity. SQ SEQUENCE 264 AA; 28129 MW; A2F2A04A3DE0ADF3 CRC64; MAAATMAITS RALVGKPAAG TRDVFGEGRI TMRKTAAKPK PARSGSPWYG ADRVLYLGPL SGSPPSYLTG EFPGDYGWDT EGLSADPETF AKNRELEVIH CRWAIAVGLG CVFPELLARN GVKFGEGVWF KAGSQIFSEG GLSHPGNPSL VHAQSILAIW ACQVVLMGAV EGYHVAGGRL GEVVDPLYLG GSFDPLGLGD DPERFAELKV KEIKNGRLAM FSMFGFFVQA IVTGKGPIEN LADHLTDPVN NNAWAYATNF VPGK // ID CBFA_MAIZE STANDARD; PRT; 179 AA. AC P25209; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE CCAAT-binding transcription factor subunit A (CBF-A) (NF-Y protein DE chain B) (NF-YB) (CAAT-box DNA binding protein subunit B). GN NFY2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92195809; PubMed=1549471; RA Li X.-Y., Mantovani R., Hooft van Huijsduijnen R., Andre I., RA Benoist C., Mathis D.; RT "Evolutionary variation of the CCAAT-binding transcription factor RT NF-Y."; RL Nucleic Acids Res. 20:1087-1091(1992). CC -!- FUNCTION: Stimulates the transcription of various genes by CC recognizing and binding to a CCAAT motif in promoters, for example CC in type 1 collagen, albumin and beta-actin genes. CC -!- SUBUNIT: Heterotrimeric transcription factor composed of three CC components, A, B and C. NF-YB and NF-YC must interact and CC dimerize for NF-YA association and DNA binding. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- DOMAIN: Can be divided into three domains: the weakly conserved A CC domain, the highly conserved B domain thought to be involved in CC subunit interaction and DNA binding, and the Glu-rich C domain. CC -!- SIMILARITY: Belongs to the CBF-A subunit family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X59714; CAA42234.1; -. DR PIR; S22820; S22820. DR HSSP; P48781; 1B67. DR TRANSFAC; T05212; -. DR MaizeDB; 69282; -. DR InterPro; IPR003956; CBFA_NFYB. DR InterPro; IPR003958; CBFA_NFYB_domain. DR InterPro; IPR003957; CBFA_NFYB_topis. DR InterPro; IPR007124; Hist_TAF. DR Pfam; PF00808; CBFD_NFYB_HMF; 1. DR PRINTS; PR00615; CCAATSUBUNTA. DR PROSITE; PS00685; CBFA_NFYB; 1. KW Transcription regulation; DNA-binding; Activator; Nuclear protein. FT DOMAIN 1 29 A domain. FT DOMAIN 30 119 B DOMAIN. FT DOMAIN 120 179 C DOMAIN. FT DNA_BIND 36 42 By similarity. SQ SEQUENCE 179 AA; 18995 MW; 30621316CE469454 CRC64; MAEAPASPGG GGGSHESGSP RGGGGGGSVR EQDRFLPIAN ISRIMKKAIP ANGKIAKDAK ETVQECVSEF ISFITSEASD KCQREKRKTI NGDDLLWAMA TLGFEDYIEP LKVYLQKYRE MEGDSKLTAK SSDGSIKKDA LGHVGASSSA AEGMGQQGAY NQGMGYMQPQ YHNGDISNV // ID CCDP_MAIZE STANDARD; PRT; 129 AA. AC Q01595; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Cortical cell delineating protein precursor (Root-specific protein DE ZRP3). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. NKH31; TISSUE=Root; RX MEDLINE=93099234; PubMed=1463822; RA John I., Wang H., Held B.M., Wurtele E.S., Colbert J.T.; RT "An mRNA that specifically accumulates in maize roots delineates a RT novel subset of developing cortical cells."; RL Plant Mol. Biol. 20:821-831(1992). CC -!- FUNCTION: Delineates a novel subset of developing cortical cells. CC It is probably involved in some aspect of transport of molecules CC to or from the vasculature. CC -!- TISSUE SPECIFICITY: Cortical ground meristem of developing roots. CC -!- SIMILARITY: Strong, to carrot DC2.15 and PEMB3. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z12103; CAA78088.1; -. DR PIR; S28009; S28009. DR HSSP; P24337; 1HYP. DR MaizeDB; 65581; -. DR InterPro; IPR003612; AAI. DR Pfam; PF00234; tryp_alpha_amyl; 1. DR SMART; SM00499; AAI; 1. KW Signal; Glycoprotein; Repeat. FT SIGNAL 1 19 Or 21 (Potential). FT CHAIN 20 129 Cortical cell delineating protein. FT CARBOHYD 25 25 N-linked (GlcNAc...) (Potential). FT DOMAIN 29 40 2 X 6 AA tandem repeats of P-V-V-P-T-P. FT REPEAT 29 34 1. FT REPEAT 35 40 2. SQ SEQUENCE 129 AA; 13526 MW; 39AAE618761D948B CRC64; MAPKVALFLA LSLLFAATAH GCEPNCSGPV VPTPPVVPTP SSHSHGRCPI DALKLKVCAK VLGLVKVGLP QYEQCCPLLE GLVDLDAALC LCTAIKANVL GIHLNVPLSL NFILNNCGRI CPEDFTCPN // ID CCSA_MAIZE STANDARD; PRT; 321 AA. AC P46659; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Cytochrome c biogenesis protein ccsA. GN CCSA. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Required during cytochrome biogenesis at the step of CC heme attachment (By similarity). CC -!- SIMILARITY: Belongs to the ccmF/cycK/ccl1/nrfE/ccsA family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60348.1; -. DR PIR; S58614; S58614. DR Gramene; P46659; -. DR MaizeDB; 118255; -. DR InterPro; IPR002541; CytC_asm. DR Pfam; PF01578; CytC_asm; 1. KW Cytochrome c-type biogenesis; Chloroplast. SQ SEQUENCE 321 AA; 36693 MW; AF981BAA461A5D1B CRC64; MLFATLEHIL THISFSTISI VITIHLITLL VRELRGLRDS SEKGMIATFF SITGFLVSRW VSSGHFPLSN LYESLIFLSW TLYILHTIPK IQNSKNDLST ITTPSTILTQ GFATSGLLTE MHQSTILVPA LQSQWLMMHV SMMLLSYATL LCGSLLSAAL LIIRFRKNFD FFSLKKNVFL KTFFFSEIEY LYAKRSALKN TSFPVFPNYY KYQLTERLDS WSYRVISLGF TLLTVGILCG AVWANEAWGS YWNWDPKETW AFITWTIFAI YLHSRKNPNW KGTNSALVAS IGFLIIWICY FGINLLGIGL HSYGSFTLPS K // ID CDC2_MAIZE STANDARD; PRT; 294 AA. AC P23111; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Cell division control protein 2 homolog (EC 2.7.1.-) (p34cdc2). GN CDC2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91195354; PubMed=2014258; RA Colasanti J., Tyers M., Sundaresan V.; RT "Isolation and characterization of cDNA clones encoding a functional RT p34cdc2 homologue from Zea mays."; RL Proc. Natl. Acad. Sci. U.S.A. 88:3377-3381(1991). CC -!- FUNCTION: Plays a key role in the control of the eukaryotic cell CC cycle. Component of the kinase complex that phosphorylates the CC repetitive carboxyl-terminus of RNA polymerase II. CC -!- ENZYME REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates CC the enzyme, while phosphorylation at Thr-161 activates it (By CC similarity). CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. CC CDC2/CDKX subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M60526; AAA33479.1; -. DR HSSP; P24941; 1HCL. DR MaizeDB; 60686; -. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Cell cycle; Cell division; Mitosis; Phosphorylation. FT DOMAIN 4 287 Protein kinase. FT NP_BIND 10 18 ATP (By similarity). FT BINDING 33 33 ATP (By similarity). FT ACT_SITE 127 127 Proton acceptor (By similarity). FT MOD_RES 14 14 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 15 15 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 161 161 PHOSPHORYLATION (BY CAK) (BY SIMILARITY). SQ SEQUENCE 294 AA; 33834 MW; 5063ECFCC2D5FFDD CRC64; MEQYEKVEKI GEGTYGVVYK ALDKATNETI ALKKIRLEQE DEGVPSTAIR EISLLKEMNH GNIVRLHDVV HSEKRIYLVF EYLDLDLKKF MDSCPEFAKN PTLIKSYLYQ ILHGVAYCHS HRVLHRDLKP QNLLIDRRTN ALKLADFGLA RAFGIPVRTF THEVVTLWYR APEILLGARQ YSTPVDVWSV GCIFAEMVNQ KPLFPGDSEI DELFKIFRIL GTPNEQSWPG VSCLPDFKTA FPRWQAQDLA TVVPNLDPAG LDLLSKMLRY EPSKRITARQ ALEHEYFKDL EVVQ // ID CDP2_MAIZE STANDARD; PRT; 513 AA. AC P49101; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Calcium-dependent protein kinase 2 (EC 2.7.1.-) (CDPK 2). GN CDPK2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Merit; TISSUE=Root tip; RX MEDLINE=95281563; PubMed=7761420; RA Patil S., Takezawa D., Poovaiah B.W.; RT "Chimeric plant calcium/calmodulin-dependent protein kinase gene with RT a neural visinin-like calcium-binding domain."; RL Proc. Natl. Acad. Sci. U.S.A. 92:4897-4901(1995). CC -!- FUNCTION: May play a role in signal transduction pathways that CC involve calcium as a second messenger. CC -!- ENZYME REGULATION: Activated by calcium (By similarity). CC Autophosphorylation may play an important role in the regulation CC of the kinase activity (By similarity). CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. CaMK CC subfamily. CC -!- SIMILARITY: Contains 4 EF-hand calcium-binding domains. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U28376; AAA69507.1; -. DR PIR; T02259; T02259. DR HSSP; Q63450; 1A06. DR MaizeDB; 56895; -. DR InterPro; IPR002048; EF-hand. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00036; efhand; 4. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000012; EF-hand; 2. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00054; EFh; 4. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00018; EF_HAND; 4. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Calcium-binding; Phosphorylation. FT DOMAIN 65 323 Protein kinase. FT NP_BIND 71 79 ATP (By similarity). FT BINDING 94 94 ATP (By similarity). FT ACT_SITE 189 189 Proton acceptor (By similarity). FT CA_BIND 379 390 EF-hand 1 (Potential). FT CA_BIND 415 426 EF-hand 2 (Potential). FT CA_BIND 451 462 EF-hand 3 (Potential). FT CA_BIND 486 497 EF-hand 4 (Potential). SQ SEQUENCE 513 AA; 58081 MW; 235A61630C0AC336 CRC64; MVMAILTRQS RRKHLRVYNP PQQAAEVRYT PSATNSSAVP PVAVPPKPTA DTILGKQYED VRSVYSFGKE LGRGQFGVTY LCTEIASGRQ YACKSISKRK LVSKADREDI RREIQIMQHL SGQPNIVEFR GAYEDKSNVH VVMELCAGGE LFDRIIAKGH YTERAAATIC RAVVNVVNIC HFMGVMHRDL KPENFLLATM EENAMLKATD FGLSVFIEEG KMYRDIVGSA YYVAPEVLRR SYGKEIDVWS AGVILYILLS GVPPFWAEIE KGIFDAILHE EIDFESQPWP SISESAKDLV RKMLTRDPKK RLTSAQVLQH QWLREGGEAS DKPIDSAVLS RMKQFRAMNK LKKMALKVIA SNLNEEEIKG LKQMFMNMDT DNSGTITYEE LKAGLAKLGS KLSEAEVKQL MEAADVDGNG SIDYVEFITA TMHRHKLERD EHLFKAFQYF DKDNSGFITR DELESALIEH EMGDTSTIRE IISEVDTDND GRINYEEFCA MMRGGMQQPM RLK // ID CEMA_MAIZE STANDARD; PRT; 230 AA. AC P46641; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast envelope membrane protein. GN CEMA OR YCF10. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: May be involved in proton extrusion. Indirectly promotes CC efficient inorganic carbon uptake into chloroplasts (By CC similarity). CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast inner CC envelope (By similarity). CC -!- SIMILARITY: Belongs to the cemA family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60297.1; -. DR PIR; S58563; S58563. DR Gramene; P46641; -. DR MaizeDB; 118235; -. DR HAMAP; MF_01308; -; 1. DR InterPro; IPR004282; CemA. DR Pfam; PF03040; CemA; 1. KW Chloroplast; Transmembrane; Transport; Hydrogen ion transport. FT TRANSMEM 7 27 Potential. FT TRANSMEM 106 126 Potential. FT TRANSMEM 145 165 Potential. FT TRANSMEM 181 201 Potential. SQ SEQUENCE 230 AA; 27155 MW; 168A4DCD3BFDF5D2 CRC64; MKKKKALPSF LYLVFIVLLP WGVSFSFNKC LELWIKNWWN TRQSETFLTD IQEKRILEGF IELEELFLLD EMIKEKPKTH VQKLPIGIHK EIIQLAKIDN EDHLHIILHF STNIICLAIL SGSFFLGKEE LVILNSWVQE FFYNLNDSIK AFFILLVTDF FVGFHSTRGW ELLIRWVYNN LGWAPNELIF TIFVCSFPVI LDTCLKFWVF FCLNRLSPSL VVIYHSISEA // ID CFI_MAIZE STANDARD; PRT; 231 AA. AC Q08704; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chalcone--flavonone isomerase (EC 5.5.1.6) (Chalcone isomerase). GN CHI OR CHI1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94104592; PubMed=8277939; RA Grotewold E., Peterson T.; RT "Isolation and characterization of a maize gene encoding chalcone RT flavonone isomerase."; RL Mol. Gen. Genet. 242:1-8(1994). CC -!- FUNCTION: Responsible for the isomerization of 4,2',4',6'- CC tetrahydroxychalcone (also termed chalcone) into naringenin. CC -!- CATALYTIC ACTIVITY: A chalcone = a flavonone. CC -!- PATHWAY: Part of the biosynthetic pathway for all classes of CC flavonoids, a large class of secondary plant metabolites, many of CC which are brightly colored. CC -!- SIMILARITY: Belongs to the chalcone isomerase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z22760; CAA80441.1; -. DR PIR; S41570; S41570. DR MaizeDB; 56296; -. DR InterPro; IPR003466; Chalcone. DR Pfam; PF02431; Chalcone; 1. KW Flavonoid biosynthesis; Isomerase. SQ SEQUENCE 231 AA; 24250 MW; AD64A8B04213F9F5 CRC64; MACRRWWSTA VVFPPVARPP GSAGSHFLGG AGVRGVEIGG NFIKFTAIGV YLEDAAVPAL AKKWGGKTAD ELASDAAFFR DVVTGDFEKF TRVTMILPLT GEQYAEKVTE NCVAFWKAAG LYTDAEGVAV EKFREVFKPE TFAPGRSILF THSPAGVLTV AFSKDSSVPA AGGVAIENKR LCEAVLESII GERGVSPAAK LSLAARVSEL LAKETAAAAD APQAEPVSIT A // ID CH61_MAIZE STANDARD; PRT; 577 AA. AC P29185; Q43251; Q43252; DT 01-DEC-1992 (Rel. 24, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Chaperonin CPN60-1, mitochondrial precursor (HSP60-1). GN CPN60I OR CPNA. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 35-70. RC STRAIN=cv. Black Mexican Sweet; TISSUE=Seed; RX MEDLINE=92256809; PubMed=1349837; RA Prasad T.K., Stewart C.R.; RT "cDNA clones encoding Arabidopsis thaliana and Zea mays mitochondrial RT chaperonin HSP60 and gene expression during seed germination and heat RT shock."; RL Plant Mol. Biol. 18:873-885(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RA Close P.S.; RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=cv. MUTIND-FR7205024; RA Burt W.J.; RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Implicated in mitochondrial protein import and CC macromolecular assembly. May facilitate the correct folding of CC imported proteins. May also prevent misfolding and promote the CC refolding and proper assembly of unfolded polypeptides generated CC under stress conditions in the mitochondrial matrix. CC -!- SUBCELLULAR LOCATION: Mitochondrial. CC -!- INDUCTION: By heat shock. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z11546; CAA77645.1; -. DR EMBL; L21007; AAA33450.1; -. DR EMBL; Z12114; CAA78100.1; -. DR PIR; S20875; S20875. DR PIR; S26582; S26582. DR HSSP; P06139; 1GRL. DR MaizeDB; 65669; -. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR008950; GroEL-ATPase. DR Pfam; PF00118; cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR PRINTS; PR00304; TCOMPLEXTCP1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. KW Chaperone; ATP-binding; Transit peptide; Mitochondrion; Heat shock. FT TRANSIT 1 34 Mitochondrion. FT CHAIN 35 577 Chaperonin CPN60-1. FT CONFLICT 21 21 T -> A (in Ref. 3). FT CONFLICT 108 109 KQ -> NR (in Ref. 1). FT CONFLICT 125 125 A -> D (in Ref. 1). FT CONFLICT 148 148 D -> N (in Ref. 1). FT CONFLICT 241 241 S -> P (in Ref. 3). FT CONFLICT 328 328 L -> F (in Ref. 1). FT CONFLICT 382 382 I -> L (in Ref. 1). FT CONFLICT 403 403 A -> P (in Ref. 2). SQ SEQUENCE 577 AA; 61211 MW; 31D3BFFD46701C0B CRC64; MYRAAASLAS KARQAGNSLA TRQVGSRLAW SRNYAAKDIK FGVEARALML RGVEELADAV KVTMGPKGRN VVIEQSFGAP KVTKDGVTVA KSIEFKDRVK NVGASLVKQV ANATNDTAGD GTTCATVLTK AIFTEGCKSV AAGMNAMDLR RGISMAVDAV VTNLKGMARM ISTSEEIAQV GTISANGERE IGELIAKAME KVGKEGVITI ADGNTLYNEL EVVEGMKLDR GYISPYFITN SKTQKCELED PLILIHDKKV TNMHAVVKVL EMALKKQKPL LIVAEDVESE ALGTLIINKL RAGIKVCAVK APGFGENRKA NLQDLAILTG GEVITEELGM NLENFEPHML GTCKKVTVSK DDTVILDGAG DKKSIEERAE QIRSAIENST SDYDKEKLQE RLAKLSGGVA VLKIGGASEA EVGEKKDRVT DALNATKAAV EEGIVPGGGV ALLYASKELD KLQTANFDQK IGVQIIQNAL KTPVHTIASN AGVEGAVVVG KLLEQENTDL GYDAAKGEYV DMVKTGIIDP LKVIRTALVD AASVSSLMTT TESIIVEIPK EEAPAPAMGG GMGGMDY // ID CH62_MAIZE STANDARD; PRT; 576 AA. AC Q43298; Q43253; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Chaperonin CPN60-2, mitochondrial precursor (HSP60-2). GN CPN60II OR CPNB. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RA Close P.S.; RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. MUTIND-FR7205024; RA Burt W.J.; RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Implicated in mitochondrial protein import and CC macromolecular assembly. May facilitate the correct folding of CC imported proteins. May also prevent misfolding and promote the CC refolding and proper assembly of unfolded polypeptides generated CC under stress conditions in the mitochondrial matrix. CC -!- SUBCELLULAR LOCATION: Mitochondrial. CC -!- INDUCTION: By heat shock. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L21008; AAA33451.1; -. DR EMBL; L21006; AAA33452.1; -. DR EMBL; Z12115; CAA78101.1; -. DR PIR; S26583; S26583. DR HSSP; P06139; 1GRL. DR MaizeDB; 65675; -. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR008950; GroEL-ATPase. DR Pfam; PF00118; cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR PRINTS; PR00304; TCOMPLEXTCP1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. KW Chaperone; ATP-binding; Transit peptide; Mitochondrion; Heat shock. FT TRANSIT 1 34 Mitochondrion (By similarity). FT CHAIN 35 576 Chaperonin CPN60-2. FT CONFLICT 117 117 T -> N (in Ref. 2). FT CONFLICT 248 248 L -> P (in Ref. 2). FT CONFLICT 258 258 K -> R (in Ref. 2). SQ SEQUENCE 576 AA; 60935 MW; 1039FB77D7895321 CRC64; MYRAAASLAS KARQAGSSSA ARQVGSRLAW SRNYAAKDIK FGVEARALML RGVEELADAV KVTMGPKGRN VVIEQSFGAP KVTKDGVTVA KSIEFKDRVK NVGASLVKQV ANATNDTAGD GTTCATVLTK AIFTEGCKSV AAGMNAMDLR RGISMAVDAV VTNLKGMARM ISTSEEIAQV GTISANGERE IGELIAKAME KVGKEGVITI ADGNTLYNEL EVVEGMKLDR GYISPYFITN SKAQKCELED PLILIHDKKV TNMHAVVKVL EMALKKQRPL LIVAEDVESE ALGTLIINKL RAGIKVCAVK APGFGENRKA NLQDLAILTG GEVITEELGM NLENVEPHML GSCKKVTVSK DDTVILDGAG DKKSIEERAD QIRSAVENST SDYDKEKLQE RLAKLSGGVA VLKIGGASEA EVGEKKDRVT DALNATKAAV EEGIVPGGGV ALLYASKELD KLQTANFDQK IGVQIIQNAL KTPVHTIASN AGVEGAVVVG KLLEQGNTDL GYDAAKDEYV DMVKAGIIDP LKVIRTALVD AASVSSLMTT TESIIVEIPK EEAPAPAMGG MGGMDY // ID CHIA_MAIZE STANDARD; PRT; 280 AA. AC P29022; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Endochitinase A precursor (EC 3.2.1.14) (Seed chitinase A). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seed; RX MEDLINE=92202208; PubMed=1551872; RA Huynh Q.K., Hironaka C.M., Levine E.B., Smith C.E., Borgmeyer J.R., RA Shah D.M.; RT "Antifungal proteins from plants. Purification, molecular cloning, RT and antifungal properties of chitinases from maize seed."; RL J. Biol. Chem. 267:6635-6640(1992). RN [2] RP SEQUENCE OF 180-195. RC TISSUE=Seed; RX MEDLINE=92156129; PubMed=1740436; RA Verburg J.G., Smith C.E., Lisek C.A., Huynh Q.K.; RT "Identification of an essential tyrosine residue in the catalytic RT site of a chitinase isolated from Zea mays that is selectively RT modified during inactivation with RT 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide."; RL J. Biol. Chem. 267:3886-3893(1992). CC -!- FUNCTION: This protein functions as a defense against chitin CC containing fungal pathogens. CC -!- CATALYTIC ACTIVITY: Hydrolysis of the 1,4-beta-linkages of N- CC acetyl-D-glucosamine polymers of chitin. CC -!- MISCELLANEOUS: Maize chitinase B seems to be less active than CC chitinase A. CC -!- SIMILARITY: Belongs to chitinase class IA (family 19 of glycosyl CC hydrolases). CC -!- SIMILARITY: Contains 1 chitin-binding type-1 domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84164; AAA33444.1; -. DR HSSP; P02877; 1HEV. DR MaizeDB; 25130; -. DR InterPro; IPR001002; Chitin_binding_1. DR InterPro; IPR000726; Glyco_hydro_19. DR Pfam; PF00187; Chitin_bind_1; 1. DR Pfam; PF00182; Glyco_hydro_19; 1. DR PRINTS; PR00451; CHITINBINDNG. DR ProDom; PD000609; Chitin_binding_1; 1. DR ProDom; PD354900; Glyco_hydro_19; 1. DR SMART; SM00270; ChtBD1; 1. DR PROSITE; PS50941; CHIT_BIND_I_2; 1. DR PROSITE; PS00026; CHIT_BIND_I_1; 1. DR PROSITE; PS00773; CHITINASE_19_1; 1. DR PROSITE; PS00774; CHITINASE_19_2; 1. KW Hydrolase; Glycosidase; Chitin degradation; Chitin-binding; Signal; KW Multigene family. FT SIGNAL 1 25 Potential. FT CHAIN 26 280 Endochitinase A. FT DOMAIN 26 60 Chitin-binding type-1. FT DOMAIN 61 77 HINGE REGION (POLY-GLY). FT DOMAIN 78 280 Catalytic. FT DISULFID 28 36 By similarity. FT DISULFID 30 42 By similarity. FT DISULFID 35 49 By similarity. FT DISULFID 53 58 By similarity. FT DISULFID 100 149 By similarity. FT DISULFID 161 170 By similarity. FT DISULFID 248 280 By similarity. SQ SEQUENCE 280 AA; 29124 MW; 4FC5BB7D938C1CC1 CRC64; MANAPRILAL GLLALLCAAA GPAAAQNCGC QPNFCCSKFG YCGTTDAYCG DGCQSGPCRS GGGGGGGGGG GGGGSGGANV ANVVTDAFFN GIKNQAGSGC EGKNFYTRSA FLSAVNAYPG FAHGGTEVEG KREIAAFFAH VTHETGHFCY ISEINKSNAY CDASNRQWPC AAGQKYYGRG PLQISWNYNY GPAGRDIGFN GLADPNRVAQ DAVIAFKTAL WFWMNNVHGV MPQGFGATIR AINGALECNG NNPAQMNARV GYYKQYCQQL RVDPGPNLIC // ID CHIB_MAIZE STANDARD; PRT; 269 AA. AC P29023; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Endochitinase B precursor (EC 3.2.1.14) (Seed chitinase B) (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seed; RX MEDLINE=92202208; PubMed=1551872; RA Huynh Q.K., Hironaka C.M., Levine E.B., Smith C.E., Borgmeyer J.R., RA Shah D.M.; RT "Antifungal proteins from plants. Purification, molecular cloning, RT and antifungal properties of chitinases from maize seed."; RL J. Biol. Chem. 267:6635-6640(1992). RN [2] RP SEQUENCE OF 169-184. RC TISSUE=Seed; RX MEDLINE=92156129; PubMed=1740436; RA Verburg J.G., Smith C.E., Lisek C.A., Huynh Q.K.; RT "Identification of an essential tyrosine residue in the catalytic RT site of a chitinase isolated from Zea mays that is selectively RT modified during inactivation with RT 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide."; RL J. Biol. Chem. 267:3886-3893(1992). CC -!- FUNCTION: This protein functions as a defense against chitin CC containing fungal pathogens. CC -!- CATALYTIC ACTIVITY: Hydrolysis of the 1,4-beta-linkages of N- CC acetyl-D-glucosamine polymers of chitin. CC -!- MISCELLANEOUS: Maize chitinase B seems to be less active than CC chitinase A. CC -!- SIMILARITY: Belongs to chitinase class IA (family 19 of glycosyl CC hydrolases). CC -!- SIMILARITY: Contains 1 chitin-binding type-1 domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84165; AAA33445.1; -. DR HSSP; P02877; 1HEV. DR MaizeDB; 25130; -. DR InterPro; IPR001002; Chitin_binding_1. DR InterPro; IPR000726; Glyco_hydro_19. DR Pfam; PF00187; Chitin_bind_1; 1. DR Pfam; PF00182; Glyco_hydro_19; 1. DR PRINTS; PR00451; CHITINBINDNG. DR ProDom; PD000609; Chitin_binding_1; 1. DR ProDom; PD354900; Glyco_hydro_19; 1. DR SMART; SM00270; ChtBD1; 1. DR PROSITE; PS50941; CHIT_BIND_I_2; 1. DR PROSITE; PS00026; CHIT_BIND_I_1; 1. DR PROSITE; PS00773; CHITINASE_19_1; 1. DR PROSITE; PS00774; CHITINASE_19_2; 1. KW Hydrolase; Glycosidase; Chitin degradation; Chitin-binding; Signal; KW Multigene family. FT NON_TER 1 1 FT SIGNAL <1 20 Potential. FT CHAIN 21 269 Endochitinase B. FT DOMAIN 21 55 Chitin-binding type-1. FT DOMAIN 58 66 HINGE REGION (GLY-RICH). FT DOMAIN 67 269 Catalytic. FT DISULFID 23 31 By similarity. FT DISULFID 25 37 By similarity. FT DISULFID 30 44 By similarity. FT DISULFID 48 53 By similarity. FT DISULFID 89 138 By similarity. FT DISULFID 150 159 By similarity. FT DISULFID 237 269 By similarity. SQ SEQUENCE 269 AA; 28166 MW; 3D38B1BADF75DE8F CRC64; PQLVALGLAL LCAVAGPAAA QNCGCQPNVC CSKFGYCGTT DEYCGDGCQS GPCRSGRGGG GSGGGGANVA SVVTSSFFNG IKNQAGSGCE GKNFYTRSAF LSAVKGYPGF AHGGSQVQGK REIAAFFAHA THETGHFCYI SEINKSNAYC DPTKRQWPCA AGQKYYGRGP LQISWNYNYG PAGRAIGFDG LGDPGRVARD AVVAFKAALW FWMNSVHGVV PQGFGATTRA MQRALECGGN NPAQMNARVG YYRQYCRQLG VDPGPNLTC // ID CHS1_MAIZE STANDARD; PRT; 400 AA. AC P24824; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Chalcone synthase WHP1 (EC 2.3.1.74) (Naringenin-chalcone synthase DE WHP1) (White pollen). GN WHP1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Line C1-P; TISSUE=Leaf; RX MEDLINE=91330885; PubMed=1714383; RA Franken P., Niesbach-Kloesgen U., Weydemann U., Marechal-Drouard L., RA Saedler H., Wienand U.; RT "The duplicated chalcone synthase genes C2 and Whp (white pollen) of RT Zea mays are independently regulated; evidence for translational RT control of Whp expression by the anthocyanin intensifying gene in."; RL EMBO J. 10:2605-2612(1991). CC -!- FUNCTION: The primary product of this enzyme is 4,2',4',6'- CC tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) CC which can under specific conditions spontaneously isomerize into CC naringenin. CC -!- CATALYTIC ACTIVITY: 3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + CC naringenin-chalcone + 3 CO(2). CC -!- PATHWAY: Part of the biosynthetic pathway for all classes of CC flavonoids, a large class of secondary plant metabolites, many of CC which are brightly colored. CC -!- SIMILARITY: Belongs to the chalcone/stilbene synthases family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60204; CAA42763.1; -. DR PIR; S16599; SYZMW1. DR MaizeDB; 13853; -. DR InterPro; IPR001099; N-C_synthase. DR Pfam; PF00195; Chal_stil_synt; 1. DR Pfam; PF02797; Chal_stil_syntC; 1. DR ProDom; PD000453; N-C_synthase; 1. DR PROSITE; PS00441; CHALCONE_SYNTH; 1. KW Flavonoid biosynthesis; Transferase; Acyltransferase; KW Multigene family. FT ACT_SITE 167 167 By similarity. SQ SEQUENCE 400 AA; 43172 MW; 8AB661A86253616C CRC64; MAGATVTVDE VRKGQRATGP ATVLAIGTAT PANCVYQADY PDYYFRITKS DHLTDLKEKF KRMCDKSMIR KRYMHLTEEF LSENPSMCAY MAPSLDARQD VVVTEVPKLG KAAAQEAIKE WGQPKSRITH LVFCTTSGVD MPGADYQLTK ALGLRVVNRL MMYQQGCFAG GTVLRVAKDV AENNRGARVM VVCSEITAVT FRGPSESHVD SLVGQALFGD GAAAGRGGAD PDGRVERPLF QLVSAAQTIL PDSEGAIDGH LREVGLAFHL LKDVPGLISK NIERALEDAF EPLGISDWNS IFWVAHPGGP AILDQVEAKV GLDKARMRAT RHVLSEYGNM SSACVLFILD EMRKRPAEDG QSTTGEGLDW GVLFGFGPGL TVETVVLHSV PITTGAPTAA // ID CHS2_MAIZE STANDARD; PRT; 400 AA. AC P24825; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Chalcone synthase C2 (EC 2.3.1.74) (Naringenin-chalcone synthase C2). GN C2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Line C1-P; TISSUE=Leaf; RX MEDLINE=91330885; PubMed=1714383; RA Franken P., Niesbach-Kloesgen U., Weydemann U., Marechal-Drouard L., RA Saedler H., Wienand U.; RT "The duplicated chalcone synthase genes C2 and Whp (white pollen) of RT Zea mays are independently regulated; evidence for translational RT control of Whp expression by the anthocyanin intensifying gene in."; RL EMBO J. 10:2605-2612(1991). CC -!- FUNCTION: The primary product of this enzyme is 4,2',4',6'- CC tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) CC which can under specific conditions spontaneously isomerize into CC naringenin. CC -!- CATALYTIC ACTIVITY: 3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + CC naringenin-chalcone + 3 CO(2). CC -!- PATHWAY: Part of the biosynthetic pathway for all classes of CC flavonoids, a large class of secondary plant metabolites, many of CC which are brightly colored. CC -!- SIMILARITY: Belongs to the chalcone/stilbene synthases family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60205; CAA42764.1; -. DR PIR; S16598; SYZMCC. DR MaizeDB; 13853; -. DR InterPro; IPR001099; N-C_synthase. DR Pfam; PF00195; Chal_stil_synt; 1. DR Pfam; PF02797; Chal_stil_syntC; 1. DR ProDom; PD000453; N-C_synthase; 1. DR PROSITE; PS00441; CHALCONE_SYNTH; 1. KW Flavonoid biosynthesis; Transferase; Acyltransferase; KW Multigene family. FT ACT_SITE 168 168 By similarity. SQ SEQUENCE 400 AA; 43195 MW; 17D1095EE077DEC3 CRC64; MAGATVTVEE VRKAQRATGP ATVLAIGTAT PANCVYQADY PDYYFRITKS EHLTDLKEKF KRMCDKSMIR KRYMHLTEEF LAENPSMCAY MAPSLDARQD VVVVEVPKLG KAAAQKAIKE WGQPKSRITH LVFCTTSGVD MPGADYQLTK ALGLRPSVNR LMMYQQGCFA GGTVLRVAKD LAENNRGARV LVVCSEITAV TFRGPSESHL DSLVGQALFG DGAAAVVVGA DPDDRVERPL FQLVSAAQTI LPDSEGAIDG HLREVGLTFH LLKDVPGLIS KNIGRALDDA FKPLGISDWN SIFWVAHPGG PAILDQVEAK VGLDKARMRA TRHVLSEYGN MSSACVLFIL DEMRKRSAED GQATTGEGLD WGVLFGFGPG LTVETVVLHS VPITTGAATA // ID CKX1_MAIZE STANDARD; PRT; 534 AA. AC Q9T0N8; O81158; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Cytokinin dehydrogenase 1 precursor (EC 1.5.99.12) (Cytokinin oxidase DE 1) (CKO 1). GN CKX1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 417-435; 490-517 AND 524-534. RC STRAIN=cv. Nobilis; TISSUE=Kernel; RX MEDLINE=99246676; PubMed=10230061; RA Houba-Herin N., Pethe C., D'Alayer J., Laloue M.; RT "Cytokinin oxidase from Zea mays: purification, cDNA cloning and RT expression in moss protoplasts."; RL Plant J. 17:615-626(1999). RN [2] RP SEQUENCE FROM N.A., SEQUENCE OF 286-308; 369-377; 388-392 AND 417-431, RP AND MASS SPECTROMETRY. RX MEDLINE=99160863; PubMed=10049708; RA Morris R.O., Bilyeu K.D., Laskey J.G., Cheikh N.N.; RT "Isolation of a gene encoding a glycosylated cytokinin oxidase from RT maize."; RL Biochem. Biophys. Res. Commun. 255:328-333(1999). RN [3] RP CHARACTERIZATION, AND TISSUE SPECIFICITY. RX MEDLINE=21068113; PubMed=11154345; RA Bilyeu K.D., Cole J.L., Laskey J.G., Riekhof W.R., Esparza T.J., RA Kramer M.D., Morris R.O.; RT "Molecular and biochemical characterization of a cytokinin oxidase RT from maize."; RL Plant Physiol. 125:378-386(2001). CC -!- FUNCTION: Catalyzes the oxidation of cytokinins, a family of N(6)- CC substituted adenine derivatives that are plant hormones, where the CC substituent is an isopentenyl group. Cleaves zeatin, CC isopentenyladenine, isopentenyladenosine, zeatin riboside and cis- CC zeatin, but not dihydrozeatin, kinetin and benzylaminopurine. CC -!- CATALYTIC ACTIVITY: N(6)-dimethylallyladenine + acceptor + H(2)O = CC adenine + 3-methylbut-2-enal + reduced acceptor. CC -!- COFACTOR: FAD. CC -!- ENZYME REGULATION: Competitive inhibition by phenylureas. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Extracellular. CC -!- TISSUE SPECIFICITY: Expressed in immature kernels and unpollinated CC cobs. Weakly expressed in kernels harvested two weeks after CC anthesis. CC -!- PTM: Glycosylated; with approximately 10 hexose residues per site. CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked CC oxidoreductase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y18377; CAA77151.1; -. DR EMBL; AF044603; AAC27500.1; -. DR PIR; T01500; T01500. DR PIR; T51929; T51929. DR MaizeDB; 194080; -. DR InterPro; IPR006094; Oxid_FAD_bind. DR InterPro; IPR006093; Oxred_FAD_BS. DR Pfam; PF01565; FAD_binding_4; 1. DR PROSITE; PS00862; OX2_COVAL_FAD; 1. KW Oxidoreductase; Flavoprotein; FAD; Signal; Glycoprotein. FT SIGNAL 1 18 Potential. FT CHAIN 19 534 Cytokinin dehydrogenase 1. FT DOMAIN 339 345 Poly-Ala. FT BINDING 105 105 FAD (covalent) (Probable). FT CARBOHYD 52 52 N-linked (GlcNAc...) (Potential). FT CARBOHYD 63 63 N-linked (GlcNAc...) (Potential). FT CARBOHYD 134 134 N-linked (GlcNAc...) (Potential). FT CARBOHYD 294 294 N-linked (GlcNAc...) (Potential). FT CARBOHYD 323 323 N-linked (GlcNAc...) (Potential). FT CARBOHYD 338 338 N-linked (GlcNAc...) (Potential). FT CARBOHYD 434 434 N-linked (GlcNAc...) (Potential). FT CONFLICT 79 79 A -> G (in Ref. 2). FT CONFLICT 168 168 T -> N (in Ref. 2). FT CONFLICT 254 254 L -> F (in Ref. 2). SQ SEQUENCE 534 AA; 57195 MW; 3DE671BC4F40918B CRC64; MAVVYYLLLA GLIACSHALA AGTPALGDDR GRPWPASLAA LALDGKLRTD SNATAAASTD FGNITSALPA AVLYPSSTAD LVALLSAANS TPGWPYTIAF RGRGHSLMGQ AFAPGGVVVN MASLGDAAAP PRINVSADGR YVDAGGEQVW IDVLRASLAR GVAPRSWTDY LYLTVGGTLS NAGISGQAFR HGPQISNVLE MDVITGHGEM VTCSKQLNAD LFDAVLGGLG QFGVITRARI AVEPAPARAR WVRLVYTDFA AFSADQERLT APRPGGGGAS FGPMSYVEGS VFVNQSLATD LANTGFFTDA DVARIVALAG ERNATTVYSI EATLNYDNAT AAAAAVDQEL ASVLGTLSYV EGFAFQRDVA YAAFLDRVHG EEVALNKLGL WRVPHPWLNM FVPRSRIADF DRGVFKGILQ GTDIVGPLIV YPLNKSMWDD GMSAATPSED VFYAVSLLFS SVAPNDLARL QEQNRRILRF CDLAGIQYKT YLARHTDRSD WVRHFGAAKW NRFVEMKNKY DPKRLLSPGQ DIFN // ID CLPP_MAIZE STANDARD; PRT; 216 AA. AC P26567; DT 01-AUG-1992 (Rel. 23, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) DE (Endopeptidase Clp). GN CLPP. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [2] RP SEQUENCE OF 186-216 FROM N.A. RC STRAIN=cv. FR9cms X FR37; TISSUE=Leaf; RX MEDLINE=92119264; PubMed=1732000; RA Wegloehner W., Subramanian A.R.; RT "Nucleotide sequence of a region of maize chloroplast DNA containing RT the 3' end of clpP, exon 1 of rps12 and rpl20 and their RT cotranscription."; RL Plant Mol. Biol. 18:415-418(1992). RN [3] RP SEQUENCE OF 189-216 FROM N.A. RC STRAIN=cv. FR9cms X FR37; TISSUE=Leaf; RX MEDLINE=88033114; PubMed=2822717; RA Giese K., Subramanian A.R., Larrinua I.M., Bogorad L.; RT "Nucleotide sequence, promoter analysis, and linkage mapping of the RT unusually organized operon encoding ribosomal proteins S7 and S12 in RT maize chloroplast."; RL J. Biol. Chem. 262:15251-15255(1987). CC -!- FUNCTION: Cleaves peptides in various proteins in a process that CC requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a CC major role in the degradation of misfolded proteins (By CC similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in CC the presence of ATP and magnesium. Alpha-casein is the usual test CC substrate. In the absence of ATP, only oligopeptides shorter than CC five residues are cleaved (such as succinyl-Leu-Tyr-|-NHMEC; and CC Leu-Tyr-Leu-|-Tyr-Trp, in which the cleavage of the -Tyr-|-Leu- CC and -Tyr-|-Trp- bond also occurs). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to peptidase family S14. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60310.1; -. DR EMBL; X60548; CAA43038.1; -. DR EMBL; M17842; AAA85358.1; -. DR PIR; S58576; S58576. DR HSSP; P19245; 1TYF. DR MEROPS; S14.002; -. DR Gramene; P26567; -. DR MaizeDB; 67210; -. DR HAMAP; MF_00444; -; 1. DR InterPro; IPR001907; Pept_S14_ClpP. DR Pfam; PF00574; CLP_protease; 1. DR PRINTS; PR00127; CLPPROTEASEP. DR TIGRFAMs; TIGR00493; clpP; 1. DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1. DR PROSITE; PS00381; CLP_PROTEASE_SER; 1. KW Hydrolase; Serine protease; Chloroplast. FT ACT_SITE 101 101 By similarity. FT ACT_SITE 126 126 By similarity. SQ SEQUENCE 216 AA; 24758 MW; F85B11C5A4D48159 CRC64; MPIGVPKVPY RIPGDEEATW VDLYNVMYRE RTLFLGQEIR CEITNHITGL MVYLSIEDGN SDIFLFINSL GGWLISGMAI FDTMQTVTPD IYTICLGIAA SMASFILLGG EPTKRIAFPH ARIMLHQPAS AYYRARTPEF LLEVEELHKV REMITRVYAL RTGKPFWVVS EDMERDVFMS ADEAKAYGLV DIVGDEMIDE HCDTDPVWFP EMFKDW // ID COMT_MAIZE STANDARD; PRT; 364 AA. AC Q06509; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Caffeic acid 3-O-methyltransferase (EC 2.1.1.68) (S-adenosysl-L- DE methionine:caffeic acid 3-O-methyltransferase) (COMT) (CAOMT). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93099238; PubMed=1463825; RA Collazo P., Montoliu L., Puigdomenech P., Rigau J.; RT "Structure and expression of the lignin O-methyltransferase gene from RT Zea mays L."; RL Plant Mol. Biol. 20:857-867(1992). CC -!- FUNCTION: Catalyzes the conversion of caffeic acid to ferulic acid CC and of 5-hydroxyferulic acid to sinapic acid. The resulting CC products may subsequently be converted to the corresponding CC alcohols that are incorporated into lignins. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 3,4-dihydroxy-trans- CC cinnamate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans- CC cinnamate. CC -!- PATHWAY: Lignin biosynthesis. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Family CC 2. COMT subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M73235; AAB03364.1; -. DR PIR; S28612; S28612. DR MaizeDB; 26027; -. DR InterPro; IPR001601; Methyltransf. DR InterPro; IPR001077; O_Met_trans2. DR InterPro; IPR000051; SAM_bind. DR Pfam; PF00891; Methyltransf_2; 1. KW Lignin biosynthesis; Transferase; Methyltransferase. SQ SEQUENCE 364 AA; 39567 MW; 089E8A6A4DDAF56A CRC64; MGSTAGDVAA VVDEEACMYA MQLASSSILP MTLKNAIELG LLEVLQKEAG GGKAALAPEE VVARMPAAPS DPAAAAAMVD RMLRLLASYD VVRCQMEDRD GRYERRYSAA PVCKWLTPNE DGVSMAALAL MNQDKVLMES WYYLKDAVLD GGIPFNKAYG MTAFEYHGTD ARFNRVFNEG MKNHSVIITK KLLDFYTGFE GVSTLVDVGG GVGATLHAIT SRHPHISGVN FDLPHVISEA PPFPGVRHVG GDMFASVPAG DAILMKWILH DWSDAHCATL LKNCYDALPE NGKVIVVECV LPVNTEATPK AQGVFHVDMI MLAHNPGGKE RYEREFRELA KGAGFSGFKA TYIYANAWAI EFIK // ID COX1_MAIZE STANDARD; PRT; 528 AA. AC P08742; DT 01-AUG-1988 (Rel. 08, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome c oxidase polypeptide I (EC 1.9.3.1). GN COX1 OR COXI. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Isaac P.G., Jones V.P., Leaver C.J.; RT "The maize cytochrome c oxidase subunit I gene: sequence, expression RT and rearrangement in cytoplasmic male sterile plants."; RL EMBO J. 4:1617-1623(1985). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits CC 1-3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) = 4 ferricytochrome CC c + 2 H(2)O. CC -!- PATHWAY: Respiratory chain; terminal step. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Mitochondrial CC inner membrane. Contains 12 potential transmembrane domains. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02660; CAA26496.1; -. DR PIR; A22840; ODZM1. DR HSSP; P98002; 1AR1. DR MaizeDB; 69214; -. DR InterPro; IPR000883; COX1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR PROSITE; PS00077; COX1; 1. KW Oxidoreductase; Heme; Copper; Mitochondrion; Transmembrane; KW Respiratory chain; Inner membrane. FT METAL 64 64 Iron (heme A axial ligand) (Probable). FT METAL 243 243 Copper B (Probable). FT METAL 247 247 Copper B (Probable). FT METAL 292 292 Copper B (Probable). FT METAL 293 293 Copper B (Probable). FT METAL 378 378 Iron (heme A3 axial ligand) (Probable). FT METAL 380 380 Iron (heme A axial ligand) (Probable). FT CROSSLNK 243 247 1'-histidyl-3'-tyrosine (His-Tyr) FT (By similarity). SQ SEQUENCE 528 AA; 58257 MW; 75FB95E5568E89E7 CRC64; MTNLVRWLFS TNHKDIGTLY FIFGAIAGVM GTCFSVLIRM ELARPGDQIL GGNHQLYNVL ITAHAFLMIF FMVMPAMIGG FGNWFVPILI GAPDMAFPRL NNISFWLLPP SLLLLLSSAL VEVGSGTGWT VYPPLSGITS HSGGAVDLAI FSLHLSGVSS ILGSINFITT IFNMRGPGMT MHRLPLFVWS VLVTAFLLLL SLPVLAGAIT MLLTDRNFNT TFFDPAGGGD PILYQHLFWF FGHPEVYILI LPGFGIISHI VSTFSRKPVF GYLGMVYAMI SIGVLGFLVW AHHMFTVGLD VDTRAYFTAA TMIIAVPTGI KIFSWIATMW GGSIQYKTPM LFAVGFIFLF TIGGLTGIVL ANSGLDIALH DTYYVVAHFH YVLSMGAVFA LFAGFYYWVG KIFGRTYPET LGQIHFWITF FGVNLTFFPM HFLGLSGMPR RIPDYPDAYA GWNALSSFGS YISVVGIRRF FVVVAITSSS GKNKRCAESP WAVEQNPTTL EWLVQSPPAF HTFGELPTIK ETRNQSSC // ID COX2_MAIZE STANDARD; PRT; 260 AA. AC P00412; DT 21-JUL-1986 (Rel. 01, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Cytochrome c oxidase polypeptide II (EC 1.9.3.1). GN COX2 OR COXII OR MOX1. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=82115309; PubMed=6276012; RA Fox T.D., Leaver C.J.; RT "The Zea mays mitochondrial gene coding cytochrome oxidase subunit II RT has an intervening sequence and does not contain TGA codons."; RL Cell 26:315-323(1981). RN [2] RP SEQUENCE FROM N.A., AND RNA EDITING. RX MEDLINE=91304421; PubMed=1712908; RA Yang A.J., Mulligan R.M.; RT "RNA editing intermediates of cox2 transcripts in maize RT mitochondria."; RL Mol. Cell. Biol. 11:4278-4281(1991). RN [3] RP SEQUENCE OF 1-248 FROM N.A., AND RNA EDITING. RC STRAIN=cv. Golden Bantam early; TISSUE=Leaf; RX MEDLINE=90384819; PubMed=1698279; RA Covello P.S., Gray M.W.; RT "Differences in editing at homologous sites in messenger RNAs from RT angiosperm mitochondria."; RL Nucleic Acids Res. 18:5189-5195(1990). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits CC 1-3 form the functional core of the enzyme complex. Subunit 2 CC transfers the electrons from cytochrome c via its binuclear copper CC A center to the bimetallic center of the catalytic subunit 1. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) = 4 ferricytochrome CC c + 2 H(2)O. CC -!- COFACTOR: Copper A. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Mitochondrial CC inner membrane. CC -!- RNA EDITING: Modified_positions=5, 11, 26, 56, 57, 87, 95, 129, CC 130, 150, 156, 161, 184, 188, 196, 207, 213, 235. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V00712; CAA24094.1; ALT_SEQ. DR EMBL; X52865; CAA37046.1; ALT_SEQ. DR PIR; B41260; OBZM2. DR MaizeDB; 69218; -. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR002429; Cyt_c_ox_2. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR PRINTS; PR01166; CYCOXIDASEII. DR ProDom; PD000131; Copper_CuA; 1. DR PROSITE; PS00078; COX2; 1. KW Oxidoreductase; Copper; Mitochondrion; Transmembrane; Inner membrane; KW Electron transport; Respiratory chain; RNA editing. FT DOMAIN 1 43 Mitochondrial intermembrane (Potential). FT TRANSMEM 44 64 Potential. FT DOMAIN 65 84 Mitochondrial matrix (Potential). FT TRANSMEM 85 105 Potential. FT DOMAIN 106 260 Mitochondrial intermembrane (Potential). FT METAL 189 189 Copper A (Probable). FT METAL 224 224 Copper A (Probable). FT METAL 228 228 Copper A (Probable). FT METAL 232 232 Copper A (Probable). SQ SEQUENCE 260 AA; 29679 MW; 2F90F35CFB1A702F CRC64; MILRLLECRF FTIALCDAAE PWQLGFQDAA TPMMQGIIDL HHDIFFFLIL ILVFVLWMLV RALWHFNEQT NPIPQRIVHG TTIEIIWTIF PSVILLFIAI PSFALLYSMD GVLVDPAITI KAIGHQWYWT YEYSDYNSSD EQSLTFDSYM IPEDDLELGQ LRLLEVDNRV VVPAKTHLRM IVTSADVLHS WAVPSLGVKC DAVPGRLNLT SILVQREGVY YGQCSEICGT NHAFMPIVVE AVTLKDYADW VSNQLILQTN // ID COX3_MAIZE STANDARD; PRT; 265 AA. AC P09138; DT 01-MAR-1989 (Rel. 10, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Cytochrome c oxidase polypeptide III (EC 1.9.3.1). GN COX3. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89041588; PubMed=2847119; RA McCarty D.M., Hehman G.L., Hauswirth W.W.; RT "Nucleotide sequence of the Zea mays mitochondrial cytochrome oxidase RT subunit III gene."; RL Nucleic Acids Res. 16:9873-9873(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. B37N; RA Kaleikau E.K., Walbot V.; RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Subunits I, II and III form the functional core of CC the enzyme complex. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) = 4 ferricytochrome CC c + 2 H(2)O. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X12728; CAA31221.1; -. DR EMBL; X53055; CAA37222.1; -. DR MaizeDB; 69221; -. DR InterPro; IPR000298; CytC_oxdse_III. DR Pfam; PF00510; COX3; 1. DR ProDom; PD000382; CytC_oxdse_III; 1. DR PROSITE; PS50253; COX3; 1. KW Oxidoreductase; Mitochondrion; Transmembrane. SQ SEQUENCE 265 AA; 29328 MW; B10D10921745180C CRC64; MIESQRHSYH LVDPSPWPIS GSLGALATTV GGVMYMHSFQ GGATLLSLGL IFLLYTMFVW WRDVLRESTL EGHHTKAVQL GPRYGSILFI VSEVMSFFLF FWASSHSSLA PTVEIGGIWP PKGIGVLDPW EIPLLNTPIL PSSGAAVTWA HHAILAGKEK RAVYALVATV LLALVSTGFQ GMEYYQAPST ISDSIYGSTF LLATGFHGFH VIIGTLFLIV CGIRQYLGHL TKKHHVGFEA AAWYWHFVDV VRLFPFVSIY WWGGT // ID CP78_MAIZE STANDARD; PRT; 547 AA. AC P48420; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Cytochrome P450 78A1 (EC 1.14.-.-) (CYPLXXVIII). GN CYP78A1 OR CYP78. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Flower; RX MEDLINE=94325460; PubMed=8049361; RA Larkin J.C.; RT "Isolation of a cytochrome P450 homologue preferentially expressed in RT developing inflorescences of Zea mays."; RL Plant Mol. Biol. 25:343-353(1994). CC -!- TISSUE SPECIFICITY: Shoot apex. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L23209; AAA61607.1; -. DR PIR; S51475; S51475. DR MaizeDB; 51340; -. DR InterPro; IPR001128; Cytochrome_P450. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Oxidoreductase; Monooxygenase; Heme. FT METAL 490 490 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 547 AA; 58399 MW; 1DF9AF44739B7328 CRC64; MAMASAACSC TDGTWWVYAL PALLGSDTLC AHPALLAGLI FLATVSVALL AWATSPGGPA WTNGRGASAS LLSWDPVVCP CSAASSRCPG AAAPRPRRDG PRRRPRAKEL MAFSVGDTPA VVSSCPATAR EVLAHPSFAD RPVKRSAREL MFARAIGFAP NGEYWRRLRR VASTHLFSPR RVASHEPGRQ GDAEAMLRSI AAEQSASGAV ALRPHLQAAA LNNIMGSVFG TRYDVTSGAG AAEAEHLKSM VREGFELLGA FNWSDHLPWL AHLYDPSNVT RRCAALVPRV QTFVRGVIDE HRRRRQNSAA LNDNADFVDV LLSLEGDEKL GDDDMVAILW EMVFRGTDTT ALLTEWCMAE LVRHPAVQAR VRAEVDAAVG AGGCPTDADV ARMPYLQAVV KETLRAHPPG PLLSWARLAT ADVPLCNGMV VPAGTTAMVN MWAITHDAAV WADPDAFAPE RFLPSEGGAD VDVRGVDLRL APFGAGRRVC PGKNLGLTTV GLWVARLVHA FQWALPDGAA AVCLDEVLKL SLEMKTPLVA AAIPRTA // ID CPTR_MAIZE STANDARD; PRT; 409 AA. AC P49133; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Triose phosphate/phosphate translocator, chloroplast precursor (CTPT). GN CPT. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 305-316. RC TISSUE=Leaf; RX MEDLINE=94198894; PubMed=8148878; RA Fischer K., Arbinger B., Kammerer B., Busch C., Brink S., RA Wallmeier H., Sauer N., Eckerskorn C., Fluegge U.-I.; RT "Cloning and in vivo expression of functional triose RT phosphate/phosphate translocators from C3- and C4-plants: evidence RT for the putative participation of specific amino acid residues in the RT recognition of phosphoenolpyruvate."; RL Plant J. 5:215-226(1994). CC -!- FUNCTION: Mediates the export of fixed carbons from the CC chloroplasts into the cytosol in the form of triose phosphates. In CC addition, it can also bind and transport phosphoenolpyruvate, CC thereby increasing the photosynthetic efficiency of C4-plants. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Located in zones CC of contact between the inner and outer membrane of the CC chloroplast. CC -!- SIMILARITY: Strong, to other plants CTPT. Also similar to CC yeast protein SLY41. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z26595; CAA81349.1; -. DR PIR; S37497; S37497. DR MaizeDB; 86189; -. DR InterPro; IPR004696; Tpt_PEP_transl. DR TIGRFAMs; TIGR00817; tpt; 1. KW Transmembrane; Chloroplast; Transit peptide; Transport. FT TRANSIT 1 85 Chloroplast (Potential). FT CHAIN 86 409 Triose phosphate/phosphate translocator. FT DOMAIN 86 104 Intermembrane space (Potential). FT TRANSMEM 105 125 Potential. FT DOMAIN 126 137 Lumenal (Potential). FT TRANSMEM 138 158 Potential. FT DOMAIN 159 215 Intermembrane space (Potential). FT TRANSMEM 216 236 Potential. FT DOMAIN 237 280 Lumenal (Potential). FT TRANSMEM 281 300 Potential. FT DOMAIN 301 378 Intermembrane space (Potential). FT TRANSMEM 379 399 Potential. FT DOMAIN 400 409 Lumenal (Potential). FT SITE 225 225 MAY BE ESSENTIAL FOR BINDING AND FT TRANSPORT OF PHOSPHOENOLPYRUVATE. SQ SEQUENCE 409 AA; 44090 MW; 8C33700CCDB3D326 CRC64; MSALGTLSGG AAGVSGLLRL RRRAAPAPAI AAPSHLPAGT VKCAAAVPDA APIVWGRQLR PALLLPAALL PSLQPARRHT LQPPAAAAES AGEAKSVGFL EKYPALVTGF FFFMWYFLNV IFNILNKKIY NYFPYPYFVS LIHLVVGVVY CLISWSVGLP KRAPINGTLL KLLFPVALCH GIGHITSNVS FAAVAVSFAH TIKALEPFFS AAATQFILGQ QVPFSLWLSL APVVIGVSMA SLTELSFNWT GFINAMISNI SFTYRSIYSK KAMTDMDSTN VYAYISIIAL IVCIPPALIF EGPKLMQHGF SDAIAKVGLT KFVSDLFLVG LFYHLYNQIA TNTLERVAPL THAVGNVLKR VFVIGFSIIV FGNKISTQTG IGTSIAIAGV AMYSYIKAKI EEEKRKKSA // ID CRI4_MAIZE STANDARD; PRT; 901 AA. AC O24585; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Putative receptor protein kinase CRINKLY4 precursor (EC 2.7.1.-). GN CR4. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RX MEDLINE=96355669; PubMed=8703079; RA Becraft P.W., Stinard P.S., McCarty D.R.; RT "CRINKLY4: a TNFR-like receptor kinase involved in maize epidermal RT differentiation."; RL Science 273:1406-1409(1996). CC -!- FUNCTION: Putative receptor protein kinase. Could play a role in a CC differentiation signal. The CRINKLY4 (CR4) mutation affects leaf CC epidermis differentiation such that cell size and morphology are CC altered, and surface functions are compromised, allowing graft- CC like fusions between organs. CC -!- SUBCELLULAR LOCATION: Type I membrane protein. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. CC -!- SIMILARITY: Contains 1 TNFR-Cys repeat. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U67422; AAB09771.1; -. DR PIR; T04108; T04108. DR MaizeDB; 128723; -. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR001368; TNFR_c6. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00020; TNFR_c6; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00208; TNFR; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00652; TNFR_NGFR_1; FALSE_NEG. DR PROSITE; PS50050; TNFR_NGFR_2; 1. KW Receptor; Transferase; Serine/threonine-protein kinase; ATP-binding; KW Repeat; Transmembrane; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 901 Putative receptor protein kinase FT CRINKLY4. FT DOMAIN 25 423 Extracellular (Potential). FT TRANSMEM 424 444 Potential. FT DOMAIN 445 901 Cytoplasmic (Potential). FT DOMAIN 33 330 7 x 36 AA repeats. FT REPEAT 33 68 1. FT REPEAT 72 107 2. FT REPEAT 125 160 3. FT REPEAT 162 195 4. FT REPEAT 203 236 5. FT REPEAT 253 287 6. FT REPEAT 292 330 7. FT REPEAT 357 391 TNFR-Cys. FT DOMAIN 505 712 Protein kinase. FT NP_BIND 511 519 ATP (By similarity). FT BINDING 533 533 ATP (By similarity). FT ACT_SITE 634 634 Proton acceptor (By similarity). SQ SEQUENCE 901 AA; 97439 MW; 52F8481AC187E061 CRC64; MDHVPALVLA GCCFLALLPG WACGLGSMSS IAVSYGEDGP VFCGLNSDGS HLVACFGADA SVLYGAPPNI PFLGLTAGDG FVCGLLLDTR QPYCWGSNSY VKSGVPQPMV EGARYSELSA GDNHLCALRA AQDGGRGSSA ATSLIDCWGY NMTATHAVDE AVSTVSAGSV FNCGLFARNR TVFCWGDETV SGVVGLAPRD LHFQSIGAGG YHVCGVLENA QVFCWGRSLE MQQVVPSSAI GDGDVNIVPM DAMSTVVGGR FHACGIRSLD HQVACWGFTL HNSTSPPKGL KMYALVAGDY FTCGVPAETS LMPRCWGNSG PLALPMAVPP GICVPTACSH GYYEYVNHGE VGSIKVCKPA NSRLCLPCST GCPEGLYESS PCNATADRVC QFDCLKCVTD ECLSFCLSQK RTKSRKLMAF QMRIFVAEIV FAVVLVLSVS VTTCLYVRHK LRHCQCSNRE LRLAKSTAYS FRKDNMKIQP DMEDLKIRRA QEFSYEELEQ ATGGFSEDSQ VGKGSFSCVF KGILRDGTVV AVKRAIKASD VKKSSKEFHN ELDLLSRLNH AHLLNLLGYC EDGSERLLVY EFMAHGSLYQ HLHGKDPNLK KRLNWARRVT IAVQAARGIE YLHGYACPPV IHRDIKSSNI LIDEDHNARV ADFGLSILGP ADSGTPLSEL PAGTLGYLDP EYYRLHYLTT KSDVYSFGVV LLEILSGRKA IDMQFEEGNI VEWAVPLIKA GDIFAILDPV LSPPSDLEAL KKIASVACKC VRMRGKDRPS MDKVTTALEH ALALLMGSPC IEQPILPTEV VLGSSRMHKV SQMSSNHSCS ENELADGEDQ GIGYRAPSWI TFPSVTSSQR RKSSASEADI VGRRATDGRN VGSSIGDGLR SLEEEIAPAS PQENLYLQHN F // ID CRTI_MAIZE STANDARD; PRT; 571 AA. AC P49086; Q41849; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Phytoene dehydrogenase, chloroplast precursor (EC 1.14.99.-) DE (Phytoene desaturase). GN PDS1 OR PDS. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96178866; PubMed=8616251; RA Li Z., Matthews P.D., Burr B., Wurtzel E.T.; RT "Cloning and characterization of a maize cDNA encoding phytoene RT desaturase, an enzyme of the carotenoid biosynthetic pathway."; RL Plant Mol. Biol. 30:269-279(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. Funkf; TISSUE=Leaf; RX MEDLINE=95357435; PubMed=7630964; RA Hable W.E., Oishi K.K.; RT "Maize phytoene desaturase maps near the viviparous5 locus."; RL Plant Physiol. 108:1329-1330(1995). CC -!- FUNCTION: This enzyme converts phytoene into zeta-carotene via the CC intermediary of phytofluene by the symmetrical introduction of two CC double bonds at the C-11 and C-11' positions of phytoene. CC -!- COFACTOR: NAD, NADP, or FAD (Probable). CC -!- PATHWAY: Carotenoid biosynthesis. CC -!- SUBCELLULAR LOCATION: Chloroplast; chromoplast. CC -!- SIMILARITY: Belongs to the phytoene dehydrogenase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U37285; AAC12846.1; -. DR EMBL; L39266; AAA99519.1; -. DR PIR; S65060; S65060. DR MaizeDB; 84977; -. DR InterPro; IPR001613; Amineoxid_fl. DR InterPro; IPR002937; Amino_oxidase. DR InterPro; IPR000205; NAD_BS. DR Pfam; PF01593; Amino_oxidase; 1. DR PRINTS; PR00757; AMINEOXDASEF. KW Carotenoid biosynthesis; Oxidoreductase; NAD; Flavoprotein; FAD; KW Chloroplast; Transit peptide. FT TRANSIT 1 96 Chloroplast (Potential). FT CHAIN 97 571 Phytoene dehydrogenase. FT CONFLICT 61 63 VVC -> LSA (in Ref. 2). FT CONFLICT 68 68 R -> S (in Ref. 2). FT CONFLICT 555 555 A -> T (in Ref. 2). SQ SEQUENCE 571 AA; 64115 MW; FAE119C7EFBE799A CRC64; MDTGCLSSMN ITGASQTRSF AGQLPPQRCF ASSHYTSFAV KKLVSRNKGR RSHRRHPALQ VVCKDFPRPP LESTINYLEA GQLSSFFRNS ERPSKPLQVV VAGAGLAGLS TAKYLADAGH KPILLEARDV LGGKVAAWKD EDGDWYETGL HIFFGAYPNI QNLFGELRIE DRLQWKEHSM IFAMPNKPGE FSRFDFPETL PAPINGIWAI LRNNEMLTWP EKVKFAIGLL PAMVGGQPYV EAQDGLTVSE WMKKQGVPDR VNDEVFIAMS KALNFINPDE LSMQCILIAL NRFLQEKHGS KMAFLDGNPP ERLCMPIVDH IRSRGGEVRL NSRIKKIELN PDGTVKHFAL SDGTQITGDA YVCATPVDIF KLLVPQEWSE ITYFKKLEKL VGVPVINVHI WFDRKLNNTY DHLLFSRSSL LSVYADMSVT CKEYYDPNRS MLELVFAPAD EWIGRSDTEI IDATMEELAK LFPDEIAADQ SKAKILKYHI VKTPRSVYKT VPNCEPCRPL QRSPIEGFYL AGDYTKQKYL ASMEGAVLSG KLCAQSIVQD YSRLALRSQK SLQSGEVPVP S // ID CYB6_MAIZE STANDARD; PRT; 215 AA. AC P05642; Q33298; Q36712; DT 01-NOV-1988 (Rel. 09, Created) DT 29-MAR-2004 (Rel. 43, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Cytochrome b6. GN PETB. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2). RX MEDLINE=88210525; PubMed=2835175; RA Rock C.D., Barkan A., Taylor W.C.; RT "The maize plastid psbB-psbF-petB-petD gene cluster: spliced and RT unspliced petB and petD RNAs encode alternative products."; RL Curr. Genet. 12:69-77(1987). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 1), AND RNA EDITING. RC TISSUE=Seedling; RX MEDLINE=94073219; PubMed=8252066; RA Freyer R., Hoch B., Neckermann K., Maier R.M., Koessel H.; RT "RNA editing in maize chloroplasts is a processing step independent of RT splicing and cleavage to monocistronic mRNAs."; RL Plant J. 4:621-629(1993). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Component of the cytochrome b6/f complex which is part CC of the photosynthetic respiratory chain. CC -!- COFACTOR: Binds two heme groups non-covalently. Heme 1 (or BL or CC b562) is low-potential and absorbs at about 562 nm, and heme 2 (or CC BH or b566) is high-potential and absorbs at about 566 nm. CC -!- SUBUNIT: The main subunits of complex b6-f are: cytochrome b6, 17 CC kDa polypeptide (petD), cytochrome f and the Rieske protein. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast CC thylakoid membrane (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P05642-1; Sequence=Displayed; CC Name=2; CC IsoId=P05642-2; Sequence=VSP_007116; CC Note=Unspliced isoform; CC -!- RNA EDITING: Modified_positions=204; Note=Editing is independent CC of both splicing and processing of the primary transcript. CC -!- SIMILARITY: Belongs to the cytochrome b family. PetB subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05422; CAA28999.1; ALT_SEQ. DR EMBL; X05422; CAA29000.1; ALT_SEQ. DR EMBL; S67283; AAB29194.1; -. DR EMBL; S67282; AAB29194.1; JOINED. DR EMBL; X86563; CAA60315.1; ALT_SEQ. DR PIR; S08592; CBZM6R. DR Gramene; P05642; -. DR Gramene; Q33298; -. DR Gramene; Q36712; -. DR MaizeDB; 56334; -. DR HAMAP; MF_00633; -; 1. DR InterPro; IPR005797; Cytb_b6_N. DR Pfam; PF00033; cytochrome_b_N; 1. DR PROSITE; PS00192; CYTOCHROME_B_HEME; 1. KW Transport; Electron transport; Photosynthesis; Chloroplast; Thylakoid; KW Heme; Metal-binding; Iron; Transmembrane; Alternative splicing; KW RNA editing. FT TRANSMEM 32 52 Potential. FT TRANSMEM 90 110 Potential. FT TRANSMEM 116 136 Potential. FT TRANSMEM 186 206 Potential. FT METAL 86 86 Iron (heme 1 axial ligand) (By FT similarity). FT METAL 100 100 Iron (heme 2 axial ligand) (By FT similarity). FT METAL 187 187 Iron (heme 1 axial ligand) (By FT similarity). FT METAL 202 202 Iron (heme 2 axial ligand) (By FT similarity). FT VARSPLIC 1 2 MS -> MKFSYTVLGGGVGLVTYLN (in isoform 2). FT /FTId=VSP_007116. SQ SEQUENCE 215 AA; 24196 MW; C2E389FA11B51F6A CRC64; MSKVYDWFEE RLEIQAIADD ITSKYVPPHV NIFYCLGGIT LTCFLVQVAT GFAMTFYYRP TVTEAFSSVQ YIMTEANFGW LIRSVHRWSA SMMVLMMILH VFRVYLTGGF KKPRELTWVT GVVLAVLTAS FGVTGYSLPW DQIGYWAVKI VTGVPEAIPV IGSPLVELLR GSASVGQSTL TRFYSLHTFV LPLLTAVFML MHFLMIRKQG ISGPL // ID CYB_MAIZE STANDARD; PRT; 388 AA. AC P04165; DT 20-MAR-1987 (Rel. 04, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome b. GN MTCYB OR COB OR CYTB. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Dawson A.J., Jones V.P., Leaver C.J.; RT "The apocytochrome b gene in maize mitochondria does not contain RT introns and is preceded by a potential ribosome binding site."; RL EMBO J. 3:2107-2113(1984). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase CC complex (complex III or cytochrome b-c1 complex), which is a CC respiratory chain that generates an electrochemical potential CC coupled to ATP synthesis (By similarity). CC -!- COFACTOR: Binds two heme groups non-covalently. Heme 1 (or BL or CC b562) is low-potential and absorbs at about 562, and heme 2 (or BH CC or b566) is high-potential and absorbs at about 566 (By CC similarity). CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b, CC cytochrome c1 and the Rieske protein (By similarity). CC -!- SIMILARITY: Belongs to the cytochrome b family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X00789; CAA25367.1; -. DR PIR; A00156; CBZM. DR MaizeDB; 69227; -. DR InterPro; IPR005798; Cytb_b6_C. DR InterPro; IPR005797; Cytb_b6_N. DR Pfam; PF00032; cytochrome_b_C; 1. DR Pfam; PF00033; cytochrome_b_N; 1. DR PROSITE; PS00192; CYTOCHROME_B_HEME; 1. DR PROSITE; PS00193; CYTOCHROME_B_QO; 1. KW Electron transport; Mitochondrion; Respiratory chain; Transmembrane; KW Heme. FT METAL 88 88 Iron 1 (heme b562 axial ligand). FT METAL 102 102 Iron 2 (heme b566 axial ligand). FT METAL 189 189 Iron 1 (heme b562 axial ligand). FT METAL 203 203 Iron 2 (heme b566 axial ligand). SQ SEQUENCE 388 AA; 43567 MW; 56CF734C2B62B3F6 CRC64; MTIRNQRFSL LKQPIYSTLN QHLIDYPTPS NLSYWWGFGC LAGICLVIQI VTGVFLAMHY TPHVDLAFNS VEHIMRDVEG GWLLRYMHAN GASMFLIVVH LHIFRGLYHA SYSSPREFVW CLGVVIFLLM IVTAFIGYVP PWGQMSFWGA TVITSLASAI PVVGDTIVTW LWGGFSVDNA TLNRFFSLHH LLPLILAGAS LLHLAALHQY GSNNPLGVHS EMDKIASYPY FYVKDLVGRV ASAIFFSIWI FFAPNVLGHP DNYIPANPMP TPPHIVPEWY FLPIHAILRS IPDKAGGVAA IAPVFISLLA LPFFKEMYVR SSSFRPIHQG IFWLLLADCL LLGWIGCQPV EAPFVTIGQI SSFFFFLFFA ITPIPGRVGR GIPKYYTE // ID CYC_MAIZE STANDARD; PRT; 111 AA. AC P00056; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome c. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RA Boulter D.; RL Unpublished results, cited by: RL (In) Fasman G.D. (eds.); RL Handbook of biochemistry and molecular biology (3rd ed.), RL pp.3:284-285, CRC Press, Cleveland (1976). CC -!- FUNCTION: Electron carrier protein. The oxidized form of the CC cytochrome c heme group can accept an electron from the heme group CC of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c CC then transfers this electron to the cytochrome oxidase complex, CC the final protein carrier in the mitochondrial electron-transport CC chain. CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix. CC -!- PTM: Binds 1 heme group per subunit. CC -!- SIMILARITY: Belongs to the cytochrome c family. DR HSSP; P00055; 1CCR. DR MaizeDB; 69233; -. DR InterPro; IPR003088; Cyt_CI. DR InterPro; IPR002327; Cyt_CIAB. DR InterPro; IPR000345; CytC_heme_BS. DR Pfam; PF00034; cytochrome_c; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR ProDom; PD000375; Cyt_CIAB; 1. DR PROSITE; PS00190; CYTOCHROME_C; 1. KW Mitochondrion; Electron transport; Respiratory chain; Heme. FT BINDING 22 22 Heme (covalent). FT BINDING 25 25 Heme (covalent). FT METAL 26 26 Iron (heme axial ligand). FT METAL 88 88 Iron (heme axial ligand). SQ SEQUENCE 111 AA; 12013 MW; FA3E96C269A1B03E CRC64; ASFSEAPPGN PKAGEKIFKT KCAQCHTVEK GAGHKQGPNL NGLFGRQSGT TAGYSYSAAN KNKAVVWEEN TLYDYLLNPX KYIPGTKMVF PGLXKPQERA DLIAYLKEAT A // ID CYF_MAIZE STANDARD; PRT; 320 AA. AC P46617; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Apocytochrome f precursor. GN PETA. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Translocates protons across the thylakoid membrane and CC transfers electrons from photosystem II to photosystem I. It CC receives electrons from the Rieske iron-sulfur protein and passes CC them to plastocyanin. CC -!- SUBUNIT: Interacts with plastocyanin and Rieske iron-sulfur CC protein (By similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. Membrane- CC anchored (By similarity). CC -!- SIMILARITY: Belongs to the cytochrome c family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60298.1; -. DR PIR; S58564; S58564. DR HSSP; P36438; 1HCZ. DR Gramene; P46617; -. DR MaizeDB; 56850; -. DR HAMAP; MF_00610; -; 1. DR InterPro; IPR002325; Apocyt_F. DR InterPro; IPR000345; CytC_heme_BS. DR Pfam; PF01333; Apocytochr_F_C; 1. DR PRINTS; PR00610; CYTOCHROMEF. DR PROSITE; PS00190; CYTOCHROME_C; 1. KW Electron transport; Heme; Chloroplast; Thylakoid; Photosynthesis; KW Photosystem I; Photosystem II; Transmembrane; Signal. FT SIGNAL 1 35 By similarity. FT CHAIN 36 320 Apocytochrome f. FT TRANSMEM 286 305 Potential. FT METAL 36 36 Iron (heme axial ligand) (via amino FT nitrogen) (By similarity). FT BINDING 56 56 Heme (covalent) (By similarity). FT BINDING 59 59 Heme (covalent) (By similarity). FT METAL 60 60 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 320 AA; 35511 MW; 693CA60F2326341E CRC64; MENRKTFSWL KEQMIRSISV SIMIYVITRT SISNAYPIFA QQGYENPREA TGRIVCANCH LANKPVDIEV PQAVLPDTVF EAVLRIPYDM QLKQVLANGK KGGLNVGAVL ILPEGFELAP PDRISPELKE KIGNLSFQSY RPNKKNILVI GPVPGKKYSE IVFPILSPDP ATKKDVHFLK YPIYVGGNRG RGQIYPDGSK SNNTVYNATS TGIVKKILRK EKGGYEISIV DASDGRQVID IIPPGPELLF SEGESIKLDQ PLTSNPNVGG FGQGDAEIVL QDPLRVQGLL FFFASVILAQ VFLVLKKKQF EKVQLYEMNF // ID CYPH_MAIZE STANDARD; PRT; 172 AA. AC P21569; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) (PPIase) (Rotamase) DE (Cyclophilin) (Cyclosporin A-binding protein). GN CYP OR ROT1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91088549; PubMed=1702215; RA Gasser C.S., Gunning D.A., Budelier K.A., Brown S.M.; RT "Structure and expression of cytosolic cyclophilin/peptidyl-prolyl RT cis-trans isomerase of higher plants and production of active tomato RT cyclophilin in Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 87:9519-9523(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95272532; PubMed=7753032; RA Marivet J., Frendo P., Burkard G.; RT "DNA sequence analysis of a cyclophilin gene from maize: RT developmental expression and regulation by salicylic acid."; RL Mol. Gen. Genet. 247:222-222(1995). CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- ENZYME REGULATION: Binds cyclosporin A (CsA). CsA mediates some of CC its effects via an inhibitory action on PPIase. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M55021; AAA63403.1; -. DR EMBL; X68678; CAA48638.1; -. DR PIR; C39252; CSZM. DR HSSP; P05092; 1CWL. DR MaizeDB; 65166; -. DR InterPro; IPR002130; CSA_PPIase. DR Pfam; PF00160; pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. KW Cyclosporin; Isomerase; Rotamase; Multigene family. SQ SEQUENCE 172 AA; 18349 MW; 16863EB1AAA33C67 CRC64; MANPRVFFDM TVGGAPAGRI VMELYANEVP KTAENFRALC TGEKGVGKSG KPLHYKGSTF HRVIPEFMCQ GGDFTRGNGT GGESIYGEKF PDEKFVRKQP APGVLSMANA GPNTNGSQFF ICTVATPWLD GKHVVFGQVV EGMDVVKAIE KVGTRNGSTS KVVKVADCGQ LS // ID CYS1_MAIZE STANDARD; PRT; 371 AA. AC Q10716; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Cysteine proteinase 1 precursor (EC 3.4.22.-). GN CCP1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96004895; PubMed=7548211; RA Domoto C., Watanabe H., Abe M., Abe K., Arai S.; RT "Isolation and characterization of two distinct cDNA clones encoding RT corn seed cysteine proteinases."; RL Biochim. Biophys. Acta 1263:241-244(1995). RN [2] RP SEQUENCE OF 227-371 FROM N.A. RC STRAIN=cv. DEA; TISSUE=Root meristem; RX MEDLINE=95359405; PubMed=7632917; RA Chevalier C., Bourgeois E., Pradet A., Raymond P.; RT "Molecular cloning and characterization of six cDNAs expressed during RT glucose starvation in excised maize (Zea mays L.) root tips."; RL Plant Mol. Biol. 28:473-485(1995). CC -!- FUNCTION: Involved in the degradation of the storage protein zein. CC May play a role in proteolysis during emergencies. CC -!- TISSUE SPECIFICITY: Expressed during the late stages of seed CC ripening, in mature seeds and during germination. CC -!- SIMILARITY: Belongs to peptidase family C1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D45402; BAA08244.1; -. DR EMBL; X82185; CAA57675.1; -. DR PIR; S59597; S59597. DR PIR; S60456; S60456. DR HSSP; P07711; 1CJL. DR MEROPS; C01.022; -. DR MaizeDB; 25431; -. DR InterPro; IPR000668; Peptidase_C1. DR InterPro; IPR000169; SHprot_acsite. DR Pfam; PF00112; Peptidase_C1; 1. DR PRINTS; PR00705; PAPAIN. DR ProDom; PD000158; Peptidase_C1; 1. DR SMART; SM00645; Pept_C1; 1. DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1. DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1. KW Hydrolase; Thiol protease; Zymogen; Glycoprotein; Signal. FT SIGNAL 1 18 Potential. FT PROPEP 19 136 Activation peptide (Potential). FT CHAIN 137 371 Cysteine proteinase 1. FT ACT_SITE 161 161 By similarity. FT ACT_SITE 303 303 By similarity. FT ACT_SITE 330 330 By similarity. FT DISULFID 158 208 By similarity. FT DISULFID 196 241 By similarity. FT DISULFID 297 345 By similarity. FT CARBOHYD 254 254 N-linked (GlcNAc...) (Potential). FT CONFLICT 269 269 L -> R (in Ref. 2). FT CONFLICT 318 318 I -> M (in Ref. 2). SQ SEQUENCE 371 AA; 40347 MW; 59042B03266E6058 CRC64; MAHRVLLLLS LASAAAVAAA VDAEDPLIRQ VVPGGDDNDL ELNAESHFLS FVQRFGKSYK DADEHAYRLS VFKDNLRRAR RHQLLDPSAE HGVTKFSDLT PAEFRRTYLG LRKSRRALLR ELGESAHEAP VLPTDGLPDD FDWRDHGAVG PVKNQGSCGS CWSFSASGAL EGAHYLATGK LEVLSEQQFV DCDHECDSSE PDSCDSGCNG GLMTTAFSYL QKAGGLESEK DYPYTGSDGK CKFDKSKIVA SVQNFSVVSV DEAQISANLI KHGPLAIGIN AAYMQTYIGG VSCPYICGRH LDHGVLLVGY GASGFAPIRL KDKPYWIIKN SWGENWGENG YYKICRGSNV RNKCGVDSMV STVSAVHASK E // ID CYS2_MAIZE STANDARD; PRT; 360 AA. AC Q10717; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Cysteine proteinase 2 precursor (EC 3.4.22.-). GN CCP2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seed; RX MEDLINE=96004895; PubMed=7548211; RA Domoto C., Watanabe H., Abe M., Abe K., Arai S.; RT "Isolation and characterization of two distinct cDNA clones encoding RT corn seed cysteine proteinases."; RL Biochim. Biophys. Acta 1263:241-244(1995). CC -!- FUNCTION: Involved in the degradation of the storage protein zein. CC May play a role in proteolysis during emergencies. CC -!- SUBCELLULAR LOCATION: Vacuolar (Probable). CC -!- TISSUE SPECIFICITY: Expressed at the onset of germination. CC -!- SIMILARITY: Belongs to peptidase family C1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D45403; BAA08245.1; -. DR PIR; S59598; S59598. DR HSSP; O46427; 8PCH. DR MEROPS; C01.041; -. DR MaizeDB; 25431; -. DR InterPro; IPR000668; Peptidase_C1. DR InterPro; IPR000169; SHprot_acsite. DR Pfam; PF00112; Peptidase_C1; 1. DR PRINTS; PR00705; PAPAIN. DR ProDom; PD000158; Peptidase_C1; 1. DR SMART; SM00645; Pept_C1; 1. DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1. DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1. KW Hydrolase; Thiol protease; Zymogen; Glycoprotein; Signal. FT SIGNAL 1 19 Potential. FT PROPEP 20 142 Activation peptide (Potential). FT CHAIN 143 360 Cysteine proteinase 2. FT ACT_SITE 167 167 By similarity. FT ACT_SITE 307 307 By similarity. FT ACT_SITE 327 327 By similarity. FT CARBOHYD 125 125 N-linked (GlcNAc...) (Potential). FT CARBOHYD 256 256 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 360 AA; 39199 MW; 8B5788F1B0C3FC1C CRC64; MVPRRLFVLA VVVLADTAAV VNSGFADSNP IRPVTDRAAS ALESTVFAAL GRTRDALRFA RFAVRYGKSY ESAAEVHKRF RIFSESLQLV RSTNRKGLSY RLGINRFADM SWEEFRATRL GAAQNCSATL TGNHRMRAAA VALPETKDWR EDGIVSPVKN QGHCGSCWTF STTGALEAAY TQATGKPISL SEQQLVDCGF AFNNFGCNGG LPSQAFEYIK YNGGLDTEES YPYQGVNGIC KFKNENVGVK VLDSVNITLG AEDELKDAVG LVRPVSVAFE VITGFRLYKS GVYTSDHCGT TPMDVNHAVL AVGYGVEDGV PYWLIKNSWG ADWGDEGYFK MEMGKNMCGV ATCASYPIVA // ID CYSK_MAIZE STANDARD; PRT; 325 AA. AC P80608; DT 01-OCT-1996 (Rel. 34, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cysteine synthase (EC 2.5.1.47) (O-acetylserine sulfhydrylase) DE (O-acetylserine (Thiol)-lyase) (CSase) (OAS-TL). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Root; RA Brander K.A., Owttrim G.W., Brunold C.; RT "Isolation of a cDNA encoding a putative chloroplastic isoform of RT cysteine synthase from maize."; RL (In) Plant Gene Register PGR95-031. RN [2] RP SEQUENCE OF 11-25. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- CATALYTIC ACTIVITY: O(3)-acetyl-L-serine + H(2)S = L-cysteine + CC acetate. CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- PATHWAY: Cysteine biosynthesis. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- CC synthase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X85803; CAA59798.1; -. DR PIR; S52738; S52738. DR Maize-2DPAGE; P80608; COLEOPTILE. DR HSSP; P12674; 1FCJ. DR MaizeDB; 123922; -. DR InterPro; IPR001926; B6_enzyme_beta. DR InterPro; IPR001216; Cys_synthase_BS. DR InterPro; IPR005859; Cys_synthK. DR InterPro; IPR005856; Cys_synthKM. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR01139; cysK; 1. DR TIGRFAMs; TIGR01136; cysKM; 1. DR PROSITE; PS00901; CYS_SYNTHASE; 1. KW Transferase; Cysteine biosynthesis; Pyridoxal phosphate. FT BINDING 49 49 Pyridoxal phosphate (By similarity). FT DOMAIN 275 280 Poly-Ala. SQ SEQUENCE 325 AA; 34206 MW; 3213A69326D7CEED CRC64; MGEASPSIAK DVTELIGNTP LVYLNKVTDG CVGRSRAKLE SMEPCSSVKD RIGYSMITDA EEKGLITPGV SVLIEPTSGN TGIGLAFMAA AKGYKLTLTM PASMSMERRI ILKAFGAELV LTDPLLGMKG AVKKAEEIQA KTPNSYILQQ FENPANPKIH YETTGPEIWK ATAGKIDGLV SGIGTGGTIT GTGRYLREQN PNVKLYGVEP VESAVLNGGK PGPHKIQGIG AGFIPGVLDV DLLDETLQVS SDEAIETAKA LALKEGLLVG ISSGAAAAAA VRLAKRPENA GKLFVVVFPS FGERYLSSVL FQSIKKEAES MVVEP // ID CYT1_MAIZE STANDARD; PRT; 135 AA. AC P31726; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Cystatin I precursor (Corn kernel cysteine proteinase inhibitor). GN RAMDAZC7. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Koshu; TISSUE=Immature kernel; RX MEDLINE=93049350; PubMed=1425699; RA Abe M., Abe K., Kuroda M., Arai S.; RT "Corn kernel cysteine proteinase inhibitor as a novel cystatin RT superfamily member of plant origin. Molecular cloning and expression RT studies."; RL Eur. J. Biochem. 209:933-937(1992). RN [2] RP SEQUENCE OF 84-135 FROM N.A. RC STRAIN=cv. B73; RX MEDLINE=94105294; PubMed=8278499; RA Keith C.S., Hoang D.O., Barrett B.M., Feigelman B., Nelson M.C., RA Thai H., Baysdorfer C.; RT "Partial sequence analysis of 130 randomly selected maize cDNA RT clones."; RL Plant Physiol. 101:329-332(1993). CC -!- DEVELOPMENTAL STAGE: Reaches a maximum 2 weeks after flowering and CC then decreases gradually. CC -!- SIMILARITY: Belongs to the cystatin family. Phytocystatin CC subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D10622; BAA01472.1; -. DR EMBL; M95070; AAA18557.1; -. DR PIR; S27239; S27239. DR HSSP; P01038; 1CEW. DR MaizeDB; 25463; -. DR MaizeDB; 30117; -. DR InterPro; IPR000010; Cystatin. DR InterPro; IPR003243; Cystatin_C/M. DR Pfam; PF00031; cystatin; 1. DR ProDom; PD001231; Cystatin_C/M; 1. DR SMART; SM00043; CY; 1. DR PROSITE; PS00287; CYSTATIN; 1. KW Thiol protease inhibitor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 135 Cystatin I. FT ACT_SITE 42 42 REACTIVE SITE (BY SIMILARITY). FT SITE 86 90 Secondary area of contact (By FT similarity). FT CONFLICT 105 105 K -> N (in Ref. 2). SQ SEQUENCE 135 AA; 14926 MW; 2C66485E6797CDF6 CRC64; MRKHRIVSLV AALLVLLALA AVSSTRSTQK ESVADNAGML AGGIKDVPAN ENDLQLQELA RFAVNEHNQK ANALLGFEKL VKAKTQVVAG TMYYLTIEVK DGEVKKLYEA KVWEKPWENF KQLQEFKPVE EGASA // ID DAPA_MAIZE STANDARD; PRT; 380 AA. AC P26259; DT 01-MAY-1992 (Rel. 22, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Dihydrodipicolinate synthase, chloroplast precursor (EC 4.2.1.52) DE (DHDPS). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 55-62. RC STRAIN=cv. Black Mexican Sweet; RX MEDLINE=91360078; PubMed=1886613; RA Frisch D.A., Tommey A.M., Somers D.A., Gengenbach B.G.; RT "Direct genetic selection of a maize cDNA for dihydrodipicolinate RT synthase in an Escherichia coli dapA-auxotroph."; RL Mol. Gen. Genet. 228:287-293(1991). CC -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + pyruvate = CC dihydrodipicolinate + 2 H(2)O. CC -!- ENZYME REGULATION: Sensitive to lysine inhibition. This inhibition CC increase in an allosteric manner with increasing concentration of CC the inhibitor. CC -!- PATHWAY: Biosynthesis of diaminopimelate and lysine from aspartate CC semialdehyde; first step. CC -!- SUBUNIT: Tetramer of modified subunits derived from two genes in CC different combinations. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the DHDPS family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52850; CAA37038.1; ALT_SEQ. DR HSSP; P05640; 1DHP. DR MaizeDB; 60647; -. DR InterPro; IPR005263; DapA. DR InterPro; IPR002220; DHDPS. DR Pfam; PF00701; DHDPS; 1. DR PRINTS; PR00146; DHPICSNTHASE. DR ProDom; PD001859; DHDPS; 1. DR TIGRFAMs; TIGR00674; dapA; 1. DR PROSITE; PS00665; DHDPS_1; 1. DR PROSITE; PS00666; DHDPS_2; 1. KW Lyase; Diaminopimelate biosynthesis; Lysine biosynthesis; KW Allosteric enzyme; Chloroplast; Transit peptide. FT TRANSIT 1 54 Chloroplast. FT CHAIN 55 380 Dihydrodipicolinate synthase. FT ACT_SITE 237 237 By similarity. SQ SEQUENCE 380 AA; 41244 MW; 61D4CAB9D1835D11 CRC64; MISPTNLLPA RKITPVSNGG AATASPSSPS VAARPRRLPS GLQSVTGRGK VSLAAITLDD YLPMRSTEVK NRTSTDDITR LRLITAVKTP YLPDGRFDLE AYDSLINMQI EGGAEGVIVG GTTGEGHLMS WDEHIMLIGH TVNCFGSRIK VIGNTGSNST REAVHATEQG FAVGMHAALH INPYYGKTSA EGMISHFEAV LPMGPTIIYN VPSRSAQDIP PEVILAISGY TNMAGVKECV GHERVKHYAD KGITIWSGND DECHDSKWKH GATGVISVTS NLVPGLMHSL MYKGENATLN EKLSPLMKWL FCQPNPIALN TALAQLGVAR PVFRLPYVPL PLEKRAEFVR IVESIGRENF VGQKEARVLD DDDFVLISRY // ID DCP1_MAIZE STANDARD; PRT; 610 AA. AC P28516; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pyruvate decarboxylase isozyme 1 (EC 4.1.1.1) (PDC). GN PDC1 OR PDC. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=92032792; PubMed=1932699; RA Kelley P.M., Godfrey K., Lal S.K., Alleman M.; RT "Characterization of the maize pyruvate decarboxylase gene."; RL Plant Mol. Biol. 17:1259-1261(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92003668; PubMed=2519113; RA Kelley P.M.; RT "Maize pyruvate decarboxylase mRNA is induced anaerobically."; RL Plant Mol. Biol. 13:213-222(1989). CC -!- CATALYTIC ACTIVITY: A 2-oxo acid = an aldehyde + CO(2). CC -!- COFACTOR: Binds 1 thiamine pyrophosphate and 1 metal ion per CC subunit. CC -!- SUBUNIT: Homooctamer (Potential). CC -!- INDUCTION: By hypoxic stress. CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X59546; CAA42120.1; -. DR EMBL; X17555; CAA35589.1; -. DR PIR; S18347; DCZMP. DR HSSP; P06169; 1PVD. DR MaizeDB; 25417; -. DR InterPro; IPR000399; Pyruvate_decarb. DR Pfam; PF00205; TPP_enzymes; 1. DR Pfam; PF02775; TPP_enzymes_C; 1. DR Pfam; PF02776; TPP_enzymes_N; 1. DR PROSITE; PS00187; TPP_ENZYMES; FALSE_NEG. KW Lyase; Decarboxylase; Flavoprotein; Thiamine pyrophosphate; KW Multigene family. FT ACT_SITE 95 95 By similarity. FT CONFLICT 567 568 TV -> MA (in Ref. 2). FT CONFLICT 571 571 A -> D (in Ref. 2). SQ SEQUENCE 610 AA; 65427 MW; 42A8C2B0E7208E93 CRC64; METLLAGNPA NGVAKPTCNG VGALPVANSH AIIATPAAAA ATLAPAGATL GRHLARRLVQ IGASDVFAVP GDFNLTLLDY LIAEPGLTLV GCCNELNAGY AADGYARSRG VGACAVTFTV GGLSVLNAIA GAYSENLPVV CIVGGPNSND YGTNRILHHT IGLPDFSQEL RCFQTITCYQ AIINNLDDAH EQIDTAIATA LRESKPVYIS VSCNLAGLSH PTFSRDPVPM FISPRLSNKA NLEYAVEAAA DFLNKAVKPV MVGGPKIRVA KAREAFAAVA DASGYPFAVM PAAKGLVPEH HPRFIGTYWG AVSTTFCAEI VESADAYLFA GPIFNDYSSV GYSLLLKREK AVIVQPDRMV VGDGPAFGCI LMPEFLRALA KRLRRNTTAY DNYRRIFVPD REPPNGKPNE PLRVNVLFKH IKGMLSGDSA VVAETGDSWF NCQKLRLPEG CGYEFQMQYG SIGWSVGATL GYAQAAKDKR VIACIGDGSF QVTAQDVSTM LRCGQKSIIF LINNGGYTIE VEIHDGPYNV IKNWDYTGLV NAIHNSEGNC WTMKVRTEEQ LKEAIATVTG AKKDCLCFIE VIVHKDDTSK ELLEWGSRVS AANSRPPNPQ // ID DCP2_MAIZE STANDARD; PRT; 106 AA. AC Q05326; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pyruvate decarboxylase isozyme 2 (EC 4.1.1.1) (PDC) (Fragment). GN PDC2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Berkeley Fast; TISSUE=Seedling; RX MEDLINE=93360899; PubMed=8102778; RA Peschke V.M., Sachs M.M.; RT "Multiple pyruvate decarboxylase genes in maize are induced by RT hypoxia."; RL Mol. Gen. Genet. 240:206-212(1993). CC -!- CATALYTIC ACTIVITY: A 2-oxo acid = an aldehyde + CO(2). CC -!- COFACTOR: Binds 1 thiamine pyrophosphate and 1 metal ion per CC subunit. CC -!- SUBUNIT: Homooctamer (Potential). CC -!- DEVELOPMENTAL STAGE: Appears in endosperm 15 days post- CC pollination. CC -!- INDUCTION: By hypoxic stress. CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z21721; CAA79818.1; -. DR EMBL; D14456; BAA03353.1; -. DR PIR; S35258; S35258. DR HSSP; P06672; 1ZPD. DR MaizeDB; 25417; -. DR InterPro; IPR000399; Pyruvate_decarb. DR Pfam; PF02775; TPP_enzymes_C; 1. DR PROSITE; PS00187; TPP_ENZYMES; PARTIAL. KW Lyase; Decarboxylase; Flavoprotein; Thiamine pyrophosphate; KW Multigene family. FT NON_TER 1 1 SQ SEQUENCE 106 AA; 11793 MW; 9CAAE594E322FA3F CRC64; QNSIIFLINN GGYTIEVEIH DGPYNVIKNW NYTGLVEAFH NGEGACYTAK VRTEEELTEA LEAALGPKKD CLCFIEVIVH KDDTSKELLE WGSRVSAANS RPPNPQ // ID DCP3_MAIZE STANDARD; PRT; 202 AA. AC Q05327; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pyruvate decarboxylase isozyme 3 (EC 4.1.1.1) (PDC) (Fragment). GN PDC3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Berkeley Fast; TISSUE=Seedling; RX MEDLINE=93360899; PubMed=8102778; RA Peschke V.M., Sachs M.M.; RT "Multiple pyruvate decarboxylase genes in maize are induced by RT hypoxia."; RL Mol. Gen. Genet. 240:206-212(1993). CC -!- CATALYTIC ACTIVITY: A 2-oxo acid = an aldehyde + CO(2). CC -!- COFACTOR: Binds 1 thiamine pyrophosphate and 1 metal ion per CC subunit. CC -!- SUBUNIT: Homooctamer (Potential). CC -!- DEVELOPMENTAL STAGE: Appears in endosperm 15 days post- CC pollination. CC -!- INDUCTION: By hypoxic stress. CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z21722; CAA79819.1; -. DR EMBL; D14457; BAA03354.1; -. DR PIR; S35259; S35259. DR HSSP; P06672; 1ZPD. DR MaizeDB; 25417; -. DR InterPro; IPR000399; Pyruvate_decarb. DR Pfam; PF02775; TPP_enzymes_C; 1. DR PROSITE; PS00187; TPP_ENZYMES; PARTIAL. KW Lyase; Decarboxylase; Flavoprotein; Thiamine pyrophosphate; KW Multigene family. FT NON_TER 1 1 SQ SEQUENCE 202 AA; 22297 MW; 2911A55C59D80AAD CRC64; PNEPLRVNVL FKHVQKMLTG DSAVIAETGD SWFNCQKLKL PEGCGYEFQM QYGSIGWSVG ALLGYPQGAN HKRVIAFIGD GSFQVTAQDV STILRCEQNS IIFLINNGGY TIEVEIHDGP YNVIKNWNYT GFVDAIHNGL GKCWTSKVKS EEDLTAAIET ALGEKDCLCF IEVIAHKDDT SKELLEWGSR VSAANSRPPN PQ // ID DFRA_MAIZE STANDARD; PRT; 357 AA. AC P51108; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Dihydroflavonol-4-reductase (EC 1.1.1.219) (DFR) (Dihydrokaempferol 4- DE reductase). GN A1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RA Schwarz-Sommer Z., Shepherd N., Tacke E., Gierl A., Rohde W., RA Leclercq L., Mattes M., Berndtgen R., Peterson P.A., Saedler H.; RT "Influence of transposable elements on the structure and function of RT the A1 gene of Zea mays."; RL EMBO J. 6:287-294(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=92167951; PubMed=1538691; RA Meyer P., Linn F., Heidmann I., Heiner Meyer Z.A., Niedenhof I., RA Saedler H.; RT "Endogenous and environmental factors influence 35S promoter RT methylation of a maize A1 gene construct in transgenic petunia and RT its colour phenotype."; RL Mol. Gen. Genet. 231:345-352(1992). CC -!- CATALYTIC ACTIVITY: Cis-3,4-leucopelargonidin + NADP(+) = (+)- CC dihydrokaempferol + NADPH. CC -!- PATHWAY: Flavonoid synthesis; anthocyanidins biosynthesis. CC -!- SIMILARITY: Belongs to the dihydroflavonol-4-reductase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05068; CAA28734.1; -. DR MaizeDB; 13795; -. KW Flavonoid biosynthesis; Oxidoreductase; NADP. SQ SEQUENCE 357 AA; 38855 MW; 6892B51E30E52804 CRC64; MERGAGASEK GTVLVTGASG FVGSWLVMKL LQAGYTVRAT VRDPANVGKT KPLMDLPGAT ERLSIWKADL AEEGSFHDAI RGCTGVFHVA TPMDFLSKDP ENEVIKPTVE GMISIMRACK EAGTVRRIVF TSSAGTVNLE ERQRPVYDEE SWTDVDFCRR VKMTGWMYFV SKTLAEKAAL AYAAEHGLDL VTIIPTLVVG PFISASMPPS LITALALITG NAPHYSILKQ VQLIHLDDLC DAEIFLFENP AAAGRYVCSS HDVTIHGLAA MLRDRYPEYD VPQRFPGIQD DLQPVRFSSK KLQDLGFTFR YKTLEDMFDA AIRTCQEKGL IPLATAAGGD GFASVRAPGE TEATIGA // ID DH1_MAIZE STANDARD; PRT; 168 AA. AC P12950; P16318; DT 01-JAN-1990 (Rel. 13, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Dehydrin DHN1 (M3) (RAB-17 protein). GN DHN1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=93357436; PubMed=2562763; RA Close T.J., Kortt A.A., Chandler P.M.; RT "A cDNA-based comparison of dehydration-induced proteins (dehydrins) RT in barley and corn."; RL Plant Mol. Biol. 13:95-108(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. AC 1503; RX MEDLINE=91346629; PubMed=2151715; RA Vilardell J., Goday A., Freire M.A., Torrent M., Martinez M.C., RA Torne J.M., Pages M.; RT "Gene sequence, developmental expression, and protein phosphorylation RT of RAB-17 in maize."; RL Plant Mol. Biol. 14:423-432(1990). RN [3] RP PHOSPHORYLATION BY CKII. RX MEDLINE=92042196; PubMed=1939268; RA Plana M., Itarte E., Eritja R., Goday A., Pages M., Martinez M.C.; RT "Phosphorylation of maize RAB-17 protein by casein kinase 2."; RL J. Biol. Chem. 266:22510-22514(1991). CC -!- DEVELOPMENTAL STAGE: ABA treatment induced the synthesis of RAB-17 CC in calli, however, the RAB-17 proteins were found to be highly CC phosphorylated only in embryos. CC -!- INDUCTION: By abscisic acid (ABA) and water stress. CC -!- PTM: Phosphorylated on serines in the serine-cluster region (poly- CC Ser). CC -!- SIMILARITY: Belongs to the plant dehydrin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15290; CAA33364.1; -. DR EMBL; X15994; CAA34123.1; -. DR PIR; A39316; A39316. DR PIR; S05545; S05545. DR PIR; S08633; S08633. DR MaizeDB; 24916; -. DR InterPro; IPR000167; Dehydrin. DR Pfam; PF00257; dehydrin; 1. DR PROSITE; PS00315; DEHYDRIN_1; 1. DR PROSITE; PS00823; DEHYDRIN_2; 2. KW Dehydrin; Repeat; Phosphorylation; Multigene family. FT DOMAIN 76 84 Poly-Ser. FT DOMAIN 2 140 3 X approximate repeats. FT REPEAT 2 10 1-1. FT REPEAT 122 130 1-2. FT REPEAT 132 140 1-3. FT DOMAIN 94 166 2 X approximate repeats. FT REPEAT 94 107 2-1. FT REPEAT 153 166 2-2. FT CONFLICT 9 9 R -> H (in Ref. 2). FT CONFLICT 13 13 R -> A (in Ref. 2). FT CONFLICT 41 41 Missing (in Ref. 2). SQ SEQUENCE 168 AA; 17161 MW; BE7758CAD37CFF39 CRC64; MEYGQQGQRG HGRTGHVDQY GNPVGGVEHG TGGMRHGTGT TGGMGQLGEH GGAGMGGGQF QPAREEHKTG GILHRSGSSS SSSSEDDGMG GRRKKGIKEK IKEKLPGGHK DDQHATATTG GAYGQQGHTG SAYGQQGHTG GAYATGTEGT GEKKGIMDKI KEKLPGQH // ID DPOM_MAIZE STANDARD; PRT; 929 AA. AC P10582; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA polymerase (EC 2.7.7.7) (S-1 DNA ORF 3). OS Zea mays (Maize). OG Mitochondrion. OG Plasmid S-1. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Paillard M., Sederoff R.R., Levings C.S. III; RT "Nucleotide sequence of the S-1 mitochondrial DNA from the S cytoplasm RT of maize."; RL EMBO J. 4:1125-1128(1985). CC -!- CATALYTIC ACTIVITY: N deoxynucleoside triphosphate = N diphosphate CC + {DNA}(N). CC -!- MISCELLANEOUS: This DNA polymerase requires a protein as a primer. CC -!- MISCELLANEOUS: The mitochondria from the S male-sterile cytoplasm CC of maize contain unique DNA-protein complexes, designated S-1 and CC S-2. These complexes consist of double-stranded linear DNAs with CC proteins covalently attached to the 5'termini. CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02451; -; NOT_ANNOTATED_CDS. DR MaizeDB; 69234; -. DR InterPro; IPR006172; DNA_pol_B. DR InterPro; IPR004868; DNA_pol_B_2. DR Pfam; PF03175; DNA_pol_B_2; 1. DR PRINTS; PR00106; DNAPOLB. DR SMART; SM00486; POLBc; 1. DR PROSITE; PS00116; DNA_POLYMERASE_B; 1. KW Transferase; DNA-directed DNA polymerase; DNA replication; KW DNA-binding; Mitochondrion; Plasmid. SQ SEQUENCE 929 AA; 107532 MW; 3652A67A6E80DCDE CRC64; MQPARRHTKK KNMNYMRYES LTREQFERFL KDVHKCYRGE PRYVIPYEGH LIAVQDFEEP YPKAGAVTML ASAFMELLIN RVYPSIQGSA KFTLQYRLNI DGNPINITLS KAIKLTYADG TRIANEFILK EIINVLNKYA ENYQSCDVEA ISVRAYSEGS IDLNQASIPT KDESLNYLKG ALIKYSDINN LEIPKMGRRS KRRYQSYIPV DKTEMKNKTL FFVADLETLL LKRRDTDVDK THVPYAGGYM MVDMEKWVNA DHITTFYAHD YSKVCQDFHD MSEKMLTEMI NRIVKDVQRR GSSMVVYFHN LSQFDGIMIL SFLTKSYKNC HIEPIMRNDC IYSIKLYKVS KNGDKRLVLT FMDSYLLLKV KLADLADSFC PELGGKGSFD HQNVTVDKLP SIREDSLTYL KQDILITAAV MQRAKAIIWE EYGIDILKVL TISALALKIF RRVYYKDDDD NWIYIPDDNE AQFIREGYYG GHTDVYKPYG ENLYYYDVNS LYPSSMLDDM PIGKTRWVSD LGSKKSKIVL NDMFGFIRAF IICPKHIKKP LLPYKKDDGT IIFPTGRFLG VYFSEELKYA VSLGYKVYPI CGYIFDRKES PFKRFVYDIY SKRLDAKAKG EKALDFIYKI TMNSLYGRFG ISPESTTTQI VSTEESRKLA LYNDGFVQSY ELSSDKCLVT CKNVRSLDLL KLSSDRPTYA AVQISAAVTG YARIRMHPFI SRDDCYYTDT DSVVVERELP EEEVSPTALG KFKHEHFVEY GIFLAPKSYM LKASSVDQPI IKFKGAGKDE ADEEWFINQL ADPRAKKVIS YVRKFSRNFR ELLVQEKMCK YTMGLESKKR EYVFDKNGVW VDTKPCHIGD FDVKSINPTS YWIIMNLLEE NEDLRNEFSN SEIMIANWEI KADAAKKRKA SKLRGKPLRG GDTPSHIEE // ID E13B_MAIZE STANDARD; PRT; 335 AA. AC P49237; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Glucan endo-1,3-beta-glucosidase, acidic isoform precursor DE (EC 3.2.1.39) ((1->3)-beta-glucan endohydrolase) ((1->3)-beta- DE glucanase) (Beta-1,3-endoglucanase). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Va26; TISSUE=Seedling; RX MEDLINE=95148758; PubMed=7846180; RA Wu S., Kriz A.L., Widholm J.M.; RT "Nucleotide sequence of a maize cDNA for a class II, acidic beta-1,3- RT glucanase."; RL Plant Physiol. 106:1709-1710(1994). CC -!- FUNCTION: Is thought to be an important plant defense-related CC product against fungal pathogens. CC -!- CATALYTIC ACTIVITY: Hydrolysis of 1,3-beta-D-glucosidic linkages CC in 1,3-beta-D-glucans. CC -!- SUBCELLULAR LOCATION: Extracellular (Potential). CC -!- TISSUE SPECIFICITY: Accumulates in aleurone layers. Much lower CC levels are found in the embryo, and none in starchy endosperm. CC -!- INDUCTION: By pathogen infection. CC -!- SIMILARITY: Belongs to family 17 of glycosyl hydrolases. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95407; AAA74320.1; -. DR PIR; T02088; T02088. DR HSSP; P15737; 1GHS. DR MaizeDB; 25482; -. DR InterPro; IPR000490; Glyco_hydro_17. DR Pfam; PF00332; Glyco_hydro_17; 1. DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1. KW Hydrolase; Glycosidase; Signal; Multigene family. FT SIGNAL 1 29 By similarity. FT CHAIN 30 335 Glucan endo-1,3-beta-glucosidase, acidic FT isoform. FT ACT_SITE 259 259 Nucleophile (By similarity). FT ACT_SITE 316 316 Proton donor (By similarity). SQ SEQUENCE 335 AA; 34894 MW; 97F89ADF5C4FBA65 CRC64; MARQGVIASM HALALLLGAF AAIPTGVQSI GVCYGVNGDN LPPASDVVQL YQSNGINLLR IYFPDANPLN ALSGTSIGLI MDVPNTDLAS LASDPSAAAA WVQSNVQASR RSACRYIAVG NEVSGGDTGS ILPAMQNLNA ALANAGLGGS IKVSTAVQSD VTQGFPPSQG TFSQGYMAPS RQYLQSTGAP LLSNVYPYFS YVGNPAQIDL KYALFTSPGT VVQDGSNAYQ NLFDALVDTF VSALEENAGA GNVPVVVSES GWPSAGGDAA TAANAQTYNQ NLINHVGQGT PKRPGPIETY IFAMFNEDQK TGAESERHFG LFNPDKSPVY PINFS // ID EC_MAIZE STANDARD; PRT; 76 AA. AC P43401; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE EC protein homolog (Zinc-metallothionein class II). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA White C.N., Rivin C.J.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Binds 5 molecules of zinc. May have a role in Zn(2+) CC homeostasis during embryogenesis (By similarity). CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Family 15. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z34469; CAA84233.1; -. DR EMBL; U10696; AAA19405.1; -. DR PIR; S47158; S47158. DR MaizeDB; 78896; -. DR InterPro; IPR000316; Metallthion_15. DR Pfam; PF02068; Metallothio_PEC; 1. DR PRINTS; PR00877; MTPLANTPEC. KW Metal-binding; Metal-thiolate cluster; Zinc. FT INIT_MET 0 0 By similarity. SQ SEQUENCE 76 AA; 7574 MW; C9803CBF7F9B1D34 CRC64; GCDDKCGCAV PCPGGKDCRC TSGSGGQREH TTCGCGEHCE CSPCTCGRAT MPSGRENRRA NCSCGASCNC ASCASA // ID EF1A_MAIZE STANDARD; PRT; 447 AA. AC Q41803; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Elongation factor 1-alpha (EF-1-alpha). GN EF1A. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Honey Vantum; RX MEDLINE=96123237; PubMed=8534856; RA Berberich T., Sugawara K., Harada M., Kusano T.; RT "Molecular cloning, characterization and expression of an elongation RT factor 1 alpha gene in maize."; RL Plant Mol. Biol. 29:611-615(1995). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. CC EF-Tu/EF-1A subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D45408; BAA08249.1; -. DR PIR; S66339; S66339. DR HSSP; P07157; 1AIP. DR MaizeDB; 25449; -. DR InterPro; IPR004539; EF1_alpha. DR InterPro; IPR000795; EF_GTPbind. DR InterPro; IPR004160; EFTU_Cterm. DR InterPro; IPR004161; EFTU_D2. DR InterPro; IPR009001; Elong_init_C. DR InterPro; IPR009000; Translat_factor. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR TIGRFAMs; TIGR00483; EF-1_alpha; 1. DR PROSITE; PS00301; EFACTOR_GTP; 1. KW Elongation factor; Protein biosynthesis; GTP-binding. FT NP_BIND 14 21 GTP (By similarity). FT NP_BIND 91 95 GTP (By similarity). FT NP_BIND 153 156 GTP (By similarity). SQ SEQUENCE 447 AA; 49233 MW; 1CBC5B54883A179C CRC64; MGKEKTHINI VVIGHVDSGK STTTGHLIYK LGGIDKRVIE RFEKEAAEMN KRSFKYAWVL DKLKAERERG ITIDIALWKF ETTKYYCTVI DAPGHRDFIK NMITGTSQAD CAVLIIDSTT GGFEAGISKD GQTREHALLA FTLGVKQMIC CCNKMDATTP KYSKARYDEI VKEVSSYLKK VGYNPDKIHF VPISGFEGDN MIERSTNLDW YKGPTLLEAL DLINEPKRPS DKPLRLPLQD VYKIGGIGTV PVGRVETGVI KPGMVVTFGP TGLTTEVKSV EMHHEALQEA LPGDNVGFNV KNVAVKDLKR GYVASGSKDD PAKEAASFTS QVIIMNHPGQ IGNGYAPVLD CHTSHIAVKF AELVTKIDRR SGKELEKEPK FLKNGDAGMV KMVPTKPMVV ETFSQYPPLG RFAVRDMRQT VAVGVIKSVE KKDPTGAKVT KAAAKKK // ID EMB5_MAIZE STANDARD; PRT; 91 AA. AC P46517; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Late embryogenesis abundant protein EMB564. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. CO255; TISSUE=Embryo; RX MEDLINE=91316231; PubMed=1830496; RA Williams B., Tsang A.; RT "A maize gene expressed during embryogenesis is abscisic RT acid-inducible and highly conserved."; RL Plant Mol. Biol. 16:919-923(1991). CC -!- FUNCTION: LEA proteins are late embryonic proteins abundant in CC higher plant seed embryos. They may play an essential role in seed CC survival and in controlling water exchanges during seed CC desiccation and imbibition. CC -!- INDUCTION: By abscisic acid (ABA) and osmotic stress. CC -!- SIMILARITY: Belongs to the small hydrophilic plant seed protein CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55388; CAA39063.1; -. DR PIR; S16249; S16249. DR MaizeDB; 120720; -. DR InterPro; IPR000389; Seed_protein. DR Pfam; PF00477; seed_protein; 1. DR PROSITE; PS00431; SMALL_HYDR_PLANT_SEED; 1. KW Seed embryo; Seed; Multigene family. SQ SEQUENCE 91 AA; 9684 MW; C78517500A7F675C CRC64; MASGQESRKE LDRKAREGET VVPGGTGGKS VEAQEHLAEG RSRGGQTRRE QLGQQGYSEM GKKGGLSTTD ESGGERAARE GVTIDESKFT K // ID ENO1_MAIZE STANDARD; PRT; 446 AA. AC P26301; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Enolase 1 (EC 4.2.1.11) (2-phosphoglycerate dehydratase 1) (2-phospho- DE D-glycerate hydro-lyase 1). GN ENO1 OR PGH1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Berkeley Fast; TISSUE=Root; RX MEDLINE=91316216; PubMed=1859865; RA Lal S.K., Johnson S., Conway T., Kelley P.M.; RT "Characterization of a maize cDNA that complements an enolase- RT deficient mutant of Escherichia coli."; RL Plant Mol. Biol. 16:787-795(1991). CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + CC H(2)O. CC -!- COFACTOR: Magnesium is required for catalysis and for stabilizing CC the dimer (By similarity). CC -!- PATHWAY: Glycolysis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the enolase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55981; CAA39454.1; -. DR PIR; S16257; S16257. DR HSSP; P56252; 1PDZ. DR MaizeDB; 30060; -. DR InterPro; IPR000941; Enolase. DR Pfam; PF00113; enolase; 1. DR Pfam; PF03952; enolase_N; 1. DR PRINTS; PR00148; ENOLASE. DR ProDom; PD000902; Enolase; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. KW Lyase; Glycolysis; Magnesium; Multigene family. FT ACT_SITE 164 164 By similarity. FT METAL 251 251 Magnesium (By similarity). FT METAL 302 302 Magnesium (By similarity). FT METAL 329 329 Magnesium (By similarity). SQ SEQUENCE 446 AA; 48063 MW; 6266C48914F35198 CRC64; MAVTITWVKA RQIFDSRGNP TVEVDVGLSD GSYARGAVPS GASTGIYEAL ELRDGGSDYL GKGVLKAVSN VNNIIGPAIV GKDPTEQVEI DNFMVQQLDG TSNEWGWCKQ KLGANAILAV SLAVCKAGAM VKKIPLYQHI ANLAGNKTLV LPVPAFNVIN GGSHAGNKLA MQEFMILPTG ASSFKEAMKM GVEVYHNLKS IIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKAAIEKA GYTGKVVIGM DVAASEFFGE KDKTYDLNFK EENNDGSNKI SGDSLKDLYK SFVSEYPIES IEDPFDQDDW STYAKLTDEI GQKVQIVGDD LLVTNPTRVA KAINEKTCNA LLLKVNQIGS VTESIEAVRM SKRAGWGVMA SHRSGETEDT FIADLSVGLS TGQIKTGAPC RSERLAKYNQ LLRIEEELGD AAVYAGAKFR APVEPY // ID ENO2_MAIZE STANDARD; PRT; 446 AA. AC P42895; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Enolase 2 (EC 4.2.1.11) (2-phosphoglycerate dehydratase 2) (2-phospho- DE D-glycerate hydro-lyase 2). GN ENO2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Root; RX MEDLINE=99063764; PubMed=9847102; RA Lal S.K., Lee C., Sachs M.M.; RT "Differential regulation of enolase during anaerobiosis in maize."; RL Plant Physiol. 118:1285-1293(1998). CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + CC H(2)O. CC -!- COFACTOR: Magnesium is required for catalysis and for stabilizing CC the dimer (By similarity). CC -!- PATHWAY: Glycolysis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the enolase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U17973; AAD04187.1; -. DR PIR; T02221; T02221. DR HSSP; P56252; 1PDZ. DR MaizeDB; 30060; -. DR InterPro; IPR000941; Enolase. DR Pfam; PF00113; enolase; 1. DR Pfam; PF03952; enolase_N; 1. DR PRINTS; PR00148; ENOLASE. DR ProDom; PD000902; Enolase; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. KW Lyase; Glycolysis; Magnesium; Multigene family. FT ACT_SITE 164 164 By similarity. FT METAL 251 251 Magnesium (By similarity). FT METAL 302 302 Magnesium (By similarity). FT METAL 329 329 Magnesium (By similarity). SQ SEQUENCE 446 AA; 48162 MW; DC27708CF92F6850 CRC64; MAATIQSVKA RQIFDSRGNP TVEVDVFCSD GTFARAAVPS GASTGVYEAL ELRDGGSYYL GKGVSKAVNN VNSVIGPALI GKDPTAQTEI DNFMVQQLDG TKNEWGWCKQ KLGANAILAV SLAVCKAGAS IKRIPLYQHI ANLAGNKQLV LPVPAFNVIN GGSHAGNKLA MQEFMILPTG AASFKEAMKM GVEVYHHLKS VIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKTAIEKA GYTGKVVIGM DVAASEFYSD KDQTYDLNFK EENNDGSQKI SGDSLKNVYK SFVSEYPIVS IEDPFDQDDW VHYAKMTEEI GEQVQIVGDD LLVTNPTRVA KAIKEKSCNA LLLKVNQIGS VTESIEAVKM SKRAGWGVMT SHRSGETEDT FIADLAVGLS TGQIKTGAPC RSERLAKYNQ LLRIEEELGA IAVYAGAKFR APVEPY // ID EXBB_MAIZE STANDARD; PRT; 191 AA. AC Q07154; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Beta-expansin 1b (Pollen allergen Zea m 1) (Zea m I) (Fragment). GN EXPB1B. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Pollen; RX MEDLINE=94010312; PubMed=8406014; RA Broadwater A.H., Rubinstein A.L., Chay C.H., Klapper D.G., RA Bedinger P.A.; RT "Zea mI, the maize homolog of the allergen-encoding Lol pI gene of RT rye grass."; RL Gene 131:227-230(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=21249159; PubMed=11351085; RA Wu Y., Meeley R.B., Cosgrove D.J.; RT "Analysis and expression of the alpha-expansin and beta-expansin gene RT families in maize."; RL Plant Physiol. 126:222-232(2001). RN [3] RP FUNCTION. RX MEDLINE=97322412; PubMed=9177257; RA Cosgrove D.J., Bedinger P.A., Durachko D.M.; RT "Group I allergens of grass pollen as cell wall-loosening agents."; RL Proc. Natl. Acad. Sci. U.S.A. 94:6559-6564(1997). CC -!- FUNCTION: May aid fertilization by loosening the cell wall of the CC stigma and style, thereby facilitating penetration of the pollen CC tube. Acts selectively on grass cell walls, which are relatively CC poor in pectins and xyloglucans and rich in glucuronoarabinoxylans CC and (1-3),(1-4)-beta-D-glucans, when compared with cell walls of CC other angiosperms, including other monocots. CC -!- TISSUE SPECIFICITY: Pollen. CC -!- DEVELOPMENTAL STAGE: Expression low before and high after pollen CC mitosis. CC -!- ALLERGEN: Causes an allergic reaction in human. Causes maize CC pollen allergy. CC -!- SIMILARITY: Belongs to the expansin family. CC -!- SIMILARITY: Contains 1 expansin-like CBD domain. CC -!- SIMILARITY: Contains 1 expansin-like EG45 domain. CC -!- DATABASE: NAME=EXPANSIN homepage; CC WWW="http://www.bio.psu.edu/expansins/". CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L14271; AAA33496.1; -. DR PIR; JC1524; JC1524. DR HSSP; P43214; 1WHO. DR MaizeDB; 65840; -. DR InterPro; IPR007112; Expan_endogl. DR InterPro; IPR007118; Expan_Lol_pI. DR InterPro; IPR007117; Expan_Lol_pI_C. DR Pfam; PF01357; Pollen_allergen; 1. DR PRINTS; PR01225; EXPANSNFAMLY. DR ProDom; PD002179; Expan_Lol_pI_C; 1. DR PROSITE; PS50843; EXPANSIN_CBD; 1. DR PROSITE; PS50842; EXPANSIN_EG45; 1. KW Cell wall; Allergen; Multigene family. FT NON_TER 1 1 FT DOMAIN <1 91 Expansin-like EG45. FT DOMAIN 105 186 Expansin-like CBD. SQ SEQUENCE 191 AA; 21362 MW; 6E2A9DF921C45C63 CRC64; MTACGNVPIF KDGKGCGSCY EVRCKEKPEC SGNPVTVFIT DMNYEPIAPY HFDLSGKAFG SLAKPGLNDK LRHCGIMDVE FRRVRCKYPA GQKIVFHIEK GCNPNYVAVL VKFVADDGDI VLMEIQDKLS AEWKPMKLSW GAIWRMDTAK ALKGPFSIRL TSESGKKVIA KDIIPANWRP DAVYTSNVQF Y // ID EXTN_MAIZE STANDARD; PRT; 267 AA. AC P14918; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Extensin precursor (Proline-rich glycoprotein). GN HRGP. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A, and cv. E41; RA Stiefel V., Perez-Grau L., Albericio F., Giralt E., Ruiz-Avila L., RA Ludevid M.D., Puigdomenech P.; RT "Molecular cloning of cDNAs encoding a putative cell wall protein from RT Zea mays and immunological identification of related polypeptides."; RL Plant Mol. Biol. 11:483-493(1988). CC -!- FUNCTION: Structural component in primary cell wall. CC -!- TISSUE SPECIFICITY: Mainly in the coleoptile node and root tip. CC -!- PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat. CC -!- PTM: O-glycosylated on hydroxyprolines. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13499; CAA31854.1; -. DR EMBL; X13506; CAA31860.1; -. DR EMBL; M36912; AAA33455.1; -. DR EMBL; M36913; AAA33456.1; -. DR EMBL; M36914; AAA33457.1; -. DR PIR; S08314; S08314. DR MaizeDB; 17152; -. DR InterPro; IPR003882; Pistil_extensin. DR PRINTS; PR01218; PSTLEXTENSIN. KW Repeat; Cell wall; Glycoprotein; Signal; Structural protein; KW Hydroxylation. FT SIGNAL 1 ? Potential. FT CHAIN ? 267 Extensin. FT DOMAIN 18 253 HIGHLY REPETITIVE ZONE. FT REPEAT 18 33 FT REPEAT 34 54 FT REPEAT 55 70 FT REPEAT 71 91 FT REPEAT 92 107 FT REPEAT 108 128 FT REPEAT 129 144 FT REPEAT 145 160 FT REPEAT 161 179 FT REPEAT 180 195 FT REPEAT 196 211 FT REPEAT 212 232 FT REPEAT 233 253 FT DOMAIN 261 265 EXTENSIN REPETITIVE ELEMENT. FT VARIANT 245 245 Missing (in strain E41). FT VARIANT 261 261 S -> C (in strain E41). SQ SEQUENCE 267 AA; 28349 MW; A6F406F4645FEECB CRC64; MCPAFSIFFN SRRYSLTPPT YTPSPKPPTP KPTPPTYTPS PKPPASKPPT PKPTPPTYTP SPKPPTPKPT PPTYTPSPKP PATKPPTPKP TPPTYTPSPK PPTPKPTPPT YTPSPKPPAT KPPTPKPTPP TYTPSPKPPT PKPTPPTYTP SPKPPTPKPT PPTYTPSPKP PTHPTPKPTP PTYTPSPKPP TPKPTPPTYT PSPKPPTPKP TPPTYTPSPK PPATKPPTPK PTPPTYTPTP KPPATKPPTY TPTPPVSHTP SPPPPYY // ID EZ1_MAIZE STANDARD; PRT; 931 AA. AC Q8S4P6; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Polycomb protein EZ1 (Enhancer of zeste protein 1). GN EZ1 OR MEZ1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC TISSUE=Seed; RX MEDLINE=21948211; PubMed=11950982; RA Springer N.M., Danilevskaya O.N., Hermon P., Helentjaris T.G., RA Phillips R.L., Kaeppler H.F., Kaeppler S.M.; RT "Sequence relationships, conserved domains, and expression patterns RT for maize homologs of the Polycomb group genes E(z), esc, and E(Pc)."; RL Plant Physiol. 128:1332-1345(2002). CC -!- FUNCTION: Polycomb group (PcG) protein. PcG proteins act by CC forming multiprotein complexes, which are required to maintain the CC transcriptionally repressive state of homeotic genes throughout CC development. PcG proteins are not required to initiate repression, CC but to maintain it during later stages of development. They CC probably act via the methylation of histones, rendering chromatin CC heritably changed in its expressibility. Its sequence suggests CC that it may participate in a potential methyltransferase activity CC of PcG complexes (By similarity). CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- SIMILARITY: Belongs to the EZ family. CC -!- SIMILARITY: Contains 1 SANT domain. CC -!- SIMILARITY: Contains 1 SET domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF443596; AAM13420.1; -. DR MaizeDB; 754841; -. DR InterPro; IPR001005; Myb_DNA_binding. DR InterPro; IPR001214; SET. DR Pfam; PF00856; SET; 1. DR SMART; SM00717; SANT; 1. DR SMART; SM00317; SET; 1. DR PROSITE; PS50280; SET; 1. DR PROSITE; PS50090; MYB_3; FALSE_NEG. KW Transcription regulation; Repressor; Nuclear protein; KW Multigene family. FT DOMAIN 565 615 SANT. FT DOMAIN 777 897 SET. FT DOMAIN 675 750 Cys-rich. FT DOMAIN 3 8 Poly-Ala. SQ SEQUENCE 931 AA; 103768 MW; 4F3CD84B17783B6C CRC64; MEAEAAAAVV ASSASASASA GRSRPSSSAA QVTSNSAVRA GEENAASLYV LSVIDSLKKR ITADRLTYIK NRIGENKTNI SSYTQRTYNL SKNRQISTSK GTDSASNLLT KRQDDALCTL HSLDIIPVDK DGGTFQDESP FSSSNVMFGG NLGPKNAIIR PIKLPEVPKL PPYTTWIFLD RNQRMTEDQS VLGRRRIYYD TSCGEALICS DSEDEAIEDE EEKKEFKHSE DHIIRMTVQE CGMSDAVLQT LARHMERAAD DIKARYEILH GEKTKDSCKK GTEHNVKVED LYCDKDLDAA LDSFDNLFCR RCLVFDCKLH GCSQDLVFPT EKQPAWSGVD DSVPCGIHCH KLASEPDAAA GADHMLFDVE EPTHSSDNVM NQPGSNRKKN GSSGRKTKSQ QSESSSTARV ISESSDSEVH PISNKSPQHS PSPSKVKIGP KGGIRKITNR RIAERILMSV KKGQREMASS DSNFVSGYLL ARDMKLRSDT RNGNKELIVS SQQSSPSTRS SKKKSTPQIG NSSAFAEAHN DSTEEANNRH SATDGYDSSR KEEFVNENLC KQEVYLRSWK AIEQGLLVKG LEIFGRNSCL IARNLLGGMK TCKDVFQYMN YIENNSASGA LSGVDSLVKG YIKGTELRTR SRYFRRRGKV RRLKYTWKSA GYNFKRITER KDQPCRQYNP CGCQSTCGKQ CPCLSNGTCC EKYCGCPKIC KNRFRGCHCA KSQCRSRQCP CFAADRECDP DVCRNCWVGC GDGTLGVPNQ RGDNYECRNM KLLLKQQQRV LLGRSDVSGW GAFLKNSVSK HEYLGEYTGE LISHKEADKR GKIYDRENSS FLFNLNNEYV LDAYRMGDKL KFANHAPDPN CYAKVIMVTG DHRVGIFAKE RILAGEELFY DYRYEPDRAP AWARKPEASG AKDDGQPFNG RAKKLAQNNR G // ID EZ2_MAIZE STANDARD; PRT; 894 AA. AC Q8S4P5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Polycomb protein EZ2 (Enhancer of zeste protein 2). GN EZ2 OR MEZ2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, AND RP ALTERNATIVE SPLICING. RC TISSUE=Seed; RX MEDLINE=21948211; PubMed=11950982; RA Springer N.M., Danilevskaya O.N., Hermon P., Helentjaris T.G., RA Phillips R.L., Kaeppler H.F., Kaeppler S.M.; RT "Sequence relationships, conserved domains, and expression patterns RT for maize homologs of the Polycomb group genes E(z), esc, and E(Pc)."; RL Plant Physiol. 128:1332-1345(2002). CC -!- FUNCTION: Polycomb group (PcG) protein. PcG proteins act by CC forming multiprotein complexes, which are required to maintain the CC transcriptionally repressive state of homeotic genes throughout CC development. PcG proteins are not required to initiate repression, CC but to maintain it during later stages of development. They CC probably act via the methylation of histones, rendering chromatin CC heritably changed in its expressibility. Its sequence suggests CC that it may participate in a potential methyltransferase activity CC of PcG complexes (By similarity). CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8S4P5-1; Sequence=Displayed; CC Name=2; Synonyms=as1; CC IsoId=Q8S4P5-2; Sequence=VSP_007783; CC Name=3; Synonyms=as2; CC IsoId=Q8S4P5-3; Sequence=VSP_007784; CC -!- SIMILARITY: Belongs to the EZ family. CC -!- SIMILARITY: Contains 1 SANT domain. CC -!- SIMILARITY: Contains 1 SET domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF443597; AAM13421.1; -. DR MaizeDB; 754843; -. DR InterPro; IPR001005; Myb_DNA_binding. DR InterPro; IPR001214; SET. DR Pfam; PF00856; SET; 1. DR SMART; SM00717; SANT; 1. DR SMART; SM00317; SET; 1. DR PROSITE; PS50280; SET; 1. DR PROSITE; PS50090; MYB_3; FALSE_NEG. KW Transcription regulation; Repressor; Nuclear protein; KW Alternative splicing; Multigene family. FT DOMAIN 527 577 SANT. FT DOMAIN 745 865 SET. FT DOMAIN 642 718 Cys-rich. FT DOMAIN 25 28 Poly-Ala. FT DOMAIN 74 77 Poly-Ala. FT VARSPLIC 342 894 Missing (in isoform 2). FT /FTId=VSP_007783. FT VARSPLIC 625 894 Missing (in isoform 3). FT /FTId=VSP_007784. SQ SEQUENCE 894 AA; 99979 MW; 9C2B04E6F80BA113 CRC64; MASSSKASDS SQRSKRSDQG MGKDAAAASV VPIHANLTQL IRQVQSGRLA YIKEKLEVNR KTLQRHSCSL FDVAAAAEVA SRGTDGGNAL SQRAAERQCG SDLANGIGER DVVSVQEENL ATGTLALSSS GATAQRTIVR FVKLPLVEKI PPYTTWIFLD KNQRMADDQS VVGRRRIYYD TVGNEALICS DSDEEIPEPE EEKHFFTKGE DHLIWRATQD HGLNQEVVNV LCQFIGATPS EIEERSEVLF EKNEKHSGSS DKIESRLSLD KTMDAVLDSF DNLFCRRCLV FDCRLHGCSQ NLVFPCEKQP YSFDPDENKK PCGHLCYLRF PQWREGFKEM HDDGLAGGAT YTMESGTASQ RVDVNVMYES EDSNRQKGNI RSMTLVGTSG SKIISSVSAE ESTTTPSADI SETENVSSDL PPSSLRKHKI SKHGPRYREH SPGKRQKVFT SDISFEGNIM NKLSIPEIRD TRLESRESGG DKLRILDEST KKTSRKDMCG ESPATTMENV GRQSNKVSST KNFLESTLSC WSALERDLYL KGIEIFGKNS CLIARNLLSG LKTCIEVANY MYNNGAAMAK RPLLNKSISG DFAENEQDYM EQDMAARTRI YRRRGRNRKL KYTWKSAGHP TVRKRTDDGK QCYTQYSPCA CQQMCGKDCP CADKGTCCEK YCGCSKSCKN KFRGCHCAKS QCRSRQCPCF AASRECDPDV CRNCWVSCGD GSLGEPLARG DGYQCGNMKL LLKQQQRILL GRSDVAGWGA FIKNPVNKND YLGEYTGELI SHKEADKRGK IYDRANSSFL FDLNDQYVLD AYRKGDKLKF ANHSSNPNCY AKVMLVAGDH RVGIYAKEHI EASEELFYDY RYGPDQAPAW ARRPEGSKKD EASVSHRRAH KVAR // ID EZ3_MAIZE STANDARD; PRT; 895 AA. AC Q8S4P4; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Polycomb protein EZ3 (Enhancer of zeste protein 3). GN EZ3 OR MEZ3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC TISSUE=Seed; RX MEDLINE=21948211; PubMed=11950982; RA Springer N.M., Danilevskaya O.N., Hermon P., Helentjaris T.G., RA Phillips R.L., Kaeppler H.F., Kaeppler S.M.; RT "Sequence relationships, conserved domains, and expression patterns RT for maize homologs of the Polycomb group genes E(z), esc, and E(Pc)."; RL Plant Physiol. 128:1332-1345(2002). CC -!- FUNCTION: Polycomb group (PcG) protein. PcG proteins act by CC forming multiprotein complexes, which are required to maintain the CC transcriptionally repressive state of homeotic genes throughout CC development. PcG proteins are not required to initiate repression, CC but to maintain it during later stages of development. They CC probably act via the methylation of histones, rendering chromatin CC heritably changed in its expressibility. Its sequence suggests CC that it may participate in a potential methyltransferase activity CC of PcG complexes (By similarity). CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- SIMILARITY: Belongs to the EZ family. CC -!- SIMILARITY: Contains 1 SANT domain. CC -!- SIMILARITY: Contains 1 SET domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF443598; AAM13422.1; -. DR MaizeDB; 754846; -. DR InterPro; IPR001005; Myb_DNA_binding. DR InterPro; IPR001214; SET. DR Pfam; PF00856; SET; 1. DR SMART; SM00717; SANT; 1. DR SMART; SM00317; SET; 1. DR PROSITE; PS50280; SET; 1. DR PROSITE; PS50090; MYB_3; FALSE_NEG. KW Transcription regulation; Repressor; Nuclear protein; KW Multigene family. FT DOMAIN 528 578 SANT. FT DOMAIN 746 866 SET. FT DOMAIN 650 719 Cys-rich. FT DOMAIN 75 78 Poly-Ala. SQ SEQUENCE 895 AA; 100392 MW; 2659DCF992A08919 CRC64; MASSSKASDS SSQRSKRSDQ GTGREAAPAS VVPIHGNLTQ LIRQIKSRRL LYIKEKLEAN RKTLQRHSCS LFDVAAAAEV ASRGSDGGNA LSQRAAEGQF RLAGSDLAHG IGERDVVYMQ EENLASGTLV LSSSGAAAQR TVVRFVKLPL VERIPPYTTW IFLDKNQRMA DDQSVVGRRR IYYDPVGNEA LICSDSDEEI PEPEEEKHFF TEGEDQLIWR ATQEHGLNRE VVNVLCQFID STPSEIEERS EVLFEKNEKN SGSSDKIERQ LSLDKTMDAV LDSFDNLFCR RCLVFDCRLH GCSQNLVFPT EKQPYSFEPD ENKKPCGRQC YLRWRGGFQE IHDVGLSGCA TYNMESGTVS HKVDVSIMSE SEDSNREKGN IRSMTLVGTS GSKIISSVSA EESTTPPSAD TSETENASSD MPPSSLRKYK ISKRGPRYRE RSPGKRQKVF TSDISFASNI LNKLSIPEIR DTRLESREPG GDKLQILDES TKKTSSKDIC GESPITTTEN MGIESKKVSS TKNFLEHTLS CWSALERDLY LKGIEIFGKN SCLIARNLLS GMKTCMEVAN YMYNNGAAMA KRPLLNKSIS GDFAETEQDY MEQDMVARTR IYRRRGRNRK LKYTWKSAGH PTVRKRIGDG KQWYTQYNPC VCQQMCGKDC PCVENGTCCE KYCGCSKSCK NKFRGCHCAK SQCRSRQCPC FAASRECDPD VCRNCWVSCG DGSLGEPPAR GDGYQCGNMK LLLKQQQRIL LGRSDVAGWG AFIKNPVNKN DYLGEYTGEL ISHKEADKRG KIYDRANSSF LFDLNDQYVL DAYRKGDKLK FANHSSNPNC YAKVMLVAGD HRVGIYAKEH IEASEELFYD YRYGPDQAPA WARRPEGSKK DEASVSHHRA HKVAR // ID FER1_MAIZE STANDARD; PRT; 150 AA. AC P27787; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Ferredoxin I, chloroplast precursor (Fd I). GN FDX1 OR PFD1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Hase T., Kimatsa Y., Yonekura K., Matsumura T., Sakakibara H.; RT "Molecular cloning and differential expression of the maize ferredoxin RT gene family."; RL Plant Physiol. 96:77-83(1991). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX MEDLINE=21109789; PubMed=11175898; RA Kurisu G., Kusunoki M., Katoh E., Yamazaki T., Teshima K., RA Onda Y., Kimata-Ariga Y., Hase T.; RT "Structure of the electron transfer complex between ferredoxin and RT ferredoxin-NADP+ reductase."; RL Nat. Struct. Biol. 8:117-121(2001). CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer CC electrons in a wide variety of metabolic reactions. CC -!- COFACTOR: Binds 1 2Fe-2S cluster. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M73829; AAA33459.1; -. DR EMBL; M73830; AAA33460.1; -. DR PIR; T03286; T03286. DR PDB; 1GAQ; 07-FEB-01. DR MaizeDB; 66392; -. DR InterPro; IPR006057; 2Fe2S. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR001041; Ferredoxin. DR Pfam; PF00111; fer2; 1. DR PRINTS; PR00159; 2FE2SFRDOXIN. DR PROSITE; PS00197; 2FE2S_FERREDOXIN; 1. KW Electron transport; Metal-binding; Iron-sulfur; Iron; 2Fe-2S; KW Chloroplast; Transit peptide; Multigene family; 3D-structure. FT TRANSIT 1 52 Chloroplast (By similarity). FT CHAIN 53 150 Ferredoxin I. FT METAL 91 91 Iron-sulfur (2Fe-2S). FT METAL 96 96 Iron-sulfur (2Fe-2S). FT METAL 99 99 Iron-sulfur (2Fe-2S). FT METAL 129 129 Iron-sulfur (2Fe-2S). FT STRAND 57 59 FT STRAND 66 66 FT HELIX 76 80 FT TURN 81 84 FT TURN 98 99 FT STRAND 101 102 FT STRAND 108 109 FT TURN 118 119 FT HELIX 120 123 FT STRAND 125 125 FT TURN 128 129 FT STRAND 132 133 FT STRAND 137 141 FT TURN 142 142 SQ SEQUENCE 150 AA; 15837 MW; 1AF43354A9BC1D3F CRC64; MATVLGSPRA PAFFFSSSSL RAAPAPTAVA LPAAKVGIMG RSASSRRRLR AQATYNVKLI TPEGEVELQV PDDVYILDQA EEDGIDLPYS CRAGSCSSCA GKVVSGSVDQ SDQSYLDDGQ IADGWVLTCH AYPTSDVVIE THKEEELTGA // ID FER3_MAIZE STANDARD; PRT; 152 AA. AC P27788; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Ferredoxin III, chloroplast precursor (Fd III). GN FDX3 OR PFD3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Hase T., Kimatsa Y., Yonekura K., Matsumura T., Sakakibara H.; RT "Molecular cloning and differential expression of the maize ferredoxin RT gene family."; RL Plant Physiol. 96:77-83(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=98061885; PubMed=9399441; RA Nakano R., Matsumura T., Sakakibara H., Sugiyama T., Hase T.; RT "Cloning of maize ferredoxin III gene: presence of a unique RT repetitive nucleotide sequence within an intron found in the RT 5'-untranslated region."; RL Plant Cell Physiol. 38:1167-1170(1997). CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer CC electrons in a wide variety of metabolic reactions. CC -!- COFACTOR: Binds 1 2Fe-2S cluster. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M73831; AAA33461.1; -. DR EMBL; AB001387; BAA19251.1; -. DR PIR; T02881; T02881. DR HSSP; P27320; 1DOX. DR MaizeDB; 66392; -. DR InterPro; IPR006057; 2Fe2S. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR001041; Ferredoxin. DR Pfam; PF00111; fer2; 1. DR PRINTS; PR00159; 2FE2SFRDOXIN. DR PROSITE; PS00197; 2FE2S_FERREDOXIN; 1. KW Electron transport; Metal-binding; Iron-sulfur; Iron; 2Fe-2S; KW Chloroplast; Transit peptide; Multigene family. FT TRANSIT 1 55 Chloroplast (By similarity). FT CHAIN 56 152 Ferredoxin III. FT METAL 95 95 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 100 100 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 103 103 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 133 133 Iron-sulfur (2Fe-2S) (By similarity). SQ SEQUENCE 152 AA; 16123 MW; 3D6CBC4B8238EFA0 CRC64; MSTSTFATSC TLLGNVRTTQ ASQTAVKSPS SLSFFSQVTK VPSLKTSKKL DVSAMAVYKV KLVGPEGEEH EFDAPDDAYI LDAAETAGVE LPYSCRAGAC STCAGKIESG SVDQSDGSFL DDGQQEEGYV LTCVSYPKSD CVIHTHKEGD LY // ID FER5_MAIZE STANDARD; PRT; 135 AA. AC P27789; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Ferredoxin V, chloroplast precursor (Fd V). GN FDX5 OR PFD5. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Hase T., Kimatsa Y., Yonekura K., Matsumura T., Sakakibara H.; RT "Molecular cloning and differential expression of the maize ferredoxin RT gene family."; RL Plant Physiol. 96:77-83(1991). CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer CC electrons in a wide variety of metabolic reactions. CC -!- COFACTOR: Binds 1 2Fe-2S cluster. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M73828; AAA33462.1; -. DR PIR; T03288; T03288. DR HSSP; P00221; 1A70. DR MaizeDB; 66392; -. DR InterPro; IPR006057; 2Fe2S. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR001041; Ferredoxin. DR Pfam; PF00111; fer2; 1. DR PRINTS; PR00159; 2FE2SFRDOXIN. DR PROSITE; PS00197; 2FE2S_FERREDOXIN; 1. KW Electron transport; Metal-binding; Iron-sulfur; Iron; 2Fe-2S; KW Chloroplast; Transit peptide; Multigene family. FT TRANSIT 1 38 Chloroplast (By similarity). FT CHAIN 39 135 Ferredoxin V. FT METAL 77 77 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 82 82 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 85 85 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 115 115 Iron-sulfur (2Fe-2S) (By similarity). SQ SEQUENCE 135 AA; 14399 MW; 8FA43C41AD4CB976 CRC64; MATVLSSPRA PAFSFSLRAA PATTVAMTRG ASSRLRAQAT YNVKLITPEG EVELQVPDDV YILDYAEEEG IDLPYSCRAG SCSSCAGKVV SGSLDQSDQS FLDDSQVADG WVLTCVAYPT SDVVIETHKE DDLIS // ID FIE1_MAIZE STANDARD; PRT; 461 AA. AC Q8VZY7; Q84YB5; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Polycomb group protein FIE1 (FERTILIZATION-INDEPENDENT ENDOSPERM 1). GN FIE1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Seed; RX MEDLINE=21948211; PubMed=11950982; RA Springer N.M., Danilevskaya O.N., Hermon P., Helentjaris T.G., RA Phillips R.L., Kaeppler H.F., Kaeppler S.M.; RT "Sequence relationships, conserved domains, and expression patterns RT for maize homologs of the Polycomb group genes E(z), esc, and E(Pc)."; RL Plant Physiol. 128:1332-1345(2002). RN [2] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RX MEDLINE=22454739; PubMed=12566582; RA Danilevskaya O.N., Hermon P., Hantke S., Muszynski M.G., Kollipara K., RA Ananiev E.V.; RT "Duplicated fie genes in maize: expression pattern and imprinting RT suggest distinct functions."; RL Plant Cell 15:425-438(2003). CC -!- FUNCTION: Polycomb group (PcG) protein. PcG proteins act by CC forming multiprotein complexes, which are required to maintain the CC transcriptionally repressive state of homeotic genes throughout CC development. PcG proteins are not required to initiate repression, CC but to maintain it during later stages of development. They CC probably act via the methylation of histones, rendering chromatin CC heritably changed in its expressibility (By similarity). CC -!- TISSUE SPECIFICITY: Specifically expressed in kernel starting from CC 6 days after pollination. CC -!- DEVELOPMENTAL STAGE: Expressed in embryo and endosperm. CC -!- SIMILARITY: Belongs to the WD-repeat ESC family. CC -!- SIMILARITY: Contains 6 WD repeats. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY061964; AAL35973.1; -. DR EMBL; AY150645; AAO26659.1; -. DR MaizeDB; 754919; -. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 4. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 6. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 2. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Transcription regulation; Repressor; Nuclear protein; KW Developmental protein; Repeat; WD repeat. FT REPEAT 143 186 WD 1. FT REPEAT 189 229 WD 2. FT REPEAT 235 275 WD 3. FT REPEAT 301 338 WD 4. FT REPEAT 351 391 WD 5. FT REPEAT 398 437 WD 6. FT CONFLICT 23 23 T -> P (in Ref. 2). FT CONFLICT 40 40 Q -> H (in Ref. 2). FT CONFLICT 447 450 Missing (in Ref. 2). SQ SEQUENCE 461 AA; 50573 MW; 6FE70DB4D32AE755 CRC64; MPPSKARRKR SLRDITATVA TGTVANSKPG SSSTNEGKQQ DKKKEGPQEP DIPPLPPVVV NIVPRQGLGC EVVEGLLVPS RKREYKPNSK YTVGNHPIYA IGFNFIDMRY YDVFAIASCN SVIIYRCLEN GGFGLLQNYV DEDKDESFYT LSWTIDQVDS SPLLVAAGSN RIIRVINCAT EKLDKSLVGH GGSIHEIRTH ASKPSLIISA SKDESIRLWN VHTGICILVF AGAGGHRHDV LSVDFHPTEV GIFASCGMDN TVKIWSMKEF WIYVEKSYSW TGHPSKFPTR NIQFPVLTAA VHSDYVDCTR WLGDFILSKS VKNAVLLWEP KPDKRRPGEG SVDVLQKYPV PKCSLWFMKF SCDFYSNQMA IGNNKGEIYV WEVQSSPPVL IDRLCNQECK SPIRQTAVSF DGSTILGAAD DGAIWRWDEV DPAASSSKPD QAAAPAAGVG AGAGADADAD A // ID FIE2_MAIZE STANDARD; PRT; 379 AA. AC Q8VZY6; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Polycomb group protein FIE2 (FERTILIZATION-INDEPENDENT ENDOSPERM 2). GN FIE2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RC TISSUE=Seed; RX MEDLINE=21948211; PubMed=11950982; RA Springer N.M., Danilevskaya O.N., Hermon P., Helentjaris T.G., RA Phillips R.L., Kaeppler H.F., Kaeppler S.M.; RT "Sequence relationships, conserved domains, and expression patterns RT for maize homologs of the Polycomb group genes E(z), esc, and E(Pc)."; RL Plant Physiol. 128:1332-1345(2002). RN [2] RP SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RX MEDLINE=22454739; PubMed=12566582; RA Danilevskaya O.N., Hermon P., Hantke S., Muszynski M.G., Kollipara K., RA Ananiev E.V.; RT "Duplicated fie genes in maize: expression pattern and imprinting RT suggest distinct functions."; RL Plant Cell 15:425-438(2003). CC -!- FUNCTION: Polycomb group (PcG) protein. PcG proteins act by CC forming multiprotein complexes, which are required to maintain the CC transcriptionally repressive state of homeotic genes throughout CC development. PcG proteins are not required to initiate repression, CC but to maintain it during later stages of development. They CC probably act via the methylation of histones, rendering chromatin CC heritably changed in its expressibility (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in the embryo sac CC before pollination. After pollination, its expression persists, CC predominantly in the embryo and at lower levels in the endosperm. CC -!- SIMILARITY: Belongs to the WD-repeat ESC family. CC -!- SIMILARITY: Contains 6 WD repeats. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY061965; AAL35974.1; -. DR EMBL; AY150644; AAO26658.1; -. DR MaizeDB; 754920; -. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 6. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 2. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Transcription regulation; Repressor; Nuclear protein; KW Repeat; WD repeat. FT REPEAT 85 128 WD 1. FT REPEAT 131 171 WD 2. FT REPEAT 177 217 WD 3. FT REPEAT 243 280 WD 4. FT REPEAT 292 333 WD 5. FT REPEAT 340 378 WD 6. SQ SEQUENCE 379 AA; 42502 MW; 714523B288285F29 CRC64; MAKLGPGQGL GCEAAEGSLV PSRKREYKPC GKHTEGKRPL YAIGFNFMDA RYYDVFATVG GNRVTTYRCL ENGSFALLQA YVDEDKDESF YTLSWARDHV DGSPLLVAAG SNGIIRVINC ATEKLAKSFV GHGDSINEIR TQPLKPSLII SASKDESVRL WNVHTGICIL IFAGAGGHRN EVLSVDFHPS DIERFASCGM DNTVKIWSMK EFWLYVDKSY SWTDLPSKFP TKYVQFPVLI AAVHSNYVDC TRWLGDFILS KSVDNEIVLW EPKTKEQSPG EGSIDILQKY PVPECDIWFI KFSCDFHFNQ LAIGNREGKI YVWEVQSSPP VLIARLYNQQ CKSPIRQTAV SFDGSTILGA GEDGTIWRWD EVDHPSSRN // ID FPPS_MAIZE STANDARD; PRT; 350 AA. AC P49353; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Farnesyl pyrophosphate synthetase (FPP synthetase) (FPS) (Farnesyl DE diphosphate synthetase) [Includes: Dimethylallyltransferase DE (EC 2.5.1.1); Geranyltranstransferase (EC 2.5.1.10)]. GN FPS. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; TISSUE=Endosperm; RX MEDLINE=96257218; PubMed=8666271; RA Li C.P., Larkins B.A.; RT "Identification of a maize endosperm-specific cDNA encoding farnesyl RT pyrophosphate synthetase."; RL Gene 171:193-196(1996). CC -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl CC pyrophosphate with the allylic pyrophosphates, dimethylallyl CC pyrophosphate, and then with the resultant geranylpyrophosphate to CC the ultimate product farnesyl pyrophosphate. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl CC diphosphate = diphosphate + geranyl diphosphate. CC -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate CC = diphosphate + trans,trans-farnesyl diphosphate. CC -!- PATHWAY: Isoprene biosynthesis, cholesterol biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L39789; AAB39276.1; -. DR PIR; T03291; T03291. DR HSSP; P08836; 1UBX. DR MaizeDB; 86802; -. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR008949; Terpenoid_synth. DR Pfam; PF00348; polyprenyl_synt; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHET_2; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHET_1; 1. KW Transferase; Isoprene biosynthesis; Cholesterol biosynthesis. SQ SEQUENCE 350 AA; 40013 MW; A606790FE79FC6C5 CRC64; MAAGGNGAGG DTRAAFARIY KTLKEELLTD PAFEFTEESR QWIDRMVDYN VLGGKCNRGL SVVDSYKLLK GADALGEEET FLACTLGWCI EWLQAFFLVL DDIMDDSHTR RGQPCWFRVP QVGLIAANDG IILRNHISRI LRRHFKGKPY YADLLDLFNE VEFKTASGQL LDLITTHEGE KDLTKYNITV HGRIVQYKTA YYSFYLPVAC ALLLSGENLD NYGDVENILV EMGTYFQVQD DYLDCYGDPE FIGKIGTDIE DYKCSWLVVQ ALERADESQK RILFENYGKK DPACVAKVKN LYKELDLEAV FQEYENESYK KLIADIEAQP SIAVQKVLKS FLHKIYKRQK // ID FRI1_MAIZE STANDARD; PRT; 254 AA. AC P29036; Q43258; DT 01-DEC-1992 (Rel. 24, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ferritin 1, chloroplast precursor (ZmFer1). GN FER1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 47-75. RC STRAIN=cv. Missouri 17; TISSUE=Root, and Seed; RX MEDLINE=92329717; PubMed=1627771; RA Lobreaux S., Massenet O., Briat J.-F.; RT "Iron induces ferritin synthesis in maize plantlets."; RL Plant Mol. Biol. 19:563-575(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; TISSUE=Seedling; RX MEDLINE=95377290; PubMed=7649160; RA Fobis-Loisy I., Loridon K., Lobreaux S., Lebrun M., Briat J.-F.; RT "Structure and differential expression of two maize ferritin genes in RT response to iron and abscisic acid."; RL Eur. J. Biochem. 231:609-619(1995). CC -!- FUNCTION: Ferritin is an intracellular molecule that stores iron CC in a soluble, nontoxic, readily available form. The functional CC molecule, which is composed of 24 chains, is roughly spherical and CC contains a central cavity into which the polymeric ferric iron CC core is deposited. CC -!- SUBCELLULAR LOCATION: Chloroplast and other plastids. CC -!- TISSUE SPECIFICITY: Ferritins accumulate in seed during CC maturation. Then, they are degraded during the first days of CC germination. Present in roots and leaves after iron treatment. CC -!- INDUCTION: By iron. CC -!- SIMILARITY: Belongs to the ferritin family. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61391; CAA43663.1; ALT_INIT. DR EMBL; X83076; CAA58146.1; -. DR PIR; S22498; S22498. DR HSSP; P07229; 1BG7. DR MaizeDB; 25278; -. DR InterPro; IPR001519; Ferritin. DR InterPro; IPR008331; Ferritin_Dps. DR InterPro; IPR009040; Ferritin_like. DR Pfam; PF00210; ferritin; 1. DR ProDom; PD000971; Ferritin; 1. DR PROSITE; PS00540; FERRITIN_1; 1. DR PROSITE; PS00204; FERRITIN_2; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. KW Iron storage; Iron; Metal-binding; Chloroplast; Transit peptide. FT TRANSIT 1 46 Chloroplast. FT CHAIN 47 254 Ferritin 1. FT DOMAIN 47 83 Extension peptide (EP). FT DOMAIN 84 237 Ferritin-like diiron. FT METAL 101 101 Iron (By similarity). FT METAL 135 135 Iron (By similarity). FT METAL 136 136 Iron (By similarity). FT METAL 138 138 Iron (By similarity). FT METAL 139 139 Iron (By similarity). FT METAL 185 185 Iron (By similarity). FT CONFLICT 32 32 Missing (in Ref. 2). FT CONFLICT 214 214 E -> D (in Ref. 2). FT CONFLICT 220 220 G -> V (in Ref. 2). SQ SEQUENCE 254 AA; 28025 MW; 7B74EBB843DBA28D CRC64; MMLRVSPSPA AAVPTQLSGA PATPAPVVRV AAPRGVASPS AGAACRAAGK GKEVLSGVVF QPFEEIKGEL ALVPQSPDKS LARHKFVDDC EAALNEQINV EYNASYAYHS LFAYFDRDNV ALKGFAKFFK ESSDEEREHA EKLMEYQNKR GGRVRLQSIV TPLTEFDHPE KGDALYAMEL ALALEKLVNE KLHNLHGVAT RCNDPQLTDF IESEFLEEQG EAINKISKYV AQLRRVGKGH GVWHFDQMLL EEEA // ID FRI2_MAIZE STANDARD; PRT; 252 AA. AC P29390; Q43259; DT 01-DEC-1992 (Rel. 24, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ferritin 2, chloroplast precursor (ZmFer2). GN FER2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 44-72. RC STRAIN=cv. Missouri 17; TISSUE=Root, and Seed; RX MEDLINE=92329717; PubMed=1627771; RA Lobreaux S., Massenet O., Briat J.-F.; RT "Iron induces ferritin synthesis in maize plantlets."; RL Plant Mol. Biol. 19:563-575(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Seedling; RX MEDLINE=95377290; PubMed=7649160; RA Fobis-Loisy I., Loridon K., Lobreaux S., Lebrun M., Briat J.-F.; RT "Structure and differential expression of two maize ferritin genes in RT response to iron and abscisic acid."; RL Eur. J. Biochem. 231:609-619(1995). CC -!- FUNCTION: Ferritin is an intracellular molecule that stores iron CC in a soluble, nontoxic, readily available form. The functional CC molecule, which is composed of 24 chains, is roughly spherical and CC contains a central cavity into which the polymeric ferric iron CC core is deposited. CC -!- SUBCELLULAR LOCATION: Chloroplast and other plastids. CC -!- TISSUE SPECIFICITY: Ferritins accumulate in seed during CC maturation. Then, they are degraded during the first days of CC germination. Present in roots and leaves after iron treatment. CC -!- INDUCTION: By iron. CC -!- SIMILARITY: Belongs to the ferritin family. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61392; CAA43664.1; ALT_INIT. DR EMBL; X83077; CAA58147.1; -. DR PIR; S24057; S24057. DR HSSP; P07229; 1BG7. DR MaizeDB; 25278; -. DR InterPro; IPR001519; Ferritin. DR InterPro; IPR008331; Ferritin_Dps. DR InterPro; IPR009040; Ferritin_like. DR Pfam; PF00210; ferritin; 1. DR ProDom; PD000971; Ferritin; 1. DR PROSITE; PS00540; FERRITIN_1; 1. DR PROSITE; PS00204; FERRITIN_2; FALSE_NEG. DR PROSITE; PS50905; FERRITIN_LIKE; 1. KW Iron storage; Iron; Metal-binding; Chloroplast; Transit peptide. FT TRANSIT 1 43 Chloroplast. FT CHAIN 44 252 Ferritin 2. FT DOMAIN 44 80 Extension peptide (EP). FT DOMAIN 81 234 Ferritin-like diiron. FT METAL 98 98 Iron (By similarity). FT METAL 132 132 Iron (By similarity). FT METAL 133 133 Iron (By similarity). FT METAL 135 135 Iron (By similarity). FT METAL 136 136 Iron (By similarity). FT METAL 182 182 Iron (By similarity). FT CONFLICT 217 217 G -> V (in Ref. 2). FT CONFLICT 251 251 A -> G (in Ref. 2). SQ SEQUENCE 252 AA; 27749 MW; D181B4A8A86ADED0 CRC64; MMLRVSSSPA AAVANHLSGG AAATTAPARV TAQRSGVSLS AAAAAGKGKE VLSGVVFQPF EEIKGELALV PQSPDRSLAR HKFVDDCEAA INEQINVEYN ASYAYHSLFA YFDRDNVALK GFAKFFKESS DEEREHAEKL MEYQNKRGGR VRLQSIVAPL TEFDHPEKGD ALYAMELTLA LEKLVNEKLH SLHGVATRCN DPQLIDFIES EFLEEQGEAI NKVSKYVAQL RRVGNKGHGV WHFDQMLLQE AA // ID FTRC_MAIZE STANDARD; PRT; 152 AA. AC P41347; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Ferredoxin-thioredoxin reductase catalytic chain, chloroplast DE precursor (EC 1.18.-.-) (FTR-C) (Ferredoxin-thioredoxin reductase DE subunit B) (FTR-B). GN FTRC. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94002243; PubMed=7916641; RA Marc-Martin S., Spielmann A., Stutz E., Schuermann P.; RT "Cloning and sequencing of a corn (Zea mays) nuclear gene coding for RT the chloroplast specific catalytic subunit of ferredoxin-thioredoxin RT reductase."; RL Biochim. Biophys. Acta 1183:207-209(1993). CC -!- FUNCTION: FTR is a [4Fe-4S] protein playing a central role in the CC ferredoxin/thioredoxin regulatory chain. It converts an electron CC signal (photoreduced ferredoxin) to a thiol signal (reduced CC thioredoxin) in the regulation of enzymes by reduction of specific CC disulfide groups. Catalyzes the light-dependent activation of CC several photosynthetic enzymes. CC -!- SUBUNIT: Heterodimer of subunit A (variable subunit) and subunit B CC (catalytic subunit). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X73549; -; NOT_ANNOTATED_CDS. DR MaizeDB; 61547; -. DR InterPro; IPR004209; FeThRed_beta. DR Pfam; PF02943; FeThRed_B; 1. KW Oxidoreductase; Iron-sulfur; 4Fe-4S; Chloroplast; Transit peptide. FT TRANSIT 1 38 Chloroplast (By similarity). FT CHAIN 39 152 Ferredoxin-thioredoxin reductase FT catalytic chain. FT METAL 91 91 Iron-sulfur (4Fe-4S) (By similarity). FT DISULFID 93 123 Redox-active (By similarity). FT METAL 110 110 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 112 112 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 121 121 Iron-sulfur (4Fe-4S) (By similarity). SQ SEQUENCE 152 AA; 16740 MW; 09618B305C682DFD CRC64; MTSTVTTTVG CGGLPVRPLS TATRGRPRRC AVRAQAAGAD ASNDKSVEVM RKFSEQYARR SNTFFCADKT VTAVVIKGLA DHRDTLGAPL CPCRHYDDKA AEVAQGFWNC PCVPMRERKE CHCMLFLTPD NDFAGKDQVI SFEEIKEATS KF // ID FTRV_MAIZE STANDARD; PRT; 97 AA. AC P80680; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Ferredoxin-thioredoxin reductase, variable chain (FTR-V) (Ferredoxin- DE thioredoxin reductase subunit A) (FTR-A). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Leaf; RX MEDLINE=97054599; PubMed=8898896; RA Iwadate H., Tsugita A., Chow L.-P., Kizuki K., Stritt-Etter A.-L., RA Li J., Schuermann P.; RT "Amino acid sequence of the maize ferredoxin:thioredoxin reductase RT variable subunit."; RL Eur. J. Biochem. 241:121-125(1996). CC -!- FUNCTION: FTR is a [4Fe-4S] protein playing a central role in the CC ferredoxin/thioredoxin regulatory chain. It converts an electron CC signal (photoreduced ferredoxin) to a thiol signal (reduced CC thioredoxin) in the regulation of enzymes by reduction of specific CC disulfide groups. Catalyzes the light-dependent activation of CC several photosynthetic enzymes. CC -!- SUBUNIT: Heterodimer of subunit A (variable subunit) and subunit CC B (catalytic subunit). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: To spinach and Synechococcus sp. FTR-V. DR PIR; JT0703; JT0703. DR MaizeDB; 134030; -. DR InterPro; IPR008990; E_transp_acc. DR InterPro; IPR004207; FeThRed_alpha. DR Pfam; PF02941; FeThRed_A; 1. KW Oxidoreductase; Chloroplast. SQ SEQUENCE 97 AA; 10886 MW; DE1ED2AEE76B0FF5 CRC64; EVASDDVAAE EAAAAPKIGR RVRVTAPLRV YHVLKAPDLD IQGMEGVVKQ YVCVWKGKRV TANFPFKVEF ELAVEGQPKP VRFFAHLRED EFEFVDG // ID G3PA_MAIZE STANDARD; PRT; 403 AA. AC P09315; P15985; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase A, chloroplast precursor DE (EC 1.2.1.13) (NADP-dependent glyceraldehydephosphate dehydrogenase DE subunit A). GN GAPA OR GPA1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90133970; PubMed=2515291; RA Quigley F., Brinkmann H., Martin W.F., Cerff R.; RT "Strong functional GC pressure in a light-regulated maize gene RT encoding subunit GAPA of chloroplast glyceraldehyde-3-phosphate RT dehydrogenase: implications for the evolution of GAPA pseudogenes."; RL J. Mol. Evol. 29:412-421(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88190130; PubMed=3357887; RA Quigley F., Martin W.F., Cerff R.; RT "Intron conservation across the prokaryote-eukaryote boundary: RT structure of the nuclear gene for chloroplast RT glyceraldehyde-3-phosphate dehydrogenase from maize."; RL Proc. Natl. Acad. Sci. U.S.A. 85:2672-2676(1988). RN [3] RP SEQUENCE OF 1-125 AND 301-403 FROM N.A. RC STRAIN=cv. W64 X W128E; TISSUE=Leaf; RA Gowri G., Campbell W.H.; RT "cDNA clones for corn leaf NADH: nitrate reductase and chloroplast RT NAD(P)(+): glyceraldehyde-3-phosphate dehydrogenase."; RL Plant Physiol. 90:792-798(1989). CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NADP(+) = 3-phospho-D-glyceroyl phosphate + NADPH. CC -!- PATHWAY: Calvin cycle. CC -!- SUBUNIT: Tetramer of either four A chains (GAPDH 2) or two A and CC two B chains (GAPDH 1) (By similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- MISCELLANEOUS: Plants contain three forms of GAPDH: a cytosolic CC form which participates in glycolysis and two chloroplast forms CC which participates in photosynthesis. These three forms are CC encoded by distinct genes. CC -!- SIMILARITY: Belongs to the glyceraldehyde 3-phosphate CC dehydrogenase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15408; CAA33455.1; -. DR EMBL; M18976; AAA33464.1; -. DR EMBL; M31481; AAA33484.1; -. DR EMBL; M31483; AAA33485.1; -. DR PIR; A30890; DEZMG3. DR HSSP; P50362; 1NLG. DR MaizeDB; 13872; -. DR InterPro; IPR000173; GAP_dhdrogenase. DR InterPro; IPR006424; GAPDH-I. DR Pfam; PF00044; gpdh; 1. DR Pfam; PF02800; gpdh_C; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. KW Calvin cycle; Oxidoreductase; NADP; Transit peptide; Chloroplast; KW Multigene family. FT TRANSIT 1 66 Chloroplast. FT CHAIN 67 403 Glyceraldehyde 3-phosphate dehydrogenase FT A. FT BINDING 220 220 Glyceraldehyde 3-phosphate. FT ACT_SITE 247 247 Activates thiol group during catalysis. SQ SEQUENCE 403 AA; 42866 MW; 0505124C3F458DD8 CRC64; MASSMLSATT VPLQQGGGLS EFSGLRSSAS LPMRRNATSD DFMSAVSFRT HAVGTSGGPR RAPTEAKLKV AINGFGRIGR NFLRCWHGRG DASPLDVIAI NDTGGVKQAS HLLKYDSTLG IFDADVKPVG DNAISVDGKV IKVVSDRNPS NLPWGELGID LVIEGTGVFV DREGAGKHIQ AGAKKVLITA PGKGDIPTYV VGVNADQYNP DEPIISNASC TTNCLAPFVK VLDQKFGIIK GTMTTTHSYT GDQRLLDASH RDLRRARAAA LNIVPTSTGA AKAVSLVLPN LKGKLNGIAL RVPTPNVSVV DLVVQVSKKT LAEEVNQAFR DAAANELTGI LEVCDVPLVS VDFRCSDVSS TIDASLTMVM GDDMVKVISW YDNEWGYSQR VVDLADICAN QWK // ID G3PC_MAIZE STANDARD; PRT; 337 AA. AC P08735; DT 01-AUG-1988 (Rel. 08, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Glyceraldehyde 3-phosphate dehydrogenase, cytosolic 1 (EC 1.2.1.12). GN GAPC1 OR GAPC OR GPC1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=90040690; PubMed=2810356; RA Martinez P., Martin W.F., Cerff R.; RT "Structure, evolution and anaerobic regulation of a nuclear gene RT encoding cytosolic glyceraldehyde-3-phosphate dehydrogenase from RT maize."; RL J. Mol. Biol. 208:551-565(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88230473; PubMed=3131533; RA Brinkmann H., Martinez P., Quigley F., Martin W.F., Cerff R.; RT "Endosymbiotic origin and codon bias of the nuclear gene for RT chloroplast glyceraldehyde-3-phosphate dehydrogenase from maize."; RL J. Mol. Evol. 26:320-328(1987). CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH. CC -!- PATHWAY: Second phase of glycolysis; first step. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- MISCELLANEOUS: Plants contain three forms of GAPDH: a cytosolic CC form which participates in glycolysis and two chloroplast forms CC which participates in photosynthesis. These three forms are CC encoded by distinct genes. CC -!- SIMILARITY: Belongs to the glyceraldehyde 3-phosphate CC dehydrogenase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07156; CAA30151.1; -. DR EMBL; X15596; CAA33620.1; -. DR PIR; S00354; DEZMGC. DR HSSP; P56649; 1DSS. DR MaizeDB; 13873; -. DR InterPro; IPR000173; GAP_dhdrogenase. DR InterPro; IPR006424; GAPDH-I. DR Pfam; PF00044; gpdh; 1. DR Pfam; PF02800; gpdh_C; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR TIGRFAMs; TIGR01534; GAPDH-I; 1. DR PROSITE; PS00071; GAPDH; 1. KW Glycolysis; Oxidoreductase; NAD; Multigene family. FT DOMAIN 1 151 BINDING TO NAD. FT DOMAIN 152 337 Catalytic. FT BINDING 154 154 Glyceraldehyde 3-phosphate. FT ACT_SITE 181 181 Activates thiol group during catalysis. FT CONFLICT 336 336 T -> S (in Ref. 2). SQ SEQUENCE 337 AA; 36522 MW; E18F580F09FDC07B CRC64; MGKIKIGING FGRIGRLVAR VALQSEDVEL VAVNDPFITT DYMTYMFKYD TVHGHWKHSD ITLKDSKTLL FGDKPVTVFG IRNPEEIPWG EAGAEYVVES TGVFTDKDKA AAHLKGGAKK VVISAPSKDA PMFVVGVNED KYTSDVNIVS NASCTTNCLA PLAKVIHDNF GIVEGLMTTV HAITATQKTV DGPSAKDWRG GRAASFNIIP SSTGAAKAVG KVLPDLNGKL TGMSFRVPTV DVSVVDLTVR IEKGASYEDI KKAIKAASEG PLKGIMGYVE EDLVSTDFLG DSRSSIFDAK AGIALNDHFV KLVSWYDNEW GYSNRVVDLI RHMFKTQ // ID G6PD_MAIZE STANDARD; PRT; 15 AA. AC P80619; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform (EC 1.1.1.49) DE (G6PD) (2D-page of etiolated coleoptile spot 243) (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = D-glucono- CC 1,5-lactone 6-phosphate + NADPH. CC -!- PATHWAY: Pentose phosphate pathway; first step. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase CC family. DR Maize-2DPAGE; P80619; COLEOPTILE. DR MaizeDB; 123946; -. DR PROSITE; PS00069; G6P_DEHYDROGENASE; PARTIAL. KW Glucose metabolism; Oxidoreductase; NADP. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1739 MW; 02038EE7471AE038 CRC64; XGRNEFVIRL QXSEA // ID G6PI_MAIZE STANDARD; PRT; 567 AA. AC P49105; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Glucose-6-phosphate isomerase, cytosolic (EC 5.3.1.9) (GPI) DE (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI). GN PHI1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Root; RX MEDLINE=95357418; PubMed=7630947; RA Lal S.K., Sachs M.M.; RT "Cloning and characterization of an anaerobically induced cDNA RT encoding glucose-6-phosphate isomerase from maize."; RL Plant Physiol. 108:1295-1296(1995). CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6- CC phosphate. CC -!- PATHWAY: Involved in glycolysis and in gluconeogenesis. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the GPI family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U17225; AAA82734.1; -. DR PIR; T02094; T02094. DR HSSP; Q9N1E2; 1HOX. DR MaizeDB; 13859; -. DR InterPro; IPR001672; G6P_Isomerase. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. KW Gluconeogenesis; Glycolysis; Isomerase. FT ACT_SITE 391 391 By similarity. FT ACT_SITE 516 516 By similarity. SQ SEQUENCE 567 AA; 62237 MW; EC135C89DAADACF2 CRC64; MASAALICGT EQWKALQAHV GAIQKTHLRD LMADADRCKA MTAEYEGIFL DYSRQQATGE TMEKLLKLAD AAKLKEKIEK MFKGEKINST ENRSVLHVAL RAPRDAVINS DGVNVVPEVW SVKDKIKQFS ETFRSGSWVG ATGKPLTNVV SVGIGGSFLG PLFVHTALQT DPEAAECAKG RQLRFLANVD PVDVARSIKD LDPETTLVVV VSKTFTTAET MLNARTLKEW IVSSLGPQAV AKHMIAVSTN LKLVKEFGID PNNAFAFWDW VGGRYSVCSA VGVLPLSLQY GFPIVQKFLE GASSIDNHFY SSSFEKNIPV LLGLLSVWNV SFLGYPARAI LPYSQALEKL APHIQQLSME SNGKGVSIDG AQLSFETGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGV VKSQQPVYLK GETVSNHDEL MSNFFAQPDA LAYGKTPEQL HSEKVPENLI PHKTFKGNRP SLSLLLPTLS AYEVGQLLSI YEHRIAVQGF IWGINSFDQW GVELGKSLAS QVRKQLHGTR MEGKPVEGFN HSTSSLLARY LAVKPSTPYD TTVLPKV // ID GAPN_MAIZE STANDARD; PRT; 498 AA. AC Q43272; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.9) DE (Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase) DE (Glyceraldehyde-3-phosphate dehydrogenase [NADP+]) (Triosephosphate DE dehydrogenase). GN GPN1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. KW5330; TISSUE=Shoot; RX MEDLINE=94180387; PubMed=7545914; RA Habenicht A., Hellman U., Cerff R.; RT "Non-phosphorylating GAPDH of higher plants is a member of the RT aldehyde dehydrogenase superfamily with no sequence homology to RT phosphorylating GAPDH."; RL J. Mol. Biol. 237:165-171(1994). CC -!- FUNCTION: Important as a means of generating NADPH for CC biosynthetic reactions. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + NADP(+) + H(2)O CC = 3-phospho-D-glycerate + NADPH. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75326; CAA53075.1; -. DR PIR; S43833; S43833. DR HSSP; P51977; 1BXS. DR MaizeDB; 78926; -. DR InterPro; IPR002086; Aldehyde_dehydr. DR Pfam; PF00171; aldedh; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. KW Oxidoreductase; NADP. FT NP_BIND 247 251 NAD (ADP part) (By similarity). FT ACT_SITE 266 266 By similarity. FT ACT_SITE 300 300 By similarity. SQ SEQUENCE 498 AA; 53146 MW; 7AF1C0DACAB4EE39 CRC64; MALAGTGVFA EILDGEVYRY YADGEWRTSA SGKSVAIVNP TTRKTQYRVQ ACTQEEVNKA MDAAKVAQKA WARTPLWKRA DVLHKAAAIL KEHKAPIAEC LVKEIAKPAK DAVSEVVRSG DLVSYTAEEG VRILGEGKLV VSDSFPGNER NKYCLSSKIP LGVVLAIPPF NYPANLAGSK IGPALIAGNA LVLKPPTQGA VAALHMVHCF HLAGFPKGLI SCVTGKGSEI GDFLTMHPGV NCISFTGGDT GIAISKKAGM VPLQMELGGK DACIVLEDAD LDLVSANIVK GGFSYSGQRC TAVKVVLIME SIADAVVQKV NAKLAKLKVG PPEDDSDITP VVTESSANFI EGLVMDAKEK GATFCQEYRR EGNLIWPLLL DHVRPDMRIA WEEPFGPVLP VIRINSVEEG IHHCNASNFG LQGCIFTRDI NKAILISDAM ETGTVQINSA PARGPDHFSF QGLKDSGIGS QGITNSINMM TKVKSTVINL PSPSYTMG // ID GBB_MAIZE STANDARD; PRT; 380 AA. AC P49178; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Guanine nucleotide-binding protein beta subunit. GN GB1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95023950; PubMed=7937804; RA Weiss C.A., Garnaat C.W., Mukai K., Hu Y., Ma H.; RT "Isolation of cDNAs encoding guanine nucleotide-binding protein beta- RT subunit homologues from maize (ZGB1) and Arabidopsis (AGB1)."; RL Proc. Natl. Acad. Sci. U.S.A. 91:9554-9558(1994). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are CC involved as a modulator or transducer in various transmembrane CC signaling systems. The beta and gamma chains are required for the CC GTPase activity, for replacement of GDP by GTP, and for G protein- CC effector interaction. CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and CC gamma. CC -!- TISSUE SPECIFICITY: Present in the root, leaf and tassel. CC -!- SIMILARITY: Contains 7 WD repeats. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U12233; AAA50446.1; -. DR PIR; T02085; T02085. DR HSSP; P04901; 1TBG. DR MaizeDB; 105669; -. DR InterPro; IPR001632; Gprotein_B. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00319; GPROTEINB. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 4. DR SMART; SM00320; WD40; 7. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Transducer; Repeat; WD repeat. FT REPEAT 64 94 WD 1. FT REPEAT 106 136 WD 2. FT REPEAT 155 186 WD 3. FT REPEAT 203 234 WD 4. FT REPEAT 247 277 WD 5. FT REPEAT 296 326 WD 6. FT REPEAT 342 372 WD 7. SQ SEQUENCE 380 AA; 41714 MW; 7D5DC5276C33DD1E CRC64; MASVAELKEK HAAATASVNS LRERLRQRRE TLLDTDVARY SKSQGRVPVS FNPTDLVCCR TLQGHSGKVY SLDWTPEKNW IVSASQDGRL IVWNALTSQK THAIKLHCPW VMACAFAPNG QSVACGGLDS ACSIFNLNSQ ADRDGNMPVS RILTGHKGYV SSCQYVPDQE TRLITSSGDQ TCVLWDVTTG QRISIFGGEF PSGHTADVQS VSINSSNTNM FVSGSCDTTV RLWDIRIASR AVRTYHGHED DVNSVKFFPD GHRFGTGSDD GTCRLFDMRT GHQLQVYSRE PDRNSNELPT VTSIAFSISG RLLFAGYSNG DCYVWDTLLA EVVLNLGNLQ NSHDGRISCL GMSSDGSALC TGSWDKNLKI WAFSGHRKIV // ID GLB1_MAIZE STANDARD; PRT; 573 AA. AC P15590; DT 01-APR-1990 (Rel. 14, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Globulin-1 S allele precursor (GLB1-S) (7S-like). GN GLB1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Va26; RA Belanger F.C., Kriz A.L.; RT "Molecular characterization of the major maize embryo globulin encoded RT by the Glb1 gene."; RL Plant Physiol. 91:636-643(1989). RN [2] RP SEQUENCE OF 87-100. RX MEDLINE=89374022; PubMed=2775172; RA Kriz A.L.; RT "Characterization of embryo globulins encoded by the maize Glb RT genes."; RL Biochem. Genet. 27:239-251(1989). CC -!- PTM: Three protein-processing steps occur in the formation of the CC mature protein from the primary translation product. CC -!- POLYMORPHISM: The three most commonly occurring GLB1 alleles have CC the designation L, I, and S for large, intermediate, and small CC proteins, respectively. CC -!- SIMILARITY: Belongs to the 7S seed storage protein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24845; AAA33467.1; -. DR HSSP; P02853; 2PHL. DR MaizeDB; 30181; -. DR InterPro; IPR006045; Cupin. DR Pfam; PF00190; Cupin; 2. KW Seed storage protein; Signal. FT SIGNAL 1 18 Or 21 (Potential). FT PROPEP 19 86 FT CHAIN 87 573 Globulin-1 S allele. FT CARBOHYD 349 349 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 573 AA; 65029 MW; 525ED1D00A062976 CRC64; MVSARIVVLL AVLLCAAAAV ASSWEDDNHH HHGGHKSGRC VRRCEDRPWH QRPRCLEQCR EEEREKRQER SRHEADDRSG EGSSEDERER EQEKEEKQKD RRPYVFDRRS FRRVVRSEQG SLRVLRPFDE VSRLLRGIRD YRVAVLEANP RSFVVPSHTD AHCIGYVAEG EGVVTTIENG ERRSYTIKQG HVFVAPAGAV TYLANTDGRK KLVITKILHT ISVPGEFQFF FGPGGRNPES FLSSFSKSIQ RAAYKTSSDR LERLFGRHGQ DKGIIVRATE EQTRELRRHA SEGGHGPHWP LPPFGESRGP YSLLDQRPSI ANQHGQLYEA DARSFHDLAE HDVSVSFANI TAGSMSAPLY NTRSFKIAYV PNGKGYAEIV CPHRQSQGGE SERERGKGRR SEEEEESSEE QEEVGQGYHT IRARLSPGTA FVVPAGHPFV AVASRDSNLQ IVCFEVHADR NEKVFLAGAD NVLQKLDRVA KALSFASKAE EVDEVLGSRR EKGFLPGPKE SGGHEEREQE EEEREERHGG RGERERHGRE EREKEEEERE GRHGRGRREE VAETLLRMVT ARM // ID GLG1_MAIZE STANDARD; PRT; 516 AA. AC P55241; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplast DE precursor (EC 2.7.7.27) (ADP-glucose synthase) (ADP-glucose DE pyrophosphorylase) (AGPASE S) (Alpha-D-glucose-1-phosphate adenyl DE transferase) (Shrunken-2). GN SH2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93044496; PubMed=1967077; RA Bhave M.R., Lawrence S., Barton C., Hannah L.C.; RT "Identification and molecular characterization of shrunken-2 cDNA RT clones of maize."; RL Plant Cell 2:581-588(1990). RN [2] RP REVISIONS, AND SEQUENCE FROM N.A. RC STRAIN=cv. Black Mexican Sweet; TISSUE=Leaf; RA Hannah L.C., Shaw J.R.; RT "Genomic nucleotide sequence of a wild-type shrunken-2 allele of Zea RT mays."; RL Plant Physiol. 98:1214-1216(1992). RN [3] RP CHARACTERIZATION. RX MEDLINE=94261107; PubMed=8202085; RA Giroux M.J., Hannah L.C.; RT "ADP-glucose pyrophosphorylase in shrunken-2 and brittle-2 mutants of RT maize."; RL Mol. Gen. Genet. 243:400-408(1994). CC -!- FUNCTION: This protein plays a role in synthesis of starch. It CC catalyzes the synthesis of the activated glycosyl donor, ADP- CC glucose from Glc-1-P and ATP. CC -!- CATALYTIC ACTIVITY: ATP + alpha-D-glucose 1-phosphate = CC diphosphate + ADP-glucose. CC -!- ENZYME REGULATION: Activated by 3'phosphoglycerate, inhibited by CC orthophosphate. Allosteric regulation. CC -!- PATHWAY: Starch biosynthesis. CC -!- SUBUNIT: Heterotetramer. CC -!- SUBCELLULAR LOCATION: Chloroplasts of leaves and amyloplasts of CC developing endosperm. CC -!- TISSUE SPECIFICITY: Endosperm. CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate CC adenylyltransferase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S48563; AAB24191.2; ALT_INIT. DR EMBL; M81603; AAB52952.1; -. DR MaizeDB; 85022; -. DR InterPro; IPR005836; ADP_Glu_pyroP. DR InterPro; IPR005835; NTP_transferase. DR Pfam; PF00483; NTP_transferase; 1. DR PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1. DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1. DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1. KW Transferase; Nucleotidyltransferase; Multigene family; KW Starch biosynthesis; Allosteric enzyme; Amyloplast; Chloroplast; KW Transit peptide. FT TRANSIT 1 45 Chloroplast (Potential). FT CHAIN 46 516 Glucose-1-phosphate adenylyltransferase FT large subunit 1. FT CONFLICT 436 436 T -> I (in Ref. 1). FT CONFLICT 454 454 V -> I (in Ref. 1). FT CONFLICT 495 514 Missing (in Ref. 1). SQ SEQUENCE 516 AA; 57071 MW; B9B517905C4B0705 CRC64; MQFALALDTN SGPHQIRSCE GDGIDRLEKL SIGGRKQEKA LRNRCFGGRV AATTQCILTS DACPETLHSQ TQSSRKNYAD ANRVSAIILG GGTGSQLFPL TSTRATPAVP VGGCYRLIDI PMSNCFNSGI NKIFVMSQFN STSLNRHIHR TYLEGGINFA DGSVQVLAAT QMPEEPAGWF QGTADSIRKF IWVLEDYYSH KSIDNIVILS GDQLYRMNYM ELVQKHVEDD ADITISCAPV DESRASKNGL VKIDHTGRVL QFFEKPKGAD LNSMRVETNF LSYAIDDAQK YPYLASMGIY VFKKDALLDL LKSKYTQLHD FGSEILPRAV LDHSVQACIF TGYWEDVGTI KSFFDANLAL TEQPSKFDFY DPKTPFFTAP RCLPPTQLDK CKMKYAFISD GCLLRECNIE HSVIGVCSRV SSGCELKDSV MMGADTYETE EEASKLLLAG KVPVGIGRNT KIRNCIIDMN ARIGKNVVIT NSKGIQEADH PEEGYYIRSG IVVILKNATI NDGSVI // ID GLG2_MAIZE STANDARD; PRT; 521 AA. AC P55234; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Glucose-1-phosphate adenylyltransferase large subunit 2, chloroplast DE precursor (EC 2.7.7.27) (ADP-glucose synthase) (ADP-glucose DE pyrophosphorylase) (AGPASE S) (Alpha-D-glucose-1-phosphate adenyl DE transferase). GN AGP2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; TISSUE=Ear; RX MEDLINE=95357437; PubMed=7630966; RA Giroux M., Smith-White B., Gilmore V., Hannah L.C., Preiss J.; RT "The large subunit of the embryo isoform of ADP glucose RT pyrophosphorylase from maize."; RL Plant Physiol. 108:1333-1334(1995). CC -!- FUNCTION: This protein plays a role in synthesis of starch. It CC catalyzes the synthesis of the activated glycosyl donor, ADP- CC glucose from Glc-1-P and ATP. CC -!- CATALYTIC ACTIVITY: ATP + alpha-D-glucose 1-phosphate = CC diphosphate + ADP-glucose. CC -!- ENZYME REGULATION: Activated by 3'phosphoglycerate, inhibited by CC orthophosphate. Allosteric regulation. CC -!- PATHWAY: Starch biosynthesis. CC -!- SUBUNIT: Heterotetramer. CC -!- SUBCELLULAR LOCATION: Chloroplasts of leaves and amyloplasts of CC developing endosperm (By similarity). CC -!- TISSUE SPECIFICITY: Abundant in the embryo and is also present in CC the endosperm. CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate CC adenylyltransferase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z38111; CAA86227.1; -. DR PIR; S49439; S49439. DR MaizeDB; 113181; -. DR InterPro; IPR005836; ADP_Glu_pyroP. DR InterPro; IPR005835; NTP_transferase. DR Pfam; PF00483; NTP_transferase; 1. DR PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1. DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1. DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1. KW Transferase; Nucleotidyltransferase; Multigene family; KW Starch biosynthesis; Allosteric enzyme; Amyloplast; Chloroplast; KW Transit peptide. FT TRANSIT 1 47 Chloroplast (Potential). FT CHAIN 48 521 Glucose-1-phosphate adenylyltransferase FT large subunit 2. SQ SEQUENCE 521 AA; 57988 MW; 9BF611A305257899 CRC64; MQFSSVLPLE GKACMSPVRR GSGGYGSERM RINCCSIRRN KALRRMCFSA RGAVSSTQCV LTSDAGPDTL VRPNHPFRRN YADPNEVAAV ILGGGTGTQL FPLTSTRATP AVPIGGCYRL IDIPMSNCFN SGINKIFVMT QFNSASLNRH IHRTYLGGGI NFTDGSVEVL AATQMPGEAA GWFQGTADAV RKFIWVLEDY YKHKAIEHIL ILSGDQLYRM DYMELVQKHV DDNADITLSC APVGESRASD YGLVKFDSSG RVIQFSEKPK GAALEEMKVD TSFLNFATCT LPAEYPYIAS MGVYVFKRDV LLDLLKSRYA ELHDFGSEIL PKALHEHNVQ AYVFTDYWED IGTIRSFFDA NMALCEQPPK FEFYDPKTPF FTSPRYLPPT KSDKCRIKDA IISHGCFLRE CAIEHSIVGV PSRLNSGCEL KNTMMMGADL YETEDEISRL LAEGKVPIGV GENTKISNCI IDMNCQGWKE RLHNKQRGRS KSPDRPGRRI LIRSGIVVVL KNATIKDGTV I // ID GLGB_MAIZE STANDARD; PRT; 799 AA. AC Q08047; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE 1,4-alpha-glucan branching enzyme IIB, chloroplast precursor DE (EC 2.4.1.18) (Starch branching enzyme IIB) (Q-enzyme). GN SBE1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 58-65. RC STRAIN=cv. W64A X 182E; TISSUE=Endosperm; RX MEDLINE=94105320; PubMed=8278524; RA Fisher D.K., Boyer C.D., Hannah L.C.; RT "Starch branching enzyme II from maize endosperm."; RL Plant Physiol. 102:1045-1046(1993). RN [2] RP SEQUENCE FROM N.A., AND SEQUENCE OF 248-271 AND 305-315. RC STRAIN=cv. B73; TISSUE=Endosperm; RX MEDLINE=95152344; PubMed=7849565; RA Guan H.P., Baba T., Preiss J.; RT "Expression of branching enzyme II of maize endosperm in Escherichia RT coli."; RL Cell. Mol. Biol. 40:981-988(1994). CC -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic CC linkages in starch by scission of a 1,4-alpha-linked CC oligosaccharide from growing alpha-1,4-glucan chains and the CC subsequent attachment of the oligosaccharide to the alpha-1,6 CC position. CC -!- CATALYTIC ACTIVITY: Formation of 1,6-glucosidic linkages of CC starch. CC -!- PATHWAY: Starch biosynthesis; third step. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast; amyloplast. CC -!- SIMILARITY: Belongs to family 13 of glycosyl hydrolases. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L08065; AAA18571.1; -. DR PIR; T02981; T02981. DR MaizeDB; 63943; -. DR InterPro; IPR006047; Alpha_amyl_cat. DR InterPro; IPR004193; Glyco_hydro_13N. DR Pfam; PF00128; alpha-amylase; 1. DR Pfam; PF02922; isoamylase_N; 1. KW Starch biosynthesis; Transferase; Glycosyltransferase; Amyloplast; KW Chloroplast; Transit peptide. FT TRANSIT 1 57 Chloroplast; amyloplast. FT CHAIN 58 799 1,4-alpha-glucan branching enzyme IIB. FT ACT_SITE 341 341 By similarity. FT ACT_SITE 376 376 By similarity. FT ACT_SITE 381 381 By similarity. FT ACT_SITE 445 445 By similarity. FT ACT_SITE 447 447 By similarity. FT ACT_SITE 502 502 By similarity. FT ACT_SITE 569 569 By similarity. FT ACT_SITE 570 570 By similarity. SQ SEQUENCE 799 AA; 90517 MW; 0B440E0377B8087A CRC64; MAFRVSGAVL GGAVRAPRLT GGGEGSLVFR HTGLFLTRGA RVGCSGTHGA MRAAAAARKA VMVPEGENDG LASRADSAQF QSDELEVPDI SEETTCGAGV ADAQALNRVR VVPPPSDGQK IFQIDPMLQG YKYHLEYRYS LYRRIRSDID EHEGGLEAFS RSYEKFGFNA SAEGITYREW APGAFSAALV GDVNNWDPNA DRMSKNEFGV WEIFLPNNAD GTSPIPHGSR VKVRMDTPSG IKDSIPAWIK YSVQAPGEIP YDGIYYDPPE EVKYVFRHAQ PKRPKSLRIY ETHVGMSSPE PKINTYVNFR DEVLPRIKKL GYNAVQIMAI QEHSYYGSFG YHVTNFFAPS SRFGTPEDLK SLIDRAHELG LLVLMDVVHS HASSNTLDGL NGFDGTDTHY FHSGPRGHHW MWDSRLFNYG NWEVLRFLLS NARWWLEEYK FDGFRFDGVT SMMYTHHGLQ VTFTGNFNEY FGFATDVDAV VYLMLVNDLI HGLYPEAVTI GEDVSGMPTF ALPVHDGGVG FDYRMHMAVA DKWIDLLKQS DETWKMGDIV HTLTNRRWLE KCVTYAESHD QALVGDKTIA FWLMDKDMYD FMALDRPSTP TIDRGIALHK MIRLITMGLG GEGYLNFMGN EFGHPEWIDF PRGPQRLPSG KFIPGNNNSY DKCRRRFDLG DADYLRYHGM QEFDQAMQHL EQKYEFMTSD HQYISRKHEE DKVIVFEKGD LVFVFNFHCN NSYFDYRIGC RKPGVYKVVL DSDAGLFGGF SRIHHAAEHF TADCSHDNRP YSFSVYTPSR TCVVYAPVE // ID GLGS_MAIZE STANDARD; PRT; 125 AA. AC P55240; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Glucose-1-phosphate adenylyltransferase small subunit (EC 2.7.7.27) DE (ADP-glucose synthase) (ADP-glucose pyrophosphorylase) (AGPASE B) DE (Alpha-D-glucose-1-phosphate adenyl transferase) (Fragment). GN GLG1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. F7.F2; TISSUE=Leaf; RX MEDLINE=94159789; PubMed=8115545; RA Prioul J.-L., Jeannette E., Reyss A., Gregory N., Giroux M., RA Hannah L.C., Causse M.; RT "Expression of ADP-glucose pyrophosphorylase in maize (Zea mays L.) RT grain and source leaf during grain filling."; RL Plant Physiol. 104:179-187(1994). CC -!- FUNCTION: This protein plays a role in synthesis of starch. It CC catalyzes the synthesis of the activated glycosyl donor, ADP- CC glucose from Glc-1-P and ATP. CC -!- CATALYTIC ACTIVITY: ATP + alpha-D-glucose 1-phosphate = CC diphosphate + ADP-glucose. CC -!- ENZYME REGULATION: Activated by 3'phosphoglycerate, inhibited by CC orthophosphate. Allosteric regulation. CC -!- PATHWAY: Starch biosynthesis. CC -!- SUBUNIT: Heterotetramer. CC -!- SUBCELLULAR LOCATION: Chloroplasts of leaves and amyloplasts of CC developing endosperm. CC -!- TISSUE SPECIFICITY: Leaves. CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate CC adenylyltransferase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S72425; AAB29961.1; -. DR PIR; T01750; T01750. DR MaizeDB; 113182; -. DR InterPro; IPR005836; ADP_Glu_pyroP. DR PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; PARTIAL. DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; PARTIAL. DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; PARTIAL. KW Transferase; Nucleotidyltransferase; Multigene family; KW Starch biosynthesis; Allosteric enzyme; Amyloplast; Chloroplast. FT NON_TER 1 1 SQ SEQUENCE 125 AA; 13246 MW; 25E1690B7FA9F1BE CRC64; VTDSVIGEGC VIKNCKIHHS VVGLRSCISE GAIIEDTLLM GADYYAETEA DKKLLAENGG IPIGIGKNSH IRKAIIDKNA RIGDNVKILN ADNVQEAARE TDGYFIKGGI VTVIKDALLP SGTVI // ID GLN1_MAIZE STANDARD; PRT; 357 AA. AC P38559; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Glutamine synthetase root isozyme 1 (EC 6.3.1.2) (Glutamate--ammonia DE ligase) (GS122). GN GLN6 OR GS1-1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; TISSUE=Seedling; RX MEDLINE=94033318; PubMed=8106013; RA Li M.-G., Villemur R., Hussey P.J., Silflow C.D., Gantt J.S., RA Snustad D.P.; RT "Differential expression of six glutamine synthetase genes in Zea RT mays."; RL Plant Mol. Biol. 23:401-407(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. Golden cross Bantam T51; TISSUE=Leaf; RA Sakakibara H., Kawabata S., Takahashi H., Hase T., Sugiyama T.; RT "Molecular cloning of the family of glutamine synthetase genes from RT maize: expression of genes for glutamine synthetase and ferredoxin- RT dependent glutamate synthase in photosynthetic and non-photosynthetic RT tissues."; RL Plant Cell Physiol. 33:49-58(1992). RN [3] RP REVISIONS. RA Sakakibara H.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays a role in the flow of nitrogen into nitrogenous CC organic compounds. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate + CC L-glutamine. CC -!- SUBUNIT: Homooctamer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- TISSUE SPECIFICITY: Found mainly in the cortical tissues of CC seedling roots, and in the root tip. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65926; CAA46719.1; -. DR EMBL; D14579; BAA03433.1; -. DR PIR; S39477; S39477. DR MaizeDB; 17151; -. DR InterPro; IPR008147; Gln_synt_beta. DR InterPro; IPR008146; Gln_synt_C. DR Pfam; PF00120; gln-synt; 1. DR Pfam; PF03951; gln-synt_N; 1. DR ProDom; PD001057; Gln_synt_C; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00181; GLNA_ATP; 1. KW Ligase; Multigene family. FT CONFLICT 48 48 I -> S (in Ref. 2). SQ SEQUENCE 357 AA; 39250 MW; 912A5E3BAF9CC2B8 CRC64; MASLTDLVNL DLSDCTDRII AEYIWIGGTG IDLRSKARTV KGPITDPIQL PKWNYDGSST GQAPGEDSEV ILYPQAIFKD PFRKGNHILV MCDCYTPQGE PIPTNKRYSA AKVFSHPDVA AEVPWYGIEQ EYTLLQKDVS WPLGWPVGGY PGPQGPYYCA AGADKAFGRD VVDAHYKACL YAGINISGIN GEVMPGQWEF QVGPSVGISA GDEIWVARYI LERITEMAGI VLSLDPKPIK GDWNGAGAHT NYSTKSMREA GGYEVIKAAI DKLGKRHKEH IAAYGEGNER RLTGRHETAD INTFKWGVAN RGASIRVGRD TEREGKGYFE DRRPASNMDP YVVTGMIAET TILWNGN // ID GLN2_MAIZE STANDARD; PRT; 368 AA. AC P38560; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Glutamine synthetase root isozyme 2 (EC 6.3.1.2) (Glutamate--ammonia DE ligase). GN GLN2 OR GS1-2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; TISSUE=Seedling; RX MEDLINE=94033318; PubMed=8106013; RA Li M.-G., Villemur R., Hussey P.J., Silflow C.D., Gantt J.S., RA Snustad D.P.; RT "Differential expression of six glutamine synthetase genes in Zea RT mays."; RL Plant Mol. Biol. 23:401-407(1993). CC -!- FUNCTION: Plays a role in the flow of nitrogen into nitrogenous CC organic compounds. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate + CC L-glutamine. CC -!- SUBUNIT: Homooctamer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- TISSUE SPECIFICITY: Found mainly in the vascular tissues of CC seedling roots. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65927; CAA46720.1; -. DR PIR; S39478; S39478. DR MaizeDB; 17151; -. DR InterPro; IPR008147; Gln_synt_beta. DR InterPro; IPR008146; Gln_synt_C. DR Pfam; PF00120; gln-synt; 1. DR Pfam; PF03951; gln-synt_N; 1. DR ProDom; PD001057; Gln_synt_C; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00181; GLNA_ATP; 1. KW Ligase; Multigene family. SQ SEQUENCE 368 AA; 40094 MW; 32F1E1AE109AEA0D CRC64; MALLSDLINL DLSGRTGKII AEYIWVGGSG MDVRSKARTL SGPVDDPSKL PKWNFDGSST GQAPGDDSEV ILCPRAIFRD PFRKGQNILV MCDCYEPNGE PIPSNKRHGA AKIFSHPDVK AEEPWFGIEQ EYTLLQKDTK WPLGWPLAYP GPQGPYYCAA GADKSYGRDI VDCAYKACLY AGIDISGING EVMPGQWEFQ VAPAVGVSAG DQLWVARYIL ERITEIAGVV VSFDPKPIPG DWNGAGAHTN YSTKSMRSDG GYEVIKKAIG KLGLRHREHI AAYGDGNERP LTGRHETADI NTFVWGVPNR GASVRVGRDT EKEGKGYFED RRPASNMDPY VVTCLIAETT MLWEPSHSNG DGKGAAAP // ID GLN3_MAIZE STANDARD; PRT; 356 AA. AC P38561; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Glutamine synthetase root isozyme 3 (EC 6.3.1.2) (Glutamate--ammonia DE ligase) (GS112). GN GLN4 OR GS1-3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; TISSUE=Seedling; RX MEDLINE=94033318; PubMed=8106013; RA Li M.-G., Villemur R., Hussey P.J., Silflow C.D., Gantt J.S., RA Snustad D.P.; RT "Differential expression of six glutamine synthetase genes in Zea RT mays."; RL Plant Mol. Biol. 23:401-407(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. Golden cross Bantam T51; TISSUE=Leaf; RA Sakakibara H., Kawabata S., Takahashi H., Hase T., Sugiyama T.; RT "Molecular cloning of the family of glutamine synthetase genes from RT maize: expression of genes for glutamine synthetase and ferredoxin- RT dependent glutamate synthase in photosynthetic and non-photosynthetic RT tissues."; RL Plant Cell Physiol. 33:49-58(1992). CC -!- FUNCTION: Plays a role in the flow of nitrogen into nitrogenous CC organic compounds. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate + CC L-glutamine. CC -!- SUBUNIT: Homooctamer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- TISSUE SPECIFICITY: Found in all the tissues examined with higher CC expression found in tissues of the root. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65928; CAA46721.1; -. DR EMBL; D14577; BAA03431.1; -. DR PIR; S39479; S39479. DR MaizeDB; 17151; -. DR InterPro; IPR008147; Gln_synt_beta. DR InterPro; IPR008146; Gln_synt_C. DR Pfam; PF00120; gln-synt; 1. DR Pfam; PF03951; gln-synt_N; 1. DR ProDom; PD001057; Gln_synt_C; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00181; GLNA_ATP; 1. KW Ligase; Multigene family. FT CONFLICT 15 15 T -> N (in Ref. 2). FT CONFLICT 289 290 DG -> ER (in Ref. 2). SQ SEQUENCE 356 AA; 39169 MW; 0112DD32D5FB474C CRC64; MACLTDLVNL NLSDTTEKII AEYIWIGGSG MDLRSKARTL SGPVTDPSKL PKWNYDGSST GQAPGEDSEV ILYPQAIFKD PFRRGNNILV MCDCYTPAGE PIPTNKRYNA AKIFSSPEVA AEEPWYGIEQ EYTLLQKDTN WPLGWPIGGF PGPQGPYYCG IGAEKSFGRD IVDAHYKACL YAGINISGIN GEVMPGQWEF QVGPSVGISS GDQVWVARYI LERITEIAGV VVTFDPKPIP GDWNGAGAHT NYSTESMRKE GGYEVIKAAI EKLKLRHREH IAAYGEGNDG RLTGRHETAD INTFSWGVAN RGASVRVGRE TEQNGKGYFE DRRPASNMDP YVVTSMIAET TIIWKP // ID GLN4_MAIZE STANDARD; PRT; 355 AA. AC P38562; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Glutamine synthetase root isozyme 4 (EC 6.3.1.2) (Glutamate--ammonia DE ligase) (GS107). GN GLN5 OR GS1-4. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; TISSUE=Seedling; RX MEDLINE=94033318; PubMed=8106013; RA Li M.-G., Villemur R., Hussey P.J., Silflow C.D., Gantt J.S., RA Snustad D.P.; RT "Differential expression of six glutamine synthetase genes in Zea RT mays."; RL Plant Mol. Biol. 23:401-407(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. Golden cross Bantam T51; TISSUE=Leaf; RA Sakakibara H., Kawabata S., Takahashi H., Hase T., Sugiyama T.; RT "Molecular cloning of the family of glutamine synthetase genes from RT maize: expression of genes for glutamine synthetase and ferredoxin- RT dependent glutamate synthase in photosynthetic and non-photosynthetic RT tissues."; RL Plant Cell Physiol. 33:49-58(1992). CC -!- FUNCTION: Plays a role in the flow of nitrogen into nitrogenous CC organic compounds. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate + CC L-glutamine. CC -!- SUBUNIT: Homooctamer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- TISSUE SPECIFICITY: Found in all the tissues examined with higher CC expression found in tissues of the root, stem and seedling shoot. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65929; CAA46722.1; -. DR EMBL; D14576; BAA03430.1; -. DR PIR; S39480; S39480. DR MaizeDB; 17151; -. DR InterPro; IPR008147; Gln_synt_beta. DR InterPro; IPR008146; Gln_synt_C. DR Pfam; PF00120; gln-synt; 1. DR Pfam; PF03951; gln-synt_N; 1. DR ProDom; PD001057; Gln_synt_C; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00181; GLNA_ATP; 1. KW Ligase; Multigene family. FT CONFLICT 316 316 A -> R (in Ref. 2). FT CONFLICT 319 319 Q -> RE (in Ref. 2). SQ SEQUENCE 355 AA; 38981 MW; 02F891F1209C50E5 CRC64; MACLTDLVNL NLSDTTEKII AEYIWIGGSG MDLRSKARTL PGPVTDPSKL PKWNYDGSST GQAPGEDSEV ILYPQAIFKD PFRRGNNILV MCDCYTPAGE PIPTNKRYSA AKIFSSPEVA AEEPWYGIEQ EYTLLQKDTN WPLGWPIGGF PGPQGPYYCG IGAEKSFGRD IVDAHYKACL YAGINISGIN GEVMPGQWEF QVGPSVGISS GDQVWVARYI LERITEIAGV VVTFDPKPIP GDWNGAGAHT NYSTESMRKE GGYEVIKAAI EKLKLRHKEH IAAYGEGNER RLTGRHETAD INTFSWGVAN RGASVAVGQT EQNGKGYFED RRPASNMDPY VVTSMIAETT IVWKP // ID GLN5_MAIZE STANDARD; PRT; 357 AA. AC P38563; DT 01-OCT-1994 (Rel. 30, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Glutamine synthetase root isozyme 5 (EC 6.3.1.2) (Glutamate--ammonia DE ligase) (GS117). GN GS1-5. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Golden cross Bantam T51; TISSUE=Leaf; RA Sakakibara H., Kawabata S., Takahashi H., Hase T., Sugiyama T.; RT "Molecular cloning of the family of glutamine synthetase genes from RT maize: expression of genes for glutamine synthetase and ferredoxin- RT dependent glutamate synthase in photosynthetic and non-photosynthetic RT tissues."; RL Plant Cell Physiol. 33:49-58(1992). RN [2] RP SEQUENCE OF 113-357 FROM N.A. RC STRAIN=cv. A188; TISSUE=Seedling; RX MEDLINE=94033318; PubMed=8106013; RA Li M.-G., Villemur R., Hussey P.J., Silflow C.D., Gantt J.S., RA Snustad D.P.; RT "Differential expression of six glutamine synthetase genes in Zea RT mays."; RL Plant Mol. Biol. 23:401-407(1993). CC -!- FUNCTION: Plays a role in the flow of nitrogen into nitrogenous CC organic compounds. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate + CC L-glutamine. CC -!- SUBUNIT: Homooctamer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- TISSUE SPECIFICITY: Found mainly in the cortical tissues of CC seedling roots, stem and seedling shoot. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D14578; BAA03432.1; ALT_SEQ. DR EMBL; X65930; CAA46723.1; -. DR PIR; S39481; S39481. DR MaizeDB; 17151; -. DR InterPro; IPR008147; Gln_synt_beta. DR InterPro; IPR008146; Gln_synt_C. DR Pfam; PF00120; gln-synt; 1. DR Pfam; PF03951; gln-synt_N; 1. DR ProDom; PD001057; Gln_synt_C; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00181; GLNA_ATP; 1. KW Ligase; Multigene family. FT CONFLICT 139 139 L -> V (in Ref. 2). FT CONFLICT 275 275 R -> K (in Ref. 2). FT CONFLICT 285 286 GE -> DG (in Ref. 2). FT CONFLICT 313 313 A -> G (in Ref. 2). SQ SEQUENCE 357 AA; 39259 MW; 183F9C15F2FF33A6 CRC64; MASLTDLVNL DLSDCTDKII AEYIWVGGSG IDLRSKARTV KGPITDPSQL PKWNYDGSST GQAPGEDSEV ILYPQAIFKD PFRKGNNILV MCDCYTPQGE PIPSNKRYKA ATVFSHPDVA AEVPWYGIEQ EYTLLQKDLS WPLGWPVGGY PGPQGPYYCA AGADKAFGRD VVDAHYKACL YAGINISGIN GEVMPGQWEF QVGPSVGISA GDEIWVARYI LERITEMAGI VLSLDPKPIK GDWNGAGAHT NYSTKSMREA GGYEVIKEAI EKLGRRHREH IAAYGEGNER RLTGRHETAD INTFKWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTGMIADT TILWKGN // ID GLNC_MAIZE STANDARD; PRT; 423 AA. AC P25462; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Glutamine synthetase, chloroplast precursor (EC 6.3.1.2) (Glutamate-- DE ammonia ligase) (GS2). GN GLN2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Black Mexican Sweet; TISSUE=Leaf; RX MEDLINE=89137924; PubMed=2906306; RA Snustad D.P., Hunsperger J.P., Chereskin B.M., Messing J.; RT "Maize glutamine synthetase cDNAs: isolation by direct genetic RT selection in Escherichia coli."; RL Genetics 120:1111-1124(1988). RN [2] RP POSSIBLE FRAMESHIFT ERROR IN REF.1. RA Patthey J.-P.; RL Unpublished observations (MAY-1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=cv. Black Mexican Sweet; TISSUE=Seedling; RX MEDLINE=94033318; PubMed=8106013; RA Li M.-G., Villemur R., Hussey P.J., Silflow C.D., Gantt J.S., RA Snustad D.P.; RT "Differential expression of six glutamine synthetase genes in Zea RT mays."; RL Plant Mol. Biol. 23:401-407(1993). CC -!- FUNCTION: The light-modulated chloroplast enzyme, encoded by a CC nuclear gene and expressed primarily in leaves, is responsible for CC the reassimilation of the ammonia generated by photorespiration. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate + CC L-glutamine. CC -!- SUBUNIT: Homooctamer. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65931; CAA46724.1; -. DR PIR; S39482; S39482. DR MaizeDB; 61728; -. DR InterPro; IPR008147; Gln_synt_beta. DR InterPro; IPR008146; Gln_synt_C. DR Pfam; PF00120; gln-synt; 1. DR Pfam; PF03951; gln-synt_N; 1. DR ProDom; PD001057; Gln_synt_C; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00181; GLNA_ATP; 1. KW Ligase; Multigene family; Chloroplast; Transit peptide. FT TRANSIT 1 51 Chloroplast (Potential). FT CHAIN 52 423 Glutamine synthetase. SQ SEQUENCE 423 AA; 46017 MW; EC799D71E0BD6C5F CRC64; MAQAVVPAMQ CRVGVKAAAG RVWSAGRTRT GRGGASPGFK VMAVSTGSTG VVPRLEQLLN MDTTPYTDKV IAEYIWVGGS GIDIRSKSRT ISKPVEDPSE LPKWNYDGSS TGQAPGEDSE VILYPQAIFK DPFRGGNNVL VICDTYTPQG EPLPTNKRHR AAQIFSDPKV GEQVPWFGIE QEYTLLQKDV NWPLGWPVGG FPGPQGPYYC AVGADKSFGR DISDAHYKAC LYAGINISGT NGEVMPGQWE YQVGPSVGIE AGDHIWISRY ILERITEQAG VVLTLDPKPI QGDWNGAGCH TNYSTKTMRE DGGFEEIKRA ILNLSLRHDL HISAYGEGNE RRLTGKHETA SIGTFSWGVA NRGCSIRVGR DTEAKGKGYL EDRRPASNMD PYIVTGLLAE TTILWQPSLE AEALAAKKLA LKV // ID GLSF_MAIZE STANDARD; PRT; 1616 AA. AC P23225; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Ferredoxin-dependent glutamate synthase, chloroplast precursor DE (EC 1.4.7.1) (Fd-GOGAT). GN GLSF. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 97-109 AND 790-802. RC STRAIN=cv. Golden cross Bantam T51; TISSUE=Leaf; RX MEDLINE=91115807; PubMed=1989968; RA Sakakibara H., Watanabe M., Hase T., Sugiyama T.; RT "Molecular cloning and characterization of complementary DNA encoding RT for ferredoxin-dependent glutamate synthase in maize leaf."; RL J. Biol. Chem. 266:2028-2035(1991). CC -!- CATALYTIC ACTIVITY: 2 L-glutamate + 2 oxidized ferredoxin = L- CC glutamine + 2-oxoglutarate + 2 reduced ferredoxin. CC -!- COFACTOR: Binds a 3Fe-4S cluster; FAD and FMN. CC -!- PATHWAY: Glutamine synthetase/GOGAT pathway which is involved in CC the assimilation of ammonia. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Chloroplast stroma. CC -!- TISSUE SPECIFICITY: Mostly in green tissues and lesser in non- CC photosynthetic tissues. CC -!- SIMILARITY: TO OTHER GLUTAMATE SYNTHASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M59190; AAA33463.1; -. DR PIR; A38596; A38596. DR MaizeDB; 40403; -. DR InterPro; IPR002489; DUF14. DR InterPro; IPR003009; FMN_enzyme. DR InterPro; IPR006982; Glu_synth_centr. DR InterPro; IPR006981; Glu_synth_NTN. DR InterPro; IPR002932; Glu_synthase. DR Pfam; PF04898; Glu_syn_central; 1. DR Pfam; PF04897; Glu_synth_NTN; 1. DR Pfam; PF01645; Glu_synthase; 1. DR Pfam; PF01493; GXGXG; 1. KW Oxidoreductase; Iron-sulfur; 3Fe-4S; Flavoprotein; FAD; FMN; KW Chloroplast; Transit peptide; Glutamate biosynthesis. FT TRANSIT 1 97 Chloroplast. FT CHAIN 98 1616 Ferredoxin-dependent glutamate synthase. FT DOMAIN 98 450 Glutamine amidotransferase (Potential). FT NP_BIND 1176 1233 FMN (By similarity). FT METAL 1229 1229 Iron-sulfur (3Fe-4S) (By similarity). FT METAL 1235 1235 Iron-sulfur (3Fe-4S) (By similarity). FT METAL 1240 1240 Iron-sulfur (3Fe-4S) (By similarity). SQ SEQUENCE 1616 AA; 175172 MW; 67724CBFA0AEB053 CRC64; MATLPRAAPP TPAALLPLPR AAPPLLLAGR AAAARRSRLR ARGPSAAARR SWVVASAASS SSRAVVGGVA RREAPPAPQK PTQQAADLNH ILSERGACGV GFVANLKNMS SFDIVRDALM ALGCMEHRGG CGADSDSGDG AGLMSAVPWD LFDDWASKQG LALFDRRNTG VGMVFLPQDE KSMEEAKAAT EKVFVDEGLE VLGWRPVPFN VSVVGRNAKE TMPNIQQIFV KVAKEDNADD IERELYISRK LIERAAKSFS WADELYFCSL SSRTIVYKGM LRSEVLGQFY LDLQNELYKS PFAIYHRRFS TNTSPRWPLA QPMRLLGHNG EINTIQGNLN WMRSRETTLK SPVWRGREHE ICPFGDPKAS DSANLDSTAE LLLRSGRSPA EALMILVPEA YKNHPTLSIK YPEVTDFYDY YKGQMEAWDG PALLLFSDGR TVGATLDRNG LRPARYWRTS DDFVYVASEV GVIPMDESKV VMKGRLGPGM MITVDLQTGQ VLENTEVKKT VASASPYGTW LQECTRLIKP VNFLSSTIMD NETVLRHQQA FGYSSEDVQM VIESMASQGK EPTFCMGDDI PLAVLSQRPH LLYDYFKQRF AQVTNPAIDP LREGLVMSLE VNIGKRGNIL EVGPENADQV ALSSPVLNEG ELETLLNDSK LKPKVLSTYF DIRKGLDGSL DKTIQALCEE ADAAVRSGSQ LLVLSDRSEA PEPTRPAIPI LLAVGAIHQH LIQNGLRMSA SIVADTAQCF STHHFACLIG YGASAVCPYL ALETCRQWRL SNKTLNLMRN GKMPTVTIEQ AQRNFIKAVK SGLLKILSKM GISLLSSYCG AQIFEIYGLG QEVVDLAFCG SVSKIGGLTL DELGRETLSF WVKAFSEDTA KRLENFGFIQ SRPGGEYHAN NPEMSKLLHK AIREKRDNAY TVYQQHLASR PVNVLRDLLE LKSDRAPIPI GKVESATSIV ERFCTGGMSL GAISRETHEA IAIAMNRIGG KSNSGEGGED PIRWNPLTDV VDGYSPTLPH LKGLQNGDTA TSAIKQVASG RFGVTPTFLV NADQIEIKIA QGAKPGEGGQ LPGKKVSAYI ARLRNSKPGV PLISPPPHHD IYSIEDLAQL IYDLHQINPK AKVSVKLVSE AGIGTVASGV SKANADIIQI SGHDGGTGAS PISSIKHAGG PWELGLTETN QTLIQNGLRE RVVLRVDGGF RSGQDVLIAA AMGADEYGFG SVAMIATGCV MARICHTNNC PVGVASQREE LRARFPGVPG DLVNYFLFVA EEVRAALAQL GYEKLDDIIG RTDLLKPKHI SLVKTQHIDL GYLLSNAGLP EWSSSQIRSQ DVHTNGPVLD ETILADPEIA DAIENEKEVS KAFQIYNVDR AVCGRVAGVI AKKYGDTGFA GQLNITFNGS AGQSFGCFLT PGMNIRLVGE ANDYVGKGMA GGELVVVPVD KTGFVPEDAT IVGNTCLYGA TGGQVFVRGK AGERFAVRNS LCQAVVEGTG DHCCEYMTGG CVVVLGKAGR NVAAGMTGGL AYILDEDDTL VPKVNKEIVK MQRVNAPAGQ MQLKGLIEAY VEKTGSEKGI AILREWEAYL PLFWQLVPPS EEDSPEACAE FERVLAKQAT TQLSAK // ID GLU2_MAIZE STANDARD; PRT; 223 AA. AC P04706; P02860; P08415; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Glutelin 2 precursor (Zein-gamma) (27 kDa zein) (Alcohol-soluble DE reduced glutelin) (ASG) (Zein ZC2). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64 X W64O2; RX MEDLINE=87248094; PubMed=3596247; RA Prat S., Perez-Grau L., Puigdomenech P.; RT "Multiple variability in the sequence of a family of maize endosperm RT proteins."; RL Gene 52:41-49(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. inbred line E-10; RX MEDLINE=85215560; PubMed=3839076; RA Prat S., Cortadas J., Puigdomenech P., Palau J.; RT "Nucleic acid (cDNA) and amino acid sequences of the maize endosperm RT protein glutelin-2."; RL Nucleic Acids Res. 13:1493-1504(1985). RN [3] RP SEQUENCE FROM N.A. RA Boronat A., Martinez M.C., Reina M., Puigdomenech P., Palau J.; RT "Isolation and sequencing of a 28 kd glutelin-2 gene from maize: RT common elements in the 5' flanking regions among zein and glutelin RT genes."; RL Plant Sci. 47:95-102(1986). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; TISSUE=Endosperm; RX MEDLINE=91057132; PubMed=2243788; RA Reina M., Ponte I., Guillen P., Boronat A., Palau J.; RT "Sequence analysis of a genomic clone encoding a Zc2 protein from Zea RT mays W64 A."; RL Nucleic Acids Res. 18:6426-6426(1990). RN [5] RP SEQUENCE OF 15-223 FROM N.A. RA Wang S.-Z., Esen A.; RT "Primary structure of a proline-rich zein and its cDNA."; RL Plant Physiol. 81:70-74(1986). RN [6] RP SEQUENCE OF 20-77. RA Esen A., Bietz J.A., Paulis J.W., Wall J.S.; RT "Tandem repeats in the N-terminal sequence of a proline-rich protein RT from corn endosperm."; RL Nature 296:678-679(1982). CC -!- FUNCTION: Glutelin 2 is a seed storage protein. It accounts for CC about 15% of the total endosperm protein content. CC -!- SUBCELLULAR LOCATION: Border of the inner part of the membrane CC of endosperm protein bodies. CC -!- SIMILARITY: TO BETA-TYPE ZEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02230; CAA26149.1; -. DR EMBL; M16066; AAA33468.1; -. DR EMBL; M16218; AAA33537.1; -. DR EMBL; X53514; CAA37594.1; -. DR EMBL; S78780; AAP32017.1; -. DR PIR; A93557; ZMZM19. DR MaizeDB; 58111; -. DR InterPro; IPR003612; AAI. DR InterPro; IPR001954; Glia_glutenin. DR InterPro; IPR000480; Glutelin. DR Pfam; PF00234; tryp_alpha_amyl; 1. DR PRINTS; PR00208; GLIADGLUTEN. DR PRINTS; PR00211; GLUTELIN. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Repeat; Signal. FT SIGNAL 1 19 FT CHAIN 20 223 Glutelin 2. FT DOMAIN 31 78 8 X 6 AA tandem repeats of P-P-P-V-H-L. FT REPEAT 31 36 1-1. FT REPEAT 37 42 1-2. FT REPEAT 43 48 1-3. FT REPEAT 49 54 1-4. FT REPEAT 55 60 1-5. FT REPEAT 61 66 1-6. FT REPEAT 67 72 1-7. FT REPEAT 73 78 1-8. FT DOMAIN 97 112 2 X 8 AA tandem repeats of Q-P-H-P-C-P- FT C-Q. FT REPEAT 97 104 2-1. FT REPEAT 105 112 2-2. FT VARIANT 28 28 C -> S (IN 66%, ACCORDING TO REF. 5). SQ SEQUENCE 223 AA; 23689 MW; 3E80C06B2DB58372 CRC64; MRVLLVALAL LALAASATST HTSGGCGCQP PPPVHLPPPV HLPPPVHLPP PVHLPPPVHL PPPVHLPPPV HVPPPVHLPP PPCHYPTQPP RPQPHPQPHP CPCQQPHPSP CQLQGTCGVG STPILGQCVE FLRHQCSPTA TPYCSPQCQS LRQQCCQQLR QVEPQHRYQA IFGLVLQSIL QQQPQSGQVA GLLAAQIAQQ LTAMCGLQQP TPCPYAAAGG VPH // ID GRPA_MAIZE STANDARD; PRT; 157 AA. AC P10979; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Glycine-rich RNA-binding, abscisic acid-inducible protein. GN RAB15. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Endosperm; RX MEDLINE=88288401; PubMed=2969461; RA Gomez J., Sanchez-Martinez D., Stiefel V., Rigau J., Puigdomenech P., RA Pages M.; RT "A gene induced by the plant hormone abscisic acid in response to RT water stress encodes a glycine-rich protein."; RL Nature 334:262-264(1988). RN [2] RP SIMILARITY TO RNA-BINDING PROTEINS. RX MEDLINE=89097302; PubMed=2521378; RA Mortenson E., Dreyfuss G.; RT "RNP in maize protein."; RL Nature 337:312-312(1989). CC -!- FUNCTION: Possibly has a role in RNA transcription or processing CC during stress. CC -!- INDUCTION: By the plant hormone abscisic acid in response to CC water stress. CC -!- SIMILARITY: Contains 1 RNA recognition motif (RRM) domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X12564; CAA31077.1; -. DR PIR; S04536; S04536. DR HSSP; P09651; 1UP1. DR MaizeDB; 69261; -. DR InterPro; IPR000504; RNA_rec_mot. DR Pfam; PF00076; rrm; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS00030; RRM_RNP_1; 1. KW RNA-binding. FT DOMAIN 8 86 RNA-binding (RRM). FT DOMAIN 88 154 Gly-rich. SQ SEQUENCE 157 AA; 15438 MW; 8A10592248D60D16 CRC64; MAAADVEYRC FVGGLAWATS NESLENAFAS YGEILDSKVI TDRETGRSRG FGFVTFSSEN SMLDAIENMN GKELDGRNIT VNQAQSRGGG GGGGGYGGGR GGGGYGGGRR DGGYGGGGGY GGRREGGGGG YGGGGGYGGR REGGGGGYGG GGGGWRD // ID GTH1_MAIZE STANDARD; PRT; 213 AA. AC P12653; DT 01-OCT-1989 (Rel. 12, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Glutathione S-transferase I (EC 2.5.1.18) (GST-I) (GST-29) (GST class- DE phi). GN GST1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88124246; PubMed=3277162; RA Grove G., Zarlengo R.P., Timmerman K.P., Li N.-Q., Tam M.F., RA Tu C.-P.D.; RT "Characterization and heterospecific expression of cDNA clones of RT genes in the maize GSH S-transferase multigene family."; RL Nucleic Acids Res. 16:425-438(1988). RN [2] RP SEQUENCE FROM N.A. RA Shah D.M., Hironaka C.M., Wiegand R.C., Harding E.I., Krivi G.G., RA Tiemeier D.C.; RT "Structural analysis of a maize gene coding for glutathione-S- RT transferase involved in herbicide detoxification."; RL Plant Mol. Biol. 6:203-211(1986). RN [3] RP SEQUENCE OF 1-15. RA Wiegand R.C., Shah D.M., Mozer T.J., Harding E.I., Diaz-Collier J., RA Saunders C., Jaworski E.G., Tiemeier D.C.; RT "Messenger RNA encoding a glutathione-S-transferase responsible for RT herbicide tolerance in maize is induced in response to safener RT treatment."; RL Plant Mol. Biol. 7:235-243(1986). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=98118476; PubMed=9417926; RA Neuefeind T., Huber R., Dasenbrock H., Prade L., Bieseler B.; RT "Crystal structure of herbicide-detoxifying maize glutathione S- RT transferase-I in complex with lactoylglutathione: evidence for an RT induced-fit mechanism."; RL J. Mol. Biol. 274:446-453(1997). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX MEDLINE=99036863; PubMed=9817846; RA Prade L., Huber R., Bieseler B.; RT "Structures of herbicides in complex with their detoxifying enzyme RT glutathione S-transferase - explanations for the selectivity of the RT enzyme in plants."; RL Structure 6:1445-1452(1998). CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of CC exogenous and endogenous hydrophobic electrophiles. Involved in CC the detoxification of certain herbicides. CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione. CC -!- SUBUNIT: Homodimer or heterodimer of GST-I and GST-IV (=GST-II). CC -!- TISSUE SPECIFICITY: Expressed in the stem and leaves, lower levels CC are seen in the pollen and endosperm. CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06754; CAA29928.1; -. DR EMBL; M16901; AAA33470.1; ALT_SEQ. DR EMBL; M16902; AAA33469.1; ALT_SEQ. DR EMBL; M16900; AAA33469.1; JOINED. DR PIR; S03726; XUZM1. DR PDB; 1AXD; 18-NOV-98. DR PDB; 1BYE; 21-OCT-98. DR MaizeDB; 65344; -. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. KW Transferase; Multigene family; 3D-structure. FT INIT_MET 0 0 FT CONFLICT 14 14 L -> V (in Ref. 2). FT STRAND 3 6 FT TURN 9 10 FT TURN 12 13 FT HELIX 14 24 FT TURN 25 25 FT STRAND 28 31 FT TURN 35 38 FT HELIX 39 41 FT HELIX 43 46 FT TURN 47 48 FT TURN 50 51 FT STRAND 56 59 FT TURN 60 61 FT STRAND 62 65 FT HELIX 67 78 FT HELIX 80 83 FT TURN 84 86 FT HELIX 88 103 FT TURN 104 104 FT HELIX 105 116 FT TURN 117 117 FT HELIX 118 122 FT TURN 123 123 FT HELIX 128 151 FT HELIX 162 165 FT TURN 166 167 FT HELIX 168 174 FT TURN 175 176 FT HELIX 178 185 FT HELIX 187 198 FT HELIX 200 208 SQ SEQUENCE 213 AA; 23690 MW; 87FE9E878913BA9A CRC64; APMKLYGAVM SWNLTRCATA LEEAGSDYEI VPINFATAEH KSPEHLVRNP FGQVPALQDG DLYLFESRAI CKYAARKNKP ELLREGNLEE AAMVDVWIEV EANQYTAALN PILFQVLISP MLGGTTDQKV VDENLEKLKK VLEVYEARLT KCKYLAGDFL SLADLNHVSV TLCLFATPYA SVLDAYPHVK AWWSGLMERP SVQKVAALMK PSA // ID GTH3_MAIZE STANDARD; PRT; 221 AA. AC P04907; P15542; DT 13-AUG-1987 (Rel. 05, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Glutathione S-transferase III (EC 2.5.1.18) (GST-III) (GST class-phi). GN GST3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88124246; PubMed=3277162; RA Grove G., Zarlengo R.P., Timmerman K.P., Li N.-Q., Tam M.F., RA Tu C.-P.D.; RT "Characterization and heterospecific expression of cDNA clones of RT genes in the maize GSH S-transferase multigene family."; RL Nucleic Acids Res. 16:425-438(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87016368; PubMed=3532034; RA Moore R.E., Davies M.S., O'Connell K.M., Harding E.I., Wiegand R.C., RA Tiemeier D.C.; RT "Cloning and expression of a cDNA encoding a maize glutathione-S- RT transferase in E. coli."; RL Nucleic Acids Res. 14:7227-7235(1986). RN [3] RP SEQUENCE OF 142-152. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of CC exogenous and endogenous hydrophobic electrophiles. Involved in CC the detoxification of certain herbicides. CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06755; CAA29929.1; -. DR EMBL; X04375; CAA27957.1; -. DR EMBL; X04455; CAA28053.1; -. DR PIR; A24703; XUZM31. DR PIR; S00717; XUZM32. DR HSSP; P12653; 1AXD. DR Maize-2DPAGE; P04907; COLEOPTILE. DR MaizeDB; 65344; -. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. KW Transferase; Multigene family. FT INIT_MET 0 0 FT CONFLICT 107 107 H -> Y (in Ref. 2). FT CONFLICT 110 126 ASPLVFQLLVRPLLGGA -> RVAAGVPAAREAAPGRR FT (in Ref. 2). FT CONFLICT 133 133 E -> D (in Ref. 2). FT CONFLICT 148 179 AHLARNKYLAGDEFTLADANHALLPALTSARP -> RTSPA FT TSTSPGTSSRSPTPTTRSYLLYLSKT (in Ref. 2). FT CONFLICT 183 188 GCVAAR -> ARRRP (in Ref. 2). FT CONFLICT 199 199 A -> V (in Ref. 2). SQ SEQUENCE 221 AA; 23718 MW; 2087293E2B2E31DF CRC64; APLKLYGMPL SPNVVRVATV LNEKGLDFEI VPVDLTTGAH KQPDFLALNP FGQIPALVDG DEVLFESRAI NRYIASKYAS EGTDLLPATA SAAKLEVWLE VESHHFHPNA SPLVFQLLVR PLLGGAPDAA VVEKHAEQLA KVLDVYEAHL ARNKYLAGDE FTLADANHAL LPALTSARPP RPGCVAARPH VKAWWEAIAA RPAFQKTVAA IPLPPPPSSS A // ID GTH4_MAIZE STANDARD; PRT; 222 AA. AC P46420; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Glutathione S-transferase IV (EC 2.5.1.18) (GST-IV) (GST-27) (GST DE class-phi). GN GST4. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. UE95; TISSUE=Seedling root; RX MEDLINE=95161709; PubMed=7858222; RA Jepson I., Lay V.J., Holt D.C., Bright S.W.J., Greenland A.J.; RT "Cloning and characterization of maize herbicide safener-induced RT cDNAs encoding subunits of glutathione S-transferase isoforms I, II RT and IV."; RL Plant Mol. Biol. 26:1855-1866(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. Pioneer hybrid 3906; RX MEDLINE=95175625; PubMed=7870838; RA Irzyk G.P., Potter S., Ward E., Fuerst E.P.; RT "A cDNA clone encoding the 27-kilodalton subunits of glutathione S- RT transferase IV from Zea mays."; RL Plant Physiol. 107:311-312(1995). RN [3] RP PARTIAL SEQUENCE, AND CHARACTERIZATION. RX MEDLINE=94105330; PubMed=8278534; RA Irzyk G.P., Fuerst E.P.; RT "Purification and characterization of a glutathione S-transferase RT from benoxacor-treated maize (Zea mays)."; RL Plant Physiol. 102:803-810(1993). CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of CC exogenous and endogenous hydrophobic electrophiles. Involved in CC the detoxification of certain herbicides. Most active with CC substrates possessing a chloroacetamide structure. Trans-cinnamic CC acid and 1-chloro-2,4-dinitrobenzene are not effective CC substrates. Active from pH 6 to 9, with a pH optimum between 7.5 CC and 8. May play an important role in the benoxacor-mediated CC protection of maize from metolachlor injury. CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione. CC -!- SUBUNIT: Homodimer or heterodimer of GST-I and GST-IV (=GST-II). CC -!- TISSUE SPECIFICITY: Seedling roots. CC -!- INDUCTION: By herbicides. CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X79515; CAA56047.1; -. DR EMBL; U12679; AAA20585.1; -. DR PIR; S52037; S52037. DR HSSP; P12653; 1AXD. DR MaizeDB; 113242; -. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. KW Transferase; Multigene family. FT INIT_MET 0 0 FT MOD_RES 1 1 BLOCKED. SQ SEQUENCE 222 AA; 24439 MW; EB7F6216AA84E40E CRC64; ATPAVKVYGW AISPFVSRAL LALEEAGVDY ELVPMSRQDG DHRRPEHLAR NPFGKVPVLE DGDLTLFESR AIARHVLRKH KPELLGGGRL EQTAMVDVWL EVEAHQLSPP AIAIVVECVF APFLGRERNQ AVVDENVEKL KKVLEVYEAR LATCTYLAGD FLSLADLSPF TIMHCLMATE YAALVHALPH VSAWWQGLAA RPAANKVAQF MPVGAGAPKE QE // ID GTX2_MAIZE STANDARD; PRT; 236 AA. AC P50472; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Probable glutathione S-transferase BZ2 (EC 2.5.1.18) (Bronze-2 DE protein). GN BZ2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seedling; RX MEDLINE=93005645; PubMed=1967051; RA Nash J., Luehrsen K.R., Walbot V.; RT "Bronze-2 gene of maize: reconstruction of a wild-type allele and RT analysis of transcription and splicing."; RL Plant Cell 2:1039-1049(1990). RN [2] RP ERRATUM. RA Nash J., Luehrsen K.R., Walbot V.; RL Plant Cell 3:103-103(1991). CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione. CC -!- PATHWAY: Anthocyanin biosynthesis. CC -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U14599; AAA50245.1; -. DR MaizeDB; 64140; -. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF02798; GST_N; 1. KW Transferase. SQ SEQUENCE 236 AA; 25563 MW; BD7C087F60FA6E9A CRC64; MRVLGGEVSP FTARARLALD LRGVAYELLD EPLGPKKSDR LLAANPVYGK IPVLLLPDGR AICESAVIVQ YIEDVARESG GAEAGSLLLP DDPYERAMHR FWTAFIDDKF WPALDAVSLA PTPGARAQAA EDTRAALSLL EEAFKDRSNG RAFFSGGDAA PGLLDLALGC FLPALRACER LHGLSLIDAS ATPLLDGWSQ RFAAHPAAKR VLPDTEKVVQ FTRFLQVQAQ FRVHVS // ID H1_MAIZE STANDARD; PRT; 245 AA. AC P23444; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Histone H1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=91227140; PubMed=1709276; RA Razafimahatratra P., Chaubet N., Philipps G., Gigot C.; RT "Nucleotide sequence and expression of a maize H1 histone cDNA."; RL Nucleic Acids Res. 19:1491-1496(1991). CC -!- FUNCTION: Histones H1 are necessary for the condensation of CC nucleosome chains into higher order structures. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Belongs to the histone H1/H5 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57077; CAA40362.1; -. DR PIR; S26826; S26826. DR MaizeDB; 25540; -. DR InterPro; IPR005818; Histone_H1/H5. DR InterPro; IPR005819; Histone_H5. DR InterPro; IPR003216; Linkerhist_N. DR Pfam; PF00538; linker_histone; 1. DR PRINTS; PR00624; HISTONEH5. DR ProDom; PD000373; Linkerhist_N; 1. DR SMART; SM00526; H15; 1. KW Chromosomal protein; Nuclear protein; DNA-binding. FT INIT_MET 0 0 FT DOMAIN 1 30 Asp/Glu-rich (acidic). FT DOMAIN 31 45 Arg/Lys-rich (basic). FT DOMAIN 46 121 Globular. SQ SEQUENCE 245 AA; 25217 MW; D1FD73DAA74A6778 CRC64; ATDVTETPAP LVDAAPEAPA DAPAAPAADA NAAKAKKATA PKKRASPTHL PYAEMVSEAI TSLKERTGSS SYAIAKFVED KHKAKLPPNF RKLLNVQLKK LVAGGKLTKV KNSYKLSSAT KPNPKPKAAP KKPKTGAKKP KAAAKPKAKT PAKAKPATKP KPAAKPKAVV KPKTPAKPKA KPAAKAKPKT AGAKPKPLAK KAGRAKAAKT SAKDTPGKKA PAKKAAPSKK AATPVRKAPS RKAKK // ID H2A_MAIZE STANDARD; PRT; 159 AA. AC P40280; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Histone H2A. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; TISSUE=Ovule; RA Bokhari-Riza A., Turcich M.P., Takacs I., Hamilton D.A., RA Mascarenhas J.P.; RT "Characterization of histone H2A and H2B cDNA clones isolated from a RT maize ovule cDNA library."; RL Maydica 39:115-118(1994). CC -!- SUBUNIT: The nucleosome is an octamer containing two molecules CC each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 CC bp of DNA. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Belongs to the histone H2A family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U08225; AAB04687.1; -. DR PIR; T02076; T02076. DR MaizeDB; 77944; -. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR002119; Histone_H2A. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00620; HISTONEH2A. DR ProDom; PD000522; Histone_H2A; 1. DR SMART; SM00414; H2A; 1. DR PROSITE; PS00046; HISTONE_H2A; 1. KW Chromosomal protein; Nucleosome core; Nuclear protein; DNA-binding. SQ SEQUENCE 159 AA; 16426 MW; 347F819C4D30186C CRC64; MDSTGTGAGG KGKKGAAGRK VGGPRKKSVS RSVKAGLQFP VGRIGRYLKK GRYAQXVGTG APVYLAAVLE YLAAEVLELA GNAARDNKKT RIIPRHVLLA IRNDEELGKL LGGVTIAHGG VLPNINPVLL PKKTAEKASS GGSKEAKSPK KAAKSPKKA // ID H2B1_MAIZE STANDARD; PRT; 151 AA. AC P30755; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Histone H2B.1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=93081719; PubMed=1450375; RA Joanin P., Gigot C., Phillipps G.; RT "Nucleotide sequence and expression of two cDNA coding for two RT histone H2B variants of maize."; RL Plant Mol. Biol. 20:581-588(1992). CC -!- SUBUNIT: The nucleosome is an octamer containing two molecules CC each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 CC bp of DNA. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Belongs to the histone H2B family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57312; CAA40564.1; -. DR PIR; S28048; S28048. DR MaizeDB; 65109; -. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR000558; Histone_H2B. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00621; HISTONEH2B. DR ProDom; PD000497; Histone_H2B; 1. DR SMART; SM00427; H2B; 1. DR PROSITE; PS00357; HISTONE_H2B; 1. KW Nuclear protein; Chromosomal protein; Nucleosome core; DNA-binding; KW Multigene family. SQ SEQUENCE 151 AA; 16420 MW; A3F3B5E18DC4A42A CRC64; MAPKAEKKPA AKKPAEEEPA TEKVEKAPAG KKPKAEKRLP AGKSKEGGEG KKGKKKAKKS VETYKIYIFK VLKQVHPDIG ISSKAMSIMN SFINDIFEKL AAESAKLARY NKKPTITSRE IQTSVRLVLP GELAKHAVSE GTKAVTKFTS S // ID H2B2_MAIZE STANDARD; PRT; 150 AA. AC P30756; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Histone H2B.2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=93081719; PubMed=1450375; RA Joanin P., Gigot C., Phillipps G.; RT "Nucleotide sequence and expression of two cDNA coding for two RT histone H2B variants of maize."; RL Plant Mol. Biol. 20:581-588(1992). CC -!- SUBUNIT: The nucleosome is an octamer containing two molecules CC each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 CC bp of DNA. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Belongs to the histone H2B family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57313; CAA40565.1; -. DR PIR; S28049; S28049. DR MaizeDB; 65109; -. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR000558; Histone_H2B. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00621; HISTONEH2B. DR ProDom; PD000497; Histone_H2B; 1. DR SMART; SM00427; H2B; 1. DR PROSITE; PS00357; HISTONE_H2B; 1. KW Nuclear protein; Chromosomal protein; Nucleosome core; DNA-binding; KW Multigene family. SQ SEQUENCE 150 AA; 16174 MW; 917A627B9B426949 CRC64; MAPKAEKKPA AKKPAEEEPA AEKAPAGKKP KAEKRVPAGK SAGKEGGEGK RGRKKGKKSV ETYKIYIFKV LKQVHPDIGI SSKAMSIMNS FINDIFEKLA AEAAKLARYN KKPTITSREI QTSVRLVLPG ELAKHAVSEG TKAVTKFTSS // ID H2B4_MAIZE STANDARD; PRT; 137 AA. AC P49120; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Histone H2B.4. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RA Joanin P., Gigot C., Phillipps G.; RT "Molecular cloning and sequence analysis of two genes encoding two RT histone H2B variants of maize."; RL Physiol. Veg. 32:693-696(1994). CC -!- SUBUNIT: The nucleosome is an octamer containing two molecules CC each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 CC bp of DNA. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Belongs to the histone H2B family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X69961; CAA49585.1; -. DR PIR; T02035; T02035. DR MaizeDB; 65109; -. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR000558; Histone_H2B. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00621; HISTONEH2B. DR ProDom; PD000497; Histone_H2B; 1. DR SMART; SM00427; H2B; 1. DR PROSITE; PS00357; HISTONE_H2B; 1. KW Nuclear protein; Chromosomal protein; Nucleosome core; DNA-binding; KW Multigene family. SQ SEQUENCE 137 AA; 15183 MW; E15246B1444CECEA CRC64; MAPKAEKKPA EKKPTEEKAE KKPRAEKRVP GKEGGEKKGK KKAKKSVETY KIYIFKVLKQ VHPDIGISSK AMSIMNSFIN DIFEKLAAEA AKLARYNKKP TITSREIQTS VRLVLPGELA KHAVSEGTKA VTKFTSS // ID H2B5_MAIZE STANDARD; PRT; 154 AA. AC P54348; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Histone H2B. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; TISSUE=Ovule; RA Bokhari-Riza A., Turcich M.P., Takacs I., Hamilton D.A., RA Mascarenhas J.P.; RT "Characterization of histone H2A and H2B cDNA clones isolated from a RT maize ovule cDNA library."; RL Maydica 39:115-118(1994). CC -!- SUBUNIT: The nucleosome is an octamer containing two molecules CC each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 CC bp of DNA. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Belongs to the histone H2B family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U08226; AAB04688.1; -. DR PIR; T02077; T02077. DR MaizeDB; 65109; -. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR000558; Histone_H2B. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00621; HISTONEH2B. DR ProDom; PD000497; Histone_H2B; 1. DR SMART; SM00427; H2B; 1. DR PROSITE; PS00357; HISTONE_H2B; 1. KW Nuclear protein; Chromosomal protein; Nucleosome core; DNA-binding; KW Multigene family. SQ SEQUENCE 154 AA; 16617 MW; 23F059A2E1F52ABF CRC64; MAPKAEKKPA AKKVAEEEPS EKAAPAEKAP AGKKPKAEKR LPAGKSAGKE GGDKKGRKKA KKSVETYKIY IFKVLKQVHP DIGISSKAMS IMNSFINDIF EKLAAEAAKL ARYNKKPTIT SREIQTSVRL VLPGELAKHA VSEGTKAVTK FTSS // ID H3_MAIZE STANDARD; PRT; 135 AA. AC P05203; P05329; P05330; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Histone H3. GN H3C2 AND H3C4. OS Zea mays (Maize), OS Oryza sativa (Rice), and OS Petroselinum crispum (Parsley) (Petroselinum hortense). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577, 4530, 4043; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RA Chaubet N., Philipps G., Chaboute M.-E., Ehling M., Gigot C.; RT "Nucleotide sequences of two corn histone H3 genes. Genomic RT organization of the corn histone H3 and H4 genes."; RL Plant Mol. Biol. 6:253-263(1986). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=O.sativa; STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=89263741; PubMed=2726464; RA Wu S.C., Vegh Z., Wang X.-M., Tan C.C., Dudits D.; RT "The nucleotide sequences of two rice histone H3 genes."; RL Nucleic Acids Res. 17:3297-3297(1989). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Maize, and O.sativa; RA Chaubet N., Chaboute M.-E., Philipps G., Gigot C.; RT "Histone genes in higher plants: organization and expression."; RL Dev. Genet. 8:461-473(1987). RN [4] RP SEQUENCE FROM N.A. (H3-7; H3-16 AND H3-20). RC SPECIES=P.crispum; TISSUE=Seedling; RA Wu S.C., Gregersen P., Hahlbrock K.; RL Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Histone H3, along with histone H4, plays a central role CC in nucleosome formation. CC -!- SUBUNIT: The nucleosome is an octamer containing two molecules CC each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 CC bp of DNA. CC -!- SIMILARITY: Belongs to the histone H3 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M13378; AAA33472.1; -. DR EMBL; M13379; AAA33473.1; -. DR EMBL; X13678; CAA31969.1; -. DR EMBL; X13680; CAA31970.1; -. DR EMBL; M35388; AAA66265.1; -. DR EMBL; M77493; AAA33852.1; -. DR EMBL; M77494; AAA33853.1; -. DR EMBL; M77495; AAA33854.1; -. DR PIR; S04099; S04099. DR PIR; S57626; S57626. DR MaizeDB; 25143; -. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR000164; Histone_H3. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00622; HISTONEH3. DR SMART; SM00428; H3; 1. DR PROSITE; PS00322; HISTONE_H3_1; 1. DR PROSITE; PS00959; HISTONE_H3_2; 1. KW Nuclear protein; Chromosomal protein; DNA-binding; Nucleosome core; KW Multigene family. FT INIT_MET 0 0 By similarity. SQ SEQUENCE 135 AA; 15137 MW; 49943AA849284358 CRC64; ARTKQTARKS TGGKAPRKQL ATKAARKSAP ATGGVKKPHR FRPGTVALRE IRKYQKSTEL LIRKLPFQRL VREIAQDFKT DLRFQSSAVA ALQEAAEAYL VGLFEDTNLC AIHAKRVTIM PKDIQLARRI RGERA // ID H4_WHEAT STANDARD; PRT; 102 AA. AC P59258; P02308; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Histone H4. OS Triticum aestivum (Wheat), OS Zea mays (Maize), OS Pisum sativum (Garden pea), OS Medicago sativa (Alfalfa), and OS Lolium temulentum. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; Pooideae; OC Triticeae; Triticum. OX NCBI_TaxID=4565, 4577, 3888, 3879, 34176; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; RX MEDLINE=83299256; PubMed=6310518; RA Tabata T., Sasaki K., Iwabuchi M.; RT "The structural organization and DNA sequence of a wheat histone H4 RT gene."; RL Nucleic Acids Res. 11:5865-5875(1983). RN [2] RP SEQUENCE FROM N.A. (VARIANT). RC SPECIES=T.aestivum; STRAIN=cv. Horoshirikomugi; RX MEDLINE=85128449; PubMed=6526273; RA Tabata T., Iwabuchi M.; RT "Molecular cloning and nucleotide sequence of a variant wheat histone RT H4 gene."; RL Gene 31:285-289(1984). RN [3] RP SEQUENCE FROM N.A. (H4C14). RC SPECIES=Maize; RX MEDLINE=86275997; PubMed=3015736; RA Philipps G., Chaubet N., Chaboute M.-E., Ehling M., Gigot C.; RT "Genomic organization and nucleotide sequences of two corn histone H4 RT genes."; RL Gene 42:225-229(1986). RN [4] RP SEQUENCE FROM N.A. (H4C13). RC SPECIES=Maize; RA Gigot C., Chaubet N., Chaboute M.-E., Ehling M., Philipps G.; RT "Nucleotide sequences of two histone H3 and H4 genes of corn. Further RT insight into the structure and organization of the histone genes in RT higher plants."; RL Physiol. Veg. 25:235-247(1987). RN [5] RP SEQUENCE. RC SPECIES=P.sativum; RX MEDLINE=70027325; PubMed=5388597; RA Delange R.J., Fambrough D.M., Smith E.L., Bonner J.; RT "Calf and pea histone IV. 3. Complete amino acid sequence of pea RT seedling histone IV; comparison with the homologous calf thymus RT histone."; RL J. Biol. Chem. 244:5669-5679(1969). RN [6] RP SEQUENCE FROM N.A. RC SPECIES=P.sativum; STRAIN=cv. Alaska; RA Devitt M.L., Price T., Stafstrom J.P.; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE FROM N.A. RC SPECIES=L.temulentum; RA Freeman D.R., Ougham H.J.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [8] RP ACETYLATION, AND PARTIAL SEQUENCE. RC SPECIES=M.sativa; STRAIN=cv. R4; RX MEDLINE=92329443; PubMed=1627562; RA Waterborg J.H.; RT "Identification of five sites of acetylation in alfalfa histone H4."; RL Biochemistry 31:6211-6219(1992). CC -!- FUNCTION: Histone H4, along with histone H3, plays a central role CC in nucleosome formation. CC -!- SUBUNIT: The nucleosome is an octamer containing two molecules CC each of H2A, H2B, H3 and H4. The octamer wraps approximately 146 CC bp of DNA. CC -!- SIMILARITY: Belongs to the histone H4 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X00043; CAA24924.1; -. DR EMBL; M12277; AAA34292.1; -. DR EMBL; M13370; AAA33475.1; -. DR EMBL; M13377; AAA33476.1; -. DR EMBL; M36659; AAA33474.1; -. DR EMBL; U10042; AAA86948.1; -. DR EMBL; X79715; CAA56154.1; ALT_SEQ. DR PIR; A02645; HSWT4. DR PIR; A24967; HSWT41. DR PIR; A25642; HSZM4. DR PIR; B43295; B43295. DR PIR; S60475; HSPM4. DR MaizeDB; 25155; -. DR InterPro; IPR007124; Hist_TAF. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR001951; Histone_H4. DR Pfam; PF00125; histone; 1. DR PRINTS; PR00623; HISTONEH4. DR ProDom; PD001827; Histone_H4; 1. DR SMART; SM00417; H4; 1. DR PROSITE; PS00047; HISTONE_H4; 1. KW Chromosomal protein; Nucleosome core; Nuclear protein; DNA-binding; KW Acetylation. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION. FT MOD_RES 5 5 ACETYLATION (IN MOST PLANTS). FT MOD_RES 8 8 ACETYLATION (IN MOST PLANTS). FT MOD_RES 12 12 ACETYLATION (IN MOST PLANTS). FT MOD_RES 16 16 ACETYLATION (IN MOST PLANTS). FT MOD_RES 20 20 ACETYLATION (IN SOME PLANTS). FT DNA_BIND 16 20 FT VARIANT 4 4 G -> D (IN WHEAT TH091 GENE). SQ SEQUENCE 102 AA; 11278 MW; 6A326B81CF831561 CRC64; SGRGKGGKGL GKGGAKRHRK VLRDNIQGIT KPAIRRLARR GGVKRISGLI YEETRGVLKI FLENVIRDAV TYTEHARRKT VTAMDVVYAL KRQGRTLYGF GG // ID HBL_MAIZE STANDARD; PRT; 165 AA. AC Q9FY42; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Non-symbiotic hemoglobin (Hbm) (ZEAma GLB1). GN HB OR GLB1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21575686; PubMed=11718894; RA Arechaga-Ocampo E., Saenz-Rivera J., Sarath G., Klucas R.V., RA Arredondo-Peter R.; RT "Cloning and expression analysis of hemoglobin genes from maize (Zea RT mays ssp. mays) and teosinte (Zea mays ssp. parviglumis)."; RL Biochim. Biophys. Acta 1522:1-8(2001). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Root; RA Guy P.A., Hill R.D.; RT "Sequence and analysis of a nonsymbiotic hemoglobin gene from maize."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May not function as an oxygen storage or transport CC protein, but might act as an oxygen sensor or play a role in CC electron transfer, possibly to a bound oxygen molecule. CC -!- TISSUE SPECIFICITY: In embryonic organs and at low levels in CC vegetative organs. CC -!- SIMILARITY: Belongs to the plant globin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AY005818; AAG01375.1; -. DR EMBL; AF236080; AAF44664.1; -. DR MaizeDB; 292897; -. DR HSSP; O04986; 1D8U. DR InterPro; IPR000971; Globin. DR InterPro; IPR001032; Leghaemoglobin. DR Pfam; PF00042; globin; 1. DR PRINTS; PR00188; PLANTGLOBIN. DR PROSITE; PS01033; GLOBIN; 1. DR PROSITE; PS00208; PLANT_GLOBIN; 1. KW Heme. FT METAL 73 73 Iron (heme distal ligand) (By FT similarity). FT METAL 108 108 Iron (heme proximal ligand) (By FT similarity). FT CONFLICT 51 51 E -> K (in Ref. 1). SQ SEQUENCE 165 AA; 18279 MW; 3BD9EF32723039ED CRC64; MALAEADDGA VVFGEEQEAL VLKSWAVMKK DAANLGLRFF LKVFEIAPSA EQMFSFLRDS DVPLEKNPKL KTHAMSVFVM TCEAAAQLRK AGKVTVRETT LKRLGATHLR YGVADGHFEV TGFALLETIK EALPADMWSL EMKKAWAEAY SQLVAAIKRE MKPDA // ID HKN1_MAIZE STANDARD; PRT; 359 AA. AC P24345; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Homeotic protein knotted-1. GN KN-1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91172321; PubMed=1672445; RA Vollbrecht E., Veit B., Sinha N., Hake S.; RT "The developmental gene Knotted-1 is a member of a maize homeobox RT gene family."; RL Nature 350:241-243(1991). RN [2] RP DEVELOPMENTAL EXPRESSION. RC STRAIN=cv. B73; RX MEDLINE=93130770; PubMed=1362381; RA Smith L.G., Green B., Veit B., Hake S.; RT "A dominant mutation in the maize homeobox gene, Knotted-1, causes its RT ectopic expression in leaf cells with altered fates."; RL Development 116:21-30(1992). CC -!- FUNCTION: Possible transcription factor that regulates genes CC involved in development. Mutations in KN-1 alter leaf development. CC Foci of cells along the lateral vein do not differentiate properly CC but continue to divide, forming knots. May participate in the CC switch from indeterminate to determinate cell fates. Probably CC binds to the DNA sequence 5'-TGAC-3'. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- TISSUE SPECIFICITY: Expressed in apical meristems of vegetative CC and floral stems as well as in the underlying ground meristem. CC Specifically expressed in vascular bundles developing both in the CC leaf and stem. Very low levels of expression in leaves. CC -!- DEVELOPMENTAL STAGE: Expressed throughout apical and vegetative CC meristem during development. Down-regulated as leaves and floral CC organs are initiated. CC -!- SIMILARITY: Belongs to the TALE/KNOX homeobox family. CC -!- SIMILARITY: Contains 1 homeobox domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61308; CAA43605.1; -. DR PIR; S14283; S14283. DR HSSP; P41778; 1DU6. DR TRANSFAC; T02062; -. DR MaizeDB; 65584; -. DR InterPro; IPR005539; ELK. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR005540; KNOX1. DR InterPro; IPR005541; KNOX2. DR Pfam; PF03789; ELK; 1. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF03790; KNOX1; 1. DR Pfam; PF03791; KNOX2; 1. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. KW DNA-binding; Homeobox; Transcription regulation; Nuclear protein. FT DOMAIN 22 30 Poly-His. FT DOMAIN 92 95 Poly-Ser. FT DOMAIN 264 270 Poly-Lys. FT DOMAIN 240 263 ELK domain. FT DNA_BIND 264 326 Homeobox; TALE-type. SQ SEQUENCE 359 AA; 39827 MW; 800FFD82082400FB CRC64; MEEITQHFGV GASSHGHGHG QHHHHHHHHH PWASSLSAVV APLPPQPPSA GLPLTLNTVA ATGNSGGSGN PVLQLANGGG LLDACVKAKE PSSSSPYAGD VEAIKAKIIS HPHYYSLLTA YLECNKVGAP PEVSARLTEI AQEVEARQRT ALGGLAAATE PELDQFMEAY HEMLVKFREE LTRPLQEAME FMRRVESQLN SLSISGRSLR NILSSGSSEE DQEGSGGETE LPEVDAHGVD QELKHHLLKK YSGYLSSLKQ ELSKKKKKGK LPKEARQQLL SWWDQHYKWP YPSETQKVAL AESTGLDLKQ INNWFINQRK RHWKPSEEMH HLMMDGYHTT NAFYMDGHFI NDGGLYRLG // ID HS21_MAIZE STANDARD; PRT; 161 AA. AC P24631; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE 17.5 kDa class II heat shock protein. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Ohio 43; TISSUE=Radicle; RX MEDLINE=91329703; PubMed=1714322; RA Goping I.S., Frappier J.R.H., Walden D.B., Atkinson B.G.; RT "Sequence, identification and characterization of cDNAs encoding two RT different members of the 18 kDa heat shock family of Zea mays L."; RL Plant Mol. Biol. 16:699-711(1991). CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54076; CAA38013.1; -. DR PIR; S14998; S14998. DR MaizeDB; 51309; -. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Heat shock; Multigene family. SQ SEQUENCE 161 AA; 17511 MW; 3E60A8DD4396577C CRC64; MDGRMFGLET PLMVALQHLL DVPDGDAGAG GDKAGGGGPT RTYVADARAM AVTPADVKEL PGAYAFVVDM PGLGTGDIKV QVEDERVLVI SGERRREERE DAKYLRMERR MGKFMRKFVL PDNADMDKIS AVCRDGVLTV TVEKLPPPEP KKPKTIEVKV A // ID HS22_MAIZE STANDARD; PRT; 164 AA. AC P24632; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE 17.8 kDa class II heat shock protein. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Ohio 43; TISSUE=Radicle; RX MEDLINE=91329703; PubMed=1714322; RA Goping I.S., Frappier J.R.H., Walden D.B., Atkinson B.G.; RT "Sequence, identification and characterization of cDNAs encoding two RT different members of the 18 kDa heat shock family of Zea mays L."; RL Plant Mol. Biol. 16:699-711(1991). CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54075; CAA38012.1; -. DR PIR; S14997; S14997. DR MaizeDB; 51309; -. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Heat shock; Multigene family. SQ SEQUENCE 164 AA; 17799 MW; AB8BBD01B9E9E163 CRC64; MDAVMFGLET PLMAALQHLL DVPDGDAGAG GDNKTGSGGS ATRTYVRDAR AMAATPADVK ELPGAYAFVV DMPGLGTGDI RVQVEDERVL VVSGERRREE REDDAKYLRM ERRMGKFMRK FVLPDNADVD KVAAVCRDGV LTVTVEKLPP PEPKKPKTIE VKVA // ID HS23_MAIZE STANDARD; PRT; 154 AA. AC Q08275; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE 17.0 kDa class II heat shock protein (HSP 18). GN HSP18. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Ohio 43; RX MEDLINE=93245391; PubMed=8482009; RA Atkinson B.G., Raizada M., Bouchard R.A., Frappier R.H., RA Walden D.B.; RT "The independent stage-specific expression of the 18-kDa heat shock RT protein genes during microsporogenesis in Zea mays L."; RL Dev. Genet. 14:15-26(1993). CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- INDUCTION: By stress; by heat shock. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S59777; AAB26481.1; -. DR PIR; A48425; A48425. DR MaizeDB; 51309; -. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20_chap. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Heat shock; Multigene family. SQ SEQUENCE 154 AA; 17047 MW; 89AC597050138B56 CRC64; MDARMFGLET PRVAALHHLL DVPDGDKAGG GATRTYVRDA RAMAATPADV KELAGAYAFV VDMPGLSTGD IRVQVEDERV LVISGERRRE EREDAKYLRM ERRMGKFMRK FVLPDNADVD KVAAVCRDGV LTVTVEKLPP PEPKKPKTIE IKVA // ID HS70_MAIZE STANDARD; PRT; 645 AA. AC P11143; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Heat shock 70 kDa protein. GN HSP70. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Rochester D.E., Winer J.A., Shah D.M.; RT "The structure and expression of maize genes encoding the major heat RT shock protein, hsp70."; RL EMBO J. 5:451-458(1986). CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03658; CAA27293.1; -. DR EMBL; X03697; CAA27330.1; -. DR EMBL; X03714; CAA27340.1; ALT_SEQ. DR PIR; A25089; A25089. DR HSSP; P08109; 1CKR. DR MaizeDB; 25911; -. DR InterPro; IPR001023; Hsp70. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR ProDom; PD000089; Hsp70; 1. DR PROSITE; PS00297; HSP70_1; 1. DR PROSITE; PS00329; HSP70_2; 1. DR PROSITE; PS01036; HSP70_3; 1. KW ATP-binding; Heat shock. SQ SEQUENCE 645 AA; 70602 MW; 4EB5CF224CB1733B CRC64; MAKSEGPAIG IDLGTTYSCV GLWQHDRVEI IANDQGNRTT PSYVGFTDTE RLIGDAAKNQ VAMNPTNTVF DAKRLIGRRF SSPAVQSSMK LWPSRHLGLG DKPMIVFNYK GEEKQFAAEE ISSMVLIKMK EIAEAYLGST IKNAVVTVPA YFNDSQRQAT KDAGVIAGLN VMRIINEPTA AAIAYGLDKK ATSSGEKNVL IFDLGGGTFD VSLLTIEEGI FEVKATAGDT HLGGEDFDNR MVNHFVQEFK RKNKKDISGN PRALRRLRTA CERAKRTLSS TAQTTIEIDS LFEGIDFTPR SSRARFEELN MDLFRKCMEP VEKCLRDAKM DKSSVHDVVL VGGSTRIPKV QQLQDFFNGK ELCKSINPDE AVAYGAAVQA AILSGEGNER SDLLLLDVTP LSLGLETAGG VMTVLIPRNT TIPTKKEQVF STYSDNQPGV LIQVYEGERA RTKDNNLLGK FELSGIPPAP RGVPQITVTF DIDVNNILNV SAEDKTTGQK NKITITNDKG RLSKEEIEKM VQEAEKYKAE DEEVKKKVDA KNALENYAYN MRNTIKDDKI ASKLPAEDKK KIEDAVDGAI SWLDSNQLAE VEEFEDKMKE LEGICNPIIA KMYXGEGAGM GAAAGMDEDA PSGGSGAGPK IEEVD // ID HS82_MAIZE STANDARD; PRT; 715 AA. AC Q08277; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Heat shock protein 82. GN HSP82. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Leaf, and Seedling; RX MEDLINE=93245392; PubMed=7683257; RA Marrs K.A., Casey E.S., Capitant S.A., Bouchard R.A., RA Dietrich P.S., Mettler I.J., Sinibaldi R.M.; RT "Characterization of two maize HSP90 heat shock protein genes: RT expression during heat shock, embryogenesis, and pollen RT development."; RL Dev. Genet. 14:27-41(1993). CC -!- FUNCTION: Molecular chaperone. Has ATPase activity (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (Potential). CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S59780; AAB26482.2; -. DR HSSP; P07900; 1YER. DR MaizeDB; 65833; -. DR InterPro; IPR003594; ATPbind_ATPase. DR InterPro; IPR001404; Hsp90. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00183; HSP90; 1. DR PRINTS; PR00775; HEATSHOCK90. DR SMART; SM00387; HATPase_c; 1. DR PROSITE; PS00298; HSP90; 1. KW Chaperone; ATP-binding; Heat shock. SQ SEQUENCE 715 AA; 81890 MW; 23EB0F3C46F08739 CRC64; MASADVHMAG GAETETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNAS DALDKIRFES LTDKSNVNAQ PELFIRLVPD KASKTLSIID SGVGMTKSDL VNNLGTIARS GTKEFMEALA AGATDVSMIG QFGVGFYSAY LVADRVMVTT KHNDDEQYVW ESQAGGSFTV THDTTGEQLG RGTKITLFLK DDQLEYLEER RLKDLVKKHS EFISYPIYLW TEKTTEKEIS DDEEEEDNKK EEEGDVEEVD DEDKDTKDKS KKKKKVKEVS HEWVQINKQK PIWLRKPEEI TRDEYASFYK SLTNDWEDHL AVKHFSVEGQ LEFKAILFVP RRAPFDLFDT RKKLNNIKLY VRRVFIMDNC EELIPEWLGF VKGVVDSDDL PLNISRETLQ QNKILKVIRK NLVKKCIEMF FEIAENKDDY AKFYDAFSKN IKLGIHEDSQ NRAKLADLLR YHSTKSGDET TSLKDYVTRM KEGQKDIYYI TGESRKAVEN SPFLERLKKK GYEVLFMVDA IDEYAVGQLK EYDGKKLVSA TKEGLKLDDE DDEEAKKRRE ERKKRFEELC KVIKDILGDR VEKVVVSDRI VDSPCCLVTG EYGWTANMER IMKAQALRDS SMSAYMSSKK TMEINPDNGI MEELRKRAEA DRNDKSVKDL VLLLFETALL TSGFSLDDPN TFAARIHRML KLGLNIDEDA AADEDADMPA LDEGAAEESK MEEVD // ID HX1A_MAIZE STANDARD; PRT; 719 AA. AC P46605; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Homeobox protein HOX1A. GN HOX1A. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Shoot; RX MEDLINE=92371444; PubMed=1354614; RA Bellmann R., Werr W.; RT "Zmhox1a, the product of a novel maize homeobox gene, interacts with RT the Shrunken 26 bp feedback control element."; RL EMBO J. 11:3367-3374(1992). CC -!- FUNCTION: Interacts with the shrunken (SHR) 26 bp feedback control CC element. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- TISSUE SPECIFICITY: Expressed in kernels, leaves and shoots but CC not in roots. CC -!- SIMILARITY: Belongs to the PHD-associated homeobox family. CC -!- SIMILARITY: Contains 1 homeobox domain. CC -!- SIMILARITY: Contains 1 PHD-type zinc finger. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67561; CAA47859.1; -. DR PIR; S25237; S25237. DR TRANSFAC; T00922; -. DR MaizeDB; 25707; -. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR001965; Znf_PHD. DR Pfam; PF00046; homeobox; 1. DR Pfam; PF00628; PHD; 1. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00249; PHD; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. KW Homeobox; DNA-binding; Nuclear protein; Transcription regulation; KW Zinc-finger. FT DOMAIN 195 464 Asp/Glu-rich (acidic). FT ZN_FING 209 266 PHD-type. FT DNA_BIND 559 618 Homeobox. SQ SEQUENCE 719 AA; 79116 MW; 5536608CA71CB318 CRC64; MEKNIAHCPV EGNGEIENGA SSSQNPESLE HSVLLSTSQT MPNNLGIRKN YKRAANRGKK GSQGLTGQAY TLMSSNSDVR VLRSTSSSKT TSTEHVQAPV QPAAKRRKMS RASNKSSTDE FSQIRKRVRY ILNRMNYEQS LIEAYASEGW KNQSLDKIRP EKELERAKSE ILRCKLRIRE VFRNIDSLLS KGKIDETLFD SEGEISCEDI FCSTCGSNDA TLGNDIILCD GACDRGFHQN CLNPPLRTED IPMGDEGWLC PACDCKIDCI DLINELHGSN ISIEDSWEKV FPDAAAMAND SKQDDAFDLP SDDSDDNDFD PNMPEEHVVG KDEESSEEDE DGGSDSDDSD FLTCSDDSEP LIDKKVDDLR LPSEDSEDDD YDPAGPDSDK DVEKKSSSDE SDFTSDSDDF CKEISKSGHD EVSSPLLPDA KVGDMEKITA QAKTTSSADD PMETEIDQGV VLPDSRRRQA ERLDYKKLYD EAYGEASSDS SDDEEWSGKN TPIIKSNEEG EANSPAGKGS RVVHHNDELT TQSTKKSLHS IHGSVDEKPG DLTSNGSNST ARKGHFGPVI NQKLHEHFKT QPYPSRSVKE SLAEELGLTF RQVNKWFETR RHSARVASSR KGISLDKHSP QNTNSQVTAS MEPKEPEGTV VEESNVCLNG GTTISKEAVS SKVGSRTPGS DVGGSKVDSA EDQNPGPDLA EKARQKAIQQ ELRKKKMGR // ID IAAG_MAIZE STANDARD; PRT; 471 AA. AC Q41819; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Indole-3-acetate beta-glucosyltransferase (EC 2.4.1.121) (IAA-Glu DE synthetase) ((Uridine 5'-diphosphate-glucose:indol-3-ylacetyl)-beta-D- DE glucosyl transferase). GN IAGLU. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-18. RC TISSUE=Endosperm; RX MEDLINE=94367368; PubMed=8085154; RA Szerszen J.B., Szczyglowski K., Bandurski R.S.; RT "Iaglu, a gene from Zea mays involved in conjugation of growth RT hormone indole-3-acetic acid."; RL Science 265:1699-1701(1994). CC -!- CATALYTIC ACTIVITY: UDP-glucose + indole-3-acetate = UDP + CC indole-3-acetyl-beta-1-D-glucose. CC -!- PATHWAY: Indole-3-acetic acid conjugation pathway; first step. CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L34847; AAA59054.1; -. DR PIR; A54739; A54739. DR MaizeDB; 83603; -. DR InterPro; IPR002213; UDP_gluco_trans. DR Pfam; PF00201; UDPGT; 1. DR PROSITE; PS00375; UDPGT; 1. KW Transferase; Glycosyltransferase. FT DOMAIN 80 85 Poly-Ala. SQ SEQUENCE 471 AA; 49710 MW; 99A7F56C2BB4EB39 CRC64; MAPHVLVVPF PGQGHMNPMV QFAKRLASKG VATTLVTTRF IQRTADVDAH PAMVEAISDG HDEGGFASAA GVAEYLEKQA AAASASLASL VEARASSADA FTCVVYDSYE DWVLPVARRM GLPAVPFSTQ SCAVSAVYYH FSQGRLAVPP GAAADGSDGG AGAAALSEAF LGLPEMERSE LPSFVFDHGP YPTIAMQAIK QFAHAGKDDW VLFNSFEELE TEVLAGLTKY LKARAIGPCV PLPTAGRTAG ANGRITYGAN LVKPEDACTK WLDTKPDRSV AYVSFGSLAS LGNAQKEELA RGLLAAGKPF LWVVRASDEH QVPRYLLAEA TATGAAMVVP WCPQLDVLAH PAVGCFVTHC GWNSTLEALS FGVPMVAMAL WTDQPTNARN VELAWGAGVR ARRDAGAGVF LRGEVERCVR AVMDGGEAAS AARKAAGEWR DRARAAVAPG GSSDRNLDEF VQFVRAGATE K // ID IAAT_MAIZE STANDARD; PRT; 206 AA. AC P13867; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Alpha-amylase/trypsin inhibitor (Antifungal protein). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RA Richardson M., Valdes-Rodriguez S., Blanco-Labra A.; RT "A possible function for thaumatin and a TMV-induced protein RT suggested by homology to a maize inhibitor."; RL Nature 327:432-434(1987). RN [2] RP SEQUENCE. RC TISSUE=Seed; RX MEDLINE=92117998; PubMed=1731773; RA Huynh Q.K., Borgmeyer J.R., Zobel J.F.; RT "Isolation and characterization of a 22 kDa protein with antifungal RT properties from maize seeds."; RL Biochem. Biophys. Res. Commun. 182:1-5(1992). CC -!- FUNCTION: Inhibits both trypsin and alpha-amylase. Inhibits the CC growth of some plant fungal pathogens. CC -!- SIMILARITY: Belongs to the thaumatin family. DR PIR; A29581; A29581. DR HSSP; P33679; 1DU5. DR MaizeDB; 69169; -. DR InterPro; IPR001938; Thaumatin. DR Pfam; PF00314; thaumatin; 1. DR PRINTS; PR00347; THAUMATIN. DR ProDom; PD001321; Thaumatin; 1. DR SMART; SM00205; THN; 1. DR PROSITE; PS00316; THAUMATIN; 1. KW Plant defense; Serine protease inhibitor; Fungicide. FT DISULFID 9 205 By similarity. FT DISULFID 51 61 By similarity. FT DISULFID 66 72 By similarity. FT DISULFID 118 194 By similarity. FT DISULFID 124 177 By similarity. FT DISULFID 132 142 By similarity. FT DISULFID 146 155 By similarity. FT DISULFID 156 164 By similarity. FT CONFLICT 108 108 Y -> M (in Ref. 2). SQ SEQUENCE 206 AA; 22075 MW; 6C73E1BACAE090DE CRC64; AVFTVVNQCP FTVWAASVPV GGGRQLNRGE SWRITAPAGT TAARIWARTG CQFDASGRGS CRTGDCGGVV QCTGYGRAPN TLAEYALKQF NNLDFFDISI LDGFNVPYSF LPDGGSGCSR GPRCAVDVNA RCPAELRQDG VCNNACPVFK KDEYCCVGSA ANNCHPTNYS RYFKGQCPDA YSYPKDDATS TFTCPAGTNY KVVFCP // ID IF1C_MAIZE STANDARD; PRT; 107 AA. AC P46618; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Translation initiation factor IF-1, chloroplast. GN INFA. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: No specific function has so far been attributed to this CC initiation factor; however, it seems to stimulate more or less all CC the activities of the other two initiation factors, IF-2 and IF-3. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the IF-1 family. CC -!- SIMILARITY: Contains 1 S1-like domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60320.1; -. DR PIR; S58586; S58586. DR HSSP; P02998; 1AH9. DR Gramene; P46618; -. DR MaizeDB; 118240; -. DR HAMAP; MF_00075; -; 1. DR InterPro; IPR008994; Nucleic_acid_OB. DR InterPro; IPR003029; S1. DR InterPro; IPR006196; S1_IF1. DR InterPro; IPR004368; TIF_IF1. DR Pfam; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR TIGRFAMs; TIGR00008; infA; 1. DR PROSITE; PS50832; S1_IF1_TYPE; 1. KW Initiation factor; Protein biosynthesis; Chloroplast. FT DOMAIN 8 83 S1-like. SQ SEQUENCE 107 AA; 12376 MW; 23AB0E01F55D0A15 CRC64; MTEKKNSREK KNPREAKVTF EGLVTEALPN GMFRVRLEND TIILGYISGK IRSSSIRILM GDRVKIEISR YDSSKGRIIY RLPHKDSKRT EDSKDTEDLK DTKDSKD // ID IF4A_MAIZE STANDARD; PRT; 410 AA. AC Q41741; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Eukaryotic initiation factor 4A (eIF4A) (eIF-4A). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ear; RX MEDLINE=95357429; PubMed=7630958; RA Jayachandran S., Bailey-Serres J.; RT "Nucleotide sequence of a cDNA for the maize protein synthesis RT initiation factor 4A."; RL Plant Physiol. 108:1317-1318(1995). CC -!- FUNCTION: EIF4A is both a subunit of a high molecular weight CC protein complex involved in cap recognition and is required as a CC single polypeptide chain for mRNA binding to ribosome. It is an CC ATP-dependent single stranded DNA-binding protein with a sequence- CC independent unwinding activity (helicase). CC -!- SUBUNIT: EIF4F is a multi-subunit complex, the composition of CC which varies with external and internal environmental conditions. CC It is composed of at least EIF4A, EIF4E and EIF4G (By similarity). CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U17979; AAA82736.1; -. DR HSSP; Q58083; 1HV8. DR MaizeDB; 112980; -. DR InterPro; IPR001410; DEAD. DR InterPro; IPR000629; DEAD_box. DR InterPro; IPR001650; Helicase_C. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. KW Initiation factor; Protein biosynthesis; ATP-binding; RNA-binding; KW DNA-binding; Helicase. FT NP_BIND 81 88 ATP (By similarity). FT SITE 186 189 DEAD box. SQ SEQUENCE 410 AA; 46536 MW; B9B8AB78ED3CE184 CRC64; MAGLAPEGSQ FDDKQYDKKM QEILTEDFFT SYDDVCESFD SMGLQENLLR GIYAYGFEKP SAIQQRGIVP FCKGLDVIQQ AQSGTGKTAT FCSGILQQLD YGLVECQALV LAPTRELAQQ IEKVMRALGD YLGVKVHACV GGTSVREDQR ILASGVHVVV GTPGRVFDML RRQSLRPDNI KMFVLDEADE MLSRGFKDQI YDIFQLLPSK IQVGVFSATM PPEALEITRK FMNKPVRILV KRDELTLEGI KQFYVNIDKE DWKLDTLCDL YETLAITQSV IFVNTRRKVD WLTDKMRSRD HTVSATHGDM DQNTRDIIMR EFRSGSSRVL ITTDLLARGI DVQQVSLVIN YDLPTQPENY LHRIGRSGRF GRKGVAINFV TRDDERIVFD VQRFYNVTVE ELPANVADLL // ID IF5A_MAIZE STANDARD; PRT; 160 AA. AC P80639; P56332; DT 01-OCT-1996 (Rel. 34, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Eukaryotic translation initiation factor 5A (eIF-5A) (eIF-4D). GN TIF5A. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RA Korn A.M., Baysdorfer C.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; RA Cordts S., Loerz H., Dresselhaus T.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 71-78 AND 118-129. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- FUNCTION: The precise role of eIF-5A in protein biosynthesis is CC not known but it functions by promoting the formation of the first CC peptide bond. CC -!- PTM: eIF-5A seems to be the only eukaryotic protein to have an CC hypusine residue which is a post-translational modification of a CC lysine by the addition of a butylamino group (from spermidine). CC -!- SIMILARITY: Belongs to the eIF-5A family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF034943; AAB88614.1; -. DR EMBL; Y07920; CAA69225.1; -. DR PIR; T01355; T01355. DR Maize-2DPAGE; P80639; COLEOPTILE. DR HSSP; Q58625; 2EIF. DR MaizeDB; 123964; -. DR InterPro; IPR001884; EIF5A_hypusine. DR InterPro; IPR005824; KOW. DR InterPro; IPR008991; Transl_SH3_like. DR Pfam; PF01287; eIF-5a; 1. DR Pfam; PF00467; KOW; 1. DR TIGRFAMs; TIGR00037; eIF_5A; 1. DR PROSITE; PS00302; IF5A_HYPUSINE; 1. KW Protein biosynthesis; Initiation factor; Hypusine. FT MOD_RES 53 53 HYPUSINE (BY SIMILARITY). SQ SEQUENCE 160 AA; 17497 MW; 7CCFADFB2EC09CAD CRC64; MSDSEEHHFE SKADAGASKT YPQQAGTVRK NGFIVIKNRP CKVVEVSTSK TGKHGHAKCH FVAIDIFNGK KLEDIVPSSH NCDIPHVNRT EYQLIDISED GFVSLLTSDG NTKDDLRLPT DETLVAQIKE GFESGKDLVV TVQSAMGEEQ ICALKDVGPK // ID IF5_MAIZE STANDARD; PRT; 451 AA. AC P55876; Q9SBX1; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Eukaryotic translation initiation factor 5 (eIF-5). GN EIF5. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97382467; PubMed=9240471; RA Lopez Ribera I.R., Ruiz-Avila L., Puigdomenech P.; RT "The eukaryotic translation initiation factor-5, elF-5, a protein from RT Zea mays, containing a zinc-finger structure, binds nucleic acids in a RT zinc-dependent manner."; RL Biochem. Biophys. Res. Commun. 236:510-516(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RX MEDLINE=20047915; PubMed=10580155; RA Lopez Ribera I.R., Puigdomenech P.; RT "Structure, organization and expression of the eukaryotic translation RT initiation factor 5, eIF-5, gene in Zea mays."; RL Gene 240:355-359(1999). CC -!- FUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S CC ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with CC the subsequent joining of a 60S ribosomal subunit resulting in the CC release of eIF-2 and the guanine nucleotide. The subsequent CC joining of a 60S ribosomal subunit results in the formation of a CC functional 80S initiation complex (80S.mRNA.Met-tRNA[F]). CC -!- SIMILARITY: Belongs to the eIF-2-beta / eIF-5 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X99517; CAA67868.1; -. DR EMBL; AJ132240; CAA10616.1; -. DR PIR; JC5595; JC5595. DR MaizeDB; 66866; -. DR InterPro; IPR002735; eIF5_eIF2B. DR InterPro; IPR003307; eIF5C. DR Pfam; PF01873; eIF5_eIF2B; 1. DR Pfam; PF02020; W2; 1. DR ProDom; PD004078; eIF5_eIF2B; 1. DR SMART; SM00653; eIF2B_5; 1. DR SMART; SM00515; eIF5C; 1. KW Initiation factor; Protein biosynthesis; GTP-binding. FT NP_BIND 29 36 GTP (Potential). FT DOMAIN 227 232 Poly-Asp. FT CONFLICT 339 339 P -> L (in Ref. 2). SQ SEQUENCE 451 AA; 48912 MW; AB6D5AC15F8EB661 CRC64; MALQNIGASN RDDAFYRYKM PRMITKIEGR GNGIKTNVVN MVDIAKALAR PASYTTKYFG CELGAQSKFD EKTGISLVNG AHDTAKLAGL LEVFIKKYVQ CYGCGNPETE ILISKTQMIS LKCAACGFVS DVDMRDKLTT FILKNPPEQK KGGKDKKAMR RAEKERLKEG EAADEEQKKL KKDAKKKGSK DSTAKGLKKK ATTATGSDED HSSSPTRSHD GDKAAADDDD DDVQWQTDTS IEAAKQRMQE QLSAATAEMV MLSTEETEKK MKQPTHKDGS TNGSAKEIPN DKPAVTKPSP YEELIGDIKA SLGSAPTPSQ LKAVLASSTL PPQDVMNAPL EALFGGVGKG FTKEVVKNKK YLAVAVPDEG AQTLLVQAIE AFGGKCNPEA LKEVPVVLKA LYDGDILDEE TIVDWYNDAV AAGKDSQVVK NAKPFVEWLQ SAESDEEGDD E // ID IFRH_MAIZE STANDARD; PRT; 309 AA. AC P52580; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Isoflavone reductase homolog IRL (EC 1.3.1.-). GN IRL. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Dekalb XL72; RX MEDLINE=96158112; PubMed=8597660; RA Petrucco S., Bolchi A., Foroni C., Percudani R., Rossi G.L., RA Ottonello S.; RT "A maize gene encoding an NADPH binding enzyme highly homologous to RT isoflavone reductases is activated in response to sulfur RT starvation."; RL Plant Cell 8:69-80(1996). CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- INDUCTION: By sulfur deprivation. CC -!- SIMILARITY: Belongs to the isoflavone reductase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U33318; AAC49210.1; -. DR PIR; T02304; T02304. DR MaizeDB; 123916; -. DR InterPro; IPR003866; Isoflav_reduct. DR Pfam; PF02716; Isoflavone_redu; 1. KW Oxidoreductase; NADP. SQ SEQUENCE 309 AA; 32851 MW; 138314D67B16BA5B CRC64; MASEKSKILV VGGTGYLGRH VVAASARLGH PTSALVRDTA PSDPAKAALL KSFQDAGVTL LKGDLYDQAS LVSAVKGADV VISVLGSMQI ADQSRLVDAI KEAGNVKRFF PSEFGLDVDR TGIVEPAKSI LGAKVGIRRA TEAAGIPYTY AVAGFFAGFG LPKVGQVLAP GPPADKAVVL GDGDTKAVFV EEGDIATYTV LAADDPRAEN KVLYIKPPAN TLSHNELLSL WEKKTGKTFR REYVPEEAVL KQIQESPIPL NIILAIGHAA FVRGEQTGFE IDPAKGVDAS ELYPDVKYTT VDEYLNRFL // ID IN21_MAIZE STANDARD; PRT; 243 AA. AC P49248; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE IN2-1 protein. GN IN2-1 OR SAF1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Missouri 17; RX MEDLINE=92003682; PubMed=1912492; RA Hershey H.P., Stoner T.D.; RT "Isolation and characterization of cDNA clones for RNA species RT induced by substituted benzenesulfonamides in corn."; RL Plant Mol. Biol. 17:679-690(1991). CC -!- TISSUE SPECIFICITY: Leaves and roots. It is more strongly induced CC in the leaves relative to the roots. CC -!- DEVELOPMENTAL STAGE: It appears in the roots within 30 min of CC induction, maximum levels are reached by 6 hrs, and remains CC constant for 2 days. In leaves it is seen 9 hrs after induction, CC and reaches maximum levels after 24 hrs. CC -!- INDUCTION: By N-(aminocarbonyl)-2-chlorobenzenesulfonamide (2- CC CBSU). CC -!- SIMILARITY: Some, to S.tuberosum pathogenesis-related protein 1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58573; CAA41447.1; -. DR PIR; S17743; S17743. DR MaizeDB; 121983; -. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR Pfam; PF00043; GST_C; 1. SQ SEQUENCE 243 AA; 26988 MW; 2A971ED2C0309E52 CRC64; MAAAAGPSSS VKESLPPALG STSQPPPVFD GTTRLYICYF CPFAQRAWVT RNLKGLQDKM ELVAIDLQDK PAWYKDKVYA QGTVPSLEHD SEVRGESLDL IRYIDSNFDG PALLPEDAAK RQFADELFAS ANAFTKALYS PLLSHAAVSD EVVAALDKLE ADLSKFDDGP FFLGQFSLAD VAYVTILERV QIYYSHLRNY DIAQGRPNLQ EFIDEMNKIE AYAQTKNDPL FLLDLAKSHL KIA // ID IN22_MAIZE STANDARD; PRT; 306 AA. AC P49249; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE IN2-2 protein. GN IN2-2 OR SAF2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Missouri 17; RX MEDLINE=92003682; PubMed=1912492; RA Hershey H.P., Stoner T.D.; RT "Isolation and characterization of cDNA clones for RNA species RT induced by substituted benzenesulfonamides in corn."; RL Plant Mol. Biol. 17:679-690(1991). CC -!- TISSUE SPECIFICITY: Leaves and roots. CC -!- DEVELOPMENTAL STAGE: It appears in roots within 30 min of CC induction, maximum levels are reached by 6 hrs, and remains CC constant for 2 days. In leaves it is seen 9 hrs after induction, CC and reaches maximum levels after 24 hrs. CC -!- INDUCTION: By N-(aminocarbonyl)-2-chlorobenzenesulfonamide (2- CC CBSU). CC -!- SIMILARITY: Belongs to the aldo/keto reductase 2 family. DR MaizeDB; 121988; -. DR InterPro; IPR001395; Aldo/ket_red. DR Pfam; PF00248; aldo_ket_red; 1. DR PRINTS; PR00069; ALDKETRDTASE. DR ProDom; PD000288; Aldo/ket_red; 1. KW Oxidoreductase. FT ACT_SITE 131 131 Hydrogen-bond donor (Probable). SQ SEQUENCE 306 AA; 33828 MW; 2E94674C7FDE3CBD CRC64; MAAALVSVPR IKLGSQGLEV SAQGLGCMGM SAFYGPPKPE SEMIKLIHHA VDAGVTFLDT SDVYGPHTNE VLLGKALQGG VREKVELATK FGVSFADGKR EIHGDPAYVR TACEGSFKRL GVDCIDLYYQ HRIDKRVPIE VTIGELKKLV EEGKIKYIGL SEASASTIRR AHAVHPITAV QLEWSLWSRD AEEDIIPTCR ELGIGIVAYS PLGRGFFSSG AKLVDSLSEQ DFRKHMPRFQ PENLDKNAQI FERVRRDGST ERMHAITARV GLGSPPRKRR LPHTWHNKNR QLQPERGGTV CEAYTG // ID INV1_MAIZE STANDARD; PRT; 670 AA. AC P49175; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Beta-fructofuranosidase 1 precursor (EC 3.2.1.26) (Sucrose-6-phosphate DE hydrolase 1) (Invertase 1). GN IVR1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RX MEDLINE=95357417; PubMed=7630946; RA Xu J., Pemberton G.H., Almira E.C., McCarty D.R., Koch K.E.; RT "The Ivr 1 gene for invertase in maize."; RL Plant Physiol. 108:1293-1294(1995). CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D- CC fructofuranoside residues in beta-D-fructofuranosides. CC -!- SUBCELLULAR LOCATION: Vacuolar. CC -!- SIMILARITY: Belongs to family 32 of glycosyl hydrolases. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U16123; AAA83439.1; -. DR PIR; T02092; T02092. DR MaizeDB; 86037; -. DR InterPro; IPR001362; Glyco_hydro_32. DR Pfam; PF00251; Glyco_hydro_32; 1. DR SMART; SM00640; Glyco_32; 1. DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1. KW Hydrolase; Glycosidase; Glycoprotein; Zymogen; Signal; KW Multigene family. FT SIGNAL 1 ? Potential. FT PROPEP ? ? Potential. FT CHAIN ? 670 Beta-fructofuranosidase 1. FT ACT_SITE 139 139 By similarity. FT CARBOHYD 165 165 N-linked (GlcNAc...) (Potential). FT CARBOHYD 275 275 N-linked (GlcNAc...) (Potential). FT CARBOHYD 518 518 N-linked (GlcNAc...) (Potential). FT CARBOHYD 595 595 N-linked (GlcNAc...) (Potential). FT CARBOHYD 639 639 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 670 AA; 71932 MW; DEDE0989C7E6AEB0 CRC64; MIPAVADPTT LDGGGARRPL LPETDPRGRA AAGAEQKRPP ATPTVLTAVV SAVLLLVLVA VTVLASQHVD GQAGGVPAGE DAVVVEVAAS RGVAEGVSEK STAPLLGSGA LQDFSWTNAM LAWQRTAFHF QPPKNWMNDP NGPLYHKGWY HLFYQWNPDS AVWGNITWGH AVSRDLLHWL HLPLAMVPDH PYDANGVWSG SATRLPDGRI VMLYTGSTAE SSAQVQNLAE PADASDPLLR EWVKSDANPV LVPPPGIGPT DFRDPTTACR TPAGNDTAWR VAIGSKDRDH AGLALVYRTE DFVRYDPAPA LMHAVPGTGM WECVDFYPVA AGSGAAAGSG DGLETSAAPG PGVKHVLKAS LDDDKHDYYA IGTYDPATDT WTPDSAEDDV GIGLRYDYGK YYASKTFYDP VLRRRVLWGW VGETDSERAD ILKGWASVQS IPRTVLLDTK TGSNLLQWPV VEVENLRMSG KSFDGVALDR GSVVPLDVGK ATQLDIEAVF EVDASDAAGV TEADVTFNCS TSAGAAGRGL LGPFGLLVLA DDDLSEQTAV YFYLLKGTDG SLQTFFCQDE LRASKANDLV KRVYGSLVPV LDGENLSVRI LVDHSIVESF AQGGRTCITS RVYPTRAIYD SARVFLFNNA THAHVKAKSV KIWQLNSAYI RPYPATTTSL // ID INVA_MAIZE STANDARD; PRT; 590 AA. AC P49174; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Beta-fructofuranosidase, cell wall isozyme precursor (EC 3.2.1.26) DE (Sucrose-6-phosphate hydrolase) (Invertase). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Black Mexican Sweet; RA Shanker S.; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D- CC fructofuranoside residues in beta-D-fructofuranosides. CC -!- SUBCELLULAR LOCATION: Cell wall. CC -!- INDUCTION: By wounding and bacterial infection. CC -!- SIMILARITY: Belongs to family 32 of glycosyl hydrolases. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U17695; AAA64487.1; -. DR PIR; T02096; T02096. DR MaizeDB; 113032; -. DR InterPro; IPR001362; Glyco_hydro_32. DR Pfam; PF00251; Glyco_hydro_32; 1. DR SMART; SM00640; Glyco_32; 1. DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; FALSE_NEG. KW Hydrolase; Glycosidase; Glycoprotein; Cell wall; Signal. FT SIGNAL 1 28 Potential. FT CHAIN 29 590 Beta-fructofuranosidase, cell wall FT isozyme. FT ACT_SITE 68 68 By similarity. FT CARBOHYD 190 190 N-linked (GlcNAc...) (Potential). FT CARBOHYD 341 341 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 590 AA; 65198 MW; 296455E61E99B892 CRC64; MGTRPRGVVL APWAVVLVLV LALRLAGASH VIHRSLEAEA APSVPASIVS PLLRTGYHFQ PPMNWINDPN APLYYKGWYH LFYQYNPKGA VWGNIVWAHS VSRDLINWVA LEPAIYPSIP SDKYGCWSGS ATILEDGTPA ILYTGIDRAD INYQVQVLAL PKDASDPLLR EWEKPEEYNP VATPAAGGIN ATQFRDPTTA WRHAGHWRML VGSVRGARGM ALVYRSRDFR KWTKAKHPLH SAALTGMWEC PDFFPVSGPG LQAGLDTSAP GTKYVLKSSL DLTRYDYYTI GSYDGGKDRY YPDDPAGDYH HRRRYDYGNY YASKTFYDPV ERRRVLLGWA NESDSVPDDK AKGWAGIHAI PRKIWLDPTG KQLLQWPIHE VEKLRGKAVS VDAKLVKPGD HFEVTGIATY QADVEVSFEL ELEAGTSLLE KAEAFDPAYD DDAQKLCGVK GADARGGVGP FGLWVLASAD LQERTAVFFR VFRDGHGKPK VLMCTDPTKS SLSPDLYKPT FAGFVDADIS SGKITLRSLI DRSVVESFGA GGKTCILSRV YPSIAVGKDA HLYVFNNGEV DVTVSGLTAW EMKKPLMNGA // ID ITRF_MAIZE STANDARD; PRT; 155 AA. AC P01088; DT 21-JUL-1986 (Rel. 01, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Trypsin/factor XIIA inhibitor precursor (Hageman factor inhibitor) DE (CHFI). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; TISSUE=Endosperm; RX MEDLINE=92216060; PubMed=1558956; RA Wen L., Huang J.K., Zen K.C., Johnson B.H., Muthukrishnan S., RA Mackay V., Manney T.R., Manney M., Reeck G.R.; RT "Nucleotide sequence of a cDNA clone that encodes the maize inhibitor RT of trypsin and activated Hageman factor."; RL Plant Mol. Biol. 18:813-814(1992). RN [2] RP SEQUENCE OF 29-138. RC TISSUE=Seed; RX MEDLINE=84239823; PubMed=6610678; RA Mahoney W.C., Hermodson M.A., Jones B., Powers D.D., Corfman R.S., RA Reeck G.R.; RT "Amino acid sequence and secondary structural analysis of the corn RT inhibitor of trypsin and activated Hageman factor."; RL J. Biol. Chem. 259:8412-8416(1984). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 33-148. RX MEDLINE=99017881; PubMed=9799488; RA Behnke C.A., Yee V.C., le Trong I., Pedersen L.C., Stenkamp R.E., RA Kim S.-S., Reeck G.R., Teller D.C.; RT "Structural determinants of the bifunctional corn Hageman factor RT inhibitor: X-ray crystal structure at 1.95-A resolution."; RL Biochemistry 37:15277-15288(1998). CC -!- FUNCTION: Potent inhibitor of mammalian trypsin and a specific CC inhibitor of factor XIIa (activated hageman factor). CC -!- SUBUNIT: Monomer. CC -!- MISCELLANEOUS: The sequence heterogeneity suggests that 2 genes CC exist for this inhibitor. The genes may be alleles, or multiple CC loci could exist. CC -!- SIMILARITY: Belongs to the cereal trypsin/alpha-amylase inhibitor CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54064; CAA37998.1; -. DR PIR; S20850; TIZM1. DR PDB; 1BEA; 12-AUG-98. DR PDB; 1BFA; 12-AUG-98. DR MaizeDB; 25928; -. DR InterPro; IPR003612; AAI. DR InterPro; IPR006106; Amylase_inhib. DR InterPro; IPR006105; Try/amyl_inhib. DR Pfam; PF00234; tryp_alpha_amyl; 1. DR PRINTS; PR00808; AMLASEINHBTR. DR SMART; SM00499; AAI; 1. DR PROSITE; PS00426; CEREAL_TRYP_AMYL_INH; 1. KW Serine protease inhibitor; Seed; Signal; 3D-structure. FT SIGNAL 1 28 FT CHAIN 29 138 Trypsin/factor XIIA inhibitor. FT PROPEP 139 155 C-terminal peptide. FT ACT_SITE 62 62 FT DISULFID 34 83 FT DISULFID 48 72 FT DISULFID 57 114 FT DISULFID 73 132 FT DISULFID 85 143 FT VARIANT 117 117 E -> A. FT CONFLICT 49 49 R -> C (in Ref. 2). FT CONFLICT 56 56 T -> R (in Ref. 2). FT CONFLICT 62 62 R -> RPR (in Ref. 2). FT CONFLICT 107 107 R -> A (in Ref. 2). FT CONFLICT 116 116 R -> A (in Ref. 2). FT CONFLICT 120 120 R -> Q (in Ref. 2). FT CONFLICT 135 135 A -> E (in Ref. 2). FT STRAND 36 36 FT TURN 37 39 FT STRAND 40 40 FT HELIX 46 57 FT HELIX 65 77 FT TURN 78 78 FT HELIX 81 83 FT HELIX 84 93 FT STRAND 95 95 FT STRAND 105 105 FT STRAND 111 111 FT TURN 112 113 FT STRAND 114 114 FT HELIX 116 123 FT TURN 124 127 FT TURN 129 132 FT TURN 137 138 FT TURN 144 146 SQ SEQUENCE 155 AA; 16302 MW; A31A8AA3BA19DE7A CRC64; MASSSSSSHR RLILAAAVLL SVLAAASASA GTSCVPGWAI PHNPLPSCRW YVTSRTCGIG PRLPWPELKR RCCRELADIP AYCRCTALSI LMDGAIPPGP DAQLEGRLED LPGCPREVQR GFAATLVTEA ECNLATISGV AECPWILGGG TMPSK // ID ITRY_MAIZE STANDARD; PRT; 65 AA. AC P01073; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 01-OCT-1994 (Rel. 30, Last annotation update) DE Trypsin inhibitor. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Seed; RX MEDLINE=70226643; PubMed=5425943; RA Hochstrasser K., Illchmann K., Werle E.; RT "Plant protease inhibitors. VII. Amino acid sequence of the specific RT trypsin inhibitor from maize seeds, and characterization of the RT polymer."; RL Hoppe-Seyler's Z. Physiol. Chem. 351:721-728(1970). CC -!- SUBUNIT: Homotrimer. CC -!- MISCELLANEOUS: After interaction with trypsin, the inhibitor CC consists of two chains (residues 1-25 and 26-65 above) linked by CC disulfide bonds. DR PIR; A01312; TIZM. DR HSSP; P01087; 1BIP. DR MaizeDB; 69176; -. KW Serine protease inhibitor. FT ACT_SITE 25 26 REACTIVE BOND (TRYPSIN). SQ SEQUENCE 65 AA; 6981 MW; EF727CAF1D5FB346 CRC64; SAGTSCVPPP SBGCHAILRT GIPGRLPPLZ KTCGIGPRQV ZRLQBLPCPG RRQLABMIAY CPRCR // ID IWP1_MAIZE STANDARD; PRT; 102 AA. AC P31862; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Bowman-Birk type wound induced proteinase inhibitor WIP1 precursor. GN WIP1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Brio; RX MEDLINE=93363912; PubMed=8358030; RA Rohrmeier T., Lehle L.; RT "WIP1, a wound-inducible gene from maize with homology to Bowman-Birk RT proteinase inhibitors."; RL Plant Mol. Biol. 22:783-792(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. Brio; TISSUE=Seedling; RX MEDLINE=93265947; PubMed=8495751; RA Eckelkamp C., Ehmann B., Schopfer P.; RT "Wound-induced systemic accumulation of a transcript coding for a RT Bowman-Birk trypsin inhibitor-related protein in maize (Zea mays L.) RT seedlings."; RL FEBS Lett. 323:73-76(1993). CC -!- INDUCTION: By wounding. CC -!- SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X71396; CAA50519.1; -. DR PIR; S36236; S36236. DR MaizeDB; 46002; -. DR InterPro; IPR000877; Bowman-Birk_leg. DR Pfam; PF00228; Bowman-Birk_leg; 2. DR ProDom; PD002168; Bowman-Birk_leg; 1. DR SMART; SM00269; BowB; 1. DR PROSITE; PS00281; BOWMAN_BIRK; 1. KW Serine protease inhibitor; Signal. FT SIGNAL 1 15 Potential. FT CHAIN 16 102 Bowman-Birk type wound induced proteinase FT inhibitor WIP1. FT ACT_SITE 52 53 Reactive bond (By similarity). FT CONFLICT 11 11 L -> V (in Ref. 2). SQ SEQUENCE 102 AA; 10976 MW; 2BDBEC44FA79C179 CRC64; MKSSPHLVLI LCLQAALVMG VFAALAKENA MVESKAIDIN PGQLKCCTNC NFSFSGLYTC DDVKKDCDPV CKKCVVAVHA SYSGNNKFRC TDTFLGMCGP KC // ID KADC_MAIZE STANDARD; PRT; 222 AA. AC P43188; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Adenylate kinase, chloroplast (EC 2.7.4.3) (ATP-AMP DE transphosphorylase). GN ADK1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Leaf; RX MEDLINE=94298837; PubMed=8026505; RA Schiltz E., Burger S., Grafmueller R., Deppert W.R., Haehnel W., RA Wagner E.; RT "Primary structure of maize chloroplast adenylate kinase."; RL Eur. J. Biochem. 222:949-954(1994). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS). RX MEDLINE=98088957; PubMed=9428681; RA Wild K., Grafmueller R., Wagner E., Schulz G.E.; RT "Structure, catalysis and supramolecular assembly of adenylate kinase RT from maize."; RL Eur. J. Biochem. 250:326-331(1997). CC -!- FUNCTION: This small ubiquitous enzyme is essential for CC maintenance and cell growth. The maize enzyme also works with CC CMP, albeit with 10% of the activity with AMP. CC -!- CATALYTIC ACTIVITY: ATP + AMP = ADP + ADP. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- MASS SPECTROMETRY: MW=24867; METHOD=Electrospray. CC -!- SIMILARITY: Belongs to the adenylate kinase family. DR PIR; S45634; S45634. DR PDB; 1ZAK; 08-APR-98. DR MaizeDB; 13836; -. DR InterPro; IPR006259; Adenyl_kin_sub. DR InterPro; IPR000850; Adenylate_kin. DR Pfam; PF00406; ADK; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR ProDom; PD000657; Adenylate_kin; 1. DR TIGRFAMs; TIGR01351; adk; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. KW Transferase; Kinase; ATP-binding; Chloroplast; 3D-structure. FT NP_BIND 12 20 ATP (By similarity). FT STRAND 8 12 FT TURN 14 15 FT HELIX 18 29 FT STRAND 32 33 FT HELIX 36 46 FT TURN 47 47 FT HELIX 49 59 FT TURN 60 61 FT HELIX 66 78 FT HELIX 80 84 FT TURN 85 85 FT STRAND 87 90 FT HELIX 96 103 FT TURN 104 106 FT STRAND 111 116 FT HELIX 119 126 FT TURN 127 128 FT STRAND 129 131 FT TURN 133 135 FT STRAND 138 140 FT HELIX 150 154 FT STRAND 156 156 FT TURN 159 160 FT TURN 163 164 FT HELIX 165 182 FT TURN 183 184 FT STRAND 188 192 FT HELIX 197 219 FT TURN 220 220 SQ SEQUENCE 222 AA; 24867 MW; 19257324F8B7630D CRC64; ALADPLKVMI SGAPASGKGT QCELIKTKYQ LAHISAGDLL RAEIAAGSEN GKRAKEFMEK GQLVPDEIVV NMVKERLRQP DAQENGWLLD GYPRSYSQAM ALETLEIRPD TFILLDVPDE LLVERVVGRR LDPVTGKIYH LKYSPPENEE IASRLTQRFD DTEEKVKLRL ETYYQNIESL LSTYENIIVK VQGDATVDAV FAKIDELLGS ILEKKNEMVS ST // ID KC2A_MAIZE STANDARD; PRT; 332 AA. AC P28523; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Casein kinase II, alpha chain (CK II) (EC 2.7.1.37) (CK2-alpha). GN ACK2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73 Inbred; RX MEDLINE=92096457; PubMed=1756176; RA Dobrowolska G., Boldyreff B., Issinger O.-G.; RT "Cloning and sequencing of the casein kinase 2 alpha subunit from Zea RT mays."; RL Biochim. Biophys. Acta 1129:139-140(1991). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX MEDLINE=98232491; PubMed=9564028; RA Niefind K., Guerra B., Pinna L.A., Issinger O.G., Schomburg D.; RT "Crystal structure of the catalytic subunit of protein kinase CK2 RT from Zea mays at 2.1-A resolution."; RL EMBO J. 17:2451-2462(1998). CC -!- FUNCTION: Casein kinases are operationally defined by their CC preferential utilization of acidic proteins such as caseins CC as substrates. The alpha chain contains the catalytic site. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains (possible). CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. CK2 CC subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61387; CAA43659.1; -. DR PIR; S19726; S19726. DR PDB; 1LP4; 20-NOV-02. DR PDB; 1LPU; 20-NOV-02. DR PDB; 1LR4; 20-NOV-02. DR PDB; 1DAW; 03-MAY-00. DR PDB; 1DAY; 03-MAY-00. DR PDB; 1DS5; 07-JAN-01. DR PDB; 1F0Q; 23-MAY-01. DR PDB; 1J91; 29-MAY-02. DR PDB; 1JAM; 31-MAY-02. DR PDB; 1M2P; 17-JUN-03. DR PDB; 1M2Q; 17-JUN-03. DR PDB; 1M2R; 17-JUN-03. DR MaizeDB; 30032; -. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW 3D-structure. FT DOMAIN 34 319 Protein kinase. FT NP_BIND 40 48 ATP. FT BINDING 63 63 ATP. FT ACT_SITE 151 151 Proton acceptor. FT TURN 8 9 FT HELIX 10 13 FT HELIX 16 19 FT HELIX 21 23 FT HELIX 31 33 FT STRAND 34 42 FT STRAND 46 53 FT TURN 54 57 FT STRAND 58 65 FT HELIX 70 83 FT TURN 84 85 FT TURN 87 88 FT STRAND 89 89 FT STRAND 92 97 FT TURN 99 101 FT STRAND 104 109 FT HELIX 116 119 FT HELIX 120 122 FT HELIX 125 144 FT TURN 145 146 FT STRAND 147 148 FT HELIX 154 156 FT STRAND 157 160 FT TURN 161 164 FT STRAND 165 168 FT TURN 172 173 FT STRAND 175 176 FT TURN 179 180 FT HELIX 190 192 FT HELIX 195 198 FT TURN 199 200 FT TURN 206 206 FT HELIX 207 222 FT TURN 223 223 FT HELIX 233 244 FT HELIX 246 255 FT TURN 256 257 FT HELIX 262 268 FT HELIX 276 279 FT TURN 282 284 FT HELIX 285 287 FT HELIX 290 299 FT HELIX 304 306 FT HELIX 310 314 FT TURN 315 315 FT HELIX 317 319 FT HELIX 320 326 FT TURN 327 327 SQ SEQUENCE 332 AA; 39230 MW; 85513A5A5C77235A CRC64; MSKARVYADV NVLRPKEYWD YEALTVQWGE QDDYEVVRKV GRGKYSEVFE GINVNNNEKC IIKILKPVKK KKIKREIKIL QNLCGGPNIV KLLDIVRDQH SKTPSLIFEY VNNTDFKVLY PTLTDYDIRY YIYELLKALD YCHSQGIMHR DVKPHNVMID HELRKLRLID WGLAEFYHPG KEYNVRVASR YFKGPELLVD LQDYDYSLDM WSLGCMFAGM IFRKEPFFYG HDNHDQLVKI AKVLGTDGLN VYLNKYRIEL DPQLEALVGR HSRKPWLKFM NADNQHLVSP EAIDFLDKLL RYDHQERLTA LEAMTHPYFQ QVRAAENSRT RA // ID KPRO_MAIZE STANDARD; PRT; 817 AA. AC P17801; DT 01-AUG-1990 (Rel. 15, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Putative receptor protein kinase ZmPK1 precursor (EC 2.7.1.37). GN PK1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Root; RX MEDLINE=90294911; PubMed=2163028; RA Walker J.C., Zhang R.; RT "Relationship of a putative receptor protein kinase from maize to the RT S-locus glycoproteins of Brassica."; RL Nature 345:743-746(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RA Zhang R., Walker J.C.; RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Probable receptor. Interaction with a ligand in the CC extracellular domain triggers the protein kinase activity of the CC cytoplasmic domain. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBCELLULAR LOCATION: Type I membrane protein. CC -!- TISSUE SPECIFICITY: Expressed predominantly in the shoots and CC roots of young maize seedlings, and to a lesser extent in the CC silks. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. CC -!- SIMILARITY: Contains 1 bulb-type lectin domain. CC -!- SIMILARITY: Contains 1 EGF-like domain. CC -!- SIMILARITY: Contains 1 PAN domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52384; CAA36611.1; -. DR EMBL; X67733; CAA47962.1; -. DR PIR; S10930; S10930. DR MaizeDB; 65910; -. DR InterPro; IPR001480; B_lectin. DR InterPro; IPR006210; IEGF. DR InterPro; IPR003014; PAN. DR InterPro; IPR003609; Pan_app. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR000858; Slocus_glycop. DR Pfam; PF01453; Agglutinin; 1. DR Pfam; PF00024; PAN; 1. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00954; S_locus_glycop; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00108; B_lectin; 1. DR SMART; SM00181; EGF; 1. DR SMART; SM00473; PAN_AP; 1. DR PROSITE; PS50927; BULB_LECTIN; 1. DR PROSITE; PS00022; EGF_1; FALSE_NEG. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS50948; PAN; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Transmembrane; Receptor; Glycoprotein; EGF-like domain; Signal. FT SIGNAL 1 28 FT CHAIN 29 817 Putative receptor protein kinase ZmPK1. FT DOMAIN 29 472 Extracellular (Potential). FT TRANSMEM 473 498 Potential. FT DOMAIN 499 817 Cytoplasmic (Potential). FT DOMAIN 29 158 Bulb-type lectin. FT DOMAIN 342 424 PAN. FT DOMAIN 534 817 Protein kinase. FT NP_BIND 540 548 ATP (By similarity). FT BINDING 562 562 ATP (By similarity). FT ACT_SITE 658 658 Proton acceptor (By similarity). FT CARBOHYD 83 83 N-linked (GlcNAc...) (Potential). FT CARBOHYD 128 128 N-linked (GlcNAc...) (Potential). FT CARBOHYD 228 228 N-linked (GlcNAc...) (Potential). FT CARBOHYD 279 279 N-linked (GlcNAc...) (Potential). FT CARBOHYD 329 329 N-linked (GlcNAc...) (Potential). FT CARBOHYD 339 339 N-linked (GlcNAc...) (Potential). FT CARBOHYD 452 452 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 817 AA; 91120 MW; F164B44719922E67 CRC64; MPRPLAALLS TACILSFFIA LFPRAASSRD ILPLGSSLVV ESYESSTLQS SDGTFSSGFY EVYTHAFTFS VWYSKTEAAA ANNKTIVWSA NPDRPVHARR SALTLQKDGN MVLTDYDGAA VWRADGNNFT GVQRARLLDT GNLVIEDSGG NTVWQSFDSP TDTFLPTQLI TAATRLVPTT QSRSPGNYIF RFSDLSVLSL IYHVPQVSDI YWPDPDQNLY QDGRNQYNST RLGMLTDSGV LASSDFADGQ ALVASDVGPG VKRRLTLDPD GNLRLYSMND SDGSWSVSMV AMTQPCNIHG LCGPNGICHY SPTPTCSCPP GYATRNPGNW TEGCMAIVNT TCDRYDKRSM RFVRLPNTDF WGSDQQHLLS VSLRTCRDIC ISDCTCKGFQ YQEGTGSCYP KAYLFSGRTY PTSDVRTIYL KLPTGVSVSN ALIPRSDVFD SVPRRLDCDR MNKSIREPFP DVHKTGGGES KWFYFYGFIA AFFVVEVSFI SFAWFFVLKR ELRPSELWAS EKGYKAMTSN FRRYSYRELV KATRKFKVEL GRGESGTVYK GVLEDDRHVA VKKLENVRQG KEVFQAELSV IGRINHMNLV RIWGFCSEGS HRLLVSEYVE NGSLANILFS EGGNILLDWE GRFNIALGVA KGLAYLHHEC LEWVIHCDVK PENILLDQAF EPKITDFGLV KLLNRGGSTQ NVSHVRGTLG YIAPEWVSSL PITAKVDVYS YGVVLLELLT GTRVSELVGG TDEVHSMLRK LVRMLSAKLE GEEQSWIDGY LDSKLNRPVN YVQARTLIKL AVSCLEEDRS KRPTMEHAVQ TLLSADD // ID LDH_MAIZE STANDARD; PRT; 354 AA. AC P29038; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE L-lactate dehydrogenase (EC 1.1.1.27) (LDH). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Leaf; RX MEDLINE=92329729; PubMed=1627781; RA Good A.G., Paetkau D.H.; RT "Identification and characterization of a hypoxically induced maize RT lactate dehydrogenase gene."; RL Plant Mol. Biol. 19:693-697(1992). CC -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- PATHWAY: Anaerobic glycolysis; final step. CC -!- SUBUNIT: Homotetramer. CC -!- INDUCTION: By hypoxia. CC -!- SIMILARITY: Belongs to the LDH family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z11754; CAA77808.1; -. DR PIR; S22492; S22492. DR HSSP; P00344; 1LDB. DR MaizeDB; 65834; -. DR InterPro; IPR001557; L_LDH. DR InterPro; IPR001236; ldh. DR InterPro; IPR000205; NAD_BS. DR Pfam; PF00056; ldh; 1. DR Pfam; PF02866; ldh_C; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR PROSITE; PS00064; L_LDH; 1. KW Oxidoreductase; NAD; Glycolysis. FT ACT_SITE 214 214 Accepts a proton during catalysis (By FT similarity). SQ SEQUENCE 354 AA; 38551 MW; 4F903F7C3E203FC2 CRC64; MKKATSLSEL GFDAGDASSG FFRPVSGDSS TPTSQHHRRR LTKVSVIGAG NVGMAIAQTI LTRDLADEIA LVDAVPDKLR GEMLDLQHAA AFLPRTRLVS GTDMSVTRGS DLVIVTAGAR QIQGETRLDL LQRNVALFRK IVPPLAEQSH DALLLVVSNP VDVLTYVAWK LSGFPASRVI GSGTNLDSSR FRFLLAEHLD VNAQDVQAYM VGEHGDSSVA VWSSVSVAGM PVLKSLQESH RCFDEEALEG IRRAVVDSAY EVISLKGYTS WAIGYSVASL AASLLRDQRR IHPVSVLARG FHGIPDGTTS SSACPPRRPR RRPGRREMEL TEEEAKRLRR SAKTIWENCQ LLGL // ID LDOX_MAIZE STANDARD; PRT; 395 AA. AC P41213; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Leucoanthocyanidin dioxygenase (EC 1.14.11.19) (LDOX) (Leucocyanidin DE oxygenase) (Leucoanthocyanidin hydroxylase). GN A2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91005996; PubMed=2170105; RA Menssen A., Hoehmann S., Martin W., Schnable P.S., Peterson P.S., RA Saedler H., Gierl A.; RT "The En/Spm transposable element of Zea mays contains splice sites at RT the termini generating a novel intron from a dSpm element in the A2 RT gene."; RL EMBO J. 9:3051-3057(1990). CC -!- FUNCTION: Oxidation of leucoanthocyanidins into anthocyanidins. CC -!- CATALYTIC ACTIVITY: Leucocyanidin + 2-oxoglutarate + O(2) = cis- CC and trans-dihydroquercetins + succinate + CO(2). CC -!- COFACTOR: Binds 1 iron ion and one ascorbate molecule per subunit CC (By similarity). CC -!- PATHWAY: Flavonoid synthesis; anthocyanidins biosynthesis. CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55314; CAA39022.1; -. DR PIR; S12043; S12043. DR MaizeDB; 99960; -. DR InterPro; IPR005123; 2OG-FeII_Oxy. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. KW Flavonoid biosynthesis; Oxidoreductase; Dioxygenase; Iron; KW Metal-binding; Vitamin C. FT METAL 254 254 Iron (By similarity). FT METAL 256 256 Iron (By similarity). FT METAL 310 310 Iron (By similarity). SQ SEQUENCE 395 AA; 43355 MW; C43B91DDC6FC7F1A CRC64; MESSPLLQLP AARVEALSLS GLSAIPPEYV RPADERAGLG DAFDLARTHA NDHTAPRIPV VDISPFLDSS SQQQQRDECV EAVRAAAADW GVMHIAGHGI PAELMDRLRA AGTAFFALPV QDKEAYANDP AAGRLQGYGS RLATNTCGQR EWEDYLFHLV HPDGLADHAL WPAYPPDYIA ATRDFGRRTR DLASTLLAIL SMGLLGTDRG DALEKALTTT TTRTAADDDL LLQLKINYYP RCPQPELAVG VEAHTDVSAL SFILHNGVPG LQVLHGARWV TARHEPGTII VHVGDALEIL SNGRYTSVLH RGLVNREAVR ISWVVFCEPP PDSVLLHPLP ELVTEGHPAR FTPRTFKQHL DRKLFKKKQQ HKAKAEEEDG GNGDHHRHEP PPQTN // ID MAOC_MAIZE STANDARD; PRT; 636 AA. AC P16243; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE NADP-dependent malic enzyme, chloroplast precursor (EC 1.1.1.40) DE (NADP-ME). GN MOD1 OR ME1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73 Inbred; RX MEDLINE=90062054; PubMed=2584183; RA Rothermel B.A., Nelson T.; RT "Primary structure of the maize NADP-dependent malic enzyme."; RL J. Biol. Chem. 264:19587-19592(1989). CC -!- FUNCTION: The chloroplastic ME isoform decarboxylates malate CC shuttled from neighboring mesophyll cells. The CO(2) released CC is then refixed by ribulose-bisphosphate carboxylase. This pathway CC eliminates the photorespiratory loss of CO(2) that occurs in most CC plants. CC -!- CATALYTIC ACTIVITY: (S)-malate + NADP(+) = pyruvate + CO(2) + CC NADPH. CC -!- COFACTOR: Can use either NADP or NAD as a cofactor. CC -!- PATHWAY: C4 photosynthetic pathway. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the malic enzymes family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J05130; AAA33487.1; -. DR PIR; A34482; DEZMMX. DR MaizeDB; 13848; -. DR InterPro; IPR001891; Malic_oxred. DR Pfam; PF00390; malic; 1. DR Pfam; PF03949; malic_N; 1. DR PRINTS; PR00072; MALOXRDTASE. DR PROSITE; PS00331; MALIC_ENZYMES; 1. KW Oxidoreductase; NADP; NAD; Transit peptide; Chloroplast. FT TRANSIT 1 62 Chloroplast (Potential). FT CHAIN 63 636 NADP-dependent malic enzyme. FT NP_BIND 380 396 NADP (By similarity). SQ SEQUENCE 636 AA; 69823 MW; DF2D36FD4B2682EA CRC64; MLSTRTAAVA ASASPASPWK LGGRSEGGAS CDGCRTYRNT LRRRAAPAKV RALPPRRVDA VAMVSNAETE TEKEQEEAAA ASEELPVMPW ATSVASGYTL LRDPHHNKGL AFTEEERDGH YLRGLLPPAV LSQELQIKKF MNTLRQYQTP LQRYIAMMNL QETDERLFYK LLIDNVVELL PFVYTPTVGE ACQKYGSIFG RPQGLYVSLK DKGKVLEVLR NWPHRNIQVI CVTDGERILG LGDLGCQGMG IPVGKLALYT ALGGVDPSVC LPITIDVGTN NEFLLNDEFY IGLRQKRATG EEYDELIEEF MSAVKQFYGE KVLIQFEDFA NHNAFDLLEK YSKSHLVFND DIQGTASVVL AGLLAALKMV GGTLAEQTYL FLGAGEAGTG IAELIALEIS KQTNAPIEEC RKKVWLVDSK GLIVDSRKGS LQPFKKPWAH EHEPLKTLYD AVQSIKPTVL IGTSGVGRTF TKEIIEAMSS FNERPIIFSL SNPTSHSECT AEQAYTWSQG RSIFASGSPF APVEYEGKTF VPGQSNNAYI FPGLGLGLVI SGAVRVHEDM LLAASKALAD QATQDNFEKG SIFPPFTSIR KISAHIAAAV AGKAYELGLA TRLPPPSDLV KYAENCMYTP VYRNYR // ID MASY_MAIZE STANDARD; PRT; 559 AA. AC P49081; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Malate synthase, glyoxysomal (EC 2.3.3.9). GN LIP. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. TX5855; TISSUE=Scutellum; RA Paek N.C., Taylor B.H., Smith J.D.; RT "Nucleotide sequence of malate synthase cDNA in maize."; RL (In) Plant Gene Register PGR95-015. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + glyoxylate = S-malate + CC CoA. CC -!- PATHWAY: Glyoxylate bypass; second step. CC -!- SUBCELLULAR LOCATION: Glyoxysomal. CC -!- SIMILARITY: Belongs to the malate synthase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L35914; AAB04118.1; -. DR PIR; T03412; T03412. DR MaizeDB; 100137; -. DR InterPro; IPR006252; Malate_synthA. DR InterPro; IPR001465; Malate_synthase. DR Pfam; PF01274; Malate_synthase; 1. DR TIGRFAMs; TIGR01344; malate_syn_A; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. KW Transferase; Glyoxylate bypass; Tricarboxylic acid cycle; Glyoxysome. FT ACT_SITE 173 173 Proton acceptor (By similarity). FT ACT_SITE 459 459 Proton donor (By similarity). FT SITE 557 559 Microbody targeting signal (Potential). SQ SEQUENCE 559 AA; 61636 MW; BC639B38D57C530B CRC64; MAASTAAPCY DAPEGVDVRG RYDREFAGIL TRDALDFVAG LQREFRGAVR YAMEQRREAQ RRYDAGELPR FDPATTLVRE GDWTCASVPP AVADRTVEIT GPAEPRKMVI NALNSGAKVF MADFEDAMSP TWENLMHGQV NLRDAVAGTI SFRDAPRGRT YELNDRTAKL FVRPRGWHLP EAHILIDGEP AIGCLVDFGL YFFHNHAAFG AGQGAGFGPL CDLPKMEHSR EARIWNGVFQ RAEKAAGIEP GSIRATVLVE TLPAVFQMNE ILHELREHSA GLNCGRWDYI FSYVKTFRAH PDRLLPDRAL VGMAQHFMRS YSHLLIHTCH RRGVHAMGGM AAQIPIKDDA AANEAALELV RKDKLREVRA GHDGTWAAHP GLIPAIREVF EGHLGGRPNQ IGDAAGHEGA SVKEEDLIQP PRGARTVDGL RLNVRVGVQY LAAWLAGSGS VPLYNLMEDA ATAEISRVQN WQWLRHGAAL DAGGVEVRAT PELLARVVEE EMARVEAEVG PDRFRKGRYA EAGRIFSRQC TAPELDDFLT LDAYNLIVAH HPGASPCKL // ID MATK_MAIZE STANDARD; PRT; 513 AA. AC P48190; DT 01-FEB-1996 (Rel. 33, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Maturase K (Intron maturase). GN MATK OR YCF14. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Probably assists in splicing chloroplast group II CC introns (By similarity). CC -!- SIMILARITY: Belongs to the intron maturase family 2. MatK CC subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60266.1; ALT_INIT. DR Gramene; P48190; -. DR MaizeDB; 118213; -. DR InterPro; IPR000442; Intron_maturse2. DR InterPro; IPR002866; MatK_N. DR Pfam; PF01348; Intron_maturas2; 1. DR Pfam; PF01824; MatK_N; 1. KW mRNA processing; Chloroplast. SQ SEQUENCE 513 AA; 61122 MW; 7A38EBFC65C1A083 CRC64; MEKFEGYSEK QKSRQHYFVY PLLFQEYIYA FAHDYGLNGS EPVEIFGCNN KKFSSLLVNR LIIRMYQQNF LINSVNYPNQ DRLLDHRNYF YSEFYSQILS EGFAIVVEIP LSLGQLSCPE EKEIPNFQNL QSIHSIFPFL EDKFLHLHYL SHIKIPYPIH LEILVQLLEY RSQDVPSLHL LRFFLYYYSN WNSFITSMKS IFLLKKENKR LFRFLYNSYV SEYEFFLLFL HKQSSCLRLT SSGTFLERII FSGKMEHFGV MYPGFFRKTI WFFMDPLMHY VRYQGKAILA SKGTLLLKKK WKSYLVNFSQ YFFSFWTQPQ RIRLNQLTNS CFDFLGYLSS VPINTLLVRN QMLENSFLID TRMKKFDTTV LATPLVGSLS KAQFCTGSGH PISKPVWTDL SDWDILDRFG RICRNIFHYH SGSSKKQTLY RLKYILRLSC ARTLARKHKS TVRTFMQRLG SVFLEEFFTE EEQVFSLMFT KTIHFSFHGS HSECIWYLDI IRINDLVNPL TLN // ID MBP1_MAIZE STANDARD; PRT; 33 AA. AC P28794; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Antimicrobial peptide MBP-1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC STRAIN=cv. B73; TISSUE=Seed; RX MEDLINE=92406801; PubMed=1527010; RA Duvick J.P., Rood T., Rao A.G., Marshak D.R.; RT "Purification and characterization of a novel antimicrobial peptide RT from maize (Zea mays L.) kernels."; RL J. Biol. Chem. 267:18814-18820(1992). CC -!- FUNCTION: Inhibitor of both bacterial and fungal growth in vitro. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Predominantly in the embryo portion of the CC kernel. DR PIR; A41822; A41822. DR MaizeDB; 69182; -. KW Plant defense; Fungicide; Antibiotic. SQ SEQUENCE 33 AA; 4131 MW; B148F1B90E823599 CRC64; RSGRGECRRQ CLRRHEGQPW ETQECMRRCR RRG // ID MCM3_MAIZE STANDARD; PRT; 600 AA. AC Q43704; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE DNA replication licensing factor MCM3 homolog (Replication origin DE activator) (ROA protein) (Fragment). GN ROA. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. LG11; TISSUE=Root; RX MEDLINE=96397491; PubMed=8804385; RA Sabelli P.A., Burgess S.R., Kush A.K., Young M.R., Shewry P.R.; RT "cDNA cloning and characterisation of a maize homologue of the MCM RT proteins required for the initiation of DNA replication."; RL Mol. Gen. Genet. 252:125-136(1996). CC -!- FUNCTION: Acts as a factor that allows the DNA to undergo a single CC round of replication per cell cycle. Required for DNA replication CC and cell proliferation (By similarity). CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- SIMILARITY: Belongs to the MCM family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z29368; CAA82556.1; -. DR PIR; S52247; S52247. DR MaizeDB; 131629; -. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR001208; MCM. DR InterPro; IPR008046; MCM_3. DR Pfam; PF00493; MCM; 1. DR PRINTS; PR01657; MCMFAMILY. DR PRINTS; PR01659; MCMPROTEIN3. DR ProDom; PD001041; MCM; 2. DR SMART; SM00382; AAA; 1. DR SMART; SM00350; MCM; 1. DR PROSITE; PS00847; MCM_1; 1. DR PROSITE; PS50051; MCM_2; 1. KW Transcription regulation; DNA-binding; Nuclear protein; KW DNA replication; ATP-binding; Cell cycle. FT NON_TER 1 1 FT DOMAIN 122 329 MCM. FT NP_BIND 172 179 ATP (Potential). SQ SEQUENCE 600 AA; 66335 MW; 7CC5797F84F5A698 CRC64; VYPTRDDNGN LLVTEYGMCE YKDHQTLSMQ EVPENSAPGQ LPRTVDVIVE DDLVDCCKPG DRVSIVGVYK ALPGKSKGSV SGVFRTVLIA NNVSLLNKEA NAPVYTREDL KRMKEISRRN DTFDLLGNSL APSIYGHLWI KKAVVLLMLG GVEKNLKNGT HLRGDINMMM VGDPSVAKSQ LLRAVMNIAP LAISTTGRGS SGVGLTAAVT SDQETGERRL EAGAMVLADR GVVCIDEFDK MNDQDRVAIH EVMEQQTVTI AKAGIHASLN ARCSVIAAAN PIYGTYDRSL TPTKNIGLPD SLLSRFRLLF IVLDQMDPEI DRQISEHVAR MHRYCTDDGG ARSLDKEGYA EEDDGDANAA IFIKYDRMLH GQDRRRGKKS KQDRLTVKFL KKYIHYAKNL IQPRLTDEAS DHIATSYAEL RDGSANAKSG GGTLPITART LESIIRLSTA HAKMKLRHEV LKSDVEAALQ VLNFAIYHKE LTEMEEREQK EMEMKQQAEH DAGATGGTVD GHGSSGNDPM DVDVGSNDQN VSAERIEAFE ALLGQHVLAN HIDQMSIDEI EQMVNRESTA PYTRSQVEFI LERMQDANRV MIRDGVVRII // ID MDHP_MAIZE STANDARD; PRT; 432 AA. AC P15719; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Malate dehydrogenase [NADP], chloroplast precursor (EC 1.1.1.82) DE (NADP-MDH). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Leaf; RA Metzler M., Rothermel B.A., Nelson T.; RT "Maize NADP-malate dehydrogenase: cDNA cloning, sequence, and mRNA RT characterization."; RL Plant Mol. Biol. 12:713-722(1989). RN [2] RP SEQUENCE OF 58-84. RX MEDLINE=88298851; PubMed=3403553; RA Decottignies P., Schmitter J.-M., Miginiac-Maslow M., le Marechal P., RA Jacquot J.-P., Gadal P.; RT "Primary structure of the light-dependent regulatory site of corn RT NADP-malate dehydrogenase."; RL J. Biol. Chem. 263:11780-11785(1988). RN [3] RP SEQUENCE OF 41-62. RA Agostino A., Jeffrey P., Hatch M.D.; RT "Amino acid sequence and molecular weight of native NADP malate RT dehydrogenase from the C4 plant Zea mays."; RL Plant Physiol. 98:1506-1510(1992). CC -!- FUNCTION: The chloroplastic, NADP-dependent form is essential for CC the photosynthesis C4 cycle, which allows plants to circumvent the CC problem of photorespiration. In C4 plants, NADP-MDH activity acts CC to convert oxaloacetate to malate in chloroplasts of mesophyll CC cells for transport to the bundle sheath cells. CC -!- CATALYTIC ACTIVITY: (S)-malate + NADP(+) = oxaloacetate + NADPH. CC -!- ENZYME REGULATION: Chloroplast NADP-MDH is activated upon CC illumination. In order to be enzymatically active, disulfides CC bridges on the protein must be reduced by thioredoxin which CC receives electrons from ferredoxin and the electron transport CC system of photosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the LDH family. MDH subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16084; CAA34213.1; -. DR PIR; S04859; DEMZMC. DR HSSP; P17606; 7MDH. DR MaizeDB; 40092; -. DR InterPro; IPR001236; ldh. DR InterPro; IPR008267; Mal_dehydrog. DR InterPro; IPR001252; Mdh_AS. DR Pfam; PF00056; ldh; 1. DR Pfam; PF02866; ldh_C; 1. DR ProDom; PD003052; Mdh; 1. DR PROSITE; PS00068; MDH; 1. KW Oxidoreductase; NADP; Chloroplast; Transit peptide. FT TRANSIT 1 40 Chloroplast. FT CHAIN 41 432 Malate dehydrogenase [NADP]. FT DISULFID 67 72 In oxidized inactive NAD-MDH. FT DISULFID 408 420 In oxidized inactive NAD-MDH (By FT similarity). FT SITE 67 67 ACTIVATION OF NADP-MDH. FT SITE 72 72 ACTIVATION OF NADP-MDH. FT ACT_SITE 244 244 Proton relay (By similarity). FT ACT_SITE 272 272 Proton relay (By similarity). SQ SEQUENCE 432 AA; 46859 MW; 45531DEF8BBF79FD CRC64; MGLSTVYSPA GPRLVPAPLG RCRSAQPRRP RRAPLATVRC SVDATKQAQD GVATAVATEA PASRKECFGV FCTTYDLKAE DKTKSWRKLV NVAVSGAAGM ISNHLLFKLA SGEVFGQDQP IALKLLGSER SFQALEGVAM ELEDSLYPLL REVSIGIDPY VVFQDVDWAL LIGAKPRGPG MERAALLDIN GQIFADQGKA LNAVASRNDE VLVVGNPCNT NALICLKNAP NIPAKNFHAL TRLDENRAKC QLALKAGVFY DKVSNVTIWG NHSTTQVPDF LNAKIDGRPV KEVIKDTKWL EEEFTLTVQK RGGVLIQKWG RSSAASTAVS IVDAIRSLVT PTPEGDWFST GVYTTGNPYG IAEDIVFSMP CRSKGDGDYE LASDVLMDDF LWERIKKSEA ELLAEKKCVA HLTGEGNAFC DLPEDTMLPG EV // ID METK_MAIZE STANDARD; PRT; 15 AA. AC P80616; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Probable S-adenosylmethionine synthetase (EC 2.5.1.6) (Methionine DE adenosyltransferase) (AdoMet synthetase) (Spot 178) (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from CC methionine and ATP. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate + CC diphosphate + S-adenosyl-L-methionine. CC -!- COFACTOR: Binds 2 divalent ions, such as magnesium or cobalt, and CC 1 potassium ion per subunit (Potential). CC -!- PATHWAY: Activated methyl cycle. CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 5.9, its MW is: 43.3 kDa. CC -!- SIMILARITY: Belongs to the AdoMet synthetase family. DR Maize-2DPAGE; P80616; COLEOPTILE. DR MaizeDB; 123938; -. DR InterPro; IPR002133; S-AdoMet_synt. DR Pfam; PF02772; S-AdoMet_syntD2; 1. DR PROSITE; PS00376; ADOMET_SYNTHETASE_1; PARTIAL. DR PROSITE; PS00377; ADOMET_SYNTHETASE_2; PARTIAL. KW Transferase; One-carbon metabolism; Multigene family; ATP-binding; KW Magnesium; Potassium; Metal-binding. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1601 MW; 232B07E9AC328D32 CRC64; RPEEIGAGDQ GHMFG // ID MF14_MAIZE STANDARD; PRT; 126 AA. AC Q01900; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE MFS14 protein precursor. GN MFS14. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. BE10; TISSUE=Tassel; RX MEDLINE=94004987; PubMed=8401606; RA Wright S.Y., Suner M.-M., Bell P.J., Vaudin M., Greenland A.J.; RT "Isolation and characterization of male flower cDNAs from maize."; RL Plant J. 3:41-49(1993). CC -!- TISSUE SPECIFICITY: Enhanced expression in male flowers. CC Accumulates in the tapetum. CC -!- DEVELOPMENTAL STAGE: Associated with microsporogenesis and CC declines as mature pollen is produced. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67323; CAA47737.1; -. DR PIR; S25104; S25104. DR MaizeDB; 69183; -. KW Signal. FT SIGNAL 1 23 Or 24, or 26 (Potential). FT CHAIN 24 126 MFS14 protein. SQ SEQUENCE 126 AA; 12653 MW; 67F2813AFF8C55E5 CRC64; MALEAATAPR ALLAACLVLL VLGGGTGPSS VLRAPGRRPA AVPAAAERLL RCRAYLVPAR RTPARTAAAL SAVCTSAPAA PWASSTACPA GATSPKPTAP LEAGTWHACC NGWQEGRGIR SVSISQ // ID MF18_MAIZE STANDARD; PRT; 128 AA. AC P32439; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE MFS18 protein precursor. GN MFS18. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. BE10; TISSUE=Tassel; RX MEDLINE=94004987; PubMed=8401606; RA Wright S.Y., Suner M.-M., Bell P.J., Vaudin M., Greenland A.J.; RT "Isolation and characterization of male flower cDNAs from maize."; RL Plant J. 3:41-49(1993). CC -!- TISSUE SPECIFICITY: Enhanced expression in male flowers. CC Accumulates in the glumes and in anther walls, paleas and lemmas CC of mature florets. CC -!- DEVELOPMENTAL STAGE: Expressed throughout tassel growth up until CC mature pollen is produced in the anthers. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67324; CAA47738.1; -. DR PIR; S25103; S25103. DR MaizeDB; 78601; -. KW Signal; Repeat. FT SIGNAL 1 25 Potential. FT CHAIN 26 128 MFS18 protein. FT DOMAIN 64 92 3 X approximate tandem repeats. FT REPEAT 64 75 1-1. FT REPEAT 69 80 1-2. FT REPEAT 81 92 1-3. FT DOMAIN 64 116 8 X 4 AA APPROXIMATE REPEATS. FT REPEAT 64 67 2-1. FT REPEAT 69 72 2-2. FT REPEAT 74 77 2-3. FT REPEAT 79 82 2-4. FT REPEAT 86 89 2-5. FT REPEAT 91 94 2-6. FT REPEAT 104 107 2-7. FT REPEAT 113 116 2-8. SQ SEQUENCE 128 AA; 12535 MW; 7661ECC596E0D778 CRC64; MARSSKMMVA ARLLALALAV STAEARNIKT TTTEKKDDAV VQPQTFPPFD RLGGGASPAF GGLPGGSIPG SSIPGFSMPG SGSSLPGFSL PGSGTMPLFG GGSPGFSGFG GMPGSPTAGS VPEHANKP // ID MI25_MAIZE STANDARD; PRT; 219 AA. AC P09004; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Mitochondrial 24 kDa protein (ORF 25). OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RX MEDLINE=88194692; PubMed=3447748; RA Stamper S.E., Dewey R.E., Bland M.M., Levings C.S. III; RT "Characterization of the gene urf13-T and an unidentified reading RT frame, ORF 25, in maize and tobacco mitochondria."; RL Curr. Genet. 12:457-463(1987). CC -!- RNA EDITING: Modified_positions=50, 96. CC -!- SIMILARITY: Belongs to the plants 22/24 kDa mitochondrial CC protein family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06667; CAA29866.1; ALT_SEQ. DR MaizeDB; 69242; -. DR InterPro; IPR007997; DUF744. DR Pfam; PF05333; DUF744; 1. KW Hypothetical protein; Mitochondrion; RNA editing. SQ SEQUENCE 219 AA; 24371 MW; DBCFE41FA6A9C6EC CRC64; MRFSGMDMKG INMLFAAIPS ICASSPKKIS IYNEEMIVAR CFIGFLILSW KSLGKTFKET LDGRIESIQE SLQQFFNPNE VILEESNEQQ RLLNLWISLR ICSTVKVVES LPAARCAPKC EKTVQALLCR NLNVKSATLL NATSSRRIRL QDDIVTGFHF SVSERLVSGS TTLVEASTVE QIREAFLLEP RDLIREGFIV LRKVRVGGIP GTCGDGVGL // ID MNBA_MAIZE STANDARD; PRT; 238 AA. AC P38564; DT 01-OCT-1994 (Rel. 30, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE DNA-binding protein MNB1A. GN MNB1A. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. H84; TISSUE=Green leaf; RX MEDLINE=93340215; PubMed=8340424; RA Yanagisawa S., Izui K.; RT "Molecular cloning of two DNA-binding proteins of maize that are RT structurally different but interact with the same sequence motif."; RL J. Biol. Chem. 268:16028-16036(1993). RN [2] RP REVISIONS. RC STRAIN=cv. H84; TISSUE=Green leaf; RA Yanagisawa S.; RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Recognizes an 5'-AAGG-3' motif at the MNF1-binding site. CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. CC -!- SIMILARITY: Contains 1 Dof-type zinc finger. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X66076; CAA46875.1; -. DR PIR; S66358; S66358. DR TRANSFAC; T01059; -. DR MaizeDB; 60791; -. DR InterPro; IPR003851; Znf_Dof. DR Pfam; PF02701; zf-Dof; 1. DR PROSITE; PS01361; ZF_DOF_1; 1. DR PROSITE; PS50884; ZF_DOF_2; 1. KW Nuclear protein; DNA-binding; Zinc-finger. FT ZN_FING 47 101 Dof-type. SQ SEQUENCE 238 AA; 24796 MW; 9E8733228DB573C3 CRC64; MQEASSAAAA GAEPGRRAAQ HQFAGVDLRR PKGYAAPAPA PAVGEGDPCP RCASRDTKFC YYNNYNTSQP RHFCKGCRRY WTKGGTLRNV PVGGGTRKKP SSSSSSSSYV AAADADRQPK KKPASKKRRV VAPAPELATA ADPGKTATTT TTTSEITTET GALEDSDSLA HLLLQPGTED AEAVALGLGL SDFPSAGKAV LDDEDSFVWP AASFDMGACW AGAGFADPDP ACIFLNLP // ID MNBB_MAIZE STANDARD; PRT; 157 AA. AC P27347; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE DNA-binding protein MNB1B (HMG1-like protein). GN MNB1B. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-29. RC TISSUE=Leaf; RX MEDLINE=91252198; PubMed=2041733; RA Grasser K.D., Feix G.; RT "Isolation and characterization of maize cDNAs encoding a high RT mobility group protein displaying a HMG-box."; RL Nucleic Acids Res. 19:2573-2577(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. H84; TISSUE=Green leaf; RX MEDLINE=93340215; PubMed=8340424; RA Yanagisawa S., Izui K.; RT "Molecular cloning of two DNA-binding proteins of maize that are RT structurally different but interact with the same sequence motif."; RL J. Biol. Chem. 268:16028-16036(1993). CC -!- FUNCTION: Recognizes an AAGG motif at the MNF1-binding site. CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. CC -!- SIMILARITY: Contains 1 HMG box domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58282; CAA41220.1; -. DR EMBL; X66077; CAA46876.1; ALT_INIT. DR PIR; B47150; B47150. DR HSSP; P07155; 1HMF. DR TRANSFAC; T01060; -. DR MaizeDB; 65274; -. DR InterPro; IPR000135; Highmoblty_12. DR InterPro; IPR000910; HMG_12_box. DR Pfam; PF00505; HMG_box; 1. DR PRINTS; PR00886; HIGHMOBLTY12. DR SMART; SM00398; HMG; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. KW Nuclear protein; DNA-binding; Phosphorylation. FT DNA_BIND 41 110 HMG box. FT DOMAIN 124 157 Asp/Glu-rich (acidic). FT MOD_RES 149 149 PHOSPHORYLATION (BY CK2) (POTENTIAL). SQ SEQUENCE 157 AA; 17146 MW; 22D8E7AB7ADE7737 CRC64; MKGAKSKGAA KADAKLAVKS KGAEKPAKGR KGKAGKDPNK PKRAPSAFFV FMEEFRKEFK EKNPKNKSVA AVGKAAGDRW KSLSESDKAP YVAKANKLKL EYNKAIAAYN KGESTAAKKA PAKEEEEEDE EESDKSKSEV NDEDDEEGSE EDEDDDE // ID MOSA_MAIZE STANDARD; PRT; 621 AA. AC P15268; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Autonomous transposable element EN-1 mosaic protein (Suppressor- DE mutator system protein) (SPM). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Pereira A., Cuypers H., Gierl A., Schwarz-Sommer Z., Saedler H.; RT "Molecular analysis of the En/Spm transposable element system of Zea RT mays."; RL EMBO J. 5:835-841(1986). CC -!- FUNCTION: This protein has most probably three functions; CC the mutator (M) function, for excision and transposition; the CC suppressor (S) function, which inhibits residual gene activity CC of certain alleles in which inhibitor elements are integrated; CC an activator (A) function is proposed, because inactive SPM can CC be activated by a second SPM. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M25427; AAA66268.1; -. DR PIR; S28365; S28365. DR MaizeDB; 65370; -. KW Transposable element; Trans-acting factor; Transposition; KW Activator; Mutator protein; Repressor; Transcription regulation. SQ SEQUENCE 621 AA; 68362 MW; 54B930960EB774AA CRC64; MFRMDSSGRR SRSRRSRGSS GAPNMFEGTT TSRSRQEQLL ASLEQMRGSS GPSNTEGTTS RAADLVAPTM APTAEAAVDA EAAVDAEAEE AAAELDDGEE TSGADASTEE AATQAPPRRA IRYRRSLTLK PSKPFDQRRV IEPKGTRAWK EVSWDGTGHR TPILTELGIC LRFAYPAMVT EGGQEIAAHY WAHWDLKPYG NDGTHTSKVW DLFWGQFRVC DPYTLDDSYV REVFNGSADR AVKGMMYKAR LRAVTVYQKR QGNYCDANMA KEIHLTAQQY KESEVDWLSH HSDAWAWMCE YWASEEFLAI SNRNRMNRLS KPGVHFFGAD GHVGKAARMA ARNGVEPTLL QVFVEGHKGP DPNHPEILND SNATEKLARY IDNVREKNGP DTDWLTGEFD TEAAYKAGGG VPHGRLAIGD GVVPRRSYTR RSNFSAGSNR PRRPSAREGE LLEKMTQMEE SMAQYKQQVQ QQMQQMQNWM LHQMYGGAGT QFGMPPFQQP PIITHPVSGQ SSDRSTAAAD GSQGSATSVQ DQLMPLGVIG GQMMPWAPRQ PGIWPPMQTQ MPPPMPWGFP PRGQSQSPGL PSHSPGSGSG SHHASPPPDQ STFMDLLMNT SGGGSNDPPT E // ID MT1_MAIZE STANDARD; PRT; 76 AA. AC P30571; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Metallothionein-like protein 1 (MT-1). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92008639; PubMed=1915859; RA de Framond A.J.; RT "A metallothionein-like gene from maize (Zea mays). Cloning and RT characterization."; RL FEBS Lett. 290:103-106(1991). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Root meristem; RX MEDLINE=95359405; PubMed=7632917; RA Chevalier C., Bourgeois E., Pradet A., Raymond P.; RT "Molecular cloning and characterization of six cDNAs expressed during RT glucose starvation in excised maize (Zea mays L.) root tips."; RL Plant Mol. Biol. 28:473-485(1995). CC -!- FUNCTION: Metallothioneins have a high content of cysteine CC residues that bind various heavy metals. CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Family 15. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S57628; AAB19992.1; -. DR EMBL; X82186; CAA57676.1; -. DR PIR; S17560; S17560. DR MaizeDB; 64922; -. DR InterPro; IPR000347; Metallothion_15. DR Pfam; PF01439; Metallothio_2; 1. DR ProDom; PD001611; Metallothion_15; 1. KW Metal-binding; Metal-thiolate cluster. SQ SEQUENCE 76 AA; 7486 MW; 94FDC4102262A8BD CRC64; MSCSCGSSCG CGSSCKCGKK YPDLEETSTA AQPTVVLGVA PEKKAAPEFV EAAAESGEAA HGCSCGSGCK CDPCNC // ID MYB1_MAIZE STANDARD; PRT; 340 AA. AC P20024; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Myb-related protein Zm1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89313655; PubMed=2664447; RA Marocco A., Wissenbach M., Becker D., Paz-Ares J., Saedler H., RA Salamini F., Rohde W.; RT "Multiple genes are transcribed in Hordeum vulgare and Zea mays that RT carry the DNA binding domain of the myb oncoproteins."; RL Mol. Gen. Genet. 216:183-187(1989). CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- SIMILARITY: Contains 2 Myb-like domains. DR PIR; S04898; S04898. DR HSSP; P06876; 1MBK. DR TRANSFAC; T02958; -. DR MaizeDB; 69590; -. DR InterPro; IPR001005; Myb_DNA_binding. DR Pfam; PF00249; myb_DNA-binding; 2. DR SMART; SM00717; SANT; 2. DR PROSITE; PS00037; MYB_1; 1. DR PROSITE; PS00334; MYB_2; 1. DR PROSITE; PS50090; MYB_3; 2. KW Nuclear protein; DNA-binding; Repeat; Transcription regulation. FT DNA_BIND 11 63 Myb 1. FT DNA_BIND 64 114 Myb 2. SQ SEQUENCE 340 AA; 36239 MW; F2341387F6263DAF CRC64; MGRGRAPCCA KVGLNRGSWT PQEDMRLIAY IQKHGHTNWR ALPKQAGLLR CGKSCRLRWI NYLRPDLKRG NFTDEEEEAI IRLHGLLGNK WSKIAACLPG RTDNEIKNVW NTHLKKKVAQ REKKKAGAGS GDAGTPATAP LSSATSSTTT HNSSGGSDSG DQCGTSREPD ATDVCTLQPE DMDVSDMLVD GAPPAAQPMP SPSSSSSLTT CVGGVEELIE LPVIDIEPEI WSIIDGESAV ARHGGDAAAP CTGTGTAVST SEAEEAAAND WWLENLEKEL GLWGYAEEDT QAHPDLLDHY TGLSPLCALE GDPVSTYFQT GPAAAEPELL VVVEPSAVLL // ID MYB3_MAIZE STANDARD; PRT; 255 AA. AC P20025; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Myb-related protein Zm38. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89313655; PubMed=2664447; RA Marocco A., Wissenbach M., Becker D., Paz-Ares J., Saedler H., RA Salamini F., Rohde W.; RT "Multiple genes are transcribed in Hordeum vulgare and Zea mays that RT carry the DNA binding domain of the myb oncoproteins."; RL Mol. Gen. Genet. 216:183-187(1989). CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- SIMILARITY: Contains 2 Myb-like domains. DR PIR; S04899; S04899. DR HSSP; P01103; 1POM. DR TRANSFAC; T02959; -. DR MaizeDB; 69594; -. DR InterPro; IPR001005; Myb_DNA_binding. DR Pfam; PF00249; myb_DNA-binding; 2. DR SMART; SM00717; SANT; 2. DR PROSITE; PS00037; MYB_1; 1. DR PROSITE; PS00334; MYB_2; 1. DR PROSITE; PS50090; MYB_3; 2. KW Nuclear protein; DNA-binding; Repeat; Transcription regulation. FT DNA_BIND 9 61 Myb 1. FT DNA_BIND 62 112 Myb 2. SQ SEQUENCE 255 AA; 27568 MW; 26AAADC8B0633E06 CRC64; MGRSPCCEKA HTNRGAWTKE EDERLVAYIR AHGEGCWRSL PKAAGLLRCG KSCRLRWINY LRPDLKRGNF TADEDDLIVK LHSLLGNKWS LIAARLPGRT DNEIKNYWNT HVRRKLLGRG IDPVTHRPIA ADAVTVTTVS FQPSPSAAAA AAAEAEATAA KAPRCPDLNL DLCISPPCQQ QEEEEVDLKP SAAVVKREVL LGGRGHGHGH GGALCFGCSL GVQKGAPGCS CSSSNGHRCL GLRGGMLDFR GLKMK // ID MYBC_MAIZE STANDARD; PRT; 273 AA. AC P10290; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Anthocyanin regulatory C1 protein. GN C1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88111545; PubMed=3428265; RA Paz-Ares J., Ghosal D., Wienand U., Peterson P.A., Saedler H.; RT "The regulatory c1 locus of Zea mays encodes a protein with homology RT to myb proto-oncogene products and with structural similarities to RT transcriptional activators."; RL EMBO J. 6:3553-3558(1987). CC -!- FUNCTION: Controls the expression of genes involved in anthocyanin CC biosynthesis. Regulates the expression of at least 3 structural CC genes: chalcone synthase, dihydroflavonol reductase and flavonol CC O(3) glucosyltransferase. C1 acts as a trans-acting factor. CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- SIMILARITY: Contains 2 Myb-like domains. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37153; AAA33482.1; -. DR PIR; S06215; TVZMMB. DR HSSP; P01103; 1POM. DR TRANSFAC; T01592; -. DR MaizeDB; 24964; -. DR InterPro; IPR001005; Myb_DNA_binding. DR Pfam; PF00249; myb_DNA-binding; 2. DR SMART; SM00717; SANT; 2. DR PROSITE; PS00037; MYB_1; 1. DR PROSITE; PS00334; MYB_2; 1. DR PROSITE; PS50090; MYB_3; 2. KW Nuclear protein; DNA-binding; Repeat; Transcription regulation; KW Activator; Trans-acting factor. FT DNA_BIND 9 61 Myb 1. FT DNA_BIND 62 112 Myb 2. FT DOMAIN 205 212 Poly-Gly. FT DOMAIN 234 273 Asp/Glu-rich (acidic). SQ SEQUENCE 273 AA; 28750 MW; 163977BBA8CE669D CRC64; MGRRACCAKE GVKRGAWTSK EDDALAAYVK AHGEGKWREV PQKAGLRRCG KSCRLRWLNY LRPNIRRGNI SYDEEDLIIR LHRLLGNRWS LIAGRLPGRT DNEIKNYWNS TLGRRAGAGA GAGGSWVVVA PDTGSHATPA ATSGACETGQ NSAAHRADPD SAGTTTTSAA AVWAPKAVRC TGGLFFFHRD TTPAHAGETA TPMAGGGGGG GGEAGSSDDC SSAASVSLRV GSHDEPCFSG DGDGDWMDDV RALASFLESD EDWLRCQTAG QLA // ID MYBD_MAIZE STANDARD; PRT; 252 AA. AC P23592; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Anthocyanin regulatory C1-I protein. GN C1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90151603; PubMed=2303027; RA Paz-Ares J., Ghosal D., Saedler H.; RT "Molecular analysis of the C1-I allele from Zea mays: a dominant RT mutant of the regulatory C1 locus."; RL EMBO J. 9:315-321(1990). CC -!- FUNCTION: Controls the expression of genes involved in anthocyanin CC biosynthesis. Regulates the expression of at least 3 structural CC genes: chalcone synthase, dihydroflavonol reductase and flavonol CC O(3) glucosyltransferase. C1 acts as a trans-acting factor. CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- MISCELLANEOUS: The C1-I allele is a dominant negative mutant which CC inhibits pigment formation. CC -!- SIMILARITY: Contains 2 Myb-like domains. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52201; CAA36456.1; -. DR HSSP; P01103; 1POM. DR TRANSFAC; T02946; -. DR MaizeDB; 24964; -. DR InterPro; IPR001005; Myb_DNA_binding. DR Pfam; PF00249; myb_DNA-binding; 2. DR SMART; SM00717; SANT; 2. DR PROSITE; PS00037; MYB_1; 1. DR PROSITE; PS00334; MYB_2; 1. DR PROSITE; PS50090; MYB_3; 2. KW Nuclear protein; DNA-binding; Repeat; Transcription regulation; KW Activator; Trans-acting factor. FT DNA_BIND 9 61 Myb 1. FT DNA_BIND 62 112 Myb 2. FT DOMAIN 203 212 Poly-Gly. SQ SEQUENCE 252 AA; 26419 MW; AD61FA2B829C5FBD CRC64; MGRRACCAKE GVKRGAWTSK EDDALAAYVK AHGEGKWREV PQKAGLRRCG KSCRLRWLNY LRPNIRRGNI SYDEEDLIIR LHRLLGNRWS LIAGRLPGRT ENEIKNYWNS TLGRRAGAGA GGSRVVVAPD TGSHATPAAT SGSSETGQKG AAPRADPDSA GTTTTSAAAV WAPKAVRCTS GLFFFHRDTT PAHAGETATP MAGGGGVGGG GGEAGSSDDC SSAASVSPRV GSHDEPCFSG DGDGDWMDSW TT // ID MYBP_MAIZE STANDARD; PRT; 399 AA. AC P27898; P27899; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Myb-related protein P. GN P. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91271238; PubMed=2052542; RA Grotewold E., Athma P., Peterson T.; RT "Alternatively spliced products of the maize P gene encode proteins RT with homology to the DNA-binding domain of myb-like transcription RT factors."; RL Proc. Natl. Acad. Sci. U.S.A. 88:4587-4591(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=92275319; PubMed=1317315; RA Athma P., Grotewold E., Peterson T.; RT "Insertional mutagenesis of the maize P gene by intragenic RT transposition of Ac."; RL Genetics 131:199-209(1992). CC -!- FUNCTION: Transcription factor postulated to regulate the CC biosynthetic pathway of a flavonoid-derived pigment in certain CC floral tissues. CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P27898-1; Sequence=Displayed; CC Name=Short; CC IsoId=P27898-2; Sequence=VSP_003301, VSP_003302; CC -!- SIMILARITY: Contains 2 Myb-like domains. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M73028; AAA33500.1; -. DR EMBL; M73029; AAA33501.1; -. DR EMBL; Z11879; CAA77939.1; -. DR PIR; A39697; A39697. DR PIR; B39697; B39697. DR HSSP; P01103; 1POM. DR TRANSFAC; T01590; -. DR TRANSFAC; T01591; -. DR MaizeDB; 69180; -. DR MaizeDB; 69181; -. DR InterPro; IPR001005; Myb_DNA_binding. DR Pfam; PF00249; myb_DNA-binding; 2. DR SMART; SM00717; SANT; 2. DR PROSITE; PS00037; MYB_1; 1. DR PROSITE; PS00334; MYB_2; 1. DR PROSITE; PS50090; MYB_3; 2. KW Nuclear protein; DNA-binding; Repeat; Transcription regulation; KW Alternative splicing. FT DNA_BIND 9 61 Myb 1. FT DNA_BIND 62 112 Myb 2. FT DOMAIN 178 181 Poly-Ala. FT DOMAIN 305 311 Poly-Leu. FT VARSPLIC 89 152 WSLIASHLPGRTDNEIKNYWNSHLSRQIHTYRRKYTAGPDD FT TAIAIDMSKLQSADRRRGGRTPG -> RHLMIEADYSPPST FT VRCLPRGALAYLTLPRQSPFQTARITYDRIGSALLRSVRFC FT FRCVPSRW (in isoform Short). FT /FTId=VSP_003301. FT VARSPLIC 153 399 Missing (in isoform Short). FT /FTId=VSP_003302. SQ SEQUENCE 399 AA; 43756 MW; EE025B00A44CF5D0 CRC64; MGRTPCCEKV GLKRGRWTAE EDQLLANYIA EHGEGSWRSL PKNAGLLRCG KSCRLRWINY LRADVKRGNI SKEEEDIIIK LHATLGNRWS LIASHLPGRT DNEIKNYWNS HLSRQIHTYR RKYTAGPDDT AIAIDMSKLQ SADRRRGGRT PGRPPKASAS RTKQADADQP GGEAKGPAAA ASSPRHSDVV NPGPNQPNSS SGSTGTAEEE GPSSEDASGP WVLEPIELGD LVWGEADSEM DALMPIGPGG TTRLPSKGLA RSAARPRWTT CSTWTGMASR PICGAGRSRT STARSCGRPP SRWKLLLLLL LRRRPAPRTI ASWRRSRLGS CPTRSDGSGH RTDQTDQIIG SRVLARSLPS RGSWFRWPNN WEKNSTARAV KPPPCAPDVD ACRVELLRI // ID NIA1_MAIZE STANDARD; PRT; 621 AA. AC P17571; DT 01-AUG-1990 (Rel. 15, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Nitrate reductase [NADH] (EC 1.7.1.1) (NR) (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64 X W128E; TISSUE=Leaf; RA Gowri G., Campbell W.H.; RT "cDNA clones for corn leaf NADH: nitrate reductase and chloroplast RT NAD(P)(+): glyceraldehyde-3-phosphate dehydrogenase."; RL Plant Physiol. 90:792-798(1989). RN [2] RP REVISIONS TO 389-390; 405-406 AND 414-417, AND CHARACTERIZATION. RC STRAIN=cv. W64 X W128E; TISSUE=Leaf; RX MEDLINE=90267474; PubMed=2189408; RA Hyde G.E., Campbell W.H.; RT "High-level expression in Escherichia coli of the catalytically RT active flavin domain of corn leaf NADH:nitrate reductase and its RT comparison to human NADH:cytochrome B5 reductase."; RL Biochem. Biophys. Res. Commun. 168:1285-1291(1990). RN [3] RP SECONDARY STRUCTURE OF FAD DOMAIN. RX MEDLINE=92084635; PubMed=1748631; RA Hyde G.E., Crawford N.M., Campbell W.H.; RT "The sequence of squash NADH:nitrate reductase and its relationship RT to the sequences of other flavoprotein oxidoreductases. A family of RT flavoprotein pyridine nucleotide cytochrome reductases."; RL J. Biol. Chem. 266:23542-23547(1991). RN [4] RP MUTAGENESIS OF CYS-593. RX MEDLINE=94245686; PubMed=8188655; RA Dwivedi U.N., Shiraishi N., Campbell W.H.; RT "Identification of an 'essential' cysteine of nitrate reductase via RT mutagenesis of its recombinant cytochrome b reductase domain."; RL J. Biol. Chem. 269:13785-13791(1994). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF FAD DOMAIN. RX MEDLINE=95111952; PubMed=7812715; RA Lu G., Campbell W.H., Schneider G., Lindqvist Y.; RT "Crystal structure of the FAD-containing fragment of corn nitrate RT reductase at 2.5-A resolution: relationship to other flavoprotein RT reductases."; RL Structure 2:809-821(1994). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 232-501. RX MEDLINE=95280311; PubMed=7760334; RA Lu G., Lindqvist Y., Schneider G., Dwivedi U., Campbell W.H.; RT "Structural studies on corn nitrate reductase: refined structure of RT the cytochrome b reductase fragment at 2.5 A, its ADP complex and an RT active- site mutant and modeling of the cytochrome b domain."; RL J. Mol. Biol. 248:931-948(1995). CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first CC step of nitrate assimilation in plants, fungi and bacteria. CC -!- CATALYTIC ACTIVITY: Nitrite + NAD(+) + H(2)O = nitrate + NADH. CC -!- COFACTOR: Requires FAD, a heme group (called cytochrome b-557) and CC one molybdenum atom. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain. CC -!- SIMILARITY: TO EUKARYOTIC MOLYBDOPTERIN OXIDOREDUCTASES IN THE N- CC TERMINAL DOMAIN. CC -!- SIMILARITY: TO FAD/NAD-BINDING CYTOCHROME REDUCTASES IN THE C- CC TERMINAL DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M27821; AAA03202.1; ALT_SEQ. DR PDB; 2CND; 20-APR-95. DR PDB; 1CNE; 20-APR-95. DR PDB; 1CNF; 20-APR-95. DR MaizeDB; 25899; -. DR InterPro; IPR001199; Cyt_B5. DR InterPro; IPR001834; Cyt_B5_reductase. DR InterPro; IPR008335; Euk_Mb_oxred. DR InterPro; IPR008333; FAD_binding_6. DR InterPro; IPR001709; FPN_cyt_redctse. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR005066; Mo-co_dimer. DR InterPro; IPR000572; Oxidored_molyb. DR InterPro; IPR001433; Oxred_FAD/NAD(P). DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00173; heme_1; 1. DR Pfam; PF03404; Mo-co_dimer; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR Pfam; PF00174; oxidored_molyb; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00363; CYTOCHROMEB5. DR PRINTS; PR00407; EUMOPTERIN. DR PRINTS; PR00371; FPNCR. DR ProDom; PD000612; Cyt_B5; 1. DR PROSITE; PS00191; CYTOCHROME_B5_1; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; PARTIAL. KW Oxidoreductase; Flavoprotein; FAD; NAD; Heme; Molybdenum; KW Nitrate assimilation; Multigene family; 3D-structure. FT NON_TER 1 1 FT DISULFID 138 138 Interchain (Potential). FT METAL 284 284 Iron (heme axial ligand) (By similarity). FT METAL 307 307 Iron (heme axial ligand) (By similarity). FT SITE 593 593 Necessary for efficient electron FT Transfer. FT MUTAGEN 593 593 C->S: Reduction of activity. FT STRAND 364 375 FT TURN 376 377 FT STRAND 378 384 FT TURN 388 389 FT TURN 396 397 FT STRAND 399 406 FT TURN 407 408 FT STRAND 409 415 FT TURN 421 422 FT STRAND 426 432 FT STRAND 439 439 FT TURN 440 441 FT STRAND 442 442 FT TURN 443 444 FT HELIX 447 454 FT TURN 457 458 FT STRAND 460 467 FT STRAND 470 471 FT STRAND 478 480 FT TURN 481 482 FT STRAND 483 485 FT STRAND 489 495 FT HELIX 496 498 FT HELIX 499 511 FT TURN 512 515 FT STRAND 519 526 FT HELIX 529 531 FT TURN 533 534 FT HELIX 535 544 FT TURN 546 548 FT STRAND 549 555 FT HELIX 561 563 FT STRAND 568 569 FT HELIX 574 580 FT STRAND 588 593 FT HELIX 596 600 FT TURN 601 603 FT HELIX 604 608 FT TURN 609 611 FT HELIX 614 617 FT STRAND 618 621 SQ SEQUENCE 621 AA; 69773 MW; ACC276E4ED0FF5D3 CRC64; GFPVRVIIPG CIGGRMVKWL KRIIVTPAES DNYYHFKDNR VLPSHVDAEL ANAEAWWYKP EYIINELNIN SVITTPCHDE ILPINAFTTQ RPYTLKGYAY SGGGKKVTRV EVTLDGGETW LVCTDHPEKP TKYGKYWCWC FWSLEVEVLD LLSAKEIAVR AWDESLNTQP EKLIWNVMGM MNNCWFRVKT NVCKPHKGEI GIVFDHPTLP GNESGGWMAK EKHLETAEAA APGLKRSTST PFMNTTDVGK EFTMSEVRKH ASQESAWIVV HGHVYDCTKF LKDHPGGADS ILINAGTDCT EEFDAIHSDK AKALLDTYRI GELITTGTGY SSDNSVHGGS VLSHLAPIRR AVRAPALSNP REKIHCRLVG KKELSRDVRL FRFSLPSPDQ VLGLPIGKHI FVCASIEGKL CMRAYTPTSM VDEIGHFDLL VKVYFKNEHP KFPNGGLMTQ YLDSLPVGSY IDVKGPLGHV EYTGRGSFVI NGKQRHASRL AMICGGSGIT PMYQIIQAVL RDQPEDHTEM HLVYANRTED DILLRDELDR WAAEYPDRLK VWYVIDQVKR PEEGWKYSVG FVTEAVLREH VPEGGDDTLA LACGPPPMIQ FAISPNLEKM KYDMANSFVV F // ID NIA2_MAIZE STANDARD; PRT; 231 AA. AC P39871; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Nitrate reductase [NAD(P)H] (EC 1.7.1.2) (NR) (Fragment). GN NAR. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A X WI82E; TISSUE=Root; RA Long D.M., Oaks A., Rothstein S.J.; RT "Regulation of maize root nitrate reductase mRNA levels."; RL Physiol. Plantarum 85:561-566(1992). CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first CC step of nitrate assimilation in plants, fungi and bacteria. CC -!- CATALYTIC ACTIVITY: Nitrite + NAD(P)(+) + H(2)O = nitrate + CC NAD(P)H. CC -!- COFACTOR: Requires FAD, a heme group (called cytochrome b-557) and CC one molybdenum atom. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain. CC -!- SIMILARITY: TO EUKARYOTIC MOLYBDOPTERIN OXIDOREDUCTASES IN THE N- CC TERMINAL DOMAIN. CC -!- SIMILARITY: TO FAD/NAD-BINDING CYTOCHROME REDUCTASES IN THE C- CC TERMINAL DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64446; CAA45776.1; -. DR PIR; S24544; S24544. DR HSSP; P17571; 2CND. DR MaizeDB; 25891; -. DR InterPro; IPR001199; Cyt_B5. DR InterPro; IPR001834; Cyt_B5_reductase. DR InterPro; IPR008333; FAD_binding_6. DR InterPro; IPR001709; FPN_cyt_redctse. DR InterPro; IPR000572; Oxidored_molyb. DR InterPro; IPR001433; Oxred_FAD/NAD(P). DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00371; FPNCR. DR PROSITE; PS00191; CYTOCHROME_B5_1; PARTIAL. DR PROSITE; PS50255; CYTOCHROME_B5_2; PARTIAL. DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; PARTIAL. KW Oxidoreductase; Flavoprotein; FAD; NAD; NADP; Heme; Molybdenum; KW Nitrate assimilation; Multigene family. FT NON_TER 1 1 SQ SEQUENCE 231 AA; 26254 MW; 9864B425C0ED45F4 CRC64; PQKLGLPVGR HVYVCASIGG KLCMRAYTPT SPVDEVGHFD LLIKIYFKDE DPKYPNGGLM SQYLDSLPLG ATIDIKGPHR HIEYTGRRRF VVNGKQRHAR RLAMIQAGRG TTPDDDTEQA VLRDQPDDDT EMHLVYANRT DHDMLLREEI DRAWLPRTRR LKVWYVVSKV PEDGWEYGVG RVDEHVMREH LPLGDSETIA LVCGPPAMIE CTVRPGLEKM GYDLDKACLV F // ID NIA3_MAIZE STANDARD; PRT; 889 AA. AC P49102; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Nitrate reductase [NADH] 3 (EC 1.7.1.1) (NR). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Seedling; RA Campbell W.H., Redinbaugh M.G., Ingemarsson B., Doughtery E.S., RA Campbell E.R.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first CC step of nitrate assimilation in plants, fungi and bacteria. CC -!- CATALYTIC ACTIVITY: Nitrite + NAD(+) + H(2)O = nitrate + NADH. CC -!- COFACTOR: Each subunit of the enzyme contains 1 equivalent of FAD, CC heme iron, and molybdenum-pterin as prosthetic groups. The heme CC group is called cytochrome b-557 (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain. CC -!- SIMILARITY: TO EUKARYOTIC MOLYBDOPTERIN OXIDOREDUCTASES IN THE N- CC TERMINAL DOMAIN. CC -!- SIMILARITY: TO FAD/NAD-BINDING CYTOCHROME REDUCTASES IN THE C- CC TERMINAL DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U20450; AAA62316.1; -. DR PIR; T02240; T02240. DR HSSP; P17571; 2CND. DR MaizeDB; 30041; -. DR InterPro; IPR001199; Cyt_B5. DR InterPro; IPR001834; Cyt_B5_reductase. DR InterPro; IPR008335; Euk_Mb_oxred. DR InterPro; IPR008333; FAD_binding_6. DR InterPro; IPR001709; FPN_cyt_redctse. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR005066; Mo-co_dimer. DR InterPro; IPR000572; Oxidored_molyb. DR InterPro; IPR001433; Oxred_FAD/NAD(P). DR InterPro; IPR001221; Phe_hydroxylase. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00173; heme_1; 1. DR Pfam; PF03404; Mo-co_dimer; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR Pfam; PF00174; oxidored_molyb; 1. DR PRINTS; PR00406; CYTB5RDTASE. DR PRINTS; PR00363; CYTOCHROMEB5. DR PRINTS; PR00407; EUMOPTERIN. DR PRINTS; PR00371; FPNCR. DR PRINTS; PR00410; PHEHYDRXLASE. DR ProDom; PD000612; Cyt_B5; 1. DR PROSITE; PS00191; CYTOCHROME_B5_1; 1. DR PROSITE; PS50255; CYTOCHROME_B5_2; 1. DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1. KW Oxidoreductase; Flavoprotein; FAD; NAD; Heme; Molybdenum; KW Nitrate assimilation; Multigene family. FT METAL 181 181 Molybdenum-pterin (Potential). FT METAL 235 235 Molybdenum-pterin (Potential). FT DISULFID 404 404 Interchain (Potential). FT METAL 555 555 Iron (heme axial ligand) (By similarity). FT METAL 578 578 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 889 AA; 98811 MW; 3614A8BB44B822F5 CRC64; MSTCVEQPTH SASLDPTAAQ RLPYPDLPVD ILRRSSVRGS GFVAAALVSS ARKADDDARH DDDDPSGDRH ETYGSHYLAN LGVEQSVRDE GTVDAWVESS QSLIRLTGKH SLNGELPRLM RHGFITPVPR HYVRNHGPVP RGDWATWTVE VTGLVRRPRA LTMDELARDF PALELPVTLV CAGNRRKEQN MVRQTLGFNW GPGAVSTSVW RGARLSDVLR RCGSMSRKGG ALFVCFEGAE DLPGGGGTKY GTSITREVAL DPTMDVMLAY QQNGGPLLPD HGFPVRLIVP GCTAGRMVKW LKRIVVAPAE SDNYYHYRDN RFLPSHVDAK LADAEGWWYK PEYVINEMNT NSVITTPAHN EFLPINAITT QRIYTMKGFA YSGGGKKVTR VEVTLDGGEN WLLCELDHPE KPTKYGRYWC WCFWSIDVEL IDLLACKEIA VRAWDQSLNT QPEFLTWNLM GMMTNCWFRV KVNVCRPRHG EKAGLAFEHP VRTNQPGGWM AQQKHLETAE RTSAATSTTN QQFTMSEVRK HASQDSAWIV VHGHVYDCTA FLKDHPGGAD SILINAGTDC TEEFDAIHSD KAKELLDTYR IGDLVTTGGA EQRSPLELAP SPPIRHEGPA APVIALSNPR EKVPCQLVAR TVLSRDVRLF RFALPSSGQV LGLPVGKHIF VCASIDGKLC MRAYTPTSSV DEVGHFDLLV KVYFRNENTK FPDGGRMTQY LDSLPVGAHV DVKGPLGHVE YVGRGGFVID GKPRKAGRLA MVAGGSGITP IYQVIQAVLR DQPEDKTEMH LVYANRTEDD ILLRAELDRW AAEYPERLKV WYVVSQVKRL DEWKYSVGIV TEAVLRDDVP EARDGTLALL CGPPSMIQSP ILPNLEKMKH QLDDSVVSF // ID NIR_MAIZE STANDARD; PRT; 569 AA. AC P17847; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ferredoxin--nitrite reductase, chloroplast precursor (EC 1.7.7.1) DE (Fragment). GN NIR. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Lahners K., Kramer V., Back E., Privalle L., Rothstein S.; RT "Molecular cloning of complementary DNA encoding maize nitrite RT reductase: molecular analysis and nitrate induction."; RL Plant Physiol. 88:741-746(1988). CC -!- CATALYTIC ACTIVITY: Ammonia + H(2)O + OH(-) + 3 oxidized CC ferredoxin = nitrite + 3 reduced ferredoxin. CC -!- COFACTOR: This enzyme contains one siroheme and one 4Fe-4S iron- CC sulfur center as prosthetic groups. CC -!- PATHWAY: Nitrate assimilation (denitrification); second step. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- INDUCTION: By nitrate. CC -!- SIMILARITY: THE C-TERMINAL DOMAIN IS A 4FE-4S/SIROHEME DOMAIN CC FOUND IN NITRITE REDUCTASES (EC 1.7.1.4 AND EC 1.7.7.1) AND CC SULFITE REDUCTASES (EC 1.8.1.2 AND EC 1.8.7.1). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23456; AAA60450.1; ALT_INIT. DR MaizeDB; 69266; -. DR InterPro; IPR008287; Fd-NiR. DR InterPro; IPR006066; Nir_Si. DR InterPro; IPR006067; Nir_Sir_4Fe4S. DR InterPro; IPR005117; Nir_sir_fer. DR Pfam; PF01077; NIR_SIR; 1. DR Pfam; PF03460; NIR_SIR_ferr; 2. DR PIRSF; PIRSF000244; Fd-NiR; 1. DR PRINTS; PR00397; SIROHAEM. DR PROSITE; PS00365; NIR_SIR; 1. KW Oxidoreductase; Chloroplast; Transit peptide; Nitrate assimilation; KW Heme; Iron-sulfur; 4Fe-4S. FT NON_TER 1 1 FT TRANSIT <1 4 Chloroplast. FT CHAIN 5 569 Ferredoxin--nitrite reductase. FT METAL 447 447 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 453 453 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 488 488 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 492 492 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 492 492 Iron (siroheme axial ligand) (By FT similarity). SQ SEQUENCE 569 AA; 63341 MW; AA31738F2944CCE3 CRC64; IPGRTGRARA AVSVPPPAGE QVPTERLEPR VEERAGGYWV LKEKYRAGLN PQEKVKLEKE PMALFMEGGI QDLARVPMEQ IDAAKLTKDD VDVRLKWLGL FHRRKHQYGR FMMRLKLPNG VTTSEQTRYL ASVIEAYGAD GCADVTTRQN WQIRGVTLPD VPAILDGLRA VGLTSLQSGM DNVRNPVGNP LAGVDPHEIV DTRPYTNLLS SYVTNNSQGN PTITNLPRKW NVCVIGSHDL YEHPHINDLA YMPAVKDGEF GFNLLVGGFI SPKRWAEALP LDAWVAGDDV VPVCKAILEA YRDLGSRGNR QKTRMMWLID ELGMEVFRSE VEKRMPNGVL ERAAPEDLVD KRWERRDYLG VHPQKQEGLS YVGLHVPVGR LQAADMFELA RLADEYGTGE LRLTVEQNIV LPNVSNERLD ALLAEPLLQE QRLSPRPSML LRGLVACTGN QFCGQAIIET KARALQVARE VEKRVAVPRP VRMHWTGCPN SCGQVQVADI GFMGCLTKDS DGKIVEAADI FVGGRVGSDS HLADVYRKSV PCKDLVPIVA DLLVERFGAV PREREEDEE // ID NLTP_MAIZE STANDARD; PRT; 120 AA. AC P19656; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Nonspecific lipid-transfer protein precursor (LTP) (Phospholipid DE transfer protein) (PLTP) (Allergen Zea m 14). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 28-120. RC TISSUE=Seed; RX MEDLINE=89034179; PubMed=3182817; RA Tchang F., This P., Stiefel V., Arondel V., Morch M.-D., Pages M., RA Puigdomenech P., Grellet F., Delseny M., Bouillon P., Huet J.-C., RA Guerbette F., Beauvais-Cante F., Duranton H., Pernollet J.-C., RA Kader J.-C.; RT "Phospholipid transfer protein: full-length cDNA and amino acid RT sequence in maize. Amino acid sequence homologies between plant RT phospholipid transfer proteins."; RL J. Biol. Chem. 263:16849-16855(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91216438; PubMed=2022320; RA Arondel V., Tchang F., Baillet B., Vignols F., Grellet F., Delseny M., RA Kader J.-C., Puigdomenech P.; RT "Multiple mRNA coding for phospholipid-transfer protein from Zea mays RT arise from alternative splicing."; RL Gene 99:133-136(1991). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX MEDLINE=95253819; PubMed=7735835; RA Shin D.H., Lee J.Y., Hwang K.Y., Kim K.K., Suh S.W.; RT "High-resolution crystal structure of the non-specific lipid-transfer RT protein from maize seedlings."; RL Structure 3:189-199(1995). RN [4] RP STRUCTURE BY NMR. RX MEDLINE=94298807; PubMed=8026483; RA Petit M.-C., Sodano P., Marion D., Ptak M.; RT "Two-dimensional 1H-NMR studies of maize lipid-transfer protein. RT Sequence-specific assignment and secondary structure."; RL Eur. J. Biochem. 222:1047-1054(1994). RN [5] RP STRUCTURE BY NMR. RX MEDLINE=96259216; PubMed=8845747; RA Gomar J., Petit M.-C., Sodano P., Sy D., Marion D., Kader J.-C., RA Vovelle F., Ptak M.; RT "Solution structure and lipid binding of a nonspecific lipid transfer RT protein extracted from maize seeds."; RL Protein Sci. 5:565-577(1996). CC -!- FUNCTION: Plant nonspecific lipid-transfer proteins transfer CC phospholipids as well as galactolipids across membranes. May play CC a role in wax or cutin deposition in the cell walls of expanding CC epidermal cells and certain secretory tissues. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist; CC Name=1; CC IsoId=P19656-1; Sequence=Displayed; CC Name=2; Synonyms=long; CC IsoId=P19656-2; Sequence=VSP_003147; CC -!- SIMILARITY: Belongs to the plant LTP family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04176; AAA33493.1; -. DR EMBL; M57249; AAA33494.1; -. DR PIR; A31779; A31779. DR PDB; 1MZL; 01-AUG-96. DR PDB; 1MZM; 01-AUG-96. DR PDB; 1AFH; 15-MAY-97. DR PDB; 1FK0; 07-JAN-03. DR PDB; 1FK1; 07-JAN-03. DR PDB; 1FK2; 31-DEC-02. DR PDB; 1FK3; 31-DEC-02. DR PDB; 1FK4; 31-DEC-02. DR PDB; 1FK5; 31-DEC-02. DR PDB; 1FK6; 31-DEC-02. DR PDB; 1FK7; 31-DEC-02. DR MaizeDB; 25447; -. DR InterPro; IPR003612; AAI. DR InterPro; IPR000528; Plant_LTP. DR Pfam; PF00234; tryp_alpha_amyl; 1. DR PRINTS; PR00382; LIPIDTRNSFER. DR SMART; SM00499; AAI; 1. DR PROSITE; PS00597; PLANT_LTP; 1. KW Lipid-binding; Transport; Signal; 3D-structure; Alternative splicing; KW Allergen. FT SIGNAL 1 27 FT CHAIN 28 120 Nonspecific lipid-transfer protein. FT DISULFID 31 79 By similarity. FT DISULFID 41 56 By similarity. FT DISULFID 57 102 By similarity. FT DISULFID 77 116 By similarity. FT VARSPLIC 119 120 VN -> YSRRMHASAD (in isoform 2). FT /FTId=VSP_003147. FT HELIX 31 38 FT HELIX 39 41 FT HELIX 42 45 FT TURN 46 47 FT HELIX 54 66 FT HELIX 70 85 FT TURN 86 86 FT TURN 88 89 FT HELIX 92 101 FT TURN 102 103 FT TURN 112 113 FT HELIX 116 118 SQ SEQUENCE 120 AA; 11705 MW; 28F27EBAE3910218 CRC64; MARTQQLAVV ATAVVALVLL AAATSEAAIS CGQVASAIAP CISYARGQGS GPSAGCCSGV RSLNNAARTT ADRRAACNCL KNAAAGVSGL NAGNAASIPS KCGVSIPYTI STSTDCSRVN // ID NU1C_MAIZE STANDARD; PRT; 362 AA. AC P25706; DT 01-MAY-1992 (Rel. 22, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE NAD(P)H-quinone oxidoreductase chain 1, chloroplast (EC 1.6.5.-) DE (NAD(P)H dehydrogenase, chain 1) (NADH-plastoquinone oxidoreductase DE chain 1). GN NDHA OR NDH1. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92361273; PubMed=1498612; RA Maier R.M., Hoch B., Zeltz P., Koessel H.; RT "Internal editing of the maize chloroplast ndhA transcript restores RT codons for conserved amino acids."; RL Plant Cell 4:609-616(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE OF 1-16 FROM N.A. RX MEDLINE=91064760; PubMed=2249254; RA Maier R.M., Doery I., Igloi G., Koessel H.; RT "The ndhH genes of gramminean plastomes are linked with the junctions RT between small single copy and inverted repeat regions."; RL Curr. Genet. 18:245-250(1990). CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast CC (Potential). CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62370; CAA44228.1; -. DR EMBL; X86563; CAA60353.1; -. DR EMBL; X56521; CAA39869.1; -. DR PIR; JQ1671; JQ1671. DR Gramene; P25706; -. DR MaizeDB; 69243; -. DR InterPro; IPR001694; Resp_NADH_dh1. DR Pfam; PF00146; NADHdh; 1. DR PROSITE; PS00667; COMPLEX1_ND1_1; 1. DR PROSITE; PS00668; COMPLEX1_ND1_2; 1. KW Oxidoreductase; NAD; NADP; Quinone; Plastoquinone; Chloroplast; KW Transmembrane. FT TRANSMEM 26 48 Potential. FT TRANSMEM 97 119 Potential. FT TRANSMEM 126 148 Potential. FT TRANSMEM 163 185 Potential. FT TRANSMEM 254 276 Potential. FT TRANSMEM 296 318 Potential. FT TRANSMEM 338 360 Potential. SQ SEQUENCE 362 AA; 40372 MW; E9A73123D68B1F6E CRC64; MIIDRVEVET INSFSKSELF KEIYGLIWIL PIFALLLGIT IEVLVIVWLE REISASIQQR IGPEYAGPLG LLQAIADGTK LLLKEDILPS RGDIPLFSIG PSIAVISILL SFLVIPLGYR FVLADLSIGV FLWIAISSIA PIGLLMAGYS SNNKYSFSGG LRAAAQSISY EIPLTFCVLA ISLLSNSSST VDIVEAQSKY GFFGWNLWRQ PIGFLVFLIS SLAECERLPF DLPEAEEELV AGYQTEYSGI KYGLFYLVSY LNLLVSSLFV TVLYLGGWNF SIPYISFFGF FQMNKIIGIL EMVIGIFITL TKAYLFLFIS ITIRWTLPRM RMDQLLNLGW KFLLPISLGN LLLTTSSQLV SL // ID NU2C_MAIZE STANDARD; PRT; 510 AA. AC P46619; DT 01-NOV-1995 (Rel. 32, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE NAD(P)H-quinone oxidoreductase chain 2, chloroplast (EC 1.6.5.-) DE (NAD(P)H dehydrogenase, chain 2) (NADH-plastoquinone oxidoreductase DE chain 2). GN (NDHB-A OR NDH2-A) AND (NDHB-B OR NDH2-B). OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND RNA EDITING. RX MEDLINE=93117088; PubMed=1282235; RA Maier R.M., Neckermann K., Hoch B., Akhmedov N.B., Koessel H.; RT "Identification of editing positions in the ndhB transcript from maize RT chloroplasts reveals sequence similarities between editing sites of RT chloroplasts and plant mitochondria."; RL Nucleic Acids Res. 20:6189-6194(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast. CC -!- RNA EDITING: Modified_positions=156, 196, 204, 246, 277, 494. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60338.1; ALT_SEQ. DR EMBL; X86563; CAA60363.1; ALT_SEQ. DR PIR; S38992; S38992. DR Gramene; P46619; -. DR MaizeDB; 105929; -. DR HAMAP; MF_00445; -; 1. DR InterPro; IPR003916; NADHub_oxred5. DR InterPro; IPR001750; Oxidored_q1. DR Pfam; PF00361; oxidored_q1; 1. DR PRINTS; PR01434; NADHDHGNASE5. KW Oxidoreductase; NAD; NADP; Quinone; Plastoquinone; Chloroplast; KW Transmembrane; RNA editing. FT TRANSMEM 24 46 Potential. FT TRANSMEM 59 79 Potential. FT TRANSMEM 99 116 Potential. FT TRANSMEM 129 151 Potential. FT TRANSMEM 183 202 Potential. FT TRANSMEM 223 242 Potential. FT TRANSMEM 297 316 Potential. FT TRANSMEM 323 342 Potential. FT TRANSMEM 352 374 Potential. FT TRANSMEM 394 416 Potential. FT TRANSMEM 426 448 Potential. SQ SEQUENCE 510 AA; 57004 MW; 991A7E227A29598E CRC64; MIWHVQNENF ILDSTRIFMK AFHLLLFHGS FIFPECILIF GLILLLMIDL TSDQKDRPWF YFISSTSLVI SITALLFRWR EEPIISFSGN FQTNNFNEIF QFLILLCSTL CIPLSVEYIE CTEMAITEFL LFVLTATLGG MFLCGANDLI TIFVALECFS LCSYLLSGYT KRDLRSNEAT MKYLLMGGAS SSILVYGFSW LYGLSGGEIE LQEIVNGLIN TQMYNSPGIS IALIFITVGL GFKLSLAPFH QWTPDVYEGS PTPVVAFLSV TSKVAALALA TRILDIPFYF SSNEWHLLLE ILAILSMILG NLLAITQTSM KRMLAYSSIG QIGYVIIGII VGDSNDGYAS MITYMLFYIS MNLGTFACIV LFGLRTGTDN IRDYAGLYTK DPFLALSLAL CLLSLGGLPP LAGFFGKLYL FWCGWQAGLY FLVSIGLLTS VLSIYYYLKI IKLLMTGRNQ EITPYVRNYR RSPLRSNNSI ELSMTVCVIA STILGISMNP ILAIAQDTLF // ID NU3C_MAIZE STANDARD; PRT; 120 AA. AC P19044; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE NAD(P)H-quinone oxidoreductase chain 3, chloroplast (EC 1.6.5.-) DE (NAD(P)H dehydrogenase, chain 3) (NADH-plastoquinone oxidoreductase DE chain 3). GN NDHC OR NDH3. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89281491; PubMed=2499764; RA Steinmueller K., Ley A.C., Steinmetz A.A., Sayre R.T., Bogorad L.; RT "Characterization of the ndhC-psbG-ORF157/159 operon of maize plastid RT DNA and of the cyanobacterium Synechocystis sp. PCC6803."; RL Mol. Gen. Genet. 216:60-69(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. CC -!- SIMILARITY: Belongs to the complex I subunit 3 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17438; CAA35481.1; ALT_SEQ. DR EMBL; X86563; CAA60291.1; -. DR PIR; S58557; S58557. DR Gramene; P19044; -. DR MaizeDB; 69246; -. DR InterPro; IPR000440; Oxidored_q4. DR Pfam; PF00507; oxidored_q4; 1. KW Oxidoreductase; NAD; NADP; Quinone; Plastoquinone; Chloroplast. SQ SEQUENCE 120 AA; 13860 MW; DF0C62041D9040B7 CRC64; MFLLHEYDIF WTFLIIASLI PILVFWISGL LAPVSEGPEK LSSYESGIEP MGGAWLQFRI RYYMFALVFV VFDVETVFLY PWAMSFDVLG VSVFIEAFIF VLILVVGLVY AWRKGALEWS // ID NU3M_MAIZE STANDARD; PRT; 118 AA. AC P16265; DT 01-AUG-1990 (Rel. 15, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE NADH-ubiquinone oxidoreductase chain 3 (EC 1.6.5.3). GN ND3 OR NAD3. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. WF9-N; RX MEDLINE=89201232; PubMed=2853827; RA Gualberto J.M., Wintz H., Weil J.-H., Grienenberger J.M.; RT "The genes coding for subunit 3 of NADH dehydrogenase and for RT ribosomal protein S12 are present in the wheat and maize RT mitochondrial genomes and are co-transcribed."; RL Mol. Gen. Genet. 215:118-127(1988). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone = NAD(+) + ubiquinol. CC -!- SIMILARITY: Belongs to the complex I subunit 3 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14709; CAA32833.1; -. DR PIR; S70025; DNZMU3. DR MaizeDB; 69626; -. DR InterPro; IPR000440; Oxidored_q4. DR Pfam; PF00507; oxidored_q4; 1. KW Oxidoreductase; NAD; Ubiquinone; Mitochondrion. SQ SEQUENCE 118 AA; 13216 MW; B5ADFE1CBB83766E CRC64; MSEFAPICIY LVISPLVSLI PLGVPFPFAS NSSTYPEKLS AYECGSDPSG DARSRFDIRF YPVPILFIIP DPEVTFSFPW AVPPNKIDLF GSWSMMAFLL ILTIGSLYEW KRGASDRE // ID NU4C_MAIZE STANDARD; PRT; 500 AA. AC P11647; DT 01-OCT-1989 (Rel. 12, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE NAD(P)H-quinone oxidoreductase chain 4, chloroplast (EC 1.6.5.-) DE (NAD(P)H dehydrogenase, chain 4) (NADH-plastoquinone oxidoreductase DE chain 4). GN NDHD OR NDH4. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Schantz R., Bogorad L.; RT "Maize chloroplast genes ndhD, ndhE and psaC. Sequences, transcripts RT and transcript pools."; RL Plant Mol. Biol. 11:239-247(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13159; CAA31558.1; ALT_INIT. DR EMBL; X86563; CAA60349.1; -. DR PIR; JU0009; QXZM4. DR Gramene; P11647; -. DR MaizeDB; 69251; -. DR HAMAP; MF_00491; -; 1. DR InterPro; IPR003918; NADHub_oxred4. DR InterPro; IPR001750; Oxidored_q1. DR Pfam; PF00361; oxidored_q1; 1. DR PRINTS; PR01437; NUOXDRDTASE4. KW Oxidoreductase; NAD; NADP; Quinone; Plastoquinone; Chloroplast. FT CONFLICT 209 209 W -> L (in Ref. 1). FT CONFLICT 472 472 V -> L (in Ref. 1). SQ SEQUENCE 500 AA; 56514 MW; 2FBAB26141993793 CRC64; MSYFPWLTIL VVLPIFAGSL IFFLPHKGNK IVRWYTIAIC LLEFLLMTYA FCYHFQLEDP LIQLKEDSKW IDVFDFHWRL GIDPLSLGSI LLTGFITTLA TLAAWPVTRN SQLFYFLMLA MYSGQIGLFS SRDLLLFFIM WELELIPVYL LLSMWGGKRR LYSATKFILY TAGGSIFFLI GVLGMGLYGS NEPGLDLERL INQSYPTTWE ILLYFGFLIA YAVKLPIIPL HTWLPYTHGE AHYSTCMLLA GILLKMGAYG LIRVNMELLP HAHYLFSPWL VIIGAVQIIY AASTSLGQRN FKKRIAYSSV SHMGFIIIGI GSITNIGLNG AILQILSHGF IGATLFFLAG TACDRMRLVY LEELGGISIP MPKIFTMFSS FSMASLALPG MSGFVAELVV FFGLITSPKF MLMPKMLITF VMAIGMILTP IYLLSMLRQM FYGYKLFHVP NKNFVDSGPR ELFLLICIFL PVIGIGIYPD LVLSLSVDRV EVLLSNYYTK // ID NU5C_MAIZE STANDARD; PRT; 738 AA. AC P46620; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE NAD(P)H-quinone oxidoreductase chain 5, chloroplast (EC 1.6.5.-) DE (NAD(P)H dehydrogenase, chain 5) (NADH-plastoquinone oxidoreductase DE chain 5). GN NDHF OR NDH5. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [2] RP SEQUENCE OF 9-709 FROM N.A. RC TISSUE=Leaf; RA Clark L.G., Zhang W., Wendel J.F.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60346.1; -. DR EMBL; U21985; AAA64703.1; -. DR PIR; S58612; S58612. DR Gramene; P46620; -. DR MaizeDB; 107782; -. DR InterPro; IPR003916; NADHub_oxred5. DR InterPro; IPR001750; Oxidored_q1. DR InterPro; IPR002128; Oxidored_q1_C. DR InterPro; IPR001516; Oxidored_q1_N. DR Pfam; PF00361; oxidored_q1; 1. DR Pfam; PF01010; oxidored_q1_C; 1. DR Pfam; PF00662; oxidored_q1_N; 1. DR PRINTS; PR01434; NADHDHGNASE5. KW Oxidoreductase; NAD; NADP; Quinone; Plastoquinone; Chloroplast. FT CONFLICT 268 268 Missing (in Ref. 2). FT CONFLICT 289 289 W -> L (in Ref. 2). FT CONFLICT 570 570 R -> G (in Ref. 2). FT CONFLICT 680 680 K -> R (in Ref. 2). SQ SEQUENCE 738 AA; 82976 MW; F4E3EBD0DD3C91FA CRC64; MEHTYQYAWV IPLLPLPVIM SMGFGLFLIP TATKNLRRIW AFPSILLLSI AMVFSLHLSI QQINGSSIYQ YLWSWTINND FSLEFGYLVD PLTSIMLILI TTVGILVLIY SDDYMSHDEG YLRFFVYISF FNTSMLGLVT SSNLIQIYFF WELVGMCSYL LIGFWFTRPI AASACQKAFV TNRVGDFGLL LGILGFFWIT GSLEFRDLFK IANNWIPNNG INSLLTTLCA FLLFLGAVAK SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLLARL LPLFISLPWI MSFISLIGTI TLFLGATLAL AQRDIKRSLA YSTMSQLGYM MLALGIGSYQ AALFHLITHA YSKALLFLGS GSVIHSMEPL VGYSPDKSQN MVLMGGLRKY VPITRTTFLC GTLSLCGIPP LACFWSKDEI LSNSWLYSPF FGIIASFTAG LTAFYMFRIY LLTFDGYLRV HFQNYSSTKE GSLYSISLWG KSISKGVNRD FVLSTMKSGV SFFSQNIPKI PANTRNKIGS FSTPFGAKNT FVYPHETGNT MLFPLLILLL FTLFIGSIGI HFDNGVKDNR ILELTILSKW LTPSINLFQE NSNSSINSYE FLTNAISSVS LAIFGLFIAY IFYGSAYSFF QNLNFQNSLV KKNPKKSFLD EVKKKIYSWS YNRGYIDFFY TRVFILGIRK LAELTHFFDK GVIDGITNGV GLAGFCIGEE IKYVGGGRIS SYLFFFLCYV SLFLFFIP // ID NU6C_MAIZE STANDARD; PRT; 176 AA. AC P46621; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE NAD(P)H-quinone oxidoreductase chain 6, chloroplast (EC 1.6.5.-) DE (NAD(P)H dehydrogenase, chain 6) (NADH-plastoquinone oxidoreductase DE chain 6). GN NDHG OR NDH6. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60351.1; -. DR PIR; S58618; S58618. DR Gramene; P46621; -. DR MaizeDB; 120725; -. DR InterPro; IPR001457; Oxidored_q3. DR Pfam; PF00499; oxidored_q3; 1. KW Oxidoreductase; NAD; NADP; Quinone; Plastoquinone; Chloroplast. SQ SEQUENCE 176 AA; 19425 MW; 0417ADF1110F2142 CRC64; MDLPGPIHEI LVLFGGFGLL LGGLGVVLLT NPIYSAFSLG LVLVCISLFY FLLNSYFVAV AQLLIYVGAI NVLIIFAVMF VNGSEWSKDK NYWTIGDGFT LLLCITIPFS LMTTIPDTSW YGILWTTRSN QIVEQGLINN VQQIGIHLAT DFYLPFELIS LILLVSLIGA ITMARQ // ID NUCC_MAIZE STANDARD; PRT; 393 AA. AC P25709; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE NAD(P)H-quinone oxidoreductase chain H, chloroplast (EC 1.6.5.-) DE (NAD(P)H dehydrogenase, chain H) (NADH-plastoquinone oxidoreductase DE 49 kDa subunit). GN NDHH. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91064760; PubMed=2249254; RA Maier R.M., Doery I., Igloi G., Koessel H.; RT "The ndhH genes of gramminean plastomes are linked with the junctions RT between small single copy and inverted repeat regions."; RL Curr. Genet. 18:245-250(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Transfer of electrons from NADH to the respiratory CC chain. The immediate electron acceptor for the enzyme is believed CC to be plastoquinone. Component of the iron-sulfur (IP) fragment of CC the enzyme. CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56521; CAA39868.1; -. DR EMBL; X86563; CAA60354.1; -. DR PIR; S13600; S13600. DR Gramene; P25709; -. DR MaizeDB; 69245; -. DR InterPro; IPR001135; Oxidored_49kDa. DR Pfam; PF00346; complex1_49Kd; 1. DR PROSITE; PS00535; COMPLEX1_49K; 1. KW Oxidoreductase; NAD; NADP; Quinone; Plastoquinone; Chloroplast. SQ SEQUENCE 393 AA; 45687 MW; 41666743B3EC5279 CRC64; MSLSLKRKDL MIVNMGPQHP SMHGVLRLIV TLDGEDVIDC EPILGYLHRG MEKIAENRSI IQYLPYVTRW DYLATMFTEA ITVNAPEFLE NIQIPKRASY IRVIMLELSR IASHLLWLGP FMADLGAQTP FFYIFREREL IYDLFEAVTG MRMMHNYFRI GGVAADLPYG WMDKCLDFCD YFLQGVVEYQ ELITQNPIFL ERVEGVGFIS GEEAVNWGLS GPMLRASGIQ WDLRKIDPYE SYNQFDWKVQ WQKEGDSLAR YLVRVGEMRE SIKIIQQAVE KIPGGPYENL EARRFKKAKN PEWNDFEYRF LGKKPSPNFE LSKQELYVRV EAPKGELGIY LVGDDSLFPW RWKIRPPGFI NLQILPQLVK KMKLADIMTI LGSIDIIMGE VDR // ID NUGC_MAIZE STANDARD; PRT; 159 AA. AC P19124; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE NAD(P)H-quinone oxidoreductase chain J, chloroplast (EC 1.6.5.-) DE (NAD(P)H dehydrogenase, chain J) (NADH-plastoquinone oxidoreductase DE subunit J). GN NDHJ. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89281491; PubMed=2499764; RA Steinmueller K., Ley A.C., Steinmetz A.A., Sayre R.T., Bogorad L.; RT "Characterization of the ndhC-psbG-ORF157/159 operon of maize plastid RT DNA and of the cyanobacterium Synechocystis sp. PCC6803."; RL Mol. Gen. Genet. 216:60-69(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. CC -!- TISSUE SPECIFICITY: Leaves. CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17438; CAA35483.1; -. DR EMBL; X86563; CAA60289.1; -. DR PIR; S58555; S58555. DR Gramene; P19124; -. DR MaizeDB; 118231; -. DR InterPro; IPR001268; Complex1_30K. DR Pfam; PF00329; complex1_30Kd; 1. DR ProDom; PD001581; Complex1_30K; 1. DR PROSITE; PS00542; COMPLEX1_30K; 1. KW Oxidoreductase; NAD; NADP; Quinone; Plastoquinone; Chloroplast. SQ SEQUENCE 159 AA; 18669 MW; BFAEA6E22113C62F CRC64; MQQGWLSNWL VKHDVVHRSL GFDHRGVETL QIKAGDWDSI AVILYVYGYN YLRSQCAYDV APGGSLASVY HLTRIQYGID NPEEVCIKVF AQKDNPRIPS VFWVWRSADF QERESYDMVG ISYDNHPRLK RILMPESWIG WPLRKDYITP NFYEIQDAH // ID NUIC_MAIZE STANDARD; PRT; 180 AA. AC P46722; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE NAD(P)H-quinone oxidoreductase chain I, chloroplast (EC 1.6.5.-) DE (NAD(P)H dehydrogenase, chain I) (NADH-plastoquinone oxidoreductase DE subunit I) (frxB protein). GN NDHI OR FRXB. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. CC -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity). CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family. CC -!- SIMILARITY: The iron-sulfur centers are similar to those of CC bacterial-type 4Fe-4S ferredoxins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60352.1; -. DR PIR; S58619; S58619. DR HSSP; P00193; 1DUR. DR Gramene; P46722; -. DR MaizeDB; 69252; -. DR InterPro; IPR001450; 4Fe4S_ferredoxin. DR InterPro; IPR004497; NdhI. DR Pfam; PF00037; fer4; 2. DR TIGRFAMs; TIGR00403; ndhI; 1. DR PROSITE; PS00198; 4FE4S_FERREDOXIN; 2. KW Oxidoreductase; NAD; NADP; Quinone; Plastoquinone; Chloroplast; Iron; KW Iron-sulfur; 4Fe-4S. FT METAL 64 64 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 67 67 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 70 70 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 74 74 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 104 104 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 107 107 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 110 110 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 114 114 Iron-sulfur 1 (4Fe-4S) (By similarity). SQ SEQUENCE 180 AA; 21157 MW; EFE69385163353B8 CRC64; MFPMLTGFIS YGQQTIRAAR YIGQSFIITL SHTNRLPITI HYPYEKSITS ERFRGRIHFE FDKCIACEVC VRVCPIDLPL VDWRFEKDIK RKQLLNYSID FGVCIFCGNC VEYCPTNCLS MTEEYELSTY DRHELNYNQI ALSRLPISIM GDYTIQTIRN SPQSKIDEEK SWNSRTITDY // ID NUKC_MAIZE STANDARD; PRT; 248 AA. AC P06670; DT 01-JAN-1988 (Rel. 06, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE NAD(P)H-quinone oxidoreductase chain K, chloroplast (EC 1.6.5.-) DE (NAD(P)H dehydrogenase, chain K) (NADH-plastoquinone oxidoreductase DE subunit K). GN NDHK OR PSBG. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86139982; PubMed=3512536; RA Steinmetz A.A., Castroviejo M., Sayre R.T., Bogorad L.; RT "Protein PSII-G. An additional component of photosystem II identified RT through its plastid gene in maize."; RL J. Biol. Chem. 261:2485-2488(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=89281491; PubMed=2499764; RA Steinmueller K., Ley A.C., Steinmetz A.A., Sayre R.T., Bogorad L.; RT "Characterization of the ndhC-psbG-ORF157/159 operon of maize plastid RT DNA and of the cyanobacterium Synechocystis sp. PCC6803."; RL Mol. Gen. Genet. 216:60-69(1989). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. CC -!- COFACTOR: Binds 1 4Fe-4S cluster (Potential). CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12704; AAA84484.1; -. DR EMBL; X17438; CAA35482.1; -. DR EMBL; X86563; CAA60290.1; -. DR PIR; A25710; F2ZMG. DR Gramene; P06670; -. DR MaizeDB; 69598; -. DR InterPro; IPR006138; Cmplx1_20kDa. DR InterPro; IPR006137; Oxidored_q6. DR Pfam; PF01058; oxidored_q6; 1. DR PROSITE; PS01150; COMPLEX1_20K; 1. KW Oxidoreductase; NAD; NADP; Quinone; Plastoquinone; Chloroplast; Iron; KW Iron-sulfur; 4Fe-4S. FT METAL 64 64 Iron-sulfur (4Fe-4S) (Potential). FT METAL 65 65 Iron-sulfur (4Fe-4S) (Potential). FT METAL 129 129 Iron-sulfur (4Fe-4S) (Potential). FT METAL 160 160 Iron-sulfur (4Fe-4S) (Potential). FT CONFLICT 19 19 G -> E (in Ref. 1 and 2). SQ SEQUENCE 248 AA; 27848 MW; 0D29CF6446BA9655 CRC64; MVLTEYSEKK KKEGKDSIGT IMSLIEFPLL DQTSSNSVIS TTPNDLSNWS RLSSLWPLLY GTSCCFIEFA SLIGSRFDFD RYGLVPRSSP RQADLILTAG TVTMKMAPSL VRLYEQMPEP KYVIAMGACT ITGGMFSTDS YSTVRGVDKL IPVDVYLPGC PPKPEAVIDA LTKLRKKIAR EIIEDRTLCQ SQKKNRSFTT RHKLYVRRST HTGTYEQELL YQSPSTLDIS SETFFKSKSS VSSYKLVN // ID NULC_MAIZE STANDARD; PRT; 101 AA. AC P11646; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE NAD(P)H-quinone oxidoreductase chain 4L, chloroplast (EC 1.6.5.-) DE (NAD(P)H dehydrogenase, chain 4L) (NADH-plastoquinone oxidoreductase DE chain 4L). GN NDHE OR NDH4L. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Schantz R., Bogorad L.; RT "Maize chloroplast genes ndhD, ndhE and psaC. Sequences, transcripts RT and transcript pools."; RL Plant Mol. Biol. 11:239-247(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13159; CAA31556.1; -. DR EMBL; X86563; CAA60350.1; -. DR PIR; JU0010; QXZM4L. DR Gramene; P11646; -. DR MaizeDB; 69254; -. DR InterPro; IPR003215; NADH_dh_ubiq1. DR InterPro; IPR001133; Oxidored_4L. DR Pfam; PF00420; oxidored_q2; 1. DR ProDom; PD002107; NADH_dh_ubiq1; 1. KW Oxidoreductase; NAD; NADP; Quinone; Plastoquinone; Chloroplast. SQ SEQUENCE 101 AA; 11356 MW; 52F4EB3E2D535B7F CRC64; MMFERVLFLS VYLFSIGIYG LITSRNMVRA LICLELILNS INLNLVTFSD LFDSRQLKGD IFAIFVIALA AAEAAIGLSI LSSIHRNRKS TRINQSNFLN N // ID OCS1_MAIZE STANDARD; PRT; 151 AA. AC P24068; DT 01-MAR-1992 (Rel. 21, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Ocs-element binding factor 1 (OCSBF-1). GN OBF1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Root; RX MEDLINE=93005679; PubMed=2152133; RA Singh K., Dennis E.S., Ellis J.G., Llewellyn D.J., Tokuhisa J.G., RA Wahleithner J.A., Peacock W.J.; RT "OCSBF-1, a maize ocs enhancer binding factor: isolation and RT expression during development."; RL Plant Cell 2:891-903(1990). RN [2] RP REVISIONS TO C-TERMINUS. RA Singh K.B.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May contribute to developmentally specific patterns of CC gene expression. Binds specifically to ocs elements which are CC transcriptional enhancer found in the promoters of several plant CC genes. OCSBF-1 is able to bind to a site within each half of the CC ocs element as well as to animal AP-1 and CREB sites. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- TISSUE SPECIFICITY: Roots and shoots of young plants, and basal CC portion of leaves. CC -!- MISCELLANEOUS: A derivative of OCSBF-1 that contains only the 76 CC N-terminal amino acids is still able to bind to the ocs element. CC -!- SIMILARITY: Belongs to the bZIP family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62745; CAA44607.1; -. DR PIR; JQ0984; JQ0984. DR PIR; T03642; T03642. DR TRANSFAC; T02664; -. DR TRANSFAC; T02999; -. DR MaizeDB; 64064; -. DR InterPro; IPR004827; TF_bZIP. DR Pfam; PF00170; bZIP; 1. DR SMART; SM00338; BRLZ; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. KW Transcription regulation; DNA-binding; Nuclear protein. FT DNA_BIND 26 45 Basic motif. FT DOMAIN 52 66 Leucine-zipper. SQ SEQUENCE 151 AA; 16976 MW; DCDB2B5F5A0245A6 CRC64; MSSSSLSPTA GRTSGSDGDS AADTHRREKR RLSNRESARR SRLRKQQHLD ELVQEVARLQ ADNARVAARA RDIASQYTRV EQENTVLRAR AAELGDRLRS VNEVLRLVEE FSGVAMDIQE EMPADDPLLR PWQLPYPAAA MPMGAPHMLH Y // ID OLE1_MAIZE STANDARD; PRT; 156 AA. AC P13436; Q43244; DT 01-JAN-1990 (Rel. 13, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Oleosin Zm-I (Oleosin 16 kDa) (Lipid body-associated major protein) DE (Lipid body-associated protein L3). GN OLE16 OR OLE1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Missouri 17; RX MEDLINE=95161719; PubMed=7858232; RA Lee K., Huang A.H.C.; RT "Genes encoding oleosins in maize kernel of inbreds Mo17 and B73."; RL Plant Mol. Biol. 26:1981-1987(1994). RN [2] RP SEQUENCE OF 10-156 FROM N.A. RX MEDLINE=87280221; PubMed=2440887; RA Vance V.B., Huang A.H.C.; RT "The major protein from lipid bodies of maize. Characterization and RT structure based on cDNA cloning."; RL J. Biol. Chem. 262:11275-11279(1987). CC -!- FUNCTION: May have a structural role to stabilize the lipid body CC during desiccation of the seed by preventing coalescence of the CC oil. Probably interacts with both lipid and phospholipid moieties CC of lipid bodies. May also provide recognition signals for specific CC lipase anchorage in lipolysis during seedling growth. CC -!- SUBCELLULAR LOCATION: Surface of oil bodies. Oleosins exist at a CC monolayer lipid/water interface. CC -!- PTM: The N-terminus is blocked. CC -!- SIMILARITY: Belongs to the oleosin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U13701; AAA68065.1; -. DR EMBL; M17225; AAA33481.1; -. DR PIR; A29788; A29788. DR PIR; S52029; S52029. DR MaizeDB; 65613; -. DR InterPro; IPR000136; Oleosin. DR Pfam; PF01277; Oleosin; 1. DR PROSITE; PS00811; OLEOSINS; 1. KW Seed; Oil body; Multigene family. FT DOMAIN 1 42 Polar. FT DOMAIN 43 114 Hydrophobic. FT CONFLICT 10 10 G -> R (in Ref. 2). FT CONFLICT 124 124 A -> G (in Ref. 2). FT CONFLICT 142 142 V -> I (in Ref. 2). SQ SEQUENCE 156 AA; 15793 MW; 8DEF0F7F69770462 CRC64; MADHHRGATG GGGGYGDLQR GGGMHGEAQQ QQKQGAMMTA LKAATAATFG GSMLVLSGLI LAGTVIALTV ATPVLVIFSP VLVPAAIALA LMAAGFVTSG GLGVAALSVF SWMYKYLTGK HPPAADQLDH AKARLASKAR DVKDAAQHRI DQAQGS // ID OLE3_MAIZE STANDARD; PRT; 187 AA. AC P21641; DT 01-MAY-1991 (Rel. 18, Created) DT 01-MAY-1991 (Rel. 18, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Oleosin Zm-II (Oleosin 18 kDa) (Lipid body-associated protein L2). GN OLE18 OR OLE3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 43-56. RC STRAIN=cv. Missouri 17; RX MEDLINE=90130481; PubMed=2298748; RA Qu R., Huang A.H.C.; RT "Oleosin KD 18 on the surface of oil bodies in maize. Genomic and RT cDNA sequences and the deduced protein structure."; RL J. Biol. Chem. 265:2238-2243(1990). CC -!- FUNCTION: May have a structural role to stabilize the lipid body CC during desiccation of the seed by preventing coalescence of the CC oil. Probably interacts with both lipid and phospholipid moieties CC of lipid bodies. May also provide recognition signals for specific CC lipase anchorage in lipolysis during seedling growth. CC -!- SUBCELLULAR LOCATION: Surface of oil bodies. Oleosins exist at a CC monolayer lipid/water interface. CC -!- PTM: The N-terminus is blocked. CC -!- SIMILARITY: Belongs to the oleosin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J05212; AAA67699.1; -. DR PIR; A35040; A35040. DR MaizeDB; 65606; -. DR InterPro; IPR000136; Oleosin. DR Pfam; PF01277; Oleosin; 1. DR PROSITE; PS00811; OLEOSINS; 1. KW Seed; Oil body; Multigene family. FT DOMAIN 1 51 Polar. FT DOMAIN 52 123 Hydrophobic. SQ SEQUENCE 187 AA; 18501 MW; 22D694B8B1697351 CRC64; MADRDRSGIY GGAHATYGQQ QQQGGGGRPM GEQVKKGMLH DKGPTASQAL TVATLFPLGG LLLVLSGLAL TASVVGLAVA TPVFLIFSPV LVPAALLIGT AVMGFLTSGA LGLGGLSSLT CLANTARQAF QRTPDYVEEA RRRMAEAAAQ AGHKTAQAGQ AIQGRAQEAG TGGGAGAGAG GGGRASS // ID OP2_MAIZE STANDARD; PRT; 453 AA. AC P12959; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Opaque-2 regulatory protein. GN O2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=AC 1503 GM 1407; RX MEDLINE=90016825; PubMed=2798113; RA Maddaloni M., di Fonzo N., Hartings H., Lazzaroni N., RA Salamini F., Thompson R.D., Motto M.; RT "The sequence of the zein regulatory gene opaque-2 (O2) of Zea Mays."; RL Nucleic Acids Res. 17:7532-7532(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=AC 1503 GM 1407; RX MEDLINE=90059860; PubMed=2479535; RA Hartings H., Maddaloni M., Lazzaroni N., di Fonzo N., Motto M., RA Salamini F., Thompson R.D.; RT "The O2 gene which regulates zein deposition in maize endosperm RT encodes a protein with structural homologies to transcriptional RT activators."; RL EMBO J. 8:2795-2801(1989). RN [3] RP FUNCTION. RX MEDLINE=91160516; PubMed=2001677; RA Lohmer S., Maddaloni M., Motto M., di Fonzo N., Hartings H., RA Salamini F., Thompson R.D.; RT "The maize regulatory locus Opaque-2 encodes a DNA-binding protein RT which activates the transcription of the b-32 gene."; RL EMBO J. 10:617-624(1991). CC -!- FUNCTION: Involved in the regulation of the endosperm-specific CC production of albumin b-32 and other zein proteins. It is a CC trans-acting transcriptional activator that binds to the consensus CC sequence 5'-GATGAYRTGR-3'. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Belongs to the bZIP family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15544; CAA33550.1; -. DR EMBL; X16618; CAA34614.1; -. DR PIR; S06022; S06022. DR HSSP; P03069; 2DGC. DR TRANSFAC; T00668; -. DR MaizeDB; 24976; -. DR InterPro; IPR004827; TF_bZIP. DR Pfam; PF00170; bZIP; 1. DR SMART; SM00338; BRLZ; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. KW Nuclear protein; DNA-binding; Transcription regulation; Activator; KW Trans-acting factor. FT DNA_BIND 228 246 Basic motif. FT DOMAIN 253 274 Leucine-zipper. FT CONFLICT 26 26 E -> EPEPEPE (in Ref. 2). FT CONFLICT 144 144 D -> A (in Ref. 2). FT CONFLICT 231 231 K -> KR (in Ref. 2). SQ SEQUENCE 453 AA; 49356 MW; 513A8AB8D5ABD999 CRC64; MEHVISMEEI LGPFWELLPP PAPEPEREQP PVTGIVVGSV IDVAAAGHGD GDMMDQQHAT EWTFERLLEE EALTTSTPPP VVVVPNSCCS GALNADRPPV MEEAVTMAPA AVSSAVVGDP MEYNAILRRK LEEDLEAFKM WRADSSVVTS DQRSQGSNNH TGGSSIRNNP VQNKLMNGED PINNNHAQTA GLGVRLATSS SSRDPSPSDE DMDGEVEILG FKMPTEERVR KKESNRESAR RSRYRKAAHL KELEDQVAQL KAENSCLLRR IAALNQKYND ANVDNRVLRA DMETLRAKVK MGEDSLKRVI EMSSSVPSSM PISAPTPSSD APVPPPPIRD SIVGYFSATA ADDDASVGNG FLRLQAHQEP ASMVVGGTLS ATEMNRVAAA THCAGAMELI QTAMGSMPPT SASGSTPPPQ IMSCWVQMGP YTWTCIRHCG FRDRWEHFIC RRR // ID PCNA_MAIZE STANDARD; PRT; 263 AA. AC Q43266; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Proliferating cell nuclear antigen (PCNA). GN PCNA. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Black Mexican Sweet; RX MEDLINE=95092787; PubMed=7999788; RA Lopez I., Khan S., Vasquez-Ramos J., Hussey P.J.; RT "Molecular cloning of a maize cDNA clone encoding a putative RT proliferating cell nuclear antigen."; RL Biochim. Biophys. Acta 1260:119-121(1995). CC -!- FUNCTION: This protein is an auxiliary protein of DNA polymerase CC delta and is involved in the control of eukaryotic DNA replication CC by increasing the polymerase's processibility during elongation of CC the leading strand (By similarity). CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Belongs to the PCNA family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X79065; CAA55669.1; -. DR PIR; S52115; S52115. DR HSSP; P12004; 1AXC. DR MaizeDB; 113516; -. DR InterPro; IPR000730; Pr_cel_nuc_antig. DR Pfam; PF00705; PCNA; 1. DR Pfam; PF02747; PCNA_C; 1. DR PRINTS; PR00339; PCNACYCLIN. DR ProDom; PD002673; Pr_cel_nuc_antig; 1. DR TIGRFAMs; TIGR00590; pcna; 1. DR PROSITE; PS00293; PCNA_2; 1. DR PROSITE; PS01251; PCNA_1; 1. KW DNA-binding; Nuclear protein; DNA replication. FT DNA_BIND 61 80 Potential. SQ SEQUENCE 263 AA; 29342 MW; 450E55EC484BD5A6 CRC64; MLELRLVQGS LLKKVLEAIR ELVNDANFDC SGTGFSLQAM DSSHVALVAL LLRAEGFEHY RCDRNLSMGM NLNNMAKMLR CAGNDDIITI KADDGSDTVT FMFESPKQDK IADFEMKLMD IDSEHLGIPD SEYQAIVRMP SSEFMRICKD LSSIGDTVVI SVTKEGVKFS TSGEIGSANI VCRQNQTIDK PEEATIIEMQ EPVSLTFALR YMNSFTKASS LSEQVTISLS SELPVVVEYK IAEMGYIRFY LAPKIEDDEE MKP // ID PDA1_MAIZE STANDARD; PRT; 812 AA. AC Q43270; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Phospholipase D alpha 1 (EC 3.1.4.4) (PLD alpha 1) (Choline DE phosphatase 1) (Phosphatidylcholine-hydrolyzing phospholipase D 1). GN PLD1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Missouri 17; RX MEDLINE=96012933; PubMed=7551587; RA Ueki J., Morioka S., Komari T., Kumashiro T.; RT "Purification and characterization of phospholipase D (PLD) from rice RT (Oryza sativa L.) and cloning of cDNA for PLD from rice and maize RT (Zea mays L.)."; RL Plant Cell Physiol. 36:903-914(1995). CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal CC phosphodiesteric bond. Plays an important role in various cellular CC processes. CC -!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a CC phosphatidate. CC -!- COFACTOR: Calcium (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding CC promotes the protein association with membranes. A lower affinity CC toward calcium can be anticipated for PLD alpha due to the absence CC of two potential calcium ligands. CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD CC subfamily. CC -!- SIMILARITY: Contains 1 C2 domain. CC -!- SIMILARITY: Contains 2 PLD phosphodiesterase domains. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D73410; BAA11135.1; -. DR PIR; T03659; T03659. DR MaizeDB; 113853; -. DR InterPro; IPR000008; C2. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR001736; PLD. DR Pfam; PF00168; C2; 1. DR Pfam; PF00614; PLDc; 2. DR SMART; SM00239; C2; 1. DR SMART; SM00155; PLDc; 2. DR PROSITE; PS50004; C2_DOMAIN_2; FALSE_NEG. DR PROSITE; PS50035; PLD; 2. KW Hydrolase; Lipid degradation; Calcium; Repeat. FT DOMAIN 1 114 C2 domain. FT DOMAIN 330 368 PLD phosphodiesterase 1. FT DOMAIN 658 685 PLD phosphodiesterase 2. FT ACT_SITE 335 335 Potential. FT ACT_SITE 337 337 Potential. FT ACT_SITE 342 342 Potential. FT ACT_SITE 663 663 Potential. FT ACT_SITE 665 665 Potential. FT ACT_SITE 670 670 Potential. SQ SEQUENCE 812 AA; 92242 MW; D05CB351655BCC61 CRC64; MAQILLHGTL HATIFEAESL SNPHRATGGA PKFIRKLVEG IEDTVGVGKG ATKIYATVDL EKARVGRTRM ISNEPVNPRW YESFHIYCAH MAADVIFTVK IDNSIGASLI GRAYLAVQDL LGGEEIDKWL EISDENREPV GDSKIHVKLQ YFDVGKDRNW ARGVRSTKYP GVPYTFFSQR QGCKVTLYQD AHVPDNFVPR IQLADGKNYE PHRCWEDIFD AISKAQHLIY ITGWSVYTEI TLVRDTNRPK PGGDVTLGEL LKRKASEGVR VLMLVWDDRT SVGLLKKDGL MATHDEETAN YFHGTDVNCV LCPRNPDDSG SFVQDLQIST MFTHHQKIVV VDHEMPNQGS QQRRIVSFIG GIDLCDGRYD TQYHSLFRTL DTVHHDDFHQ PNFEGGSIKK GGPREPWHDI HSRLEGPIAW DVLYNFEQRW RKQGGKDLLV RLRDLPDIII PPSPVMFPED RETWNVQLFR SIDGGAAFGF PETPEEAARA GLVSGKDQII DRSIQDAYVN AIRRAKNFIY IENQYFLGSS YGWKPEGIKP EEIGALHLIP KELSLKIVSK IEAGERFTVY VVVPMWPEGV PESASVQAIL DWQRRTMEMM YTDIAQALEA NGIEANPKDY LTFFCLGNRE VKQEGEYEPE EHPEPDTDYI RAQEARRFMI YVHTKMMIVD DEYIIIGSAN INQRSMDGAR DSEIAMGAYQ PYHLATRQPA RGQIHGFRMS LWYEHLGMLE DVFQRPESVE CVQKVNEVAE KYWDLYSSDD LEQDLPGHLL SYPIGVTADG SVTELPGMEN FPDTRARVLG NKSDYLPPIL TT // ID PDI_MAIZE STANDARD; PRT; 513 AA. AC P52588; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Protein disulfide isomerase precursor (EC 5.3.4.1) (PDI). GN PDI. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; TISSUE=Endosperm; RX MEDLINE=96270367; PubMed=8639747; RA Li C.P., Larkins B.A.; RT "Expression of protein disulfide isomerase is elevated in the RT endosperm of the maize floury-2 mutant."; RL Plant Mol. Biol. 30:873-882(1996). CC -!- FUNCTION: Participates in the folding of proteins containing CC disulfide bonds, may be involved in glycosylation, prolyl CC hydroxylation and triglyceride transfer (By similarity). CC -!- CATALYTIC ACTIVITY: Rearrangement of both intrachain and CC interchain disulfide bonds in proteins to form the native CC structures. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (Potential). CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family. CC -!- SIMILARITY: Contains 2 thioredoxin domains. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L39014; AAB08519.1; -. DR PIR; S69181; S69181. DR HSSP; P07237; 1MEK. DR MaizeDB; 86830; -. DR InterPro; IPR005788; Disulph_isom. DR InterPro; IPR005792; Disulphide_isom. DR InterPro; IPR000886; ER_target_S. DR InterPro; IPR006662; Thiored. DR InterPro; IPR006663; Thioredox_dom2. DR Pfam; PF00085; thiored; 3. DR PRINTS; PR00421; THIOREDOXIN. DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1. DR TIGRFAMs; TIGR01126; pdi_dom; 2. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00194; THIOREDOXIN; 2. KW Redox-active center; Isomerase; Endoplasmic reticulum; Repeat; Signal. FT SIGNAL 1 23 By similarity. FT CHAIN 24 513 Protein disulfide isomerase. FT DISULFID 63 66 Redox-active (By similarity). FT DISULFID 408 411 Redox-active (By similarity). FT CARBOHYD 279 279 N-linked (GlcNAc...) (Potential). FT SITE 510 513 Prevent secretion from ER (Potential). SQ SEQUENCE 513 AA; 57096 MW; 29302DD01A3DEB80 CRC64; MAIRSKAWIS LLLALAVALS ARAEEEPAAA AEGEAVLTLD VDSFDEAVAK HPFMVVEFYA PWCGHCKKLA PEYENAAKAL SKHDPPIVLA KVDANEEKNR PLATKYEIQG FPTIKIFRDR GKNIQEYKGP READGIVDYL KKQVGPASKE IKSPEDATAL IDDKKIYIVG IFAEFSGTEF TNFMEVAEKL RSDYDFGHTL HANHLPRGDA AVERPLVRLL KPFDELVVDS KDFDVAALMK FIDASTIPRV VTFDKNPDNH PYLMKFFQSS APKAMLFLNF STGPFDSFKS AYSAAAEEFK DKEIKFLIGD IEASQGAFQY FGLKEDQTPL ILIQDGDSKK FLKVHVEADQ IVAWLKEYFD GKLTPFRNSE PIPEVNNEPV KVVVADNVHD FVFKSGKNVL IEFYAPWCGH CKKLAPILDE AATTLQSDEE VVIAKMDATA NDVPSEFDVQ GYPTLYFVTP SGKVTSYDSG RTADDIVDFI KKSKETAAPH HHHHPGATGI REGSRAEPVK DEL // ID PETD_MAIZE STANDARD; PRT; 160 AA. AC P05643; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Cytochrome b6-f complex subunit 4 (17 kDa polypeptide). GN PETD. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seedling; RX MEDLINE=94073219; PubMed=8252066; RA Freyer R., Hoch B., Neckermann K., Maier R.M., Koessel H.; RT "RNA editing in maize chloroplasts is a processing step independent RT of splicing and cleavage to monocistronic mRNAs."; RL Plant J. 4:621-629(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE OF 1-67 FROM N.A. RX MEDLINE=88210525; PubMed=2835175; RA Rock C.D., Barkan A., Taylor W.C.; RT "The maize plastid psbB-psbF-petB-petD gene cluster: spliced and RT unspliced petB and petD RNAs encode alternative products."; RL Curr. Genet. 12:69-77(1987). CC -!- FUNCTION: This polypeptide of unknown function is one of the CC components of the cytochrome b6-f complex. CC -!- SUBUNIT: The main subunits of complex b6-f are: cytochrome b6, 17 CC kDa polypeptide (petD), cytochrome f and the Rieske protein. CC -!- SIMILARITY: Belongs to the cytochrome b family. PetD subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S67284; AAB29195.2; -. DR EMBL; S67283; AAB29195.2; JOINED. DR EMBL; X86563; CAA60316.1; -. DR EMBL; X05422; CAA29001.1; -. DR PIR; S58582; S58582. DR Gramene; P05643; -. DR MaizeDB; 56341; -. DR InterPro; IPR005870; Cytb6/f_IV. DR InterPro; IPR005798; Cytb_b6_C. DR Pfam; PF00032; cytochrome_b_C; 1. DR TIGRFAMs; TIGR01156; cytb6/f_IV; 1. DR PROSITE; PS00193; CYTOCHROME_B_QO; 1. KW Electron transport; Chloroplast; Photosynthesis; Transmembrane. SQ SEQUENCE 160 AA; 17489 MW; F8B6325B4D5B3E00 CRC64; MGVTKKPDLN DPVLRAKLAK GMGHNYYGEP AWPNDLLYIF PVVILGTIAC NVGLAVLEPS MIGEPADPFA TPLEILPEWY FFPVFQILRT VPNKLLGVLL MVSVPTGLLT VPFLENVNKF QNPFRRPVAT TVFLIGTAVA LWLGIGATLP IDKSLTLGLF // ID PETG_ORYSA STANDARD; PRT; 37 AA. AC P12121; P32973; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Cytochrome b6-f complex subunit V (Cytochrome b6f complex subunit DE petG). GN PETG OR PETE. OS Oryza sativa (Rice), OS Zea mays (Maize), OS Nicotiana tabacum (Common tobacco), OS Oenothera hookeri (Hooker's evening primrose), OS Lotus japonicus, OS Spinacia oleracea (Spinach), OS Triticum aestivum (Wheat), OS Populus deltoides (Poplar), and OS Beta vulgaris (Sugar beet). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530, 4577, 4097, 85636, 34305, 3562, 4565, 3696, 161934; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=O.sativa; STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=89364698; PubMed=2770692; RA Hiratsuka J., Shimada H., Whittier R., Ishibashi T., Sakamoto M., RA Mori M., Kondo C., Honji Y., Sun C.-R., Meng B.-Y., Li Y.-Q., RA Kanno A., Nishizawa Y., Hirai A., Shinozaki K., Sugiura M.; RT "The complete sequence of the rice (Oryza sativa) chloroplast genome: RT intermolecular recombination between distinct tRNA genes accounts for RT a major plastid DNA inversion during the evolution of the cereals."; RL Mol. Gen. Genet. 217:185-194(1989). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=89160811; PubMed=2922397; RA Haley J., Bogorad L.; RT "A 4-kDa maize chloroplast polypeptide associated with the cytochrome RT b6-f complex: subunit 5, encoded by the chloroplast petE gene."; RL Proc. Natl. Acad. Sci. U.S.A. 86:1534-1538(1989). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=N.tabacum; STRAIN=cv. Bright Yellow 4; RA Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N., RA Matsubayashi T., Zaita N., Chunwongse J., Obokata J., RA Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B.-Y., Sugita M., RA Deno H., Kamogashira T., Yamada K., Kusuda J., Takaiwa F., Kato A., RA Tohdoh N., Shimada H., Sugiura M.; RT "The complete nucleotide sequence of the tobacco chloroplast genome: RT its gene organization and expression."; RL EMBO J. 5:2043-2049(1986). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=O.hookeri; STRAIN=cv. Johansen; RX MEDLINE=20309318; PubMed=10852478; RA Hupfer H., Swiatek M., Hornung S., Herrmann R.G., Maier R.M., RA Chiu W.-L., Sears B.; RT "Complete nucleotide sequence of the Oenothera elata plastid RT chromosome, representing plastome I of the five distinguishable RT Euoenothera plastomes."; RL Mol. Gen. Genet. 263:581-585(2000). RN [6] RP SEQUENCE FROM N.A. RC SPECIES=L.japonicus; STRAIN=Accession MG-20; RX MEDLINE=21082929; PubMed=11214967; RA Kato T., Kaneko T., Sato S., Nakamura Y., Tabata S.; RT "Complete structure of the chloroplast genome of a legume, Lotus RT japonicus."; RL DNA Res. 7:323-330(2000). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=S.oleracea; STRAIN=cv. Geant d'hiver, and cv. Monatol; RX MEDLINE=21187424; PubMed=11292076; RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., RA Herrmann R.G., Mache R.; RT "The plastid chromosome of spinach (Spinacia oleracea): complete RT nucleotide sequence and gene organization."; RL Plant Mol. Biol. 45:307-315(2001). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=S.oleracea; STRAIN=cv. Monatol; TISSUE=Seedling; RA Oelmueller R.; RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases. RN [9] RP SEQUENCE OF 1-20. RC SPECIES=S.oleracea; RA Schmidt C.L., Malkin R.; RT "Low molecular weight subunits associated with the cytochrome b6f RT complexes from spinach and Chlamydomonas reinhardtii."; RL Photosyn. Res. 38:73-81(1993). RN [10] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; STRAIN=cv. Chinese Spring; RA Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T., RA Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., RA Gojobori T., Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., RA Tsunewaki K.; RT "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: RT complete sequence and contig clones."; RL Plant Mol. Biol. Rep. 18:243-253(2000). RN [11] RP SEQUENCE FROM N.A. RC SPECIES=P.deltoides; RX MEDLINE=98011435; PubMed=9350351; RA Naithani S., Trivedi P.K., Sane P.V.; RT "Characterization of the orf31-petG gene cluster from the plastid RT genome of Populus deltoides."; RL Biochem. Mol. Biol. Int. 43:433-442(1997). RN [12] RP SEQUENCE FROM N.A. RC SPECIES=B.vulgaris; STRAIN=cv. Altissima; TISSUE=Leaf; RA Ran Z., Michaelis G.; RT "Mapping of a chloroplast RFLP marker associated with the CMS RT cytoplasm of sugar beet (Beta vulgaris)."; RL Theor. Appl. Genet. 91:836-840(1995). RN [13] RP SEQUENCE FROM N.A. RC SPECIES=B.vulgaris; STRAIN=cv. TK81-O; TISSUE=Leaf; RX MEDLINE=95254673; PubMed=7736615; RA Kubo T., Yanai Y., Kinoshita T., Mikami T.; RT "The chloroplast trnP-trnW-petG gene cluster in the mitochondrial RT genomes of Beta vulgaris, B. trigyna and B. webbiana: evolutionary RT aspects."; RL Curr. Genet. 27:285-289(1995). CC -!- FUNCTION: The cytochrome b6-f complex functions in the linear CC cross-membrane transport of electrons between photosystem II and CC I, as well as in cyclic electron flow around photosystem I. PetG CC is required for either the stability or assembly of the cytochrome CC b6-f complex. CC -!- SUBCELLULAR LOCATION: Thylakoid membrane-associated. CC -!- SIMILARITY: Belongs to the petG family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15901; CAA33967.1; -. DR EMBL; J04502; AAA84480.1; -. DR EMBL; X86563; CAA60304.1; -. DR EMBL; Z00044; CAA77420.1; -. DR EMBL; X87636; CAA60964.1; -. DR EMBL; X87637; CAA60969.1; -. DR EMBL; AJ271079; CAB67176.1; -. DR EMBL; AP002983; BAB33215.1; -. DR EMBL; AJ400848; CAB88747.1; -. DR EMBL; X74430; CAA52449.1; -. DR EMBL; AB042240; BAB47052.1; -. DR EMBL; Y15429; CAA75627.1; -. DR EMBL; D38019; BAA07216.1; -. DR EMBL; D38020; BAA07222.1; -. DR EMBL; D38021; BAA07223.1; -. DR PIR; A32159; A32159. DR PIR; JQ0245; WMRZ4. DR PIR; S68166; S68166. DR PIR; T09122; T09122. DR Gramene; P12121; -. DR MaizeDB; 56865; -. DR HAMAP; MF_00432; -; 1. DR InterPro; IPR003683; Cytochrmb6/f_5. DR Pfam; PF02529; PetG; 1. KW Electron transport; Chloroplast; Respiratory chain; Thylakoid; KW Transmembrane. FT DOMAIN 1 4 Lumenal (Potential). FT TRANSMEM 5 25 Potential. FT DOMAIN 26 37 Stromal (Potential). FT CONFLICT 15 15 P -> G (in Ref. 9). FT CONFLICT 20 20 G -> P (in Ref. 8). SQ SEQUENCE 37 AA; 4170 MW; A98EA4D30CB983C5 CRC64; MIEVFLFGIV LGLIPITLAG LFVTAYLQYR RGDQLDL // ID PETL_MAIZE STANDARD; PRT; 31 AA. AC P19445; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome b6-f complex subunit VI (Cytochrome b6f complex subunit DE petL). GN PETL. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9cms X FR37; RX MEDLINE=89160811; PubMed=2922397; RA Haley J., Bogorad L.; RT "A 4-kDa maize chloroplast polypeptide associated with the cytochrome RT b6-f complex: subunit 5, encoded by the chloroplast petE gene."; RL Proc. Natl. Acad. Sci. U.S.A. 86:1534-1538(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: The cytochrome b6-f complex functions in the linear CC cross-membrane transport of electrons between photosystem II and CC I, as well as in cyclic electron flow around photosystem I. PetL CC is important for photoautotrophic growth as well as for electron CC transfer efficiency and stability of the cytochrome b6-f complex. CC -!- SUBUNIT: The cytochrome b6-f complex is composed of 4 large CC subunits: cytochromes b6 and f, subunit IV (petD), the Rieske CC iron-sulfur protein, and several small subunits: petG, petL, petM CC and possibly petN (By similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane (By CC similarity). CC -!- SIMILARITY: Belongs to the petL family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04502; AAA84479.1; -. DR EMBL; X86563; CAA60303.1; -. DR PIR; S58569; S58569. DR Gramene; P19445; -. DR MaizeDB; 69195; -. DR HAMAP; MF_00433; -; 1. DR InterPro; IPR007802; PetL. DR Pfam; PF05115; PetL; 1. KW Respiratory chain; Electron transport; Thylakoid; Transmembrane; KW Chloroplast. FT TRANSMEM 4 26 Potential. SQ SEQUENCE 31 AA; 3456 MW; 0AE4294FA7E8B48E CRC64; MLTITSYFGF LLAALTITPA LFISLNKIRL I // ID PGLR_MAIZE STANDARD; PRT; 410 AA. AC P26216; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Exopolygalacturonase precursor (EC 3.2.1.67) (ExoPG) (Pectinase) DE (Galacturan 1,4-alpha-galacturonidase). GN PG1 AND PG2 AND PG3 AND PG6 AND PG14. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 23-37. RC STRAIN=cv. Missouri 17; TISSUE=Pollen; RX MEDLINE=92032781; PubMed=1932692; RA Niogret M.F., Dubald M., Mandaron P., Mache R.; RT "Characterization of pollen polygalacturonase encoded by several cDNA RT clones in maize."; RL Plant Mol. Biol. 17:1155-1164(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. Missouri 17; TISSUE=Leaf; RX MEDLINE=93164262; PubMed=8433375; RA Barakate A., Martin W., Quigley F., Mache R.; RT "Characterization of a multigene family encoding an RT exopolygalacturonase in maize."; RL J. Mol. Biol. 229:797-801(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73, and cv. W22; RX MEDLINE=93004490; PubMed=1391780; RA Allen R.L., Lonsdale D.M.; RT "Sequence analysis of three members of the maize polygalacturonase RT gene family expressed during pollen development."; RL Plant Mol. Biol. 20:343-345(1992). RN [4] RP SEQUENCE OF 1-306 FROM N.A. RX MEDLINE=94035141; PubMed=8106080; RA Allen R.L., Lonsdale D.M.; RT "Molecular characterization of one of the maize polygalacturonase RT gene family members which are expressed during late pollen RT development."; RL Plant J. 3:261-271(1993). CC -!- FUNCTION: May function in depolymerizing pectin during pollen CC development, germination, and tube growth. Acts as an exo- CC polygalacturonase. CC -!- CATALYTIC ACTIVITY: {(1,4)-alpha-D-galacturonide}(N) + H(2)O = CC {(1,4)-alpha-D-galacturonide}(N-1) + D-galacturonate. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Pollen. CC -!- DEVELOPMENTAL STAGE: Late stages of pollen development. CC -!- SIMILARITY: Belongs to family 28 of glycosyl hydrolases. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57627; CAA40850.1; -. DR EMBL; X57628; CAA40851.1; ALT_INIT. DR EMBL; X57743; CAA40910.1; -. DR EMBL; X57575; CAA40803.1; -. DR EMBL; X65844; CAA46679.1; -. DR EMBL; X65845; CAA46680.1; -. DR EMBL; X62384; CAA44248.1; -. DR EMBL; X62385; CAA44249.1; -. DR EMBL; X66692; CAA47234.1; -. DR PIR; S18570; S18570. DR PIR; S25824; S25824. DR PIR; S30064; S30064. DR MaizeDB; 25864; -. DR InterPro; IPR000743; Glyco_hydro_28. DR InterPro; IPR006626; PbH1. DR Pfam; PF00295; Glyco_hydro_28; 1. DR SMART; SM00710; PbH1; 5. DR PROSITE; PS00502; POLYGALACTURONASE; 1. KW Hydrolase; Glycosidase; Cell wall; Signal; Glycoprotein; KW Multigene family. FT SIGNAL 1 22 FT CHAIN 23 410 Exopolygalacturonase. FT ACT_SITE 256 256 Probable. FT CARBOHYD 89 89 N-linked (GlcNAc...) (Potential). FT CARBOHYD 246 246 N-linked (GlcNAc...) (Potential). FT CARBOHYD 349 349 N-linked (GlcNAc...) (Potential). FT CARBOHYD 387 387 N-linked (GlcNAc...) (Potential). FT VARIANT 359 359 A -> V (IN PGG14). SQ SEQUENCE 410 AA; 43443 MW; 0A6E779644D818BA CRC64; MACTNNAMRA LFLLVLFCIV HGEKEESKGI DAKASGPGGS FDITKLGASG NGKTDSTKAV QEAWASACGG TGKQTILIPK GDFLVGQLNF TGPCKGDVTI QVDGNLLATT DLSQYKDHGN WIEILRVDNL VITGKGNLDG QGPAVWSKNS CTKKYDCKIL PNSLVMDFVN NGEVSGVTLL NSKFFHMNMY RCKDMLIKDV TVTAPGDSPN TDGIHMGDSS GITITNTVIG VGDDCISIGP GTSKVNITGV TCGPGHGISI GSLGRYKDEK DVTDINVKDC TLKKTMFGVR IKAYEDAASV LTVSKIHYEN IKMEDSANPI FIDMKYCPNK LCTANGASKV TVKDVTFKNI TGTSSTPEAV SLLCTAKVPC TGVTMDDVNV EYSGTNNKTM AICTNAKGST KGCLKELACF // ID PGLS_MAIZE STANDARD; PRT; 410 AA. AC P35338; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Exopolygalacturonase precursor (EC 3.2.1.67) (ExoPG) (Pectinase) DE (Galacturan 1,4-alpha-galacturonidase). GN PG9. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Missouri 17; TISSUE=Leaf; RX MEDLINE=93164262; PubMed=8433375; RA Barakate A., Martin W., Quigley F., Mache R.; RT "Characterization of a multigene family encoding an RT exopolygalacturonase in maize."; RL J. Mol. Biol. 229:797-801(1993). CC -!- FUNCTION: May function in depolymerizing pectin during pollen CC development, germination, and tube growth. Acts as an exo- CC polygalacturonase. CC -!- CATALYTIC ACTIVITY: {(1,4)-alpha-D-galacturonide}(N) + H(2)O = CC {(1,4)-alpha-D-galacturonide}(N-1) + D-galacturonate. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Pollen. CC -!- DEVELOPMENTAL STAGE: Late stages of pollen development. CC -!- SIMILARITY: Belongs to family 28 of glycosyl hydrolases. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64408; CAA45751.1; -. DR PIR; S30066; S30066. DR MaizeDB; 25864; -. DR InterPro; IPR000743; Glyco_hydro_28. DR InterPro; IPR006626; PbH1. DR Pfam; PF00295; Glyco_hydro_28; 1. DR SMART; SM00710; PbH1; 5. DR PROSITE; PS00502; POLYGALACTURONASE; 1. KW Hydrolase; Glycosidase; Cell wall; Signal; Glycoprotein; KW Multigene family. FT SIGNAL 1 22 FT CHAIN 23 410 Exopolygalacturonase. FT ACT_SITE 256 256 Probable. FT CARBOHYD 89 89 N-linked (GlcNAc...) (Potential). FT CARBOHYD 246 246 N-linked (GlcNAc...) (Potential). FT CARBOHYD 349 349 N-linked (GlcNAc...) (Potential). FT CARBOHYD 387 387 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 410 AA; 43415 MW; 942153CB550DEABA CRC64; MACTDNAMRA LFLLVLFCIV HGEKEESKGI DAKASGPGGS FDITKLGASG NGKTDSTKAV QEAWASACGG TGKQTILIPK GDFLVGQLNF TGPCKGDVTI QVDGNLLATT DLSQYKEHGN WIEILRVDNL VITGKGNLDG QGPAVWSKNS CTKKYDCKIL PNSLVMDFVN NGEVSGVTLL NSKFFHMNMY QCKNMLIKDV TVTAPGDSPN TDGIHMGDSS GITITNTVIG VGDDCISIGP GTSKVNITGV TCGPGHGISI GSLGRYKDEK DVTDINVKDC TLKKTMFGVR IKAYEDAASV LTVSKIHYEN IKMEDSANPI FIDMKYCPNK LCTANGASKV TVKDVTFKNI TGTSSTPEAI SLLCTAKVPC TGATMDDVNV EYSGTNNKTM AICTNAKGST KGCLKELACF // ID PGLT_MAIZE STANDARD; PRT; 410 AA. AC P35339; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Exopolygalacturonase precursor (EC 3.2.1.67) (ExoPG) (Pectinase) DE (Galacturan 1,4-alpha-galacturonidase). GN PG2C. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Missouri 17; TISSUE=Leaf; RX MEDLINE=93164262; PubMed=8433375; RA Barakate A., Martin W., Quigley F., Mache R.; RT "Characterization of a multigene family encoding an RT exopolygalacturonase in maize."; RL J. Mol. Biol. 229:797-801(1993). CC -!- FUNCTION: May function in depolymerizing pectin during pollen CC development, germination, and tube growth. Acts as an exo- CC polygalacturonase. CC -!- CATALYTIC ACTIVITY: {(1,4)-alpha-D-galacturonide}(N) + H(2)O = CC {(1,4)-alpha-D-galacturonide}(N-1) + D-galacturonate. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Pollen. CC -!- DEVELOPMENTAL STAGE: Late stages of pollen development. CC -!- SIMILARITY: Belongs to family 28 of glycosyl hydrolases. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X66422; CAA47052.1; -. DR PIR; S30067; S30067. DR MaizeDB; 65847; -. DR InterPro; IPR000743; Glyco_hydro_28. DR InterPro; IPR006626; PbH1. DR Pfam; PF00295; Glyco_hydro_28; 1. DR SMART; SM00710; PbH1; 5. DR PROSITE; PS00502; POLYGALACTURONASE; 1. KW Hydrolase; Glycosidase; Cell wall; Signal; Glycoprotein; KW Multigene family. FT SIGNAL 1 22 FT CHAIN 23 410 Exopolygalacturonase. FT ACT_SITE 256 256 Probable. FT CARBOHYD 89 89 N-linked (GlcNAc...) (Potential). FT CARBOHYD 246 246 N-linked (GlcNAc...) (Potential). FT CARBOHYD 349 349 N-linked (GlcNAc...) (Potential). FT CARBOHYD 387 387 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 410 AA; 43296 MW; 5BD1310F588AE7CA CRC64; MACIDNAMRA LFLLALFCVV HGEKAKSKDN DAKASGPGGS FDITKLGASG NGKTDSTKAV QEAWASACGG TGKQTILIPK GDFLVGPLNF TGPCKGDVTI QVNGNLLATT DLSQYKDHGN WIEILRVDNL VITGKGKLDG QGPAVWSKNS CVKKYDCKIL PNSLVMDFVN NGEVSGITLL NSKFFHMNMY KCKDMLIKDV NVTAPGDSPN TDGIHMGDSS GVTITNTVIG VGDDCISIGP GTSKVNITGV TCGPGHGISI GSLGRYKDEK DVTDINVKDC TLKKTANGVR IKAYEDAASV LTASKIHYEN IKMEDSGYPI IIDMKYCPNK LCTANGASKV TVKDVTFKNI TGTSSTPEAV NLLCTAKIPC TGVTMDDVNI KYSGTNNKTM AVCKNAKGSA KGCLKELACF // ID PHYA_MAIZE STANDARD; PRT; 1131 AA. AC P19862; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Phytochrome A. GN PHYA1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90185212; PubMed=2628175; RA Christensen A.H., Quail P.H.; RT "Structure and expression of a maize phytochrome-encoding gene."; RL Gene 85:381-390(1989). CC -!- FUNCTION: Regulatory photoreceptor which exists in two forms that CC are reversibly interconvertible by light: the Pr form that absorbs CC maximally in the red region of the spectrum and the Pfr form that CC absorbs maximally in the far-red region. Photoconversion of Pr in CC Pfr induces an array of morphogenic responses, whereas CC reconversion of Pfr to Pr cancels the induction of those CC responses. Pfr controls the expression of a number of nuclear CC genes including those encoding the small subunit of ribulose- CC bisphosphate carboxylase, chlorophyll A/B binding protein, CC protochlorophyllide reductase, rRNA, etc. It also controls the CC expression of its own gene(s) in a negative feedback fashion. CC -!- SUBUNIT: Homodimer. CC -!- PTM: Contains one covalently linked tetrapyrrole chromophore. CC -!- SIMILARITY: Belongs to the phytochrome family. CC -!- SIMILARITY: Contains 1 histidine kinase domain. CC -!- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) dimerization domains. DR PIR; JQ0382; JQ0382. DR MaizeDB; 65582; -. DR InterPro; IPR003594; ATPbind_ATPase. DR InterPro; IPR003018; GAF. DR InterPro; IPR003661; His_kinA_N. DR InterPro; IPR005467; His_kinase. DR InterPro; IPR000014; PAS_domain. DR InterPro; IPR001294; Phytochrome. DR Pfam; PF01590; GAF; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF00989; PAS; 2. DR Pfam; PF00360; phytochrome; 1. DR PRINTS; PR01033; PHYTOCHROME. DR SMART; SM00065; GAF; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SMART; SM00091; PAS; 2. DR TIGRFAMs; TIGR00229; sensory_box; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50112; PAS; 2. DR PROSITE; PS00245; PHYTOCHROME_1; 1. DR PROSITE; PS50046; PHYTOCHROME_2; 1. KW Transcription regulation; Photoreceptor; Phytochrome; Chromophore; KW Repeat; Multigene family. FT DOMAIN 620 690 PAS 1. FT DOMAIN 750 834 PAS 2. FT DOMAIN 904 1124 Histidine kinase. FT BINDING 324 324 Chromophore. SQ SEQUENCE 1131 AA; 125149 MW; 6EEB2EF5FC6701C4 CRC64; MSSSRPAHSS SSSSRTRQSS RARILAQTTL DAELNAEYEE SGDSFDYSKL VEAQRSTPPE QQGRSGKVIA YLQHIQRGKL IQPFGCLLAL DEKSFRVIAF SENAPEMLTT VSHAVPNVDD PPKLGIGTNV RSLFTDPGAT ALQKALGFAD VSLLNPILVQ CKTSGKPFYA IVHRATGCLV VDFEPVKPTE FPATAAGALQ SYKLAAKAIS KIQSLPGGSM EALCNTVVKE VFDLTGYDRV MAYKFHEDEH GEVFAEITKP GIEPYIGLHY PATDIPQAAR FLFMKNKVRM ICDCRARSVK IIEDEALSID ISLCGSTLRA PHSCHLKYME NMNSIASLVM AVVVNENEED DEPEPEQPPQ QQKKKRLWGL IVCHHESPRY VPFPLRYACE FLAQVFAVHV NKEFELEKQI REKNILRMQT MLSDMLFKES SPLSIVSGSP NIMDLVKCDG AALLYGDKVW RLQTAPTESQ IRDIAFWLSE VHGDSTGLST DSLQDAGYPG AASLGDMICG MAVAKITSKD ILFWFRSHTA AEIKWGGAKH DPSDKDDNRR MHPRLSFKAF LEVVKTKSLP WSDYEMDAIH SLQLILRGTL NDASKPAQAS GLDNQIGDLK LDGLAELQAV TSEMVRLMET ATVPILAVDG NGLVNGWNQK VAELSGLRVD EAIGRHILTL VEDSSVSLVQ RMLYLALQGR EEKEVRFELK THGSKRDDGP VILVVNACAS RDLHDHVVGV CFVAQDMTVH KLVMDKFTRV EGDYKAIIHN PNPLIPPIFG ADQFGWCSEW NAAMTKLTGW HRDEVVDKML LGEVFNSSNA SCLLKSKDAF VRLCIVINSA LAGEEAEKAS FGFFDRNEKY VECLLSVNRK VNADGVVTGV FCFIHVPSDD LQHALHVQQA SEQTAQRKLK AFSYMRHAIN KPLSGMLYSR ETLKSTGLNE EQMRQVRVGD NCHRQLNKIL ADLDQDNITD KSSCLDLDMA EFVLQDVVVS AVSQVLIGCQ AKGIRVACNL PERSMKQKVY GDGIRLQQIV SDFLFVSVKF SPAGGSVDIS SKLTKNSIGE NLHLIDFELR IKHRGAGVPA EILSQMYEED NKEQSEEGFS LAVSRNLLRL MNGDIRHLRE AGMSTFILTA ELAAAPSAVG R // ID PMGI_MAIZE STANDARD; PRT; 559 AA. AC P30792; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE 2,3-bisphosphoglycerate-independent phosphoglycerate mutase DE (EC 5.4.2.1) (Phosphoglyceromutase) (BPG-independent PGAM) (PGAM-I). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE=92316968; PubMed=1535626; RA Grana X., de Lecea L., El-Maghrabi M.R., Urena J.M., Caellas C., RA Carreras J., Puigdomenech P., Pilkis S.J., Climent F.; RT "Cloning and sequencing of a cDNA encoding 2,3-bisphosphoglycerate- RT independent phosphoglycerate mutase from maize. Possible relationship RT to the alkaline phosphatase family."; RL J. Biol. Chem. 267:12797-12803(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=94380030; PubMed=8093040; RA Perez de la Ossa P., Grana X., Ruiz-Lozano P., Climent F.; RT "Isolation and characterization of cofactor-independent RT phosphoglycerate mutase gene from maize."; RL Biochem. Biophys. Res. Commun. 203:1204-1209(1994). RN [3] RP SEQUENCE OF 223-236. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and CC 3-phosphoglycerate (By similarity). CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate. CC -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity). CC -!- PATHWAY: Glycolysis. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- TISSUE SPECIFICITY: Found ubiquitously in germinating seed. CC -!- DEVELOPMENTAL STAGE: Expression most important during germination, CC it decreases during development. CC -!- PTM: The N-terminus is blocked. CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M80912; AAA33499.1; -. DR EMBL; Z33611; CAA83914.1; -. DR EMBL; Z33612; CAA83914.1; JOINED. DR PIR; A42807; A42807. DR Maize-2DPAGE; P30792; COLEOPTILE. DR MaizeDB; 30148; -. DR InterPro; IPR006124; Metalloenzyme. DR InterPro; IPR005995; Pgm_bpd_ind. DR Pfam; PF01676; Metalloenzyme; 1. DR ProDom; PD004429; Pgm_bpd_ind; 1. DR TIGRFAMs; TIGR01307; pgm_bpd_ind; 1. KW Isomerase; Glycolysis; Metal-binding; Manganese. FT ACT_SITE 81 81 Phosphoserine intermediate (By FT similarity). FT METAL 28 28 Manganese 2 (By similarity). FT METAL 81 81 Manganese 2 (By similarity). FT METAL 430 430 Manganese 1 (By similarity). FT METAL 434 434 Manganese 1 (By similarity). FT METAL 471 471 Manganese 2 (By similarity). FT METAL 472 472 Manganese 2 (By similarity). FT METAL 501 501 Manganese 1 (By similarity). FT CONFLICT 21 21 S -> P (in Ref. 2). FT CONFLICT 60 60 W -> R (in Ref. 1; AA sequence). FT CONFLICT 303 303 D -> N (in Ref. 1; AA sequence). FT CONFLICT 493 494 DR -> GG (in Ref. 1; AA sequence). SQ SEQUENCE 559 AA; 60619 MW; 52D1FA3388A7A21A CRC64; MGSSGFSWTL PDHPKLPKGK SVAVVVLDGW GEANPDQYNC IHVAQTPVMD SLKNGAPEKW RLVKAHGTAV GLPSDDDMGN SEVGHNALGA GRIFAQGAKL VDQALASGKI YDGDGFNYIK ESFESGTLHL IGLLSDGGVH SRLDQLQLLL KGVSERGAKK IRVHILTDGR DVLDGSSIGF VETLENDLLE LRAKGVDAQI ASGGGRMYVT MDRYENDWDV VKRGWDAQVL GEAPYKFKSA LEAVKTLRAQ PKANDQYLPP FVIVDDSGNA VGPVLDGDAV VTINFRADRM VMLAKALEYA DFDNFDRVRV PKIRYAGMLQ YDGELKLPSR YLVSPPEIDR TSGEYLVKNG IRTFACSETV KFGHVTFFWN GNRSGYFDAT KEEYVEVPSD SGITFNVAPN MKALEIAEKA RDALLSGKFD QVRVNLPNGD MVGHTGDIEA TVVACKAADE AVKIILDAVE QVGGIYLVTA DHGNAEDMVK RNKSGKPLLD KNDRIQILTS HTLQPVPVAI GGPGLHPGVK FRNDIQTPGL ANVAATVMNL HGFEAPADYE QTLIEVADN // ID PODK_MAIZE STANDARD; PRT; 947 AA. AC P11155; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Pyruvate,phosphate dikinase, chloroplast precursor (EC 2.7.9.1) DE (Pyruvate,orthophosphate dikinase). GN PPDK. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 71-89. RX MEDLINE=88298745; PubMed=2841317; RA Matsuoka M., Ozeki Y., Yamamoto N., Hirano H., Kano-Murakami Y., RA Tanaka Y.; RT "Primary structure of maize pyruvate, orthophosphate dikinase as RT deduced from cDNA sequence."; RL J. Biol. Chem. 263:11080-11083(1988). RN [2] RP SEQUENCE OF 521-535. RX MEDLINE=88198234; PubMed=2834385; RA Roeske C.A., Kutny R.M., Budde R.J.A., Chollet R.; RT "Sequence of the phosphothreonyl regulatory site peptide from RT inactive maize leaf pyruvate, orthophosphate dikinase."; RL J. Biol. Chem. 263:6683-6687(1988). CC -!- FUNCTION: Formation of phosphoenolpyruvate, which is the primary CC acceptor of CO(2) in C4 and some Crassulacean acid metabolism CC plants. CC -!- CATALYTIC ACTIVITY: ATP + pyruvate + phosphate = AMP + CC phosphoenolpyruvate + diphosphate. CC -!- ENZYME REGULATION: Controlled by light through a phosphorylation/ CC dephosphorylation mechanism. CC -!- PATHWAY: C4 photosynthetic pathway. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- TISSUE SPECIFICITY: Mainly localized in mesophyll cells and only a CC low level is found in bundle sheath cells. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03901; AAA33495.1; -. DR HSSP; P22983; 1DIK. DR MaizeDB; 25385; -. DR InterPro; IPR008279; PEP_mobile. DR InterPro; IPR000121; PEP_utilizers. DR InterPro; IPR002192; PPDK_N_term. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF02896; PEP-utilizers_C; 1. DR Pfam; PF01326; PPDK_N_term; 1. DR ProDom; PD000940; PEP_utilizers; 1. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. KW Transferase; Kinase; ATP-binding; Phosphorylation; Photosynthesis; KW Chloroplast; Transit peptide. FT TRANSIT 1 71 Chloroplast. FT CHAIN 72 947 Pyruvate,phosphate dikinase. FT ACT_SITE 529 529 Tele-phosphohistidine intermediate (By FT similarity). FT MOD_RES 527 527 PHOSPHORYLATION (LIGHT-DEPENDENT). FT MOD_RES 529 529 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 947 AA; 103072 MW; 11EF9F1B1365785A CRC64; MAASVSRAIC VQKPGSKCTR DREATSFARR SVAAPRPPHA KARRRHPLRL RRGTGPHCSP LRAVVDAAPI QTTKKRVFHF GKGKSEGNKT MKELLGGKGA NLAEMASIGL SVPPGFTVST EACQQYQDAG CALPAGLWAE IVDGLQWVEE YMGATLGDPQ RPLLLSVRSG AAVSMPGMMD TVLNLGLNDE VAAGLAAKSG ERFAYDSFRR FLDMFGNVVM DIPRSLFEEK LEHMKESKGL KNDTDLTASD LKELVGQYKE VYLSAKGEPF PSDPKKQLEL AVLAVFNSWE SPRAKKYRSI NQITGLRGTA VNVQCMVFGN MGNTSGTGVL FTRNPNTGEK KLYGEFLVNA QGEDVVAGIR TPEDLDAMKN LMPQAYDELV ENCNILESHY KEMQDIEFTV QENRLWMLQC RTGKRTGKSA VKIAVDMVNE GLVEPRSAIK MVEPGHLDQL LHPQFENPSA YKDQVIATGL PASPGAAVGQ VVFTAEDAEA WHSQGKAAIL VRAETSPEDV GGMHAAVGIL TERGGMTSHA AVVARWWGKC CVSGCSGIRV NDAEKLVTIG SHVLREGEWL SLNGSTGEVI LGKQPLSPPA LSGDLGTFMA WVDDVRKLKV LANADTPDDA LTARNNGAQG IGLCRTEHMF FASDERIKAV RQMIMAPTLE LRQQALDRLL TYQRSDFEGI FRAMDGLPVT IRLLDHPSYE FLPEGNIEDI VSELCAETGA NQEDALARIE KLSEVNPMLG FRGCRLGISY PELTEMQARA IFEAAIAMTN QGVQVFPEIM VPLVGTPQEL GHQVTLIRQV AEKVFANVGK TIGYKVGTMI EIPRAALVAD EIAEQAEFFS FGTNDLTQMT FGYSRDDVGK FIPVHLAQGI LQHDPFEVLD QRGVGELVKF ATERGRKARP NLKVGICGEH GGEPSSVAFF AKAGLDFVSC SPFRVPIARL AAAQVLV // ID POLB_MAIZE STANDARD; PRT; 740 AA. AC P15718; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Retrovirus-related Pol polyprotein from transposon element BS1 (ORF 1) DE [Contains: Protease (EC 3.4.23.-); Reverse transcriptase DE (EC 2.7.7.49); Endonuclease]. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seedling; RA Johns M.A., Babcock M.S., Fuerstenberg S.M., Fuerstenberg S.I., RA Freeling M., Simpson R.B.; RT "An unusually compact retrotransposon in maize."; RL Plant Mol. Biol. 12:633-642(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=89345638; PubMed=2474829; RA Jin Y.K., Bennetzen J.L.; RT "Structure and coding properties of Bs1, a maize retrovirus-like RT transposon."; RL Proc. Natl. Acad. Sci. U.S.A. 86:6235-6239(1989). CC -!- FUNCTION: BS1 is probably an active plant retrotransposon. CC -!- CATALYTIC ACTIVITY: N deoxynucleoside triphosphate = N diphosphate CC + {DNA}(N). CC -!- SIMILARITY: Contains 1 RNase H domain. CC -!- SIMILARITY: The protease belongs to peptidase family U24. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16080; CAA34210.1; -. DR EMBL; M25397; AAA66269.1; -. DR PIR; T03975; T03975. DR MEROPS; A12.001; -. DR MaizeDB; 69184; -. DR InterPro; IPR008250; E1-E2_ATPase_reg. DR InterPro; IPR008979; Gal_bind_like. DR InterPro; IPR002885; PPR. DR InterPro; IPR008941; TPR-like. DR Pfam; PF00122; E1-E2_ATPase; 2. DR Pfam; PF01535; PPR; 3. DR TIGRFAMs; TIGR00756; PPR; 1. KW Hydrolase; Aspartyl protease; RNA-directed DNA polymerase; KW Transferase; Endonuclease; Polyprotein; Transposable element. FT ACT_SITE 129 129 Protease (By similarity). FT DOMAIN 77 113 RNase H (By similarity). FT DOMAIN 157 404 Reverse transcriptase (By similarity). SQ SEQUENCE 740 AA; 81168 MW; F5565FA4CD13CDEB CRC64; MEPTLQSAME EQLKILREIS DRLAAQEARW RSRESTVTQH SRSIHDLEVA MASAPSATLR AELDAPVAVT YERLDATEAA SAARVSALES TTATFDMLFD NSDIVEKFNA EVVADDWGGL FGQHAHPLDS GGARLLLPSA ALPFASATDT AFSSIYGVEC GTIHTYTAAL TRPAALHKPL VVAHAKCSTP GHNRVCAETQ RQGPRQARRQ CRLRVHVRRL HFTGLQLHVR QHGRRRQHVV HVQRVLPGAE LDGRGLRLPW PRVAHGDRPF RAHLQLHHID PDGGGGGGHG ITPPERWLSR AGAYNAAAPN EVDVLRWTLK GVLWPRVTYC IAGWIDLGDG VAEGADHAVR VRFRVDDGCV VEGGTVCAES GSWTEIKGVF RLKRNARVME VYVQGAVAGI DVKVTDPQVF ATNVIQNLAY VDFFTKHFDW AVFEKEFRWY HVEDAAKVFD KMLTKGEEAP SVQRGVVMTA VAHNLLVQAL FMDGRASDAY VVLEEMQNNG PFPDVFTYTL KVLKNGQWAE EESTILVPGD IIGVKLGDII SADTRLLEGD PLKIDQSALT GNFCICSIVA GMLVEFIVMY PIQDMVYRPR IDKLLVLLIG GIPIAMPTVL SVTMSIGAYR LAQQGAITKR MTTIEEMAGM DVPCSDKTGT LPWTKLTVIK SLVDVFQRGA DQDAVILMDA RASCTKNQDA IEATIVSMLA APKEACAGVQ EIQFLPFNPN DKRTAVTYMS LIYALSPGKA // ID PORI_MAIZE STANDARD; PRT; 277 AA. AC P42057; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Outer plastidial membrane protein porin (Voltage-dependent anion- DE selective channel protein) (VDAC). GN POR1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Merit; TISSUE=Root; RX MEDLINE=95014384; PubMed=7523392; RA Fischer K., Weber A., Brink S., Arbinger B., Schuenemann D., RA Borchert S., Heldt H.W., Popp B., Benz R., Link T., Eckerskorn C., RA Fluegge U.I.; RT "Porins from plants. Molecular cloning and functional RT characterization of two new members of the porin family."; RL J. Biol. Chem. 269:25754-25760(1994). CC -!- FUNCTION: Forms a channel through the cell membrane that allows CC diffusion of small hydrophilic molecules. The channel adopts an CC open conformation at low or zero membrane potential and a closed CC conformation at potentials above 30-40 mV. The open state has a CC weak anion selectivity whereas the closed state is cation- CC selective (By similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast; non-green plastidial outer CC membrane. CC -!- DOMAIN: Consists mainly of membrane-spanning sided beta-sheets. CC -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X73429; CAA51828.1; -. DR PIR; S34146; S34146. DR MaizeDB; 106348; -. DR InterPro; IPR001925; Porin_Euk. DR Pfam; PF01459; Euk_porin; 1. DR PROSITE; PS00558; EUKARYOTIC_PORIN; 1. KW Outer membrane; Porin; Chloroplast. SQ SEQUENCE 277 AA; 29977 MW; 2BE787804FEB5797 CRC64; MVVAVGLYTD IGKKTRDLLY KDYNTHQKFC LTTSSPNGVA ITAAGTRKNE SIFGELHTQI KNKKLTVDVK ANSESDLLTT ITVDEFGTPG LKSIINLVVP DQRSGKLEFQ YLHEYAGVNA SVGLNSNPMV NLSGAFGSKA LSVGVDVSFD TATSDFTKYN AALSLTSPDL IASLHLNNHG DTLVASYYHL VKNHSGTAVG AELSHSMSRN ESTLIFGSQH SLDPHTTIKT RFNNYGMASA LVQHEWRPKS FVTISGDVDT KAIEKSTKVG LSLVLKH // ID PP1_MAIZE STANDARD; PRT; 316 AA. AC P22198; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serine/threonine protein phosphatase PP1 (EC 3.1.3.16). GN PP1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Smith R.D., Walker J.C.; RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein + CC phosphate. CC -!- COFACTOR: Binds 1 iron ion and 1 manganese ion per subunit (By CC similarity). CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M60215; AAA33545.1; -. DR PIR; S29317; S29317. DR HSSP; P08129; 1FJM. DR MaizeDB; 30136; -. DR InterPro; IPR004843; M-ppestrase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR ProDom; PD000252; T_phtase_apaH; 1. DR SMART; SM00156; PP2Ac; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. KW Hydrolase; Metal-binding; Iron; Manganese; Multigene family. FT METAL 61 61 Iron (By similarity). FT METAL 63 63 Iron (By similarity). FT METAL 89 89 Iron and manganese (By similarity). FT METAL 121 121 Manganese (By similarity). FT ACT_SITE 122 122 General acid (By similarity). FT METAL 170 170 Manganese (By similarity). FT METAL 245 245 Manganese (By similarity). SQ SEQUENCE 316 AA; 35763 MW; ED71EB1ABF308680 CRC64; MDPALLDDVI RRLLEVKNLK PGKNAQLSES EIKQLCAAAK EIFLQQPNLL ELEAPIKICG DVHGQYSDLL RLFDYGGYPP QANYLFLGDY VDRGKQSLET ICLLLAYKVK YPENFFLLRG NHECASVNRI YGFYDECKRR FSVKLWKTFT DCFNCLPVSA LIDEKILCMH GGLSPELNKL EQILNLNRPT DVPDTGLLCD LLWSDPSNEA TGWAINDRGV SFTFGPDKVS EFLEKHDLDL ICRAHQVVED GYEFFASRQL VTIFSAPNYC GEFDNAGAMM SVDDTLMCSF QILKPARKMM GGSTNNKSGF KSFRGW // ID PRMS_MAIZE STANDARD; PRT; 167 AA. AC Q00008; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Pathogenesis-related protein PRMS precursor. GN PRMS. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; TISSUE=Seed; RX MEDLINE=91329688; PubMed=1714315; RA Casacuberta J.M., Puigdomenech P., San Segundo B.; RT "A gene coding for a basic pathogenesis-related (PR-like) protein RT from Zea mays. Molecular cloning and induction by a fungus (Fusarium RT moniliforme) in germinating maize seeds."; RL Plant Mol. Biol. 16:527-536(1991). CC -!- FUNCTION: Probably involved in the defense reaction of plants CC against pathogens. CC -!- INDUCTION: By fungal infection in germinating seeds. CC -!- SIMILARITY: Belongs to the CRISP family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X54325; CAA38223.1; -. DR PIR; S14969; S14969. DR HSSP; P04284; 1CFE. DR MaizeDB; 66057; -. DR InterPro; IPR001283; Allrgn_V5/Tpx1. DR Pfam; PF00188; SCP; 1. DR PRINTS; PR00837; V5TPXLIKE. DR ProDom; PD000542; Allrgn_V5/Tpx1; 1. DR SMART; SM00198; SCP; 1. DR PROSITE; PS01009; SCP_AG5_PR1_SC7_1; 1. DR PROSITE; PS01010; SCP_AG5_PR1_SC7_2; 1. KW Plant defense; Pathogenesis-related protein; Signal. FT SIGNAL 1 27 Potential. FT CHAIN 28 167 Pathogenesis-related protein PRMS. FT DISULFID 71 143 By similarity. FT DISULFID 116 122 By similarity. FT DISULFID 138 153 By similarity. SQ SEQUENCE 167 AA; 18390 MW; C8437A140C3C5F0E CRC64; MEASNKLAVL LLWLVMAAAT AVHPSYSENS PQDYLTPQNS ARAAVGVGPV TWSTKLQQFA EKYAAQRAGD CRLQHSGGPY GENIFWGSAG FDWKAVDAVR SWVDEKQWYN YATNSCAAGK VCGHYTQVVW RATTSIGCAR VVCRDNRGVF IICNYEPRGN IAGMKPY // ID PRO1_MAIZE STANDARD; PRT; 131 AA. AC P35081; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Profilin 1 (ZmPRO1). GN PRO1 OR PRF1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; TISSUE=Pollen; RX MEDLINE=94073220; PubMed=8252067; RA Staiger C.J., Goodbody K.C., Hussey P.J., Valenta R., Droebak B.K., RA Lloyd C.W.; RT "The profilin multigene family of maize: differential expression of RT three isoforms."; RL Plant J. 4:631-641(1993). RN [2] RP CHARACTERIZATION. RC STRAIN=cv. B73; RX MEDLINE=20225529; PubMed=10760246; RA Kovar D.R., Droebak B.K., Staiger C.J.; RT "Maize profilin isoforms are functionally distinct."; RL Plant Cell 12:583-598(2000). CC -!- FUNCTION: Binds to actin and affects the structure of the CC cytoskeleton. At high concentrations, profilin prevents the CC polymerization of actin, whereas it enhances it at low CC concentrations. By binding to PIP2, it inhibits the formation of CC IP3 and DG. CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric CC actin in a 1:1 ratio. CC -!- TISSUE SPECIFICITY: Pollen specific. CC -!- SIMILARITY: Belongs to the profilin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X73279; CAA51718.1; -. DR PIR; S35796; S35796. DR HSSP; P25816; 1CQA. DR MaizeDB; 51451; -. DR InterPro; IPR002097; Profilin. DR InterPro; IPR005455; Profilin_plant. DR Pfam; PF00235; profilin; 1. DR PRINTS; PR00392; PROFILIN. DR PRINTS; PR01640; PROFILINPLNT. DR SMART; SM00392; PROF; 1. DR PROSITE; PS00414; PROFILIN; 1. KW Actin-binding; Cytoskeleton; Multigene family. SQ SEQUENCE 131 AA; 14147 MW; 3AA320DD721BEBB8 CRC64; MSWQTYVDEH LMCEIEGHHL TSAAIVGHDG ATWAQSTAFP EFKPEEMAAI MKDFDEPGHL APTGLILGGT KYMVIQGEPG AVIRGKKGSG GITVKKTGQS LIIGIYDEPM TPGQCNLVVE RLGDYLLEQG M // ID PRO2_MAIZE STANDARD; PRT; 131 AA. AC P35082; DT 01-FEB-1994 (Rel. 28, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Profilin 2 (ZmPRO2). GN PRO2 OR PRF2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; TISSUE=Pollen; RX MEDLINE=94073220; PubMed=8252067; RA Staiger C.J., Goodbody K.C., Hussey P.J., Valenta R., Droebak B.K., RA Lloyd C.W.; RT "The profilin multigene family of maize: differential expression of RT three isoforms."; RL Plant J. 4:631-641(1993). CC -!- FUNCTION: Binds to actin and affects the structure of the CC cytoskeleton. At high concentrations, profilin prevents the CC polymerization of actin, whereas it enhances it at low CC concentrations. By binding to PIP2, it inhibits the formation of CC IP3 and DG. CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric CC actin in a 1:1 ratio. CC -!- TISSUE SPECIFICITY: Pollen specific. CC -!- SIMILARITY: Belongs to the profilin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X73280; CAA51719.1; ALT_INIT. DR PIR; S35797; S35797. DR HSSP; P25816; 1CQA. DR MaizeDB; 78603; -. DR InterPro; IPR002097; Profilin. DR InterPro; IPR005455; Profilin_plant. DR Pfam; PF00235; profilin; 1. DR PRINTS; PR00392; PROFILIN. DR PRINTS; PR01640; PROFILINPLNT. DR SMART; SM00392; PROF; 1. DR PROSITE; PS00414; PROFILIN; 1. KW Actin-binding; Cytoskeleton; Multigene family. SQ SEQUENCE 131 AA; 14122 MW; 0A5F8DDA38B3C666 CRC64; MSWQAYVDEH LMCEIEGHHL AAAAIVGHDG AAWAQSTAFP EFKTEDMANI MKDFDEPGHL APTGLFLGPT KYMVIQGEPG AVIRGKKGSG GITVKKTGQA LVVGIYDEPM TPGQCNMVVE RLGDYLLEQG M // ID PRO3_MAIZE STANDARD; PRT; 131 AA. AC P35083; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Profilin 3 (ZmPRO3). GN PRO3 OR PRF3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; TISSUE=Pollen; RX MEDLINE=94073220; PubMed=8252067; RA Staiger C.J., Goodbody K.C., Hussey P.J., Valenta R., Droebak B.K., RA Lloyd C.W.; RT "The profilin multigene family of maize: differential expression of RT three isoforms."; RL Plant J. 4:631-641(1993). CC -!- FUNCTION: Binds to actin and affects the structure of the CC cytoskeleton. At high concentrations, profilin prevents the CC polymerization of actin, whereas it enhances it at low CC concentrations. By binding to PIP2, it inhibits the formation of CC IP3 and DG. CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric CC actin in a 1:1 ratio. CC -!- TISSUE SPECIFICITY: Pollen specific. CC -!- SIMILARITY: Belongs to the profilin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X73281; CAA51720.1; -. DR PIR; S35798; S35798. DR HSSP; P25816; 1CQA. DR MaizeDB; 78604; -. DR InterPro; IPR002097; Profilin. DR InterPro; IPR005455; Profilin_plant. DR Pfam; PF00235; profilin; 1. DR PRINTS; PR00392; PROFILIN. DR PRINTS; PR01640; PROFILINPLNT. DR SMART; SM00392; PROF; 1. DR PROSITE; PS00414; PROFILIN; 1. KW Actin-binding; Cytoskeleton; Multigene family. SQ SEQUENCE 131 AA; 14237 MW; A746F90BFA9B8386 CRC64; MSWQTYVDEH LMCEIEGHHL SSAAIVGHDG AVWAQSTAFP QFKPEEMTNI IKDFDEPGFL APIGLFLGPT KYMVIQGEPG AVIRGKKGSG GITVKKTGQA LVIGIYDEPM TPGQCNMVVE RLGDYLVEQG L // ID PSAA_MAIZE STANDARD; PRT; 751 AA. AC P04966; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Photosystem I P700 chlorophyll A apoprotein A1 (PsaA) (PSI-A). GN PSAA OR PS1A1. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85104999; PubMed=3881431; RA Fish L.E., Kueck U., Bogorad L.; RT "Two partially homologous adjacent light-inducible maize chloroplast RT genes encoding polypeptides of the P700 chlorophyll a-protein complex RT of photosystem I."; RL J. Biol. Chem. 260:1413-1421(1985). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE OF 1-17 FROM N.A. RC STRAIN=cv. B73N Inbred; TISSUE=Seedling leaf; RX MEDLINE=91355944; PubMed=1884003; RA Kangasjaervi J., McCullough A., Gengenbach B.G.; RT "Nucleotide sequence and transcription of maize plastid genome Bam HI RT fragment 14 containing ORF170."; RL Plant Mol. Biol. 17:513-515(1991). CC -!- FUNCTION: PsaA and psaB bind P700, the primary electron donor of CC photosystem I (PSI), as well as the electron acceptors A0, A1 and CC FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting CC photonic excitation into a charge separation, which transfers an CC electron from the donor P700 chlorophyll pair to the CC spectroscopically characterized acceptors A0, A1, FX, FA and FB in CC turn. Oxidized P700 is reduced on the lumenal side of the CC thylakoid membrane by plastocyanin. CC -!- COFACTOR: P700 is a chlorophyll A/chlorophyll A' dimer, A0 is one CC or more chlorophyll A, A1 is one or both phylloquinones and FX is CC a shared 4Fe-4S iron-sulfur center (By similarity). CC -!- SUBUNIT: The psaA/B heterodimer binds the P700 chlorophyll special CC pair and subsequent electron acceptors. PSI consists of a core CC antenna complex that captures photons, and an electron transfer CC chain that converts photonic excitation into a charge separation. CC The eukaryotic PSI reaction center is composed of at least 11 CC subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast CC thylakoid membrane (By similarity). CC -!- SIMILARITY: Belongs to the psaA/psaB family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M11203; AAA84485.1; -. DR EMBL; X86563; CAA60286.2; -. DR EMBL; X58080; CAA41109.1; -. DR PIR; S58552; S58552. DR HSSP; P25896; 1JB0. DR Gramene; P04966; -. DR MaizeDB; 57301; -. DR HAMAP; MF_00458; -; 1. DR InterPro; IPR006243; PsaA. DR InterPro; IPR001280; PSI_PsaA/B. DR Pfam; PF00223; psaA_psaB; 1. DR PRINTS; PR00257; PHOTSYSPSAAB. DR TIGRFAMs; TIGR01335; psaA; 1. DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1. KW Transport; Electron transport; Photosynthesis; Thylakoid; KW Photosystem I; Chlorophyll; Metal-binding; Iron; Magnesium; KW Iron-sulfur; 4Fe-4S; Transmembrane; Chloroplast. FT TRANSMEM 71 94 I (Potential). FT TRANSMEM 157 180 II (Potential). FT TRANSMEM 196 220 III (Potential). FT TRANSMEM 292 310 IV (Potential). FT TRANSMEM 347 370 V (Potential). FT TRANSMEM 386 412 VI (Potential). FT TRANSMEM 434 456 VII (Potential). FT TRANSMEM 532 550 VIII (Potential). FT TRANSMEM 590 611 IX (Potential). FT TRANSMEM 665 687 X (Potential). FT TRANSMEM 725 745 XI (Potential). FT METAL 574 574 Iron-sulfur (4Fe-4S) (shared with dimeric FT partner) (By similarity). FT METAL 583 583 Iron-sulfur (4Fe-4S) (shared with dimeric FT partner) (By similarity). FT METAL 676 676 Magnesium (chlorophyll-A' A1 axial FT ligand; P700 special pair) (By FT similarity). FT METAL 684 684 Magnesium (chlorophyll-A A3 axial ligand) FT (By similarity). FT BINDING 692 692 Chlorophyll-A A3 (By similarity). FT BINDING 693 693 Phylloquinone A (By similarity). SQ SEQUENCE 751 AA; 83222 MW; E7EAEDFB9EE61EBC CRC64; MIIRSSEPEV KIAVDRDPIK TSFEEWARPG HFSRTIAKGN PDTTTWIWNL HADAHDFDSH TGDLEEISRK VFSAHFGQLS IIFLWLSGMY FHGARFSNYE AWLSDPTHIG PSAQVVWPIV GQEILNGDVG GGFRGIQITS GFFQIWRASG ITSELQLYCT AIGALIFASL MLFAGWFHYH KAAPKLAWFQ DVESMLNHHL AGLLGLGSLS WAGHQIHVSL PINQFLDAGV DPKEIPLPHE FILNRDLLAQ LYPSFAEGAT PFFTLNWSKY AEFLSFRGGL DPITGGLWLS DIAHHHLAIA ILFLIAGHMY RTNWGIGHGL KDILEAHKGP FTGQGHKGLY EILTTSWHAQ LSLNLAMLGS TTIVVAHHMY SMPPYPYLAT DYGTQLSLFT HHMWIGGFLI VGAAAHAAIF MVRDYDPTTR YNDLLDRVLR HRDAIISHLN WVCIFLGFHS FGLYIHNDTM SALGRPQDMF SDAAIQLQPI FAQWIQNIHA GAPGVTAPGA TTSTSLTWGG GELVAIGGKV ALLPIPLGTA DFLVHHIHAF TIHVTVLILL KGVLFARSSR LIPDKANLGF RFPCDGPGRG GTCQVSAWDH VFLGLFWMYN SISVVIFHFS WKMQSDVWGT ISDQGIVTHI TGGNFAQSSI TINGWLRDFL WAQASQVIQS YGSSLSAYGL FFLGAHFVWA FSLMFLFSGR GYWQELIESI VWAHNKLKVA PATQPRALSI IQGRAVGVTH YLLGGIATTW AFFLARIIAV G // ID PSAB_MAIZE STANDARD; PRT; 735 AA. AC P04967; DT 13-AUG-1987 (Rel. 05, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Photosystem I P700 chlorophyll A apoprotein A2 (PsaB) (PSI-B). GN PSAB OR PS1A2. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85104999; PubMed=3881431; RA Fish L.E., Kueck U., Bogorad L.; RT "Two partially homologous adjacent light-inducible maize chloroplast RT genes encoding polypeptides of the P700 chlorophyll a-protein complex RT of photosystem I."; RL J. Biol. Chem. 260:1413-1421(1985). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: PsaA and psaB bind P700, the primary electron donor of CC photosystem I (PSI), as well as the electron acceptors A0, A1 and CC FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting CC photonic excitation into a charge separation, which transfers an CC electron from the donor P700 chlorophyll pair to the CC spectroscopically characterized acceptors A0, A1, FX, FA and FB in CC turn. Oxidized P700 is reduced on the lumenal side of the CC thylakoid membrane by plastocyanin. CC -!- COFACTOR: P700 is a chlorophyll A/chlorophyll A' dimer, A0 is one CC or more chlorophyll A, A1 is one or both phylloquinones and FX is CC a shared 4Fe-4S iron-sulfur center (By similarity). CC -!- SUBUNIT: The psaA/B heterodimer binds the P700 chlorophyll special CC pair and subsequent electron acceptors. PSI consists of a core CC antenna complex that captures photons, and an electron transfer CC chain that converts photonic excitation into a charge separation. CC The eukaryotic PSI reaction center is composed of at least 11 CC subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast CC thylakoid membrane (By similarity). CC -!- SIMILARITY: Belongs to the psaA/psaB family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M11203; AAA84486.1; -. DR EMBL; X86563; CAA60285.1; -. DR PIR; S58551; S58551. DR HSSP; P25897; 1JB0. DR Gramene; P04967; -. DR MaizeDB; 57312; -. DR HAMAP; MF_00482; -; 1. DR InterPro; IPR006244; PsaB. DR InterPro; IPR001280; PSI_PsaA/B. DR Pfam; PF00223; psaA_psaB; 1. DR PRINTS; PR00257; PHOTSYSPSAAB. DR TIGRFAMs; TIGR01336; psaB; 1. DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1. KW Transport; Electron transport; Photosynthesis; Thylakoid; KW Photosystem I; Chlorophyll; Metal-binding; Iron; Magnesium; KW Iron-sulfur; 4Fe-4S; Transmembrane; Chloroplast. FT TRANSMEM 46 69 I (Potential). FT TRANSMEM 135 158 II (Potential). FT TRANSMEM 175 199 III (Potential). FT TRANSMEM 274 292 IV (Potential). FT TRANSMEM 331 354 V (Potential). FT TRANSMEM 370 396 VI (Potential). FT TRANSMEM 418 440 VII (Potential). FT TRANSMEM 518 536 VIII (Potential). FT TRANSMEM 576 597 IX (Potential). FT TRANSMEM 644 666 X (Potential). FT TRANSMEM 708 728 XI (Potential). FT METAL 560 560 Iron-sulfur (4Fe-4S) (shared with dimeric FT partner) (By similarity). FT METAL 569 569 Iron-sulfur (4Fe-4S) (shared with dimeric FT partner) (By similarity). FT METAL 655 655 Magnesium (chlorophyll-a B1 axial ligand; FT P700 special pair) (By similarity). FT METAL 663 663 Magnesium (chlorophyll-A B3 axial ligand) FT (By similarity). FT BINDING 671 671 Chlorophyll-A B3 (By similarity). FT BINDING 672 672 Phylloquinone B (By similarity). SQ SEQUENCE 735 AA; 82657 MW; 22D3CB5B1891D5CE CRC64; MELRFPRFSQ GLAQDPTTRR IWFGIATAHD FESHDDITEE RLYQNIFASH FGQLAIIFLW TSGNLFHVAW QGNFESWIQD PLHVRPIAHA IWDPHFGQPA VEAFTRGGAA GPVNIAYSGV YQWWYTIGLR TNEDLYTGAL FLLFLSTLSL IGGWLHLQPK WKPSLSWFKN AESRLNHHLS GLFGVSSLAW TGHLVHVAIP GSSRGEYVRW NNFLDVLPYP QGLGPLLTGQ WNLYAQNPDS SNHLFGTTQG AGTAILTLLG GFHPQTQSLW LTDIAHHHLA IAFIFLIAGH MYRTNFGIGH SIKDLLEAHT PPGGRLGRGH KGLYDTINNS IHFQLGLALA SLGVITSLVA QHMYSLPAYA FIAQDFTTQA ALYTHHQYIA GFIMTGAFAH GAIFFIRDYN PEQNEDNVLA RMLDHKEAII SHLSWASLFL GFHTLGPYVH NDVMLAFGTP EKQILIEPIF AQWIQSAHGK TTYGFDILLS STNGPTFNAG RNIWLPGWLN AVNENSNSLF LTIGPGDFLV HHAIALGLHT TTLILVKGAL DARGSKLMPD KKDFGYSFPC DGPGRGGTCD ISAWDAFYLA VFWMLNTIGW VTFYWHWKHI TLWQGNVSQF NESSTYLMGW LRDYLWLNSS QLINGYNPFG MNSLSVWAWM FLFGHLVWAT GFMFLISWRG YWQELIETLA WAHERTPLAN LIRWRDKPVA LSVVQARLVG LAHFSVGYIF TYAAFLIAST SGKFG // ID PSAC_MAIZE STANDARD; PRT; 80 AA. AC P11601; DT 01-OCT-1989 (Rel. 12, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Photosystem I iron-sulfur center (Photosystem I subunit VII) (9 kDa DE polypeptide) (PSI-C) (PsaC). GN PSAC OR FRXA. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Schantz R., Bogorad L.; RT "Maize chloroplast genes ndhD, ndhE and psaC. Sequences, transcripts RT and transcript pools."; RL Plant Mol. Biol. 11:239-247(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of CC photosystem I (PSI); essential for photochemical activity. FB is CC the terminal electron acceptor of PSI, donating electrons to CC ferredoxin. The C-terminus interacts with psaA/B/D and helps CC assemble the protein into the PSI complex. Required for binding of CC psaD and psaE to PSI. PSI is a plastocyanin-ferredoxin CC oxidoreductase, converting photonic excitation into a charge CC separation, which transfers an electron from the donor P700 CC chlorophyll pair to the spectroscopically characterized acceptors CC A0, A1, FX, FA and FB in turn. CC -!- COFACTOR: Binds two 4Fe-4S clusters. Cluster 2 is most probably CC the spectroscopically characterized electron acceptor FA and CC cluster 1 is most probably FB (By similarity). CC -!- SUBUNIT: The eukaryotic PSI reaction center is composed of at CC least 11 subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast; tightly associated with stromal CC side of the thylakoid membrane (By similarity). CC -!- SIMILARITY: Contains 2 bacterial-type 4Fe-4S ferredoxin domains. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13159; CAA31557.1; -. DR EMBL; X86563; CAB75860.1; -. DR PIR; JU0008; FEZM1C. DR Gramene; P11601; -. DR MaizeDB; 57318; -. DR HAMAP; MF_01303; -; 1. DR InterPro; IPR001450; 4Fe4S_ferredoxin. DR Pfam; PF00037; fer4; 2. DR PROSITE; PS00198; 4FE4S_FERREDOXIN; 2. KW Transport; Electron transport; Photosynthesis; Thylakoid; KW Photosystem I; Metal-binding; Iron; Iron-sulfur; 4Fe-4S; Repeat; KW Chloroplast. FT INIT_MET 0 0 By similarity. FT METAL 10 10 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 13 13 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 16 16 Iron-sulfur 1 (4Fe-4S) (By similarity). FT METAL 20 20 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 47 47 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 50 50 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 53 53 Iron-sulfur 2 (4Fe-4S) (By similarity). FT METAL 57 57 Iron-sulfur 1 (4Fe-4S) (By similarity). SQ SEQUENCE 80 AA; 8777 MW; 16C7C5A2576003BF CRC64; SHSVKIYDTC IGCTHCVRAC PTDVLEMIPW DGCKAKQIAS APRTEDCVGC KRCESACPTD FLSVRVYLGP ETTRSMALSY // ID PSAF_MAIZE STANDARD; PRT; 20 AA. AC P13193; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE Photosystem I reaction centre subunit III (Light-harvesting complex I DE 17 kDa protein) (PSI-F) (Fragment). GN PSAF. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC STRAIN=cv. N273; RX MEDLINE=90033290; PubMed=2680596; RA Anandan S., Vainstein A., Thornber J.P.; RT "Correlation of some published amino acid sequences for photosystem I RT polypeptides to a 17 kDa LHCI pigment-protein and to subunits III and RT IV of the core complex."; RL FEBS Lett. 256:150-154(1989). CC -!- FUNCTION: Probably participates in efficiency of electron transfer CC from plastocyanin to P700 (or cytochrome c553 in algae and CC cyanobacteria). This plastocyanin-docking protein contributes to CC the specific association of plastocyanin to PSI. CC -!- SUBCELLULAR LOCATION: Associated with lumenal side of the CC thylakoid membrane. CC -!- SIMILARITY: Belongs to the psaF family. DR PIR; S06150; S06150. DR MaizeDB; 69542; -. KW Photosynthesis; Photosystem I; Chloroplast; Thylakoid; Membrane. FT NON_TER 20 20 SQ SEQUENCE 20 AA; 2110 MW; F0499F98F6188997 CRC64; AIAGLTPPKE SKAFAKXEKN // ID PSAI_MAIZE STANDARD; PRT; 36 AA. AC P30980; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Photosystem I reaction center subunit VIII (PSI-I). GN PSAI. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Rodermel S.R.; RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: May help in the organization of the psaL subunit. CC -!- SIMILARITY: Belongs to the psaI family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61188; CAA43491.1; -. DR EMBL; X86563; CAA60295.1; -. DR PIR; S58561; S58561. DR Gramene; P30980; -. DR MaizeDB; 57460; -. DR HAMAP; MF_00431; -; 1. DR InterPro; IPR001302; PSI_8. DR Pfam; PF00796; PSI_8; 1. DR ProDom; PD003995; PSI_8; 1. KW Chloroplast; Photosystem I; Photosynthesis; Transmembrane. FT TRANSMEM 10 30 Potential. SQ SEQUENCE 36 AA; 4028 MW; 459A02A4E33486C5 CRC64; MTDFNLPSIF VPLVGLVFPA IAMTSLFLYV QKNKIV // ID PSAJ_MAIZE STANDARD; PRT; 42 AA. AC P19443; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Photosystem I reaction center subunit IX (PSI-J). GN PSAJ. OS Zea mays (Maize), and OS Triticum aestivum (Wheat). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577, 4565; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Z.mays; RA Haley J., Bogorad L.; RL Submitted (MAY-1989) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Z.mays; RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; STRAIN=cv. Chinese Spring; RA Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T., RA Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., RA Gojobori T., Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., RA Tsunewaki K.; RT "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: RT complete sequence and contig clones."; RL Plant Mol. Biol. Rep. 18:243-253(2000). CC -!- FUNCTION: May help in the organization of the psaE and psaF CC subunits (By similarity). CC -!- SIMILARITY: Belongs to the psaJ family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04502; AAA84481.1; -. DR EMBL; X86563; CAA60305.1; -. DR EMBL; AB042240; BAB47053.1; -. DR PIR; S58571; S58571. DR Gramene; P19443; -. DR MaizeDB; 69547; -. DR HAMAP; MF_00522; -; 1. DR InterPro; IPR002615; PSI_PsaJ. DR Pfam; PF01701; PSI_PsaJ; 1. DR ProDom; PD004198; PSI_PsaJ; 1. KW Chloroplast; Photosystem I; Photosynthesis; Transmembrane. FT TRANSMEM 7 27 Potential. SQ SEQUENCE 42 AA; 4745 MW; DD29FAE6CAB485F6 CRC64; MRDIKTYLSV APVLSTLWFG ALAGLLIEIN RLFPDALSFP FF // ID PSBA_MAIZE STANDARD; PRT; 353 AA. AC P48183; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Photosystem Q(B) protein (32 kDa thylakoid membrane protein) DE (Photosystem II protein D1). GN PSBA. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: This is one of the two reaction center proteins of the CC chloroplast photosystem II. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast CC thylakoid membrane. CC -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil CC bind to Q(B) and blocks the electron transport. CC -!- SIMILARITY: Belongs to the reaction center pufL/M / psbA/D family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60265.1; -. DR PIR; S58531; S58531. DR HSSP; P02955; 1DOP. DR Gramene; P48183; -. DR MaizeDB; 105976; -. DR InterPro; IPR005867; Photo_DI. DR InterPro; IPR000484; Photo_RC. DR Pfam; PF00124; photoRC; 1. DR PRINTS; PR00256; REACTNCENTRE. DR ProDom; PD000551; Photo_RC; 1. DR TIGRFAMs; TIGR01151; psbA; 1. DR PROSITE; PS00244; REACTION_CENTER; 1. KW Transmembrane; Electron transport; Thylakoid; Photosystem II; KW Chloroplast; Iron; Herbicide resistance. FT TRANSMEM 36 56 Potential. FT TRANSMEM 109 129 Potential. FT TRANSMEM 141 164 Potential. FT TRANSMEM 192 218 Potential. FT TRANSMEM 269 289 Potential. FT METAL 215 215 Iron (non heme). FT METAL 272 272 Iron (non heme). SQ SEQUENCE 353 AA; 39010 MW; AA6BFB415FCE1C79 CRC64; MTAILERRES TSLWGRFCNW ITSTENRLYI GWFGVLMIPT LLTATSVFII AFIAAPPVDI DGIREPVSGS LLYGNNIISG AIIPTSAAIG LHFYPIWEAA SVDEWLYNGG PYELIVLHFL LGVACYMGRE WELSFRLGMR PWIAVAYSAP VAAATAVFLI YPIGQGSFSD GMPLGISGTF NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANEGYKFG QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGIWFTALGI STMAFNLNGF NFNQSVVDSQ GRVINTWADI INRANLGMEV MHERNAHNFP LDLAALEVPY LNG // ID PSBB_MAIZE STANDARD; PRT; 508 AA. AC P05641; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Photosystem II P680 chlorophyll A apoprotein (CP-47 protein). GN PSBB. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88210525; PubMed=2835175; RA Rock C.D., Barkan A., Taylor W.C.; RT "The maize plastid psbB-psbF-petB-petD gene cluster: spliced and RT unspliced petB and petD RNAs encode alternative products."; RL Curr. Genet. 12:69-77(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: This protein conjugates with chlorophyll and catalyzes CC the primary light-induced photochemical processes of photosystem CC II. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast CC thylakoid membrane. CC -!- SIMILARITY: Belongs to the psbB / psbC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05422; CAA28997.1; -. DR EMBL; X86563; CAA60311.1; -. DR PIR; S07171; QJZMBB. DR Gramene; P05641; -. DR MaizeDB; 69549; -. DR InterPro; IPR000932; PSIIprot. DR Pfam; PF00421; PSII; 1. KW Photosynthesis; Photosystem II; Thylakoid; Chlorophyll; Chloroplast; KW Transmembrane. FT TRANSMEM 19 40 Potential. FT TRANSMEM 95 118 Potential. FT TRANSMEM 138 163 Potential. FT TRANSMEM 197 219 Potential. FT TRANSMEM 236 260 Potential. FT TRANSMEM 449 468 Potential. SQ SEQUENCE 508 AA; 56106 MW; 536204771D113D27 CRC64; MGLPWYRVHT VVLNDPGRLL SVHIMHTALV SGWAGSMALY ELAVFDPSDP VLDPMWRQGM FVIPFMTRLG ITNSWGGWSI SGGTVTNPGI WSYEGVAGAH IVFSGLCFLA AIWHWVYWDL EIFCDERTGK PSLDLPKIFG IHLFLAGVAC FGFGAFHVTG LYGPGIWVSD PYGLTGKVQA VNPAWGAEGF DPFVPGGIAS HHIAAGTLGI LAGLFHLSVR PPQRLYKGLR MGNIETVLSS SIAAVFFAAF VVAGTMWYGS ATTPIELFGP TRYQWDQGYF QQEIYRRVSD GLAENLSLSE AWSKIPEKLA FYDYIGNNPA KGGLFRAGSM DNGDGIAVGW LGHPVFRDKE GRELFVRRMP TFFETFPVVL VDEEGIVRAD VPFRRAESKY SVEQVGVTVE FYGGELNGVS YSDPATVKKY ARRAQLGEIF ELDRATLKSD GVFRSSPRGW FTFGHATFAL LFFFGHIWHG ARTLFRDVFA GIDPDLDAQV EFGTFQKVGD PTTRRQAA // ID PSBC_MAIZE STANDARD; PRT; 473 AA. AC P48187; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Photosystem II 44 kDa reaction center protein (P6 protein) (CP43). GN PSBC. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: The 43 kDa protein (p6) is a component of the core of CC photosystem II. It is a chlorophyll binding protein. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast CC thylakoid membrane. CC -!- SIMILARITY: Belongs to the psbB / psbC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60271.1; -. DR PIR; S58537; S58537. DR Gramene; P48187; -. DR MaizeDB; 105980; -. DR InterPro; IPR005869; Photo44. DR InterPro; IPR000932; PSIIprot. DR Pfam; PF00421; PSII; 1. DR TIGRFAMs; TIGR01153; psbC; 1. KW Photosynthesis; Photosystem II; Thylakoid; Chlorophyll; Chloroplast; KW Transmembrane. SQ SEQUENCE 473 AA; 51899 MW; A53D37BA9FE8B86B CRC64; MKILYSLRRF YHVETLFNGT FVLAGRDQET TGFPWWAGNA RLINLSGKLL GAHVAHAGLI VFWAGAMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG SGGEVLDTFP YFVSGVLHLI SSAVLGFGGI YHALLGPETL EESFPFFGYV WQDRNKMTTL LGIHLILLGL GAFLLVLKAL YFGGVYDTWA PGGGDVRKIT NLTLSPGVIF GYLLKSPFGG EGWIVSVDDL EDIIGGHVWL GSICVLGGIW HILTKPFAWA RRAFVWSGEA YLSYSLGALS VFGFIACCFV WFNNTAYPSE FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY LMRSPTGEVI FGGETMRFWD LRAPWLEPLR GPNGLDLSRL KKDGQPWQER RSGEYMTHAP LGSLNSVGGV ATEINAVNYV SPRSWLATSH FVLGFFFFVG HLWHAGRARA AAAGFEKGID RDLEPVVYMT PLN // ID PSBD_MAIZE STANDARD; PRT; 353 AA. AC P48184; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Photosystem II D2 protein (Photosystem Q(A) protein) (PSII D2 DE protein). GN PSBD. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: This is one of the two reaction center proteins of PSII, CC D2 protein is needed for assembly of a stable PSII complex. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Chloroplast CC thylakoid membrane. CC -!- SIMILARITY: Belongs to the reaction center pufL/M / psbA/D family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60270.1; -. DR PIR; S58536; S58536. DR HSSP; P02955; 1DOP. DR Gramene; P48184; -. DR MaizeDB; 105984; -. DR InterPro; IPR005868; Photo_DII. DR InterPro; IPR000484; Photo_RC. DR Pfam; PF00124; photoRC; 1. DR PRINTS; PR00256; REACTNCENTRE. DR ProDom; PD000551; Photo_RC; 1. DR TIGRFAMs; TIGR01152; psbD; 1. DR PROSITE; PS00244; REACTION_CENTER; 1. KW Transmembrane; Electron transport; Thylakoid; Photosystem II; KW Chloroplast; Iron. FT TRANSMEM 36 57 Potential. FT TRANSMEM 109 129 Potential. FT TRANSMEM 142 164 Potential. FT TRANSMEM 192 218 Potential. FT TRANSMEM 266 286 Potential. FT METAL 215 215 Iron (non heme). FT METAL 225 225 Iron (non heme). FT METAL 269 269 Iron (non heme). SQ SEQUENCE 353 AA; 39603 MW; 1C6ABAAA98F75C77 CRC64; MTIAVGRVTK EENDLFPLID DWLRRDRFVF VGWSGLLLFP CAYFALGGWF TGTTFVTSWY THGLASSYLE GCNFLTAAVS TPANSLAHSL LLLWGPEAQG DFTRWSQLGG LWTFLALHGA FALIGFMLRQ FELARPVQLR PYNAISFSGP IAVFLSVFLI YPLGQSGWFF SPSFGVAAIF RFILFFQGFH NWTLKPFHMM GVAGVLGAVL LCAIHGATVE NTLFEDGDGA NTFRAFNPTQ AEETYSMVTA NRFWSQIFGV AFSNKRWLHF FMLFVPVTGL WMSAIGVVGL ALNLRAYDFV SQEIRAAEDP EFETFYTKNI LLNEGIRAWM AAQDQPHENL IFPEEVLPRG NAL // ID PSBE_WHEAT STANDARD; PRT; 82 AA. AC P05169; P10879; Q95H57; DT 13-AUG-1987 (Rel. 05, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome b559 alpha subunit (PSII reaction center subunit V). GN PSBE. OS Triticum aestivum (Wheat), OS Secale cereale (Rye), OS Zea mays (Maize), OS Oryza sativa (Rice), and OS Hordeum vulgare (Barley). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; Pooideae; OC Triticeae; Triticum. OX NCBI_TaxID=4565, 4550, 4577, 4530, 4513; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; RA Hird S.M., Willey D.L., Dyer T.A., Gray J.C.; RT "Location and nucleotide sequence of the gene for cytochrome b-559 in RT wheat chloroplast DNA."; RL Mol. Gen. Genet. 203:95-100(1986). RN [2] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-15. RC SPECIES=T.aestivum; STRAIN=cv. Sentry; TISSUE=Leaf; RA Webber A.N., Hird S.M., Packman L.C., Dyer T.A., Gray J.C.; RT "A photosystem II polypeptide is encoded by an open reading frame RT co-transcribed with genes for cytochrome b-559 in wheat chloroplast RT DNA."; RL Plant Mol. Biol. 12:141-151(1989). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; STRAIN=cv. Chinese Spring; RA Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T., RA Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., RA Gojobori T., Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., RA Tsunewaki K.; RT "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: RT complete sequence and contig clones."; RL Plant Mol. Biol. Rep. 18:243-253(2000). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=S.cereale; RX MEDLINE=89160331; PubMed=2646599; RA Zolotarev A.S., Kolosov V.L.; RT "Nucleotide sequence of the rye chloroplast DNA fragment, comprising RT psbE and psbF genes."; RL Nucleic Acids Res. 17:1760-1760(1989). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RA Haley J., Bogorad L.; RL Submitted (MAY-1989) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=O.sativa; STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=89364698; PubMed=2770692; RA Hiratsuka J., Shimada H., Whittier R., Ishibashi T., Sakamoto M., RA Mori M., Kondo C., Honji Y., Sun C.-R., Meng B.-Y., Li Y.-Q., RA Kanno A., Nishizawa Y., Hirai A., Shinozaki K., Sugiura M.; RT "The complete sequence of the rice (Oryza sativa) chloroplast genome: RT intermolecular recombination between distinct tRNA genes accounts for RT a major plastid DNA inversion during the evolution of the cereals."; RL Mol. Gen. Genet. 217:185-194(1989). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=H.vulgare; STRAIN=cv. Sabarlis; RX MEDLINE=89240046; PubMed=2654886; RA Andreeva A.V., Buryakova A.A., Reverdatto S.V., Chakhmakhcheva O.G., RA Efimov V.A.; RT "Nucleotide sequence of the barley chloroplast psbE, psbF genes and RT flanking regions."; RL Nucleic Acids Res. 17:2858-2858(1989). RN [9] RP SEQUENCE FROM N.A. RC SPECIES=H.vulgare; STRAIN=cv. Sabarlis; RX MEDLINE=92207253; PubMed=1804121; RA Efimov V.A., Andreeva A.V., Reverdatto S.V., Chakhmakhcheva O.G.; RT "Photosystem II of rye. Nucleotide sequence of the psbB, psbC, psbE, RT psbF, psbH genes of rye and chloroplast DNA regions adjacent to RT them."; RL Bioorg. Khim. 17:1369-1385(1991). RN [10] RP SEQUENCE FROM N.A. RC SPECIES=H.vulgare; RX MEDLINE=89374539; PubMed=3256307; RA Krupinska K., Berry-Lowe S.; RT "Characterization and in vitro expression of the cytochrome b-559 RT genes of barley. I. Localization and sequence of the genes."; RL Carlsberg Res. Commun. 53:43-55(1988). RN [11] RP SEQUENCE FROM N.A. RC SPECIES=H.vulgare; RX MEDLINE=89351277; PubMed=3255312; RA Krupinska K.; RT "Characterization and in vitro expression of the cytochrome b-559 RT genes of barley. II. In vitro transcription and translation."; RL Carlsberg Res. Commun. 53:233-246(1988). RN [12] RP SEQUENCE OF 1-14. RC SPECIES=T.aestivum; RX MEDLINE=89121082; PubMed=2644131; RA Ikeuchi M., Takio K., Inoue Y.; RT "N-terminal sequencing of photosystem II low-molecular-mass proteins. RT 5 and 4.1 kDa components of the O2-evolving core complex from higher RT plants."; RL FEBS Lett. 242:263-269(1989). CC -!- FUNCTION: This b-type cytochrome is tightly associated with the CC reaction center of photosystem II and possibly is part of the CC water-oxidation complex. CC -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit. CC -!- SIMILARITY: Belongs to the psbE / psbF family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03776; CAA27405.1; -. DR EMBL; X15225; CAA33294.1; -. DR EMBL; AB042240; BAB47050.1; -. DR EMBL; X13326; CAA31698.1; -. DR EMBL; J04502; AAA84478.1; -. DR EMBL; X86563; CAA60302.1; -. DR EMBL; X15901; CAA33965.1; -. DR EMBL; X14108; CAA32270.1; -. DR EMBL; M35977; AAA84044.1; -. DR EMBL; M35616; AAA84048.1; -. DR PIR; A29956; A29956. DR PIR; JQ0243; CBRZ55. DR PIR; S03191; S03191. DR PIR; S03621; CBWT5E. DR PIR; S58568; S58568. DR Gramene; Q95H57; -. DR Gramene; P05169; -. DR MaizeDB; 69552; -. DR HAMAP; MF_00642; -; 1. DR InterPro; IPR006216; Cyt_b559. DR InterPro; IPR006217; Cyt_b559_alpha. DR Pfam; PF00283; cytochr_b559; 1. DR Pfam; PF00284; cytochr_b559a; 1. DR ProDom; PD004478; Cyt_b559_alpha; 1. DR TIGRFAMs; TIGR01332; cyt_b559_alpha; 1. DR PROSITE; PS00537; CYTOCHROME_B559; 1. KW Chloroplast; Photosystem II; Heme; Electron transport; Transmembrane. FT INIT_MET 0 0 FT DOMAIN 1 17 Stromal (Potential). FT TRANSMEM 18 43 Potential. FT DOMAIN 44 82 Lumenal (Potential). FT METAL 22 22 Iron (heme axial ligand) (By similarity). FT CONFLICT 15 15 S -> C (in Ref. 8). FT CONFLICT 22 22 H -> R (in Ref. 8). FT CONFLICT 49 49 P -> L (in Ref. 3). SQ SEQUENCE 82 AA; 9313 MW; 6173EF444BF4025C CRC64; SGSTGERSFA DIITSIRYWV IHSITIPSLF IAGWLFVSTG LAYDVFGSPR PNEYFTESRQ GIPLITDRFD SLEQLDEFSR SF // ID PSBF_ORYSA STANDARD; PRT; 39 AA. AC P12088; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Cytochrome b559 beta subunit (PSII reaction center subunit VI). GN PSBF. OS Oryza sativa (Rice), OS Zea mays (Maize), and OS Mesembryanthemum crystallinum (Common ice plant). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530, 4577, 3544; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=O.sativa; STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=89364698; PubMed=2770692; RA Hiratsuka J., Shimada H., Whittier R., Ishibashi T., Sakamoto M., RA Mori M., Kondo C., Honji Y., Sun C.-R., Meng B.-Y., Li Y.-Q., RA Kanno A., Nishizawa Y., Hirai A., Shinozaki K., Sugiura M.; RT "The complete sequence of the rice (Oryza sativa) chloroplast genome: RT intermolecular recombination between distinct tRNA genes accounts for RT a major plastid DNA inversion during the evolution of the cereals."; RL Mol. Gen. Genet. 217:185-194(1989). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=O.sativa; TISSUE=Leaf; RA Zhao X.P., Luo Z.-X., Cote J.-C., Wu R.; RL Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RA Haley J., Bogorad L.; RL Submitted (MAY-1989) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=M.crystallinum; RX MEDLINE=94345017; PubMed=8066140; RA Forsthoefel N.R., Cushman J.C.; RT "Characterization and expression of photosystem II genes (psbE, psbF, RT and psbL) from the facultative crassulacean acid metabolism plant RT Mesembryanthemum crystallinum."; RL Plant Physiol. 105:761-762(1994). CC -!- FUNCTION: This b-type cytochrome is tightly associated with the CC reaction center of photosystem II and possibly is part of the CC water-oxidation complex. CC -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit. CC -!- SIMILARITY: Belongs to the psbE / psbF family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15901; CAA33964.1; -. DR EMBL; X15057; CAA33156.1; -. DR EMBL; J04502; AAA84477.1; -. DR EMBL; X86563; CAA60301.1; -. DR EMBL; U04314; AAA21858.1; -. DR PIR; JQ0242; F2RZ4. DR PIR; S58567; S58567. DR Gramene; P12088; -. DR MaizeDB; 69554; -. DR HAMAP; MF_00643; -; 1. DR InterPro; IPR006216; Cyt_b559. DR InterPro; IPR006241; Cyt_b559_beta. DR Pfam; PF00283; cytochr_b559; 1. DR ProDom; PD004747; Cyt_b559_beta; 1. DR TIGRFAMs; TIGR01333; cyt_b559_beta; 1. DR PROSITE; PS00537; CYTOCHROME_B559; 1. KW Chloroplast; Photosystem II; Heme; Electron transport; Transmembrane. FT DOMAIN 1 13 Stromal (Potential). FT TRANSMEM 14 34 Potential. FT DOMAIN 35 39 Lumenal (Potential). FT METAL 18 18 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 39 AA; 4484 MW; F61251852D6E1C6F CRC64; MTIDRTYPIF TVRWLAVHGL AVPTVFFLGS ISAMQFIQR // ID PSBH_MAIZE STANDARD; PRT; 72 AA. AC P24993; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Photosystem II reaction center H protein (Photosystem II 10 kDa DE phosphoprotein) (PSII-H). GN PSBH. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88210525; PubMed=2835175; RA Rock C.D., Barkan A., Taylor W.C.; RT "The maize plastid psbB-psbF-petB-petD gene cluster: spliced and RT unspliced petB and petD RNAs encode alternative products."; RL Curr. Genet. 12:69-77(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- PTM: Phosphorylation is a light-dependent reaction catalyzed by a CC membrane-bound kinase (By similarity). CC -!- SIMILARITY: Belongs to the psbH family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05422; CAA28998.1; -. DR EMBL; X86563; CAA60314.1; -. DR PIR; S08591; F2ZMBH. DR Gramene; P24993; -. DR MaizeDB; 69555; -. DR HAMAP; MF_00752; -; 1. DR InterPro; IPR001056; PSII_PsbH. DR Pfam; PF00737; PsbH; 1. DR ProDom; PD003584; PSII_PsbH; 1. KW Photosystem II; Phosphorylation; Chloroplast; Thylakoid; KW Transmembrane. FT INIT_MET 0 0 By similarity. FT TRANSMEM 40 60 Potential. FT MOD_RES 2 2 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 72 AA; 7656 MW; C6679B06FD036341 CRC64; ATQTVEDSSR PKPKRTGAGS LLKPLNSEYG KVAPGWGTTP FMGVAMALFA IFLSIILEIY NSSVLLDGIL TN // ID PSBI_ARATH STANDARD; PRT; 36 AA. AC P09970; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Photosystem II reaction center I protein (PSII 4.8 kDa protein) (PSII DE I-protein). GN PSBI OR ATCG00080. OS Arabidopsis thaliana (Mouse-ear cress), OS Zea mays (Maize), OS Nicotiana tabacum (Common tobacco), OS Triticum aestivum (Wheat), OS Lotus japonicus, OS Oenothera hookeri (Hooker's evening primrose), OS Secale cereale (Rye), OS Sinapis alba (White mustard) (Brassica hirta), and OS Spinacia oleracea (Spinach). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702, 4577, 4097, 4565, 34305, 85636, 4550, 3728, 3562; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=A.thaliana; STRAIN=cv. Columbia; RX MEDLINE=20039611; PubMed=10574454; RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.; RT "Complete structure of the chloroplast genome of Arabidopsis RT thaliana."; RL DNA Res. 6:283-290(1999). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=N.tabacum; STRAIN=cv. Bright Yellow 4; RA Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N., RA Matsubayashi T., Zaita N., Chunwongse J., Obokata J., RA Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B.-Y., Sugita M., RA Deno H., Kamogashira T., Yamada K., Kusuda J., Takaiwa F., Kato A., RA Tohdoh N., Shimada H., Sugiura M.; RT "The complete nucleotide sequence of the tobacco chloroplast genome: RT its gene organization and expression."; RL EMBO J. 5:2043-2049(1986). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; RX MEDLINE=88270574; PubMed=3390875; RA Howe C.J., Barker R.F., Bowman C.M., Dyer T.A.; RT "Common features of three inversions in wheat chloroplast DNA."; RL Curr. Genet. 13:343-349(1988). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; STRAIN=cv. Chinese Spring; RA Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T., RA Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., RA Gojobori T., Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., RA Tsunewaki K.; RT "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: RT complete sequence and contig clones."; RL Plant Mol. Biol. Rep. 18:243-253(2000). RN [6] RP SEQUENCE FROM N.A. RC SPECIES=L.japonicus; STRAIN=Accession MG-20; RX MEDLINE=21082929; PubMed=11214967; RA Kato T., Kaneko T., Sato S., Nakamura Y., Tabata S.; RT "Complete structure of the chloroplast genome of a legume, Lotus RT japonicus."; RL DNA Res. 7:323-330(2000). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=O.hookeri; STRAIN=cv. Johansen; RX MEDLINE=20309318; PubMed=10852478; RA Hupfer H., Swiatek M., Hornung S., Herrmann R.G., Maier R.M., RA Chiu W.-L., Sears B.; RT "Complete nucleotide sequence of the Oenothera elata plastid RT chromosome, representing plastome I of the five distinguishable RT Euoenothera plastomes."; RL Mol. Gen. Genet. 263:581-585(2000). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=S.cereale; RX MEDLINE=89128450; PubMed=2644624; RA Bukharov A.A., Kolosov V.L., Klezovich O.N., Zolotarev A.S.; RT "Nucleotide sequence of rye chloroplast DNA fragment, comprising psbD, RT psbC and trnS genes."; RL Nucleic Acids Res. 17:798-798(1989). RN [9] RP SEQUENCE FROM N.A. RC SPECIES=S.cereale; RX MEDLINE=91362697; PubMed=1888340; RA Kolosov V.L., Bukharov A.A., Zolotarev A.S.; RT "Photosystem II of rye. Nucleotide sequence of psbD, psbI genes RT encoding reaction center proteins."; RL Bioorg. Khim. 17:448-455(1991). RN [10] RP SEQUENCE FROM N.A. RC SPECIES=S.alba; RX MEDLINE=90221826; PubMed=2183183; RA Neuhaus H., Pfannschmidt T., Link G.; RT "Nucleotide sequence of the chloroplast psbI and trnS-GCU genes from RT mustard (Sinapis alba)."; RL Nucleic Acids Res. 18:368-368(1990). RN [11] RP SEQUENCE FROM N.A. RC SPECIES=S.oleracea; STRAIN=cv. Geant d'hiver, and cv. Monatol; RX MEDLINE=21187424; PubMed=11292076; RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., RA Herrmann R.G., Mache R.; RT "The plastid chromosome of spinach (Spinacia oleracea): complete RT nucleotide sequence and gene organization."; RL Plant Mol. Biol. 45:307-315(2001). RN [12] RP SEQUENCE OF 1-20. RC SPECIES=S.oleracea; RX MEDLINE=89065114; PubMed=3058517; RA Ikeuchi M., Inoue Y.; RT "A new photosystem II reaction center component (4.8 kDa protein) RT encoded by chloroplast genome."; RL FEBS Lett. 241:99-104(1988). RN [13] RP SEQUENCE OF 1-20. RC SPECIES=S.oleracea; RX MEDLINE=89121082; PubMed=2644131; RA Ikeuchi M., Takio K., Inoue Y.; RT "N-terminal sequencing of photosystem II low-molecular-mass proteins. RT 5 and 4.1 kDa components of the O2-evolving core complex from higher RT plants."; RL FEBS Lett. 242:263-269(1989). RN [14] RP SEQUENCE OF 1-5, AND MASS SPECTROMETRY. RC SPECIES=S.oleracea; RX MEDLINE=98298118; PubMed=9632665; RA Zheleva D., Sharma J., Panico M., Morris H.R., Barber J.; RT "Isolation and characterization of monomeric and dimeric CP47-reaction RT center photosystem II complexes."; RL J. Biol. Chem. 273:16122-16127(1998). CC -!- FUNCTION: This protein is a component of the reaction center of CC photosystem II. Its exact function is not yet known. CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- MASS SPECTROMETRY: MW=4195.5; METHOD=MALDI. CC -!- SIMILARITY: Belongs to the psbI family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AP000423; BAA84369.1; -. DR EMBL; X86563; CAA60269.1; -. DR EMBL; Z00044; -; NOT_ANNOTATED_CDS. DR EMBL; X07742; CAA30562.1; -. DR EMBL; AB042240; BAB47018.1; -. DR EMBL; AP002983; BAB33202.1; -. DR EMBL; AJ271079; CAB67161.1; -. DR EMBL; X61674; CAA43849.1; -. DR EMBL; X17616; CAA35617.1; -. DR EMBL; AJ400848; CAB88709.1; -. DR PIR; JN0315; JN0315. DR PIR; S01044; S01044. DR PIR; S05608; F2NTI. DR PIR; S07877; S07877. DR PIR; S58535; S58535. DR MaizeDB; 118219; -. DR HAMAP; MF_01316; -; 1. DR InterPro; IPR003686; PSII_PsbI. DR Pfam; PF02532; PsbI; 1. KW Photosynthesis; Chloroplast; Thylakoid; Photosystem II; KW Reaction center; Transmembrane; Formylation. FT MOD_RES 1 1 FORMYLATION. FT TRANSMEM 7 24 Potential. SQ SEQUENCE 36 AA; 4168 MW; 6B6C7FCB57BB6236 CRC64; MLTLKLFVYT VVIFFVSLFI FGFLSNDPGR NPGREE // ID PSBJ_MAIZE STANDARD; PRT; 40 AA. AC P19444; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Photosystem II reaction center J protein. GN PSBJ. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Haley J., Bogorad L.; RL Submitted (MAY-1989) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: This protein is a component of the reaction center of CC photosystem II. Its exact function is not yet known. CC -!- SIMILARITY: Belongs to the psbJ family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04502; AAA84475.1; -. DR EMBL; X86563; CAA60299.1; -. DR PIR; S58565; S58565. DR Gramene; P19444; -. DR MaizeDB; 69556; -. DR HAMAP; MF_01305; -; 1. DR InterPro; IPR002682; PSII_PsbJ. DR Pfam; PF01788; PsbJ; 1. KW Photosynthesis; Photosystem II; Reaction center; Chloroplast; KW Transmembrane. FT TRANSMEM 9 31 Potential. SQ SEQUENCE 40 AA; 4195 MW; 571C20BE0F161E97 CRC64; MADTTGRIPL WLIGTVTGIL VIGLIGFFFY GSYSGLGSSL // ID PSBK_MAIZE STANDARD; PRT; 61 AA. AC P48188; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Photosystem II reaction center protein K precursor (PSII-K). GN PSBK. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: This protein is a component of the reaction center of CC photosystem II. CC -!- SIMILARITY: Belongs to the psbK family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60268.1; -. DR PIR; S58534; S58534. DR Gramene; P48188; -. DR MaizeDB; 118217; -. DR HAMAP; MF_00441; -; 1. DR InterPro; IPR003687; PSII_PsbK. DR Pfam; PF02533; PsbK; 1. KW Photosystem II; Chloroplast. FT PROPEP 1 24 Potential. FT CHAIN 25 61 Photosystem II reaction center protein K. SQ SEQUENCE 61 AA; 6874 MW; D67361066179A2C1 CRC64; MPNILSLTCI CFNSVLCPTS FFFAKLPEAY AIFNPIVDVM PVIPVLFFLL AFVWQAAVSF R // ID PSBL_MAIZE STANDARD; PRT; 38 AA. AC P60138; O47030; P12166; P12167; Q34007; DT 01-OCT-1989 (Rel. 12, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Photosystem II reaction center L protein (PSII 5 kDa protein). GN PSBL. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9cms X FR37; RX MEDLINE=89160811; PubMed=2922397; RA Haley J., Bogorad L.; RT "A 4-kDa maize chloroplast polypeptide associated with the cytochrome RT b6-f complex: subunit 5, encoded by the chloroplast petE gene."; RL Proc. Natl. Acad. Sci. U.S.A. 86:1534-1538(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Not known, it is however required for PSII activity (By CC similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- SIMILARITY: Belongs to the psbL family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J04502; AAA84476.1; -. DR EMBL; X86563; CAA60300.1; -. DR PIR; S58566; S58566. DR MaizeDB; 69558; -. DR HAMAP; MF_01317; -; 1. DR InterPro; IPR003372; PSII_PsbL. DR Pfam; PF02419; PsbL; 1. DR ProDom; PD005113; PSII_PsbL; 1. KW Photosynthesis; Chloroplast; Thylakoid; Photosystem II; KW Reaction center; Transmembrane. FT TRANSMEM 15 36 Potential. SQ SEQUENCE 38 AA; 4497 MW; 55537AEC50D25E8D CRC64; MTQSNPNEQN VELNRTSLYW GLLLIFVLAV LFSNYFFN // ID PSBM_MAIZE STANDARD; PRT; 34 AA. AC P48189; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Photosystem II reaction center M protein (PSII-M). GN PSBM. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Not known. CC -!- SIMILARITY: Belongs to the psbM family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60274.1; -. DR PIR; S58540; S58540. DR Gramene; P48189; -. DR MaizeDB; 118228; -. DR HAMAP; MF_00438; -; 1. DR InterPro; IPR007826; PsbM. DR Pfam; PF05151; PsbM; 1. KW Photosystem II; Transmembrane; Chloroplast. FT TRANSMEM 5 25 Potential. SQ SEQUENCE 34 AA; 3754 MW; 70D38C04FBBB4222 CRC64; MEVNILAFIA TALFILVPTA FLLIIYVKTA SQND // ID PSBN_ORYSA STANDARD; PRT; 43 AA. AC P12171; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Photosystem II reaction center N protein (PSII N-protein). GN PSBN. OS Oryza sativa (Rice), OS Zea mays (Maize), OS Triticum aestivum (Wheat), OS Secale cereale (Rye), OS Oenothera hookeri (Hooker's evening primrose), OS Oenothera argillicola (Appalachian evening primrose), OS Lotus japonicus, and OS Populus deltoides (Poplar). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530, 4577, 4565, 4550, 85636, 3940, 34305, 3696; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=O.sativa; STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=89364698; PubMed=2770692; RA Hiratsuka J., Shimada H., Whittier R., Ishibashi T., Sakamoto M., RA Mori M., Kondo C., Honji Y., Sun C.-R., Meng B.-Y., Li Y.-Q., RA Kanno A., Nishizawa Y., Hirai A., Shinozaki K., Sugiura M.; RT "The complete sequence of the rice (Oryza sativa) chloroplast genome: RT intermolecular recombination between distinct tRNA genes accounts for RT a major plastid DNA inversion during the evolution of the cereals."; RL Mol. Gen. Genet. 217:185-194(1989). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; STRAIN=cv. Mardler; RX MEDLINE=91330334; PubMed=1714358; RA Hird S.M., Webber A.N., Wilson R.J., Dyer T.A., Gray J.C.; RT "Differential expression of the psbB and psbH genes encoding the 47 RT kDa chlorophyll a-protein and the 10 kDa phosphoprotein of RT photosystem II during chloroplast development in wheat."; RL Curr. Genet. 19:199-206(1991). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; STRAIN=cv. Chinese Spring; RA Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T., RA Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., RA Gojobori T., Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., RA Tsunewaki K.; RT "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: RT complete sequence and contig clones."; RL Plant Mol. Biol. Rep. 18:243-253(2000). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=S.cereale; RX MEDLINE=90056620; PubMed=2684168; RA Bukharov A.A., Kolosov V.L., Zolotarev A.S., Abdulaev N.G.; RT "Photosystem II of rye. Nucleotide sequence of psbB and psbH genes, RT coding 47-kDa of chlorophyll(a)-binding and 10-kDa phosphorylated RT subunits."; RL Bioorg. Khim. 15:927-939(1989). RN [6] RP SEQUENCE FROM N.A. RC SPECIES=O.argillicola, and O.hookeri; RX MEDLINE=91057156; PubMed=2243806; RA Offermann-Steinhard K., Herrmann R.G.; RT "Nucleotide sequences of psbB and psbH, the plastid encoded genes for RT CP47 and the 10 kDa phosphoprotein of photosystem II in Oenothera RT hookeri and argillicola."; RL Nucleic Acids Res. 18:6452-6452(1990). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=O.hookeri; STRAIN=cv. Johansen; RX MEDLINE=20309318; PubMed=10852478; RA Hupfer H., Swiatek M., Hornung S., Herrmann R.G., Maier R.M., RA Chiu W.-L., Sears B.; RT "Complete nucleotide sequence of the Oenothera elata plastid RT chromosome, representing plastome I of the five distinguishable RT Euoenothera plastomes."; RL Mol. Gen. Genet. 263:581-585(2000). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=L.japonicus; STRAIN=Accession MG-20; RX MEDLINE=21082929; PubMed=11214967; RA Kato T., Kaneko T., Sato S., Nakamura Y., Tabata S.; RT "Complete structure of the chloroplast genome of a legume, Lotus RT japonicus."; RL DNA Res. 7:323-330(2000). RN [9] RP SEQUENCE FROM N.A. RC SPECIES=P.deltoides; STRAIN=cv. Stoneville D121; TISSUE=Leaf; RA Dixij R.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Not known. CC -!- SIMILARITY: Belongs to the psbN family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15901; CAA33975.1; -. DR EMBL; X86563; CAA60313.1; -. DR EMBL; X54749; CAA38543.1; -. DR EMBL; AB042240; BAB47061.1; -. DR EMBL; X55899; CAA39389.1; -. DR EMBL; X55900; CAA39392.1; -. DR EMBL; AJ271079; CAB67187.1; -. DR EMBL; AP002983; BAB33224.1; -. DR EMBL; Y13328; CAA73767.1; -. DR PIR; JN0417; JN0417. DR PIR; JQ0255; F2RZN. DR PIR; S12130; S12130. DR PIR; S12133; S12133. DR PIR; S14142; S14142. DR PIR; S58579; S58579. DR Gramene; P12171; -. DR MaizeDB; 118238; -. DR HAMAP; MF_00293; -; 1. DR InterPro; IPR003398; PSII_PsbN. DR Pfam; PF02468; PsbN; 1. DR ProDom; PD005510; PSII_PsbN; 1. KW Photosystem II; Transmembrane; Chloroplast. FT TRANSMEM 6 28 Potential. SQ SEQUENCE 43 AA; 4662 MW; 06173171041707AD CRC64; METATLVAIS ISGLLVSFTG YALYTAFGQP SQQLRDPFEE HGD // ID PSBT_MAIZE STANDARD; PRT; 33 AA. AC P37257; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Photosystem II reaction center T protein (PSII-T). GN PSBT OR YCF8. OS Zea mays (Maize), and OS Lotus japonicus. OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577, 34305; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=88210525; PubMed=2835175; RA Rock C.D., Barkan A., Taylor W.C.; RT "The maize plastid psbB-psbF-petB-petD gene cluster: spliced and RT unspliced petB and petD RNAs encode alternative products."; RL Curr. Genet. 12:69-77(1987). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=L.japonicus; STRAIN=Accession MG-20; RX MEDLINE=21082929; PubMed=11214967; RA Kato T., Kaneko T., Sato S., Nakamura Y., Tabata S.; RT "Complete structure of the chloroplast genome of a legume, Lotus RT japonicus."; RL DNA Res. 7:323-330(2000). CC -!- FUNCTION: Exact function not known. It is essential to maintain CC photosynthetic activity under adverse growth conditions (By CC similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast thylakoid membrane. CC -!- SIMILARITY: Belongs to the psbT family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05422; -; NOT_ANNOTATED_CDS. DR EMBL; X86563; CAA60312.1; -. DR EMBL; AP002983; BAB33223.1; -. DR PIR; S58578; S58578. DR Gramene; P37257; -. DR MaizeDB; 85519; -. DR InterPro; IPR001743; PSII_PsbT. DR Pfam; PF01405; PsbT; 1. DR ProDom; PD004453; PSII_PsbT; 1. KW Photosynthesis; Photosystem II; Chloroplast; Transmembrane; KW Thylakoid. FT TRANSMEM 3 23 Potential. SQ SEQUENCE 33 AA; 3818 MW; A51F72A372756A79 CRC64; MEALVYTFLL VSTLGIIFFA IFFREPPKVP TKK // ID PSY_MAIZE STANDARD; PRT; 410 AA. AC P49085; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Phytoene synthase, chloroplast precursor (EC 2.5.1.-). GN Y1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96304610; PubMed=8722797; RA Buckner B., Sanmiguel P., Janick-Buckner D., Bennetzen J.L.; RT "The y1 gene of maize codes for phytoene synthase."; RL Genetics 143:479-488(1996). CC -!- FUNCTION: Catalyzes the reaction from prephytoene diphosphate to CC phytoene. CC -!- CATALYTIC ACTIVITY: 2 geranylgeranyl diphosphate = diphosphate + CC prephytoene diphosphate. CC -!- CATALYTIC ACTIVITY: Prephytoene diphosphate = diphosphate + CC phytoene. CC -!- PATHWAY: Carotenoid biosynthesis. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the phytoene/squalene synthetase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U32636; AAB60314.1; -. DR PIR; S68307; S68307. DR MaizeDB; 66643; -. DR InterPro; IPR002060; Squ/phyt_synthse. DR InterPro; IPR008949; Terpenoid_synth. DR Pfam; PF00494; SQS_PSY; 1. DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1. DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1. KW Multifunctional enzyme; Carotenoid biosynthesis; KW Isoprene biosynthesis; Transferase; Chloroplast; Transit peptide. FT TRANSIT 1 ? Chloroplast (Potential). FT CHAIN ? 410 Phytoene synthase. FT VARIANT 344 344 N -> T (in allele B73). SQ SEQUENCE 410 AA; 46481 MW; 21070A33624EED79 CRC64; MAIILVRAAS PGLSAADSIS HQGTLQCSTL LKTKRPAARR WMPCSLLGLH PWEAGRPSPA VYSSLPVNPA GEAVVSSEQK VYDVVLKQAA LLKRQLRTPV LDARPQDMDM PRNGLKEAYD RCGEICEEYA KTFYLGTMLM TEERRRAIWA IYVWCRRTDE LVDGPNANYI TPTALDRWEK RLEDLFTGRP YDMLDAALSD TISRFPIDIQ PFRDMIEGMR SDLRKTRYNN FDELYMYCYY VAGTVGLMSV PVMGIATESK ATTESVYSAA LALGIANQLT NILRDVGEDA RRGRIYLPQD ELAQAGLSDE DIFKGVVTNR WRNFMKRQIK RARMFFEEAE RGVNELSQAS RWPVWASLLL YRQILDEIEA NDYNNFTKRA YVGKGKKLLA LPVAYGKSLL LPCSLRNGQT // ID R141_MAIZE STANDARD; PRT; 149 AA. AC P19950; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE 40S ribosomal protein S14 (Clone MCH1). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89252825; PubMed=2470645; RA Larkin J.C., Hunsperger J.P., Culley D., Rubenstein I., Silflow C.D.; RT "The organization and expression of a maize ribosomal protein gene RT family."; RL Genes Dev. 3:500-509(1989). CC -!- SIMILARITY: Belongs to the S11P family of ribosomal proteins. DR PIR; A30097; A30097. DR MaizeDB; 69559; -. DR InterPro; IPR001971; Ribosomal_S11. DR Pfam; PF00411; Ribosomal_S11; 1. DR ProDom; PD001010; Ribosomal_S11; 1. DR PROSITE; PS00054; RIBOSOMAL_S11; 1. KW Ribosomal protein; Multigene family. SQ SEQUENCE 149 AA; 16258 MW; 9B8F9E063C4AC2D0 CRC64; MSRRKTREPK EENVLGPTVR EGEFVFGVAH IFASFNDTFI HVTDLSGRET LVRITGGMKV KADRDESSPY AAMLAAQDVA QRCKELGITA LHIKLRATGG NKTKTPGPGA QSALRALARS GMKIGRIEDV TPVPTDSTRR KGGRRGRRL // ID R142_MAIZE STANDARD; PRT; 150 AA. AC P19951; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE 40S ribosomal protein S14 (Clone MCH2). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89252825; PubMed=2470645; RA Larkin J.C., Hunsperger J.P., Culley D., Rubenstein I., Silflow C.D.; RT "The organization and expression of a maize ribosomal protein gene RT family."; RL Genes Dev. 3:500-509(1989). CC -!- SIMILARITY: Belongs to the S11P family of ribosomal proteins. DR PIR; B30097; B30097. DR MaizeDB; 69559; -. DR InterPro; IPR001971; Ribosomal_S11. DR Pfam; PF00411; Ribosomal_S11; 1. DR ProDom; PD001010; Ribosomal_S11; 1. DR PROSITE; PS00054; RIBOSOMAL_S11; 1. KW Ribosomal protein; Multigene family. SQ SEQUENCE 150 AA; 16263 MW; 70822B40751EBE68 CRC64; MSGRKKTREP KEENVLGPAV REGEHVFGVA HIFASFNDTF IHVTDLSGRE TLVRITGGMK VKADRDESSP YAAMLASQDV AQRCKELGIT ALHIKLRATG GNKTKTPGPG AQSALRALAR SGMKIGRIED VTPVPTDSTR RKGGRRGRRL // ID R27A_MAIZE STANDARD; PRT; 79 AA. AC P27923; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE 40S ribosomal protein S27a. GN UBF9. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92084112; PubMed=1660830; RA Chen K., Rubenstein I.; RT "Characterization of the structure and transcription of a ubiquitin RT fusion gene from maize."; RL Gene 107:205-212(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. DEA; TISSUE=Root tip; RA Chevalier C., le Querrec F., Raymond P.; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. CC -!- MISCELLANEOUS: This ribosomal protein is synthesized as a C- CC terminal extension protein (CEP) of ubiquitin. CC -!- SIMILARITY: Belongs to the S27ae family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M68937; AAA33519.1; ALT_INIT. DR EMBL; X92422; CAA63150.1; ALT_INIT. DR MaizeDB; 26015; -. DR InterPro; IPR002906; Ribosomal_S27. DR Pfam; PF01599; Ribosomal_S27; 1. KW Ribosomal protein; Zinc-finger; Metal-binding. FT DOMAIN 1 23 Lys-rich (highly basic). FT ZN_FING 46 69 C4-type. FT CONFLICT 4 4 R -> P (in Ref. 2). FT CONFLICT 45 45 E -> D (in Ref. 2). FT CONFLICT 49 49 T -> A (in Ref. 2). FT CONFLICT 52 52 G -> H (in Ref. 2). FT CONFLICT 78 78 K -> Q (in Ref. 2). SQ SEQUENCE 79 AA; 9175 MW; A6A28087FB3ECAD2 CRC64; AKKRKKKTYT KPKKIKHKHK KVKLAVLQFY KVDDATGKVT RLRKECPNTE CGAGVFMANH FDRHYCGKCG LTYVYNQKA // ID RA2A_MAIZE STANDARD; PRT; 111 AA. AC P46252; DT 01-NOV-1995 (Rel. 32, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE 60S acidic ribosomal protein P2A (P2). GN RPP2A OR RPP2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. RTCS 2; RX MEDLINE=96189277; PubMed=8605314; RA Goddemeier M.L., Rensing S.A., Feix G.; RT "Characterization of a maize ribosomal P2 protein cDNA and RT phylogenetic analysis of the P1/P2 family of ribosomal proteins."; RL Plant Mol. Biol. 30:655-658(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A2; RA Vangala S., Bailey-Serres J.N.; RT "Nucleotide sequence of a maize (Zea mays L.) cDNA coding for a P2- RT type acidic ribosomal protein."; RL (In) Plant Gene Register PGR95-064. RN [3] RP SEQUENCE OF 1-11. RC STRAIN=cv. B73; TISSUE=Ear; RX MEDLINE=97422884; PubMed=9276949; RA Bailey-Serres J., Vangala S., Szick K., Lee C.H.; RT "Acidic phosphoprotein complex of the 60S ribosomal subunit of maize RT seedling roots. Components and changes in response to flooding."; RL Plant Physiol. 114:1293-1305(1997). CC -!- FUNCTION: Plays an important role in the elongation step of CC protein synthesis. CC -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit. CC -!- PTM: Phosphorylated. CC -!- SIMILARITY: Belongs to the L12P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86553; CAA60251.1; -. DR EMBL; U29383; AAC49360.1; -. DR PIR; S65781; S54179. DR MaizeDB; 84942; -. DR InterPro; IPR001813; Ribosomal_60S. DR Pfam; PF00428; 60s_ribosomal; 1. KW Ribosomal protein; Phosphorylation. FT INIT_MET 0 0 FT CONFLICT 2 2 F -> Y (in Ref. 3). FT CONFLICT 8 8 L -> V (in Ref. 3). FT CONFLICT 83 83 A -> R (in Ref. 2). SQ SEQUENCE 111 AA; 11231 MW; 44A21E5044176EC9 CRC64; KFVAAYLLAV LAGNASPSAD DLTAILESVG CEVDNEKMEL LLSQLSGKDI TELIAAGREK FASVPCGGGG VAVAAAAPAA GGAAPAAEAK KEEKVEEKEE SDDDMGFSLF D // ID RB2A_MAIZE STANDARD; PRT; 209 AA. AC P49103; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ras-related protein Rab-2-A. GN RAB2A. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Laughner B.J., Ferl R.J., Almira E.C.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protein transport. Probably involved in vesicular CC traffic (By similarity). CC -!- SUBCELLULAR LOCATION: Associated with a structure having the CC characteristics of an intermediate compartment between the CC endoplasmic reticulum and the Golgi apparatus (By similarity). CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U22432; AAA63901.1; -. DR PIR; T02242; T02242. DR HSSP; P05713; 3RAB. DR MaizeDB; 121973; -. DR InterPro; IPR003579; GTPase_Rab. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Lipoprotein; Prenylation; Protein transport. FT NP_BIND 13 20 GTP (By similarity). FT NP_BIND 61 65 GTP (By similarity). FT NP_BIND 119 122 GTP (By similarity). FT DOMAIN 35 43 Effector region (By similarity). FT LIPID 207 207 S-geranylgeranyl cysteine FT (By similarity). FT LIPID 208 208 S-geranylgeranyl cysteine FT (By similarity). SQ SEQUENCE 209 AA; 23001 MW; 294E8C21DE22085F CRC64; MSYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMINI DNKPIKLQIW DTAGQESFRS ITRSYYRGAA GALLVYDITR RETFNHLASW LEDARQHANA NMTIMLVGNK CDLSHRRAVS YEEGEQFAKE HGLIFMEASA KTAQNVEEAF VKTAGAIYKK IQDGVFDVSN ESYGIKVGYV VPGQSGGAGS SSQGGGCCS // ID RB2B_MAIZE STANDARD; PRT; 210 AA. AC P49104; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ras-related protein Rab-2-B. GN RAB2B. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Laughner B.J., Ferl R.J., Almira E.C.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protein transport. Probably involved in vesicular CC traffic (By similarity). CC -!- SUBCELLULAR LOCATION: Associated with a structure having the CC characteristics of an intermediate compartment between the CC endoplasmic reticulum and the Golgi apparatus (By similarity). CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U22433; AAA63902.1; -. DR PIR; T02248; T02248. DR HSSP; P05713; 3RAB. DR MaizeDB; 121973; -. DR InterPro; IPR003579; GTPase_Rab. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Lipoprotein; Prenylation; Protein transport. FT NP_BIND 13 20 GTP (By similarity). FT NP_BIND 61 65 GTP (By similarity). FT NP_BIND 119 122 GTP (By similarity). FT DOMAIN 35 43 Effector region (By similarity). FT LIPID 208 208 S-geranylgeranyl cysteine FT (By similarity). FT LIPID 209 209 S-geranylgeranyl cysteine FT (By similarity). SQ SEQUENCE 210 AA; 23061 MW; AD881F3018F28CBF CRC64; MSYAYLFKYI IIGDTGVGKS CLLLQFTDKR FQPVHDLTIG VEFGARMITI DNKPIKLQIW DTAGQESFRS ITRSYYRGAA GALLVYDITR RETFNHLASW LEDARQHANA NMTIMLVGNK CDLSHRRAVS YEEGEQFAKE HGLIFMEASA KTAQNVEEAF VKTAGAIYKK IQDGVFDVSN ESYGIKVGYA IPGQSGGAGS SSSQGGGCCS // ID RBL_MAIZE STANDARD; PRT; 476 AA. AC P00874; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Ribulose bisphosphate carboxylase large chain precursor (EC 4.1.1.39) DE (RuBisCO large subunit). GN RBCL. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA McIntosh L., Poulsen C., Bogorad L.; RT "Chloroplast gene sequence for the large subunit of ribulose RT bisphosphatecarboxylase of maize."; RL Nature 288:556-560(1980). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Leaf; RX MEDLINE=93021154; PubMed=1404415; RA Gaut B.S., Muse S.V., Clark W., Clegg M.T.; RT "Relative rates of nucleotide substitution at the rbcL locus of RT monocotyledonous plants."; RL J. Mol. Evol. 35:292-303(1992). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- CC ribulose 1,5-bisphosphate, the primary event in photosynthetic CC carbon dioxide fixation, as well as the oxidative fragmentation of CC the pentose substrate in the photorespiration process. Both CC reactions occur simultaneously and in competition at the same CC active site. CC -!- CATALYTIC ACTIVITY: D-ribulose 1,5-bisphosphate + CO(2) + H(2)O = CC 2 3-phospho-D-glycerate. CC -!- CATALYTIC ACTIVITY: D-ribulose 1,5-bisphosphate + O(2) = CC 3-phospho-D-glycerate + 2-phosphoglycolate. CC -!- SUBUNIT: 8 large chains + 8 small chains. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V00171; CAA23474.1; -. DR EMBL; Z11973; CAA78027.1; -. DR EMBL; X86563; CAA60294.1; -. DR PIR; A01093; RKZML. DR PIR; S58560; S58560. DR HSSP; P09657; 1BXN. DR Gramene; P00874; -. DR MaizeDB; 69185; -. DR InterPro; IPR000685; RuBisCO_large. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR PROSITE; PS00157; RUBISCO_LARGE; 1. KW Photosynthesis; Carbon dioxide fixation; Photorespiration; KW Lyase; Oxidoreductase; Monooxygenase; Chloroplast; Acetylation. FT PROPEP 1 2 By similarity. FT CHAIN 3 476 Ribulose bisphosphate carboxylase large FT chain. FT MOD_RES 3 3 ACETYLATION (BY SIMILARITY). FT ACT_SITE 201 201 Binding of CO(2) activates the enzyme. FT CONFLICT 63 63 T -> AA (in Ref. 1). FT CONFLICT 153 153 H -> R (in Ref. 1). FT CONFLICT 155 155 I -> M (in Ref. 1). FT CONFLICT 228 228 A -> S (in Ref. 1). FT CONFLICT 248 248 E -> D (in Ref. 1). FT CONFLICT 253 253 R -> G (in Ref. 1). FT CONFLICT 259 259 E -> Q (in Ref. 1). FT CONFLICT 291 291 Missing (in Ref. 1). FT CONFLICT 394 394 F -> L (in Ref. 1). FT CONFLICT 415 415 P -> H (in Ref. 1). FT CONFLICT 441 443 GNE -> VQ (in Ref. 1). SQ SEQUENCE 476 AA; 52701 MW; 07ECB650E0C8F6E3 CRC64; MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQLGVPP EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGDPDQYICY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRACY ECLRGGLDFT KDDENVNSQP FMRWRDRFVF CAEAIYKAQA ETGEIKGHYL NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERE ITLGFVDLLR DDFIEKDRSR GIFFTQDWVS MPGVIPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAAAN RVALEACVQA RNEGRDLARE GNEIIKAACK WSAELAAACE IWKEIKFDGF KAMDTI // ID RBS_MAIZE STANDARD; PRT; 170 AA. AC P05348; Q43355; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Ribulose bisphosphate carboxylase small chain, chloroplast precursor DE (EC 4.1.1.39) (RuBisCO small subunit). GN RBCS. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88139216; PubMed=3436948; RA Matsuoka M., Kano-Murakami Y., Tanaka Y., Ozeki Y., Ymamoto N.; RT "Nucleotide sequence of cDNA encoding the small subunit of RT ribulose-1,5-bisphosphate carboxylase from maize."; RL J. Biochem. 102:673-676(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. F2; RX MEDLINE=87231019; PubMed=3588298; RA Lebrun M., Waksman G., Freyssinet G.; RT "Nucleotide sequence of a gene encoding corn RT ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit RT (rbcs)."; RL Nucleic Acids Res. 15:4360-4360(1987). RN [3] RP SEQUENCE OF 48-170. RX MEDLINE=89134398; PubMed=3066367; RA Ren L., Salnikow J., Vater J.; RT "Ribulose-1,5-bisphosphate carboxylase/oxygenase from Zea mays: RT amino-acid sequence of the small subunit."; RL Biol. Chem. Hoppe-Seyler 369:609-615(1988). RN [4] RP SEQUENCE OF 1-10 FROM N.A. RX MEDLINE=92361248; PubMed=1822995; RA Schaffner A.R., Sheen J.; RT "Maize rbcS promoter activity depends on sequence elements not found RT in dicot rbcS promoters."; RL Plant Cell 3:997-1012(1991). CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- CC ribulose 1,5-bisphosphate, the primary event in photosynthetic CC carbon dioxide fixation, as well as the oxidative fragmentation of CC the pentose substrate in the photorespiration process. Both CC reactions occur simultaneously and in competition at the same CC active site. CC -!- CATALYTIC ACTIVITY: D-ribulose 1,5-bisphosphate + CO(2) + H(2)O = CC 2 3-phospho-D-glycerate. CC -!- CATALYTIC ACTIVITY: D-ribulose 1,5-bisphosphate + O(2) = CC 3-phospho-D-glycerate + 2-phosphoglycolate. CC -!- SUBUNIT: 8 large chains + 8 small chains. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the RuBisCO small chain family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D00170; BAA00120.1; -. DR EMBL; X06535; CAA29784.1; -. DR EMBL; Y00322; CAA68419.1; -. DR EMBL; S42508; AAD13825.1; -. DR EMBL; S42568; AAD13826.1; -. DR PIR; S00534; RKZMS. DR MaizeDB; 62391; -. DR InterPro; IPR000894; RuBisCO_small. DR Pfam; PF00101; RuBisCO_small; 1. DR PRINTS; PR00152; RUBISCOSMALL. DR ProDom; PD000290; RuBisCO_small; 1. KW Photosynthesis; Carbon dioxide fixation; Photorespiration; KW Lyase; Oxidoreductase; Monooxygenase; Chloroplast; Transit peptide. FT TRANSIT 1 47 Chloroplast. FT CHAIN 48 170 Ribulose bisphosphate carboxylase small FT chain. FT VARIANT 53 53 A -> I. FT VARIANT 81 82 LR -> IV. FT VARIANT 85 85 W -> E. FT VARIANT 92 92 S -> V. FT VARIANT 94 94 V -> L. FT VARIANT 124 124 N -> T. FT VARIANT 128 128 Q -> L. FT VARIANT 132 132 E -> V. FT VARIANT 138 139 KS -> AA. FT VARIANT 142 142 D -> G. FT VARIANT 153 154 IK -> VR. FT VARIANT 163 163 A -> L. FT VARIANT 165 165 K -> G. FT CONFLICT 81 81 Missing (in Ref. 2). SQ SEQUENCE 170 AA; 19151 MW; 4625A5FDED3C2663 CRC64; MAPTVMMASS ATAVAPFQGL KSTASLPVAR RSSRSLGNVS NGGRIRCMQV WPAYGNKKFE TLSYLPPLST DDLLKQVDYL LRNGWIPCLE FSKVGFVYRE NSTSPCYYDG RYWTMWKLPM FGCNDATQVY KELQEAIKSY PDAFHRVIGF DNIKQTQCVS FIAYKPPGSD // ID RCA_MAIZE STANDARD; PRT; 433 AA. AC Q9ZT00; DT 16-OCT-2001 (Rel. 40, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ribulose bisphosphate carboxylase/oxygenase activase, chloroplast DE precursor (RuBisCO activase) (RA). GN RCA1 OR RCA. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Chalqueno; TISSUE=Leaf; RA Ayala-Ochoa A., Loza-Tavera H., Sanchez de Jimenez E.; RT "A cDNA from maize (Zea mays L) encoding ribulose-1,5-bisphosphate RT carboxylase/oxygenase activase."; RL (In) Plant Gene Register PGR98-207. RN [2] RP REVISIONS TO 57-68; 160; 219 AND 347. RA Ayala-Ochoa A., Loza-Tavera H., Sanchez de Jimenez E.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Activation of RuBisCO (ribulose-1,5-bisphosphate CC carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent CC carboxylation of the epsilon-amino group of lysine leading to a CC carbamate structure. CC -!- SUBCELLULAR LOCATION: Chloroplast stroma. CC -!- SIMILARITY: Belongs to the RuBisCO activase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF084478; AAC97932.3; -. DR MaizeDB; 114858; -. DR InterPro; IPR003959; AAA_ATPase_centr. DR Pfam; PF00004; AAA; 1. KW Chloroplast; Transit peptide; ATP-binding. FT TRANSIT 1 53 Chloroplast (Potential). FT CHAIN 54 433 Ribulose bisphosphate FT carboxylase/oxygenase activase. FT NP_BIND 161 168 ATP (Potential). SQ SEQUENCE 433 AA; 47938 MW; 5730A336E6D378D2 CRC64; MAAAFSSTVG APASTPTRSS FLGKKLNKPQ VSAAVTYHGK SSSSNSRFKA MAAKEVDETK QTDEDRWKGL AYDISDDQQD ITRGKGLVDN LFQAPMGDGT HVAVLSSYDY ISQGQKSYNF DNMMDGFYIA KGFMDKLVVH LSKNFMTLPN IKVPLILGIW GGKGQGKSFQ CELVFAKMGI TPIMMSAGEL ESGNAGEPAK LIRQRYREAS DLIKKGKMSC LFINDLDAGA GRMGGTTQYT VNNQMVNATL MNIADNPTNV QLPGMYNKED NPRVPIIVTG NDFSTLYAPL IRDGRMEKFY WAPTREDRIG VCKGIFRTDG VDEEHVVQLV DTFPGQSIDF FGALRARVYD DEVRRWVSET GVENIARKLV NSKEGPPTFE QPKITIEKLL EYGHMLVAEQ ENVKRVQLAD KYLNEAALGE ANEDAMKTGS FFK // ID RIP3_MAIZE STANDARD; PRT; 300 AA. AC P25891; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Ribosome-inactivating protein 3 (rRNA N-glycosidase) (EC 3.2.2.22) DE (B-32 protein). GN CRIP3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92338851; PubMed=1633495; RA Bass H.W., Webster C., Obrian G.R., Roberts J.K.M., Boston R.S.; RT "A maize ribosome-inactivating protein is controlled by the RT transcriptional activator Opaque-2."; RL Plant Cell 4:225-234(1992). CC -!- FUNCTION: Possesses features of some constitutive defense agent. CC The coordinate Opaque-2-controlled synthesis of this protein and CC the major seed storage proteins (zeins) may provide the CC germinating seedling with both nutritional benefits and protection CC against pathogen invasion of the surrounding endosperm. CC -!- CATALYTIC ACTIVITY: Endohydrolysis of the N-glycosidic bond at one CC specific adenosine on the 28S rRNA. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- TISSUE SPECIFICITY: Accumulates to high levels in seeds. CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. CC Type 1 RIP subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M83926; AAA33453.1; -. DR MaizeDB; 30000; -. DR InterPro; IPR001574; RIP. DR Pfam; PF00161; RIP; 1. DR PRINTS; PR00396; SHIGARICIN. DR PROSITE; PS00275; SHIGA_RICIN; 1. KW Plant defense; Protein synthesis inhibitor; Hydrolase; Toxin; KW Multigene family. FT ACT_SITE 207 207 By similarity. FT DOMAIN 183 188 Poly-Ala. SQ SEQUENCE 300 AA; 33257 MW; 6877DBE944F7A127 CRC64; MAEITLEPSD LMAQTNKRIV PKFTEIFPVE DANYPYSAFI ASVRKDVIKH CTDHKGIFQP VLPPEKKVPE LWLYTELKTR TSSITLAIRM DNLYLVGFRT PGGVWWEFGK DGDTHLLGDN PRWLGFGGRY QDLIGNKGLE TVTMGRAEMT RAVNDLAKKK KMATLEEEEV QMQMQMPEAA DLAAAAAADP QADTKSKLVK LVVMVCEGLR FNTVSRTVDA GFNSQHGVTL TVTQGKQVQK WDRISKAAFE WADHPTAVIP DMQKLGIKDK NEAARIVALV KNQTTACATA ASADNDDDEA // ID RIP9_MAIZE STANDARD; PRT; 304 AA. AC P25892; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Ribosome-inactivating protein 9 (EC 3.2.2.22) (rRNA N-glycosidase) DE (B-32 protein). GN CRIP9. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 282-301. RC STRAIN=cv. W64A; RX MEDLINE=92338851; PubMed=1633495; RA Bass H.W., Webster C., Obrian G.R., Roberts J.K.M., Boston R.S.; RT "A maize ribosome-inactivating protein is controlled by the RT transcriptional activator Opaque-2."; RL Plant Cell 4:225-234(1992). CC -!- FUNCTION: Possesses features of some constitutive defense agent. CC The coordinate Opaque-2-controlled synthesis of this protein and CC the major seed storage proteins (zeins) may provide the CC germinating seedling with both nutritional benefits and protection CC against pathogen invasion of the surrounding endosperm. CC -!- CATALYTIC ACTIVITY: Endohydrolysis of the N-glycosidic bond at one CC specific adenosine on the 28S rRNA. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- TISSUE SPECIFICITY: Accumulates to high levels in seeds. CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. CC Type 1 RIP subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M83927; AAA33454.1; -. DR MaizeDB; 30000; -. DR InterPro; IPR001574; RIP. DR Pfam; PF00161; RIP; 1. DR PRINTS; PR00396; SHIGARICIN. DR PROSITE; PS00275; SHIGA_RICIN; 1. KW Plant defense; Protein synthesis inhibitor; Hydrolase; Toxin; KW Multigene family. FT ACT_SITE 208 208 By similarity. FT DOMAIN 183 189 Poly-Ala. FT DOMAIN 287 295 Poly-Ala. SQ SEQUENCE 304 AA; 33514 MW; 978789A2DD2BBF3C CRC64; MAETNPELSD LMAQTNKKIV PKFTEIFPVE DVNYPYSAFI ASVRKDVIKH CTDHKGIFQP VLPPEKKVPE LWFYTELKTR TSSITLAIRM DNLYLVGFRT PGGVWWEFGK AGDTHLLGDN PRWLGFGGRY QDLIGNKGLE TVTMGRAEMT RAVNDLAKKK KMATLEEEEV QMQMQMPEAA ELAAAAAAAD PQADTKSKLV KLVVMVCEGL RFNTVSRTVD AGFNSQHGVT LTVTQGKQVQ KWDRISKAAF EWADHPTAVI PDMQKLGIKD KNEAARIVAL VKNQTTAAAA AATAASADND DDEA // ID RIPX_MAIZE STANDARD; PRT; 301 AA. AC P28522; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Ribosome-inactivating protein precursor (EC 3.2.2.22) (rRNA N- DE glycosidase). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 13-49; 155-161 AND 187-215. RX MEDLINE=92078221; PubMed=1744135; RA Walsh T.A., Morgan A.E., Hey T.D.; RT "Characterization and molecular cloning of a proenzyme form of a RT ribosome-inactivating protein from maize. Novel mechanism of RT proenzyme activation by proteolytic removal of a 2.8-kilodalton RT internal peptide segment."; RL J. Biol. Chem. 266:23422-23427(1991). CC -!- FUNCTION: Potent catalytic inactivator of eukaryotic protein CC synthesis. It may be a component of natural defense mechanisms CC involved in protecting the kernel against soil-borne fungal CC infections. CC -!- CATALYTIC ACTIVITY: Endohydrolysis of the N-glycosidic bond at one CC specific adenosine on the 28S rRNA. CC -!- SUBUNIT: Synthesized and stored in the kernel as a 34 kDa inactive CC precursor. During germination, this neutral precursor is converted CC into a basic, active form by limited proteolysis, which removes CC 25 AA of net charge -6 from the center of the polypeptide chain. CC Additional processing also occurs at the N- and C-termini of the CC polypeptide. A two-chain active RIP (comprised of 16.5 and 8.5 kDa CC fragments that remain tightly associated) is produced from this CC processing event. CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. CC Type 1 RIP subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77122; AAA33508.1; -. DR PIR; A41590; RLZMRI. DR MaizeDB; 30000; -. DR InterPro; IPR001574; RIP. DR Pfam; PF00161; RIP; 1. DR PRINTS; PR00396; SHIGARICIN. DR PROSITE; PS00275; SHIGA_RICIN; 1. KW Plant defense; Protein synthesis inhibitor; Hydrolase; Toxin; Zymogen; KW Multigene family. FT PROPEP 1 16 Or 12 (in 10% of the molecules). FT CHAIN 17 161 Ribosome-inactivating protein alpha FT chain. FT PROPEP 162 186 FT CHAIN 187 ?257 Ribosome-inactivating protein beta FT chain. FT PROPEP ?258 301 FT ACT_SITE 207 207 By similarity. SQ SEQUENCE 301 AA; 33330 MW; C73F599A2121D360 CRC64; MAEITLEPSD LMAQTNKRIV PKFTEIFPVE DANYPYSAFI ASVRKDVIKH CTDHKGIFQP VLPPEKKVPE LWFYTELKTR TSSITLAIRM DNLYLVGFRT PGGVWWEFGK DGDTHLLGDN PRWLGFGGRY QDLIGNKGLE TVTMGRAEMT RAVNDLAKKK KMATLEEEEV KMQMQMPEAA DLAAAAAADP QADTKSKLVK LVVMVCEGLR FNTVSRTVDA GFNSQHGVTL TVTQGKQVQK WDRISKAAFE WADHPTAVIP DMQKLGIKDK NEAARIVALV KNQTTAAAAT AASADNDDDE A // ID RK14_MAIZE STANDARD; PRT; 123 AA. AC P08529; DT 01-AUG-1988 (Rel. 08, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Chloroplast 50S ribosomal protein L14. GN RPL14. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88111635; PubMed=2828044; RA Markmann-Mulisch U., Subramanian A.R.; RT "Nucleotide sequence and linkage map position of the genes for RT ribosomal proteins L14 and S8 in the maize chloroplast genome."; RL Eur. J. Biochem. 170:507-514(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SIMILARITY: Belongs to the L14P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06734; CAA29912.1; -. DR EMBL; X86563; CAA60322.1; -. DR PIR; S00279; R5ZM14. DR HSSP; P04450; 1WHI. DR Gramene; P08529; -. DR MaizeDB; 67056; -. DR InterPro; IPR000218; Ribosomal_L14. DR InterPro; IPR005745; Ribosomal_L14b/o. DR Pfam; PF00238; Ribosomal_L14; 1. DR ProDom; PD001093; Ribosomal_L14; 1. DR TIGRFAMs; TIGR01067; rplN_bact; 1. DR PROSITE; PS00049; RIBOSOMAL_L14; 1. KW Ribosomal protein; Chloroplast. SQ SEQUENCE 123 AA; 13494 MW; D5489FF50FF95C9D CRC64; MIQPQTLLNV ADNSGARKLM CIRVIGAAGN QRYARIGDVI IAVIKDAVPQ MPLERSEVIR AVIVRTRKEF KGDDGIIIRY DDNAAVIIDQ KGNPKGTRVF GAVAEELREL NLTKIVSLAP EVL // ID RK16_MAIZE STANDARD; PRT; 136 AA. AC P08528; DT 01-AUG-1988 (Rel. 08, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Chloroplast 50S ribosomal protein L16. GN RPL16. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [2] RP SEQUENCE OF 4-136 FROM N.A. RX MEDLINE=87092362; PubMed=3025853; RA Gold B., Carrillo N., Tewari K.K., Bogorad L.; RT "Nucleotide sequence of a preferred maize chloroplast genome template RT for in vitro DNA synthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 84:194-198(1987). RN [3] RP SEQUENCE OF 88-136 FROM N.A. RX MEDLINE=88111635; PubMed=2828044; RA Markmann-Mulisch U., Subramanian A.R.; RT "Nucleotide sequence and linkage map position of the genes for RT ribosomal proteins L14 and S8 in the maize chloroplast genome."; RL Eur. J. Biochem. 170:507-514(1988). CC -!- SIMILARITY: Belongs to the L16P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60323.1; -. DR EMBL; M15176; AAA84482.1; ALT_INIT. DR EMBL; X06734; CAA29911.1; -. DR PIR; S58589; S58589. DR Gramene; P08528; -. DR MaizeDB; 67057; -. DR InterPro; IPR000114; Ribosomal_L16. DR Pfam; PF00252; Ribosomal_L16; 1. DR PRINTS; PR00060; RIBOSOMALL16. DR TIGRFAMs; TIGR01164; rplP_bact; 1. DR PROSITE; PS00586; RIBOSOMAL_L16_1; 1. DR PROSITE; PS00701; RIBOSOMAL_L16_2; 1. KW Ribosomal protein; Chloroplast. SQ SEQUENCE 136 AA; 15531 MW; 46B68633847F52CD CRC64; MLSPKRTRFR KQHRGRMKGK SCRGNHICFG RYALQVLEPA WITARQIEAG RRAMTRYARR GGKIWVRIFP DKPVTIRPTE TRMGSGKGSP EYWVAVVKPG RILYEMSGVS ETVARAAISI AASKMPIRSQ FLRLEI // ID RK20_MAIZE STANDARD; PRT; 118 AA. AC P26566; DT 01-AUG-1992 (Rel. 23, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast 50S ribosomal protein L20. GN RPL20. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9CMSSR37; TISSUE=Leaf; RX MEDLINE=92119264; PubMed=1732000; RA Wegloehner W., Subramanian A.R.; RT "Nucleotide sequence of a region of maize chloroplast DNA containing RT the 3' end of clpP, exon 1 of rps12 and rpl20 and their RT cotranscription."; RL Plant Mol. Biol. 18:415-418(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: This protein binds directly to 23S ribosomal RNA and is CC necessary for the in vitro assembly process of the 50s ribosomal CC subunit. It is not involved in the protein synthesizing functions CC of that subunit (By similarity). CC -!- SIMILARITY: Belongs to the L20P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60548; CAA43040.1; -. DR EMBL; X86563; CAA60308.1; -. DR PIR; S19128; R5ZM20. DR Gramene; P26566; -. DR MaizeDB; 67051; -. DR HAMAP; MF_00382; -; 1. DR InterPro; IPR005813; Ribosomal_L20. DR InterPro; IPR005812; Ribosomal_L20b/o. DR Pfam; PF00453; Ribosomal_L20; 1. DR PRINTS; PR00062; RIBOSOMALL20. DR ProDom; PD002389; L20; 1. DR TIGRFAMs; TIGR01032; rplT_bact; 1. DR PROSITE; PS00937; RIBOSOMAL_L20; 1. KW Ribosomal protein; rRNA-binding; Chloroplast. FT INIT_MET 0 0 By similarity. SQ SEQUENCE 118 AA; 14108 MW; D4786194C09EA2D9 CRC64; TRVPRGYIAR RRRTKMRSFA SNFRGAHLRL NRVITQQVRR AFVSSHRDRG RQKRDFRRLW ITRINAATRV YNVFNSYSKL IHNLSKKELI LNRKMLAQVA VSNPNNLYTI SNKIRIIN // ID RK22_MAIZE STANDARD; PRT; 148 AA. AC P06589; DT 01-JAN-1988 (Rel. 06, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Chloroplast 50S ribosomal protein L22. GN RPL22. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87231016; PubMed=3295778; RA McLaughlin W.E., Larrinua I.M.; RT "The sequence of the maize plastid encoded rpl 22 locus."; RL Nucleic Acids Res. 15:4356-4357(1987). RN [2] RP REVISIONS. RX MEDLINE=92007753; PubMed=1915281; RA Gantt J.S., Baldauf S.L., Calie P.J., Weeden N.F., Palmer J.D.; RT "Transfer of rpl22 to the nucleus greatly preceded its loss from the RT chloroplast and involved the gain of an intron."; RL EMBO J. 10:3073-3078(1991). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SIMILARITY: Belongs to the L22P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00329; CAA68422.1; ALT_SEQ. DR EMBL; X86563; CAA60325.1; -. DR PIR; S58591; S58591. DR HSSP; P48286; 1BXE. DR Gramene; P06589; -. DR MaizeDB; 66429; -. DR InterPro; IPR001063; Ribosomal_L22. DR InterPro; IPR005727; Ribosomal_L22b/o. DR Pfam; PF00237; Ribosomal_L22; 1. DR ProDom; PD001032; Ribosomal_L22; 1. DR TIGRFAMs; TIGR01044; rplV_bact; 1. DR PROSITE; PS00464; RIBOSOMAL_L22; 1. KW Ribosomal protein; rRNA-binding; Chloroplast. SQ SEQUENCE 148 AA; 17655 MW; CB170DC7DAD45C10 CRC64; MTSFKLVKYT PRIKKKKGLR KLARKVPTDR LLKFERVFKA QKRIHMSVFK AQRVLDEIRW RYYEETVMIL NLMPYRASYP ILKLVYSAAA NATHYRDFDK TNLFITKAEV SRSTIMKKFR PRARGRSYSI KKTMCNITIV LNIVKKSK // ID RK23_MAIZE STANDARD; PRT; 93 AA. AC P09387; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Chloroplast 50S ribosomal protein L23. GN RPL23-A AND RPL23-B. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88335565; PubMed=3419911; RA McLaughlin W.E., Larrinua I.M.; RT "The sequence of the maize plastid encoded rpl 23 locus."; RL Nucleic Acids Res. 16:8183-8183(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE OF 81-93 FROM N.A. RX MEDLINE=91367263; PubMed=1653905; RA Hoch B., Maier R.M., Appel K., Igloi G.L., Koessel H.; RT "Editing of a chloroplast mRNA by creation of an initiation codon."; RL Nature 353:178-180(1991). CC -!- SIMILARITY: Belongs to the L23P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07864; CAA30712.1; -. DR EMBL; X86563; CAA60330.1; -. DR EMBL; X86563; CAA60370.1; -. DR EMBL; X62070; CAA43984.1; -. DR PIR; S01396; R5ZM23. DR Gramene; P09387; -. DR MaizeDB; 66085; -. DR InterPro; IPR001014; Ribosomal_L23. DR Pfam; PF00276; Ribosomal_L23; 1. DR ProDom; PD001141; Ribosomal_L23; 1. DR PROSITE; PS00050; RIBOSOMAL_L23; 1. KW Ribosomal protein; Chloroplast; rRNA-binding. SQ SEQUENCE 93 AA; 10737 MW; 720C2D893CF77566 CRC64; MDGIKYAVFT EKSLRLLGKN QYTFNVESGF TKTEIKHWVE LFFGVKVVAV NSHRLPGKGR RMGPILGHTM HYRRMIITLQ PGYSIPLLDR ETN // ID RK2_MAIZE STANDARD; PRT; 273 AA. AC P17788; DT 01-AUG-1990 (Rel. 15, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Chloroplast 50S ribosomal protein L2. GN RPL2-A AND RPL2-B. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9CMSSR37; RX MEDLINE=90332419; PubMed=2377464; RA Kavousi M., Giese K., Larrinua I.M., Subramanian A.R.; RT "Nucleotide sequence and map positions of the duplicated gene for RT maize (Zea mays) chloroplast ribosomal protein L2."; RL Nucleic Acids Res. 18:4244-4244(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE OF 1-150 FROM N.A., AND RNA EDITING OF INITIATOR METHIONINE. RX MEDLINE=91367263; PubMed=1653905; RA Hoch B., Maier R.M., Appel K., Igloi G.L., Koessel H.; RT "Editing of a chloroplast mRNA by creation of an initiation codon."; RL Nature 353:178-180(1991). RN [4] RP RNA EDITING OF INITIATOR METHIONINE. RC TISSUE=Seedling; RX MEDLINE=94073219; PubMed=8252066; RA Freyer R., Hoch B., Neckermann K., Maier R.M., Koessel H.; RT "RNA editing in maize chloroplasts is a processing step independent of RT splicing and cleavage to monocistronic mRNAs."; RL Plant J. 4:621-629(1993). CC -!- SUBUNIT: Part of the 50S ribosomal subunit. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- RNA EDITING: Modified_positions=1; Note=The initiator methionine CC is created by RNA editing. CC -!- SIMILARITY: Belongs to the L2P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53066; CAA37241.1; -. DR EMBL; X86563; CAA60329.1; -. DR EMBL; X86563; CAA60371.1; -. DR EMBL; X62070; CAA43983.1; -. DR PIR; S10500; R5ZM2. DR HSSP; P04257; 1RL2. DR MaizeDB; 66413; -. DR HAMAP; MF_01320; -; 1. DR InterPro; IPR002171; Ribosomal_L2. DR InterPro; IPR005880; Ribosomal_L2_b/o. DR Pfam; PF00181; Ribosomal_L2; 1. DR Pfam; PF03947; Ribosomal_L2_C; 1. DR TIGRFAMs; TIGR01171; rplB_bact; 1. DR PROSITE; PS00467; RIBOSOMAL_L2; 1. KW Ribosomal protein; Chloroplast; RNA editing. SQ SEQUENCE 273 AA; 30065 MW; BA65197231EA3CA0 CRC64; MAKHLYKTPI PSTRKGTVDR QVKSNPRNKL IHGRHRCGKG RNARGIITAR HRGGGHKRLY RKIDFRRNQK DISGRIITIE YDPNRNAYIC LIHYGDGEKR YILHPRGAII GDTIVSGTKV PISMGNALPL TDMPLGTAIH NIEITRGRGG QLARAAGAVA KLIAKEGKLA TLRLPSGEVR LVSQNCLATV GQVGNVGVNQ KSLGRAGSKC WLGKRPVVRG VVMNPVDHPH GGGEGKAPIG RKKPTTPWGY PALGRRTRKR KKYSDSFILR RRK // ID RK32_MAIZE STANDARD; PRT; 58 AA. AC Q05566; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast 50S ribosomal protein L32. GN RPL32. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93184210; PubMed=8443346; RA Wegloehner W., Subramanian A.R.; RT "Nucleotide sequence of maize chloroplast rpl32: completing the RT apparent set of plastid ribosomal protein genes and their tentative RT operon organization."; RL Plant Mol. Biol. 21:543-548(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SIMILARITY: Belongs to the L32P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60347.1; -. DR EMBL; X64099; CAA45467.1; -. DR PIR; S31306; S31306. DR Gramene; Q05566; -. DR MaizeDB; 67049; -. DR HAMAP; MF_00340; -; 1. DR InterPro; IPR002677; Ribosomal_L32p. DR Pfam; PF01783; Ribosomal_L32p; 1. KW Ribosomal protein; Chloroplast. FT INIT_MET 0 0 By similarity. SQ SEQUENCE 58 AA; 6728 MW; 1005003FAB9BF60E CRC64; AVPKKRTSMS KKRIRKNLWK KKTYFSIVQS YSLAKSRSFS RGNEHPKPKG FSGQQANK // ID RK33_MAIZE STANDARD; PRT; 65 AA. AC P25461; DT 01-MAY-1992 (Rel. 22, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast 50S ribosomal protein L33. GN RPL33. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9CMSSR37; TISSUE=Leaf; RX MEDLINE=91160712; PubMed=1840527; RA Wegloehner W., Subramanian A.R.; RT "A heptapeptide repeat contributes to the unusual length of RT chloroplast ribosomal protein S18. Nucleotide sequence and map RT position of the rpl33-rps18 gene cluster in maize."; RL FEBS Lett. 279:193-197(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SIMILARITY: Belongs to the L33P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56673; CAA39995.1; -. DR EMBL; X86563; CAA60306.1; -. DR PIR; S13611; R5ZM33. DR Gramene; P25461; -. DR MaizeDB; 67055; -. DR HAMAP; MF_00294; -; 1. DR InterPro; IPR001705; Ribosomal_L33. DR Pfam; PF00471; Ribosomal_L33; 1. DR ProDom; PD002595; Ribosomal_L33; 1. DR TIGRFAMs; TIGR01023; rpmG_bact; 1. DR PROSITE; PS00582; RIBOSOMAL_L33; 1. KW Ribosomal protein; Chloroplast. FT INIT_MET 0 0 By similarity. SQ SEQUENCE 65 AA; 7617 MW; BFED7E7795AFCF45 CRC64; AKGKDVRIRV ILECISCVRK GTNKESTGIS RYSTQKNRHN TPGQLELRKF CRYCRKHTTH NEIKK // ID RK36_ORYSA STANDARD; PRT; 37 AA. AC P12143; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast 50S ribosomal protein L36. GN RPL36. OS Oryza sativa (Rice), OS Zea mays (Maize), and OS Triticum aestivum (Wheat). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530, 4577, 4565; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=O.sativa; STRAIN=cv. Japonica / Nipponbare; RX MEDLINE=89364698; PubMed=2770692; RA Hiratsuka J., Shimada H., Whittier R., Ishibashi T., Sakamoto M., RA Mori M., Kondo C., Honji Y., Sun C.-R., Meng B.-Y., Li Y.-Q., RA Kanno A., Nishizawa Y., Hirai A., Shinozaki K., Sugiura M.; RT "The complete sequence of the rice (Oryza sativa) chloroplast genome: RT intermolecular recombination between distinct tRNA genes accounts for RT a major plastid DNA inversion during the evolution of the cereals."; RL Mol. Gen. Genet. 217:185-194(1989). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=88134318; PubMed=2829909; RA Markmann-Mulisch U., von Knoblauch K., Lehmann A., RA Subramanian A.R.; RT "Nucleotide sequence and linkage map position of the secX gene in RT maize chloroplast and evidence that it encodes a protein belonging to RT the 50S ribosomal subunit."; RL Biochem. Int. 15:1057-1067(1987). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; STRAIN=cv. Chinese Spring; RA Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T., RA Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., RA Gojobori T., Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., RA Tsunewaki K.; RT "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: RT complete sequence and contig clones."; RL Plant Mol. Biol. Rep. 18:243-253(2000). CC -!- SIMILARITY: Belongs to the L36P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15901; CAA33981.1; -. DR EMBL; M35956; AAA84493.1; -. DR EMBL; X86563; CAA60319.1; -. DR EMBL; AB042240; BAB47067.1; -. DR PIR; JQ0260; R5RZ36. DR PIR; S58585; S58585. DR HSSP; P80256; 1DFE. DR Gramene; P12143; -. DR MaizeDB; 67068; -. DR HAMAP; MF_00251; -; 1. DR InterPro; IPR000473; Ribosomal_L36. DR Pfam; PF00444; Ribosomal_L36; 1. DR ProDom; PD002101; Ribosomal_L36; 1. DR TIGRFAMs; TIGR01022; rpmJ_bact; 1. DR PROSITE; PS00828; RIBOSOMAL_L36; 1. KW Ribosomal protein; Chloroplast. SQ SEQUENCE 37 AA; 4447 MW; DA827429507E0515 CRC64; MKIRASVRKI CTKCRLIRRR GRIRVICSNP KHKQRQG // ID RL10_MAIZE STANDARD; PRT; 220 AA. AC P45633; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 60S ribosomal protein L10 (QM protein homolog). GN RPL10. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RX MEDLINE=94362669; PubMed=8081358; RA Neill J.D.; RT "Extreme evolutionary conservation of QM, a novel c-Jun associated RT transcription factor."; RL Hum. Mol. Genet. 3:723-728(1994). CC -!- SIMILARITY: Belongs to the L10e family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U06108; AAA17419.1; -. DR PIR; T02068; T02068. DR MaizeDB; 77933; -. DR InterPro; IPR001197; Ribosomal_L10E. DR Pfam; PF00826; Ribosomal_L10e; 1. DR TIGRFAMs; TIGR00279; L10e; 1. DR PROSITE; PS01257; RIBOSOMAL_L10E; 1. KW Ribosomal protein. SQ SEQUENCE 220 AA; 24919 MW; 5B338061E25893E8 CRC64; MGRRPARCYR QIKNKPCPKS RYCRGVPDPK IRIYDVGMKR KGVDEFPYCV HLVSWERENV SSEALEAARI VCNKYMTKSA GKDAFHLRVR VHPFHVLRIN KMLSCAGADR LQTGMRGAFG KPQGTCARVD IGQVLLSVRC KDNNAAHASE ALRRAKFKFP ARQKIIESRK WGFTKFSRAD YLKYKSEGRI VPDGVNAKLL ANHGRLEKRA PGKAFLDAVA // ID RL19_MAIZE STANDARD; PRT; 62 AA. AC Q08066; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 60S ribosomal protein L19 (Fragment). GN RPL19. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94105294; PubMed=8278499; RA Keith C.S., Hoang D.O., Barrett B.M., Feigelman B., Nelson M.C., RA Thai H., Baysdorfer C.; RT "Partial sequence analysis of 130 randomly selected maize cDNA RT clones."; RL Plant Physiol. 101:329-332(1993). CC -!- SIMILARITY: Belongs to the L19E family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95065; AAA18552.1; -. DR MaizeDB; 25469; -. DR InterPro; IPR000196; Ribosomal_L19e. DR Pfam; PF01280; Ribosomal_L19e; 1. DR ProDom; PD004823; Ribosomal_L19e; 1. DR PROSITE; PS00526; RIBOSOMAL_L19E; 1. KW Ribosomal protein. FT NON_TER 1 1 FT NON_TER 62 62 SQ SEQUENCE 62 AA; 7176 MW; AE58654959F482BC CRC64; LKLQKRLAAS YLKCGKGKVW LDPNEVSEIS MANSRQNIRK LVKDGFIIKK PHKIHSRSRC KK // ID RL32_MAIZE STANDARD; PRT; 42 AA. AC P51421; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 60S ribosomal protein L32 (Fragment). GN RPL32. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. HD5 X HD7; RA Bates E.E.M., Vergne P., Dumas C.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the L32E family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X75646; CAA53301.1; -. DR PIR; S38633; S38633. DR MaizeDB; 61651; -. DR InterPro; IPR001515; Ribosomal_L32E. DR Pfam; PF01655; Ribosomal_L32e; 1. DR ProDom; PD003823; Ribosomal_L32E; 1. DR PROSITE; PS00580; RIBOSOMAL_L32E; PARTIAL. KW Ribosomal protein. FT NON_TER 1 1 SQ SEQUENCE 42 AA; 4709 MW; FA9E004E030D1BF4 CRC64; TYCAEIAHNV STKKRKEIVE RAAQLDIVVP TKLARAPSQE DE // ID RL39_MAIZE STANDARD; PRT; 51 AA. AC P51425; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 60S ribosomal protein L39. GN RPL39 OR EC2E. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; RA Heuer S., Richerr J., Loerz H., Dresselhaus T.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the L39E family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95458; CAA64728.1; -. DR PIR; T03943; T03943. DR MaizeDB; 123917; -. DR InterPro; IPR000077; Ribosomal_L39. DR Pfam; PF00832; Ribosomal_L39; 1. DR ProDom; PD007914; Ribosomal_L39; 1. DR PROSITE; PS00051; RIBOSOMAL_L39E; 1. KW Ribosomal protein. SQ SEQUENCE 51 AA; 6513 MW; 4E776376F34FC2D6 CRC64; MPSHKTFRIK KKLAKKMRQN RPIPYWIRMR TDNTIRYNAK RRHWRRTKLG F // ID RLA1_MAIZE STANDARD; PRT; 109 AA. AC P52855; O24414; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE 60S acidic ribosomal protein P1 (L12). GN RPP1A. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RA Hamilton D.A., Turcich M.P., Bokhari-Riza A., Mascarenhas J.P.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A., AND SEQUENCE OF 18-21. RC STRAIN=cv. B73; TISSUE=Ear; RX MEDLINE=97422884; PubMed=9276949; RA Bailey-Serres J., Vangala S., Szick K., Lee C.H.; RT "Acidic phosphoprotein complex of the 60S ribosomal subunit of maize RT seedling roots. Components and changes in response to flooding."; RL Plant Physiol. 114:1293-1305(1997). CC -!- FUNCTION: Plays an important role in the elongation step of CC protein synthesis (By similarity). CC -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit CC (By similarity). CC -!- PTM: Phosphorylated. CC -!- PTM: The N-terminus is blocked. CC -!- SIMILARITY: Belongs to the L12P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U40147; AAA91168.1; -. DR EMBL; U62752; AAB71079.1; -. DR PIR; T02039; T02039. DR PIR; T02716; T02716. DR MaizeDB; 84941; -. DR InterPro; IPR001813; Ribosomal_60S. DR InterPro; IPR001859; Ribosomal_P2. DR Pfam; PF00428; 60s_ribosomal; 1. DR PRINTS; PR00456; RIBOSOMALP2. KW Ribosomal protein; Phosphorylation. FT CONFLICT 9 9 R -> T (in Ref. 2). SQ SEQUENCE 109 AA; 11096 MW; 1BFEC8E34391F080 CRC64; MASGELACRY AALILSDDGI AITAEKIATI VKAANIKVES YWPALFAKLL EKRNVEDLIL SVGSGGGAAP VAAAAPAGGA AAAAAPAVEE KKEEAKEESD DDMGFSLFD // ID RM16_MAIZE STANDARD; PRT; 185 AA. AC P27927; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Mitochondrial 60S ribosomal protein L16. GN RPL16. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91216097; PubMed=1708720; RA Hunt M.D., Newton K.J.; RT "The NCS3 mutation: genetic evidence for the expression of ribosomal RT protein genes in Zea mays mitochondria."; RL EMBO J. 10:1045-1052(1991). CC -!- SUBCELLULAR LOCATION: Mitochondrial. CC -!- SIMILARITY: Belongs to the L16P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57445; CAA40691.1; -. DR PIR; S15026; R5ZM6M. DR MaizeDB; 69578; -. DR InterPro; IPR000114; Ribosomal_L16. DR Pfam; PF00252; Ribosomal_L16; 1. DR PRINTS; PR00060; RIBOSOMALL16. DR TIGRFAMs; TIGR01164; rplP_bact; 1. DR PROSITE; PS00586; RIBOSOMAL_L16_1; 1. DR PROSITE; PS00701; RIBOSOMAL_L16_2; 1. KW Ribosomal protein; Mitochondrion. SQ SEQUENCE 185 AA; 21033 MW; F9CD590F773506A5 CRC64; MEKHLVMYLT RKSIMLLRKY LLVTEFQVSK CGSHIVKIRR DVLYPKRTKY SKYSKCRCSR GREPDGTQLG FGRYGTKSSR AGRLSYRAIE AARRATIGQF RRAMSGQFRR NCKIWVRVLA DLPITGKPAE VRMGRGKGNP TGWIARVSTG QIPFEMDGVS LSNARQAARL AAHKPCSSTK FVQWS // ID RPOA_MAIZE STANDARD; PRT; 339 AA. AC P09562; DT 01-MAR-1989 (Rel. 10, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE DNA-directed RNA polymerase alpha chain (EC 2.7.7.6) (PEP) (Plastid- DE encoded RNA polymerase alpha subunit) (RNA polymerase alpha subunit). GN RPOA. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Inrakorn; RX MEDLINE=88289331; PubMed=3399379; RA Ruf M., Koessel H.; RT "Structure and expression of the gene coding for the alpha-subunit of RT DNA-dependent RNA polymerase from the chloroplast genome of Zea RT mays."; RL Nucleic Acids Res. 16:5741-5754(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE OF 1-18. RX MEDLINE=90160360; PubMed=2304916; RA Hu J., Bogorad L.; RT "Maize chloroplast RNA polymerase: the 180-, 120-, and 38-kilodalton RT polypeptides are encoded in chloroplast genes."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1531-1535(1990). RN [4] RP SEQUENCE OF 1-9 FROM N.A. RX MEDLINE=89193772; PubMed=3149198; RA Markmann-Mulisch U., Subramanian A.R.; RT "Nucleotide sequence of maize chloroplast rpS11 with conserved amino RT acid sequence between eukaryotes, bacteria and plastids."; RL Biochem. Int. 17:655-664(1988). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: N nucleoside triphosphate = N diphosphate + CC {RNA}(N). CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core CC is composed of four subunits: alpha, beta, beta', and beta''. When CC a (nuclear-encoded) sigma factor is associated with the core the CC holoenzyme is formed, which can initiate transcription (By CC similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and CC basal transcription, whereas the C-terminal domain is involved in CC interaction with transcriptional regulators and with upstream CC promoter elements (By similarity). CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07810; CAA30670.1; -. DR EMBL; X86563; CAA60317.1; -. DR EMBL; M35831; AAA84495.1; -. DR PIR; S00977; RNZMA. DR PIR; S58583; S58583. DR HSSP; P00574; 1BDF. DR Gramene; P09562; -. DR MaizeDB; 67212; -. DR HAMAP; MF_00059; -; 1. DR InterPro; IPR009025; RBP11-like_RNApo. DR InterPro; IPR001700; RNA_polA_bac_org. DR Pfam; PF01000; RNA_pol_A_bac; 1. DR Pfam; PF03118; RNA_pol_A_CTD; 1. DR ProDom; PD001179; RNA_polA_bac_org; 1. DR SMART; SM00662; RPOLD; 1. KW Transferase; Transcription; DNA-directed RNA polymerase; Chloroplast. FT DOMAIN 1 233 Alpha N-terminal domain (alpha-NTD) (By FT similarity). FT DOMAIN 264 339 Alpha C-terminal domain (alpha-CTD) (By FT similarity). FT CONFLICT 130 130 V -> D (in Ref. 1). FT CONFLICT 208 208 S -> K (in Ref. 1). FT CONFLICT 214 215 AL -> GGI (in Ref. 1). FT CONFLICT 293 294 HT -> PSA (in Ref. 1). FT CONFLICT 300 300 S -> V (in Ref. 1). FT CONFLICT 307 308 MQ -> IK (in Ref. 1). FT CONFLICT 313 313 R -> G (in Ref. 1). SQ SEQUENCE 339 AA; 38946 MW; EA46E76F92ECA20D CRC64; MVREEITGST QTLEWKCVES RVDSKRLYYG RFILSPLRKG QADTVGIALR RALLGEIEGT CITRAKFGNV PHEYSTIVGI EESIQEILLN LKEIVLRSNL YGVRDASICV KGPRYITAQD IILPPSVEIV DTTQPIANLR EPVDFCIELQ IKRDRAYHTE LRKNSQDGSY PIDAVFMPVR NVNYSIFSCG NGNEKHEILF LEIWTNGSLT PKEALYEASR NLIDLFLPFL HTEEEGTSFE ENKNRLTPPL LTFQKRFTNL KKNKKGIPLN CIFIDQLELP SRTYNCLKRA NIHTLLDLLS KTEEDLMQIN SFRMEDGKLI WDTLEKHLPI DLPKNKFSL // ID RPOB_MAIZE STANDARD; PRT; 1075 AA. AC P16023; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE DNA-directed RNA polymerase beta chain (EC 2.7.7.6) (PEP) (Plastid- DE encoded RNA polymerase beta subunit) (RNA polymerase beta subunit). GN RPOB. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90340289; PubMed=2381419; RA Igloi G.L., Meinke A., Doery I., Koessel H.; RT "Nucleotide sequence of the maize chloroplast rpo B/C1/C2 operon: RT comparison between the derived protein primary structures from RT various organisms with respect to functional domains."; RL Mol. Gen. Genet. 221:379-394(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90175001; PubMed=2308853; RA Igloi G.L., Meinke A., Doery I., Koessel H.; RT "Nucleotide and derived amino acid sequence of rps2 from maize RT chloroplasts."; RL Nucleic Acids Res. 18:663-663(1990). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [4] RP SEQUENCE OF 1-88 FROM N.A. RX MEDLINE=90160360; PubMed=2304916; RA Hu J., Bogorad L.; RT "Maize chloroplast RNA polymerase: the 180-, 120-, and 38-kilodalton RT polypeptides are encoded in chloroplast genes."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1531-1535(1990). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: N nucleoside triphosphate = N diphosphate + CC {RNA}(N). CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core CC is composed of four subunits: alpha, beta, beta', and beta''. When CC a (nuclear-encoded) sigma factor is associated with the core the CC holoenzyme is formed, which can initiate transcription (By CC similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17318; CAA35195.1; -. DR EMBL; X86563; CAA60276.1; -. DR EMBL; M31206; AAA84490.1; -. DR PIR; S12800; RNZMB. DR HSSP; Q9KWU7; 1HQM. DR Gramene; P16023; -. DR MaizeDB; 69580; -. DR HAMAP; MF_01321; -; 1. DR InterPro; IPR007121; RNA_pol_B. DR InterPro; IPR007644; RNA_pol_Rpb2_1. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007120; RNA_pol_Rpb2_6. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 1. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. KW Transcription; Transferase; DNA-directed RNA polymerase; Chloroplast. FT CONFLICT 16 16 S -> M (in Ref. 4). SQ SEQUENCE 1075 AA; 121571 MW; 67043F73FBA6CD75 CRC64; MLRNGNEGMS TIPGFSQIQF EGFCRFINQG LAEELEKFPT IKDPDHEIAF QLFAKGYQLL EPSIKERNAV YESLTYSSEL YVSARLIFGF DVQKETISIG NIPIMNSLGT FIINGIYRIV INQILLSPGI YYRSELDHKG ISIYTGTIIS DWGGRSELAI DKKERIWARV SRKQKISILV LSSAMGSNLR EILDNVSYPE IFLSFPNAKE KKRIESKEKA ILEFYQQFAC VGGDLVFSES LCEELQKKFF QQKCELGRVG RRNMNRRLNL DIPQNNTFLL PRDVLAATDH LIGMKFGTGI LDDDDMNHLK NKRIRSVADL LQDQFGLALG RLQHAVQKTI RRVFIRQSKP TPQTLVTPTS TSILLITTYE TFFGTYPLAQ VFDQTNPLTQ TVHGRKVSCL GPGGLTGRTA SFRSRDIHPS HYGRICPIDT SEGINVGLTG SLAIHARIDH WWGSIESPFY EISEKAKEKK ERQVVYLSPN RDEYYMIAAG NSLSLNQGIQ EEQVVPARYR QEFLTIAWEQ IHVRSIFPFQ YFSIGGSLIP FIEHNDANRA LMSSNMQRQA VPLSRSEKCI VGTGLERQTA LDSRVSVIAQ REGKIISSDS HKILLSSSGK TISIPLVAHR RSNKNTCMHQ KPRVPRGKSI KKGQILAEGA ATVGGELALG KNVLVAYMPW EGYNFEDAVL ISERLVYEDI YTSFHIRKYE IQTDTTSQGS AEKITKQIPH LEEHLLRNLD RNGVVRLGSW VETGDILVGK LTPQIASESS YIAEAGLLRA IFGLEVSTSK ETSLKLPIGG RGRVIDVKWI QRDPFDIMVR VYILQKREIK VGDKVAGRHG NKGIISKILP RQDMPYLQDG APVDMVFNPL GVPSRMNVGQ IFESSLGLAG DLLKKHYRIA PFDERYEQEA SRKLVFSELY EASKQTKNPW VFEPEYPGKS RIFDGRTGDP FEQPVLIGKS YILKLIHQVD EKIHGRSTGP YSLVTQQPVR GRAKQGGQRI GEMEVWALEG FGVAHILQEI LTYKSDHLIA RQEILNATIW GKRMPNHEDP PESFRVLVRE LRSLALELNH FLVSEKNFQV NREDV // ID RPOC_MAIZE STANDARD; PRT; 683 AA. AC P16024; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE DNA-directed RNA polymerase beta' chain (EC 2.7.7.6) (PEP) (Plastid- DE encoded RNA polymerase beta' subunit) (RNA polymerase beta' subunit). GN RPOC1. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90340289; PubMed=2381419; RA Igloi G.L., Meinke A., Doery I., Koessel H.; RT "Nucleotide sequence of the maize chloroplast rpo B/C1/C2 operon: RT comparison between the derived protein primary structures from RT various organisms with respect to functional domains."; RL Mol. Gen. Genet. 221:379-394(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90175001; PubMed=2308853; RA Igloi G.L., Meinke A., Doery I., Koessel H.; RT "Nucleotide and derived amino acid sequence of rps2 from maize RT chloroplasts."; RL Nucleic Acids Res. 18:663-663(1990). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [4] RP SEQUENCE OF 1-54 FROM N.A. RX MEDLINE=90160360; PubMed=2304916; RA Hu J., Bogorad L.; RT "Maize chloroplast RNA polymerase: the 180-, 120-, and 38-kilodalton RT polypeptides are encoded in chloroplast genes."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1531-1535(1990). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: N nucleoside triphosphate = N diphosphate + CC {RNA}(N). CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core CC is composed of four subunits: alpha, beta, beta', and beta''. When CC a (nuclear-encoded) sigma factor is associated with the core the CC holoenzyme is formed, which can initiate transcription (By CC similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. CC RpoC1 subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17318; CAA35196.1; -. DR EMBL; X86563; CAA60277.1; -. DR EMBL; M31207; AAA84488.1; -. DR PIR; S12801; RNZMB1. DR HSSP; Q9KWU6; 1HQM. DR Gramene; P16024; -. DR MaizeDB; 69581; -. DR HAMAP; MF_01323; -; 1. DR InterPro; IPR000722; RNA_pol_A. DR InterPro; IPR007080; RNA_pol_Rpb1_1. DR InterPro; IPR007066; RNA_pol_Rpb1_3. DR InterPro; IPR006592; RNA_polA_N. DR Pfam; PF04997; RNA_pol_Rpb1_1; 1. DR Pfam; PF00623; RNA_pol_Rpb1_2; 1. DR Pfam; PF04983; RNA_pol_Rpb1_3; 1. DR SMART; SM00663; RPOLA_N; 1. KW Transcription; Transferase; DNA-directed RNA polymerase; Chloroplast. SQ SEQUENCE 683 AA; 78322 MW; FDBF04DEB555B30A CRC64; MIDQYKHKQL QIGLVSPQQI KAWAKKILPN GEVVGEVTRP STFHYKTDKP EKDGLFCERI FGPIKSGICA CGNSRASVRE NEDERFCQKC GVEFVDSRIR RYQMGYIKLA CPVTHVWYLK GLPSYIANLL DKPLKKLEGL VYGDFSFARP SAKKPTFLRL RGLFEDEISS CNHSISPFFS TPGFATFRNR EIATGAGAIR EQLADLDLRI IIENSLVEWK ELEDEGYSGD EWEDRKRRIR KVFLIRRMQL AKHFIQTNVE PEWMVLCLLP VLPPELRPIV YRSGDKVVTS DINELYKRVI RRNNNLAYLL KRSELAPADL VMCQEKLVQE AVDTLLDSGS RGQPTRDGHN KVYKSLSDVI EGKEGRFRET LLGKRVDYSG RSVIVVGPSL SLHQCGLPLE IAIKLFQLFV IRDLITKRAT SNVRIAKRKI WEKEPIVWEI LQEVMRGHPV LLNRAPTLHR LGIQAFQPTL VEGRTICLHP LVCKGFNADF DGDQMAVHLP LSLEAQAEAR LLMFSHMNLL SPAIGDPICV PTQDMLIGLY VLTIGNRLGI CANRYNSCGN SPNKKVNYNN NNYYKYTKDK EPHFSSSYDA LGAYRQKRIG LNSPLWLRWK LDQRIVGSRE VPIEVQYESF GTYHEIYAHY LVVGNRKKEI RSIYIRTTLG HISFYREIEE AIQGFSRAYS YTI // ID RPOD_MAIZE STANDARD; PRT; 1527 AA. AC P16025; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE DNA-directed RNA polymerase beta'' chain (EC 2.7.7.6) (PEP) (Plastid- DE encoded RNA polymerase beta'' subunit) (RNA polymerase beta'' DE subunit). GN RPOC2. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90340289; PubMed=2381419; RA Igloi G.L., Meinke A., Doery I., Koessel H.; RT "Nucleotide sequence of the maize chloroplast rpo B/C1/C2 operon: RT comparison between the derived protein primary structures from RT various organisms with respect to functional domains."; RL Mol. Gen. Genet. 221:379-394(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90175001; PubMed=2308853; RA Igloi G.L., Meinke A., Doery I., Koessel H.; RT "Nucleotide and derived amino acid sequence of rps2 from maize RT chloroplasts."; RL Nucleic Acids Res. 18:663-663(1990). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [4] RP SEQUENCE OF 1-52 FROM N.A. RX MEDLINE=90160360; PubMed=2304916; RA Hu J., Bogorad L.; RT "Maize chloroplast RNA polymerase: the 180-, 120-, and 38-kilodalton RT polypeptides are encoded in chloroplast genes."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1531-1535(1990). RN [5] RP SEQUENCE OF 1316-1527 FROM N.A. RC STRAIN=cv. FR9cms X FR37; TISSUE=Leaf; RX MEDLINE=90272437; PubMed=2140888; RA Stahl D., Rodermel S., Subramanian A.R., Bogorad L.; RT "Nucleotide sequence of a 3.46 kb region of maize chloroplast DNA RT containing the gene cluster rpoC2-rps2-atpI-atpH."; RL Nucleic Acids Res. 18:3073-3074(1990). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: N nucleoside triphosphate = N diphosphate + CC {RNA}(N). CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core CC is composed of four subunits: alpha, beta, beta', and beta''. When CC a (nuclear-encoded) sigma factor is associated with the core the CC holoenzyme is formed, which can initiate transcription (By CC similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. CC RpoC2 subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17318; CAA35197.1; -. DR EMBL; M31208; AAA84489.1; -. DR EMBL; X86563; CAA60278.1; -. DR EMBL; X52270; CAA36511.1; -. DR PIR; S12802; RNZMB2. DR HSSP; Q9KWU6; 1HQM. DR Gramene; P16025; -. DR MaizeDB; 69586; -. DR HAMAP; MF_01324; -; 1. DR InterPro; IPR007066; RNA_pol_Rpb1_3. DR InterPro; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR Pfam; PF04983; RNA_pol_Rpb1_3; 1. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 1. KW Transcription; Transferase; DNA-directed RNA polymerase; Chloroplast. FT CONFLICT 25 25 R -> S (in Ref. 4). SQ SEQUENCE 1527 AA; 176082 MW; 98BEA0C3165A8C3D CRC64; MAERANLVFH NKEIDGTAMK RLISRLIDHF GMGYTSHILD QIKTLGFHQA TTTSISLGIE DLLTIPSKGW LVQDAEQQSF LLEKHYYYGA IHAVEKLRQS VEIWYATSEY LKQEMNSNFR ITDPSNPVYL MSFSGARGNA SQVHQLVGMR GLMADPQGQM IHLPIQSNLR EGLSLTEYII SCYGARKGVV DTAVRTADAG YLTRRLVEVV QHIIVRRRDC GTIQGISVSP QNGMTEKLFV QTLIGRVLAD DIYIGSRCIA SRNQDIGIGL VNRFITAFRA QPFRAQPIYI RTPFTCRSTS WICQLCYGRS PTHGDLVELG EAVGIIAGQS IGEPGTQLTL RTFHTGGVFT GGTADLIRSP SNGKIQFNED LVHPTRTRHG QPAFLCYIDL HVTIQSQDIL HSVNIPLKSL ILVQNDQYVE SEQVIAEIRA GTSTLHFKEK VQKHIYSESD GEMHWSTDVY HAPEYQYGNL RRLPKTSHLW ILSVSMCRSS IASFSLHKDQ DQMNTYSFSV DGRYIFDFSM ANDQVSHRLL DTFGKKDREI LDYLTPDRIV FNGHWNCFYP SILQDNSDLL AKKRRNRLVV PLQYHQEQEK ERISCLGISM EIPFMGVLRR NTIFAYFDDP RYRKDKRGSG IVKFRYRTLE EEYRTQEEEY RTREEEYRTR EEDSEDEYES PENKYRTREG EGEYKILEDE YRTLEDEYET LEDEYGILED EYRTLEKDSE EEYGSLENKY RTREGEGEYE ILEEESEEEY GSSEDGSEKE YGTLEEDSEE DSEEDSEDEY GSPEEDSILK KEGFIEHRGT KEFSLKYQKE VDRFFFILQE LHILPRSSSL KVLDNSIIGV DTQLTKNTRS RLGGLVRVKR KKSHTELKIF SGDIHFPEEA DKILGGSLIP PEREKKDSKE SKKRKNWVYV QRKKFLKSKE KYFVSVRPAV AYEMDEGINL ATLFPQDLLQ EEDNLQLRLV NFISHENSKL TQRIYHTNSQ FVRTCLVVNW EQEEKEGARA SLVEVKTNDL IRDFLRIELV KSTILYTRRR YDRTSVGLIP NNRLDRNNTN SFYSKAKIQS LSQHQEVIGT LLNRNKEYPS LMILLASNCS RIGLFKNSKY PNAVKESNPR IPIRDIFGLL GVIVPSISNF SSSYYLLTHN QILLKKYLFL DNLKQTLQVL QGLKYSLIDE NKRISNFDSN IMLEPFHLNW HFLHHDSWEE TLAIIHLGQF ICENLCLFKL HIKKSGQIFI VNMDSFVLRA AKPYLATIGA TVHGHYGKIL YKGDRLVTFI YEKSRSSDIT QGLPKVEQIF EARSIDSLSP NLERRIEDWN ERIPRILGVP WGFLIGAELT IAQSRISLVN KIQKVYRSQG VQIHNRHIEI IIRQVTSKVR VSEDGMSNVF LPGELIGLLR AERAGRALDE SIYYRAILLG ITRASLNTQS FISEASFQET ARVLAKAALR GRIDWLKGLK ENVVLGGIIP VGTGFQKFVH RSPQDKNLYL EIQKKNLFAS EMRDILFLHT ELVSSDSDVT NNFYETSETP FTPIYTI // ID RPOP_MAIZE STANDARD; PRT; 1098 AA. AC P10581; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Probable DNA-directed RNA polymerase (EC 2.7.7.6) (S-2 DNA ORF1). OS Zea mays (Maize). OG Mitochondrion. OG Plasmid S-2. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Levings C.S. III, Sederoff R.R.; RT "Nucleotide sequence of the S-2 mitochondrial DNA from the S cytoplasm RT of maize."; RL Proc. Natl. Acad. Sci. U.S.A. 80:4055-4059(1983). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: N nucleoside triphosphate = N diphosphate + CC {RNA}(N). CC -!- MISCELLANEOUS: The mitochondria from the S male-sterile cytoplasm CC of maize contain unique DNA-protein complexes, designated S-1 and CC S-2. These complexes consist of double-stranded linear DNAs with CC proteins covalently attached to the 5'termini. CC -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J01426; -; NOT_ANNOTATED_CDS. DR MaizeDB; 69623; -. DR InterPro; IPR002092; RNA_pol_phage. DR Pfam; PF00940; RNA_pol; 1. DR PROSITE; PS00489; RNA_POL_PHAGE_2; 1. DR PROSITE; PS00900; RNA_POL_PHAGE_1; 1. KW Transferase; Transcription; DNA-directed RNA polymerase; KW Mitochondrion; Plasmid. FT ACT_SITE 663 663 By similarity. FT ACT_SITE 750 750 By similarity. FT ACT_SITE 915 915 By similarity. SQ SEQUENCE 1098 AA; 128016 MW; D448F26EC90FC314 CRC64; PIRESVRVST DRDPDLEDEK REQLGESMQT ELERLTWGVE VGTSEDINVD TVKRWGLQNN KYNAEHWIPP GGQRTAEDMG KLYQFWDEFI ETYENEVMMN SGYREPLNKD KVFNTLLDHS NNKTNQTAEE LKGIQTKIER MTMYFYEANV YESLGQLKNK FINIDEQTAK DYLLDKLEKP DDLDIVRAMG TYTLECIVVF VLSKQFNVFA LDKASVQVAT LVSELDSAAK IEYNRIIAED RKRKKAKWGD KQINEDENIL LQDKGVDTFN GDVHSELDRK KKSISKQTNR KRVRISKHKE PGIGEALFGW LASRKLIEVK KPVFLFDKKN KKPKNVIYPG YVDCLFDIKD LPFCSTLPMV YPPADWELWP TATAEVSDPY ITNLTPLSSY RGGYLTSLQR ESGDSPTLLS EKDYGVFDIH IDRERSQPVL SAVKKLQWQP YRINKLVYDF IQKHWSVLVS VGLLRPKNLA LFKRKEALRL LSSLLFKHEE LSTIYRYSEL KSVLLKNIHA STFELYTMKI AEAYLDYKIY FPIFLDFRGR NYRHGPFHFH ERDLVRSLII FDESDDSAAH TINSDVGDRI LHNFLISAAY HKSKFGVYRE ALEFIYNKIE DMQSKPTFFE KDIFVDTLCC RHPFQYISSC ISLKTYADTK DLSVLRYTPV FQDASASAYQ IMSYFLLDID YGIHTNLLKK TNTDGRYIRD IYEFMWGCLI KYLIAEEKIE LAIKLLTPNE KDQESVLAKI VSIFDRNVVK KMFMPMMYGK TDYTLKKDVE DLLKGKSDSE GINLISKHIS TYWKVNFGKM KDLMDLINYV SWFGAGQDKP VVYSTPYWVT LQTYKWRKRV KMKIQYETTK NNEKEVKTTS AKMLIPLNDN DIRKSSTSTF ANFIHQKDAF TAIQLVDFIN KLENASSIPI YAVHDNFITM PEYASILPTL YRDSIFRMGH PLIIINKFLF DHILIPAIQN EHPQNKHLFS VEERSMLDRM MIDLQNPLIP DFGSVDITKA RIKSIVIPKD LLLKCFSCLW MSKTKKISLV RWESCRDKII KVYMRYTDDI SSDEGVSRWL EYKNNLEFAS DPVWSSDNTN GTQADSLDKG EDDYCIHY // ID RR11_MAIZE STANDARD; PRT; 143 AA. AC P09561; DT 01-MAR-1989 (Rel. 10, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast 30S ribosomal protein S11. GN RPS11. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89193772; PubMed=3149198; RA Markmann-Mulisch U., Subramanian A.R.; RT "Nucleotide sequence of maize chloroplast rpS11 with conserved amino RT acid sequence between eukaryotes, bacteria and plastids."; RL Biochem. Int. 17:655-664(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE OF 63-143 FROM N.A. RC STRAIN=cv. Inrakorn; RX MEDLINE=88289331; PubMed=3399379; RA Ruf M., Koessel H.; RT "Structure and expression of the gene coding for the alpha-subunit of RT DNA-dependent RNA polymerase from the chloroplast genome of Zea RT mays."; RL Nucleic Acids Res. 16:5741-5741(1988). CC -!- SUBUNIT: Part of the 30S ribosomal subunit. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the S11P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M35831; AAA84494.1; -. DR EMBL; X86563; CAA60318.1; -. DR EMBL; X07810; CAA30669.1; -. DR PIR; S58584; S58584. DR Gramene; P09561; -. DR MaizeDB; 66411; -. DR HAMAP; MF_01310; -; 1. DR InterPro; IPR001971; Ribosomal_S11. DR Pfam; PF00411; Ribosomal_S11; 1. DR ProDom; PD001010; Ribosomal_S11; 1. DR PROSITE; PS00054; RIBOSOMAL_S11; 1. KW Ribosomal protein; RNA-binding; rRNA-binding; Chloroplast. FT CONFLICT 63 66 SAGT -> PPQY (in Ref. 3). SQ SEQUENCE 143 AA; 15610 MW; A01A98BA3669D9E5 CRC64; MTKAIPKIGS RKKVRIGLRR NARFSLRKSA RRITKGIIHV QASFNNTIIT VTDPQGRVVF WSSAGTCGFK SSRKASPYAG QRTAVDAIRT VGLQRAEVMV KGAGSGRDAA LRAIAKSGVR LSCIRDVTPM PHNGCRPPKK RRL // ID RR12_MAIZE STANDARD; PRT; 124 AA. AC P12340; DT 01-OCT-1989 (Rel. 12, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast 30S ribosomal protein S12. GN RPS12-A AND RPS12-B. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9CMSSR37; TISSUE=Leaf; RX MEDLINE=88033114; PubMed=2822717; RA Giese K., Subramanian A.R., Larrinua I.M., Bogorad L.; RT "Nucleotide sequence, promoter analysis, and linkage mapping of the RT unusually organized operon encoding ribosomal proteins S7 and S12 in RT maize chloroplast."; RL J. Biol. Chem. 262:15251-15255(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE OF 1-38 FROM N.A. RC STRAIN=cv. FR9cms X FR37; TISSUE=Leaf; RX MEDLINE=92119264; PubMed=1732000; RA Wegloehner W., Subramanian A.R.; RT "Nucleotide sequence of a region of maize chloroplast DNA containing RT the 3' end of clpP, exon 1 of rps12 and rpl20 and their RT cotranscription."; RL Plant Mol. Biol. 18:415-418(1992). CC -!- FUNCTION: With S4 and S5 plays an important role in translational CC accuracy. Located at the interface of the 30S and 50S subunits (By CC similarity). CC -!- SUBUNIT: Part of the 30S ribosomal subunit. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the S12P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M17841; AAA85359.1; -. DR EMBL; M17842; AAA85359.1; JOINED. DR EMBL; X86563; CAA60309.1; -. DR EMBL; X60548; CAA43039.1; -. DR PIR; S58629; S58629. DR Gramene; P12340; -. DR MaizeDB; 67069; -. DR HAMAP; MF_00403; -; 1. DR InterPro; IPR008994; Nucleic_acid_OB. DR InterPro; IPR006032; Ribosomal_S12_23. DR InterPro; IPR005679; Ribosomal_S12b/c. DR Pfam; PF00164; Ribosomal_S12; 1. DR PRINTS; PR01034; RIBOSOMALS12. DR ProDom; PD000576; Ribosomal_S12_23; 1. DR TIGRFAMs; TIGR00981; rpsL_bact; 1. DR PROSITE; PS00055; RIBOSOMAL_S12; 1. KW Ribosomal protein; RNA-binding; rRNA-binding; Chloroplast. SQ SEQUENCE 124 AA; 13822 MW; 84D1EACDCC4C2BBF CRC64; MPTVKQLIRN ARQPIRNARK SAALKGCPQR RGTCARVYTI NPKKPNSALR KVARVRLTSG FEITAYIPGI GHNLQEHSVV LVRGGRVKDL PGVRYRIIRG TLDAVAVKNR QQGRSKYGAK KPKK // ID RR14_MAIZE STANDARD; PRT; 103 AA. AC P08527; DT 01-AUG-1988 (Rel. 08, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Chloroplast 30S ribosomal protein S14. GN RPS14. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87260027; PubMed=3601681; RA Rodermel S., Orlin P., Bogorad L.; RT "The transcription termination region between two convergently- RT transcribed photoregulated operons in the maize plastid chromosome RT contains rps14, trnR (UCU) and a putative trnfM pseudogene."; RL Nucleic Acids Res. 15:5493-5493(1987). RN [2] RP SEQUENCE FROM N.A. RA Srinivasa B.R., Subramanian A.R.; RT "Nucleotide sequence and linkage map position of the gene for maize RT chloroplast ribosomal protein S14."; RL Biochemistry 26:3188-3192(1987). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SIMILARITY: Belongs to the S14P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00359; CAA68437.1; -. DR EMBL; M16559; AAA84487.1; -. DR EMBL; X86563; CAA60284.1; -. DR PIR; S00640; R3ZM14. DR Gramene; P08527; -. DR MaizeDB; 67126; -. DR InterPro; IPR001209; Ribosomal_S14. DR Pfam; PF00253; Ribosomal_S14; 1. DR PROSITE; PS00527; RIBOSOMAL_S14; 1. KW Ribosomal protein; Chloroplast. FT CONFLICT 10 10 E -> Q (in Ref. 1). FT CONFLICT 40 40 L -> F (in Ref. 2). SQ SEQUENCE 103 AA; 12122 MW; AD2032B131B3A839 CRC64; MAKKSLIQRE KKRQKLEQKY HLIRRSSKKK IRSKVSPLSL SEKTKMQEKL QSLPRNSAPT RLHRRCFLTG RPRANYRDFG LSGHILREMV YACLLPGATR SSW // ID RR15_MAIZE STANDARD; PRT; 90 AA. AC P17703; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Chloroplast 30S ribosomal protein S15. GN RPS15-A AND RPS15-B. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9CMSSR37; TISSUE=Leaf; RX MEDLINE=90287730; PubMed=2129550; RA Fitzky B., Subramanian A.R.; RT "Nucleotide sequence and map positions of the duplicated gene for RT chloroplast ribosomal protein S15 in Zea mays (maize)."; RL Nucleic Acids Res. 18:3407-3407(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SIMILARITY: Belongs to the S15P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52614; CAA36843.1; ALT_INIT. DR EMBL; X86563; CAA60355.1; ALT_INIT. DR EMBL; X86563; CAA60345.1; ALT_INIT. DR PIR; S10153; R3ZM15. DR HSSP; P80378; 1AB3. DR Gramene; P17703; -. DR MaizeDB; 67129; -. DR InterPro; IPR000589; Ribosomal_S15. DR InterPro; IPR005290; Ribosomal_S15_b. DR Pfam; PF00312; Ribosomal_S15; 1. DR ProDom; PD157043; RS15_bact; 1. DR TIGRFAMs; TIGR00952; S15_bact; 1. DR PROSITE; PS00362; RIBOSOMAL_S15; 1. KW Ribosomal protein; Chloroplast; rRNA-binding. FT CONFLICT 19 19 E -> Q (in Ref. 2). SQ SEQUENCE 90 AA; 10824 MW; EEC0034EC78421F4 CRC64; MKKKGGRKIF GFMVKEEKEE NRGSVEFQVF SFTNKIRRLA SHLELHKKDF SSERGLRRLL GKRQRLLAYL AKKNRVRYKK LISQLDIREK // ID RR16_MAIZE STANDARD; PRT; 85 AA. AC P27723; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast 30S ribosomal protein S16. GN RPS16. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9CMSSR37; TISSUE=Leaf; RX MEDLINE=92119265; PubMed=1732001; RA Kanakari S., Timmler G., von Knoblauch K., Subramanian A.R.; RT "Nucleotide sequence, map position and transcript pattern of the RT intron-containing gene for maize chloroplast ribosomal protein RT S16."; RL Plant Mol. Biol. 18:419-422(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SIMILARITY: Belongs to the S16P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60823; CAA43215.1; -. DR EMBL; X86563; CAA60267.1; -. DR PIR; S19119; R3ZM16. DR HSSP; P80379; 1EMW. DR Gramene; P27723; -. DR MaizeDB; 67053; -. DR HAMAP; MF_00385; -; 1. DR InterPro; IPR000307; Ribosomal_S16. DR Pfam; PF00886; Ribosomal_S16; 1. DR ProDom; PD003791; Ribosomal_S16; 1. DR TIGRFAMs; TIGR00002; S16; 1. DR PROSITE; PS00732; RIBOSOMAL_S16; 1. KW Ribosomal protein; Chloroplast. SQ SEQUENCE 85 AA; 10090 MW; 16E9D1615C86B8AB CRC64; MVKLRLKRCG RKQQAIYRIV AIDVRSRREG RDLRKVGFYD PIKNQTCLNV PAILYFLEKG AQPTRTVYDI LRKAEFFKDK ERTLS // ID RR18_MAIZE STANDARD; PRT; 170 AA. AC P25459; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Chloroplast 30S ribosomal protein S18. GN RPS18. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9CMSSR37; TISSUE=Leaf; RX MEDLINE=91160712; PubMed=1840527; RA Wegloehner W., Subramanian A.R.; RT "A heptapeptide repeat contributes to the unusual length of RT chloroplast ribosomal protein S18. Nucleotide sequence and map RT position of the rpl33-rps18 gene cluster in maize."; RL FEBS Lett. 279:193-197(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SUBUNIT: Part of the 30S ribosomal subunit. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the S18P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56673; CAA39996.1; -. DR EMBL; X86563; CAA60307.1; -. DR PIR; S13612; R3ZM18. DR Gramene; P25459; -. DR MaizeDB; 67054; -. DR HAMAP; MF_00270; -; 1. DR InterPro; IPR001648; Ribosomal_S18. DR Pfam; PF01084; Ribosomal_S18; 1. DR PRINTS; PR00974; RIBOSOMALS18. DR ProDom; PD002239; Ribosomal_S18; 1. DR TIGRFAMs; TIGR00165; S18; 1. DR PROSITE; PS00057; RIBOSOMAL_S18; 1. KW Ribosomal protein; RNA-binding; rRNA-binding; Chloroplast; Repeat. FT DOMAIN 4 52 7 X 7 AA tandem repeats. FT REPEAT 4 10 FT REPEAT 11 17 FT REPEAT 18 24 FT REPEAT 25 31 FT REPEAT 32 38 FT REPEAT 39 45 FT REPEAT 46 52 SQ SEQUENCE 170 AA; 20599 MW; 6B02D4E8DF2F7743 CRC64; MYISKQPFRK SKQPFRKSKQ TFHKSKQPFR KFKQPFRKSK QPFRKSKQPF RRRSRIGPGD RIDYRNMSLI NRFISEQGKI LSRRINRLTL KQQRLITLAI KQARILSFLP FRNYENEKQF QAQAISIITG PRHRKNRHIP QLTQKFNSNR NLRNSNQNLR NNNRNLSSDC // ID RR19_MAIZE STANDARD; PRT; 92 AA. AC P06588; DT 01-JAN-1988 (Rel. 06, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Chloroplast 30S ribosomal protein S19. GN RPS19-A AND RPS19-B. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87231092; PubMed=3588315; RA McLaughlin W.E., Larrinua I.M.; RT "The sequence of the maize rps19 locus and of the inverted RT repeat/unique region junctions."; RL Nucleic Acids Res. 15:3932-3932(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Protein S19 forms a complex with S13 that binds strongly CC to the 16S ribosomal RNA (By similarity). CC -!- SIMILARITY: Belongs to the S19P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00141; CAC35460.1; -. DR EMBL; X86563; CAA60374.1; -. DR EMBL; X86563; CAA60326.1; -. DR PIR; S07388; R3ZM19. DR HSSP; P80381; 1QKF. DR Gramene; P06588; -. DR MaizeDB; 66100; -. DR HAMAP; MF_00531; -; 1. DR InterPro; IPR002222; Ribosomal_S19. DR InterPro; IPR005732; Ribosomal_S19b/o. DR Pfam; PF00203; Ribosomal_S19; 1. DR PRINTS; PR00975; RIBOSOMALS19. DR ProDom; PD001012; Ribosomal_S19; 1. DR TIGRFAMs; TIGR01050; rpsS_bact; 1. DR PROSITE; PS00323; RIBOSOMAL_S19; 1. KW Ribosomal protein; rRNA-binding; Chloroplast. FT INIT_MET 0 0 By similarity. SQ SEQUENCE 92 AA; 10625 MW; FD088C0C39D730AD CRC64; TRKKTNPFVA RHLLAKIEKV NMKEEKEIIV TWSRASSILP AMVGHTIAIH NGKEHIPIYI TNPMVGRKLG EFVPTRHFTS YESTRKDTKS RR // ID RR2_MAIZE STANDARD; PRT; 236 AA. AC P16037; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast 30S ribosomal protein S2. GN RPS2. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90175001; PubMed=2308853; RA Igloi G.L., Meinke A., Doery I., Koessel H.; RT "Nucleotide and derived amino acid sequence of rps2 from maize RT chloroplasts."; RL Nucleic Acids Res. 18:663-663(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9CMSSR37; TISSUE=Leaf; RX MEDLINE=90272437; PubMed=2140888; RA Stahl D., Rodermel S., Subramanian A.R., Bogorad L.; RT "Nucleotide sequence of a 3.46 kb region of maize chloroplast DNA RT containing the gene cluster rpoC2-rps2-atpI-atpH."; RL Nucleic Acids Res. 18:3073-3074(1990). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [4] RP SEQUENCE OF 1-36 FROM N.A. RX MEDLINE=90340289; PubMed=2381419; RA Igloi G.L., Meinke A., Doery I., Koessel H.; RT "Nucleotide sequence of the maize chloroplast rpo B/C1/C2 operon: RT comparison between the derived protein primary structures from RT various organisms with respect to functional domains."; RL Mol. Gen. Genet. 221:379-394(1990). CC -!- SIMILARITY: Belongs to the S2P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17318; CAA35198.1; -. DR EMBL; X52270; CAA36512.1; -. DR EMBL; X86563; CAA60279.1; -. DR PIR; S08249; R3ZM2. DR Gramene; P16037; -. DR MaizeDB; 66014; -. DR HAMAP; MF_00291; -; 1. DR InterPro; IPR001865; Ribosomal_S2. DR InterPro; IPR005706; Ribosomal_S2_b/o. DR Pfam; PF00318; Ribosomal_S2; 1. DR PRINTS; PR00395; RIBOSOMALS2. DR TIGRFAMs; TIGR01011; rpsB_bact; 1. DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1. DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1. KW Ribosomal protein; Chloroplast. SQ SEQUENCE 236 AA; 26881 MW; 80A3F99A8955FAD5 CRC64; MTRRYWNINL KEMIEAGVHF GHGIKKWNPK MAPYISAKRK GTHITNLART ARFLSEACDL VFDAASQGKS FLIVGTKKRA ADLVASAAIR SRCHYVNKKW FSGMLTNWSI TKTRLSQFRD LRAEEKMGKF HHLPKRDAAI LKRKLSTLQR YLGGIKYMTR LPDIVIVLDQ QKEYIALQEC AILGIPTISL VDTNCDPDLA NISIPANDDT MTSIRLILNK LVFAISEGRS LYIRNR // ID RR3_MAIZE STANDARD; PRT; 224 AA. AC P06586; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast 30S ribosomal protein S3. GN RPS3. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87231045; PubMed=3588305; RA McLaughlin W.E., Larrinua I.M.; RT "The sequence of the maize plastid encoded rps3 locus."; RL Nucleic Acids Res. 15:4689-4689(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SUBUNIT: Part of the 30S ribosomal subunit. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the S3P family of ribosomal proteins. CC -!- SIMILARITY: Contains 1 KH type-2 domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y00340; CAA68427.1; -. DR EMBL; X86563; CAA60324.1; -. DR PIR; S58590; S58590. DR Gramene; P06586; -. DR MaizeDB; 66303; -. DR HAMAP; MF_01309; atypical; 1. DR InterPro; IPR009019; KH_prok. DR InterPro; IPR004044; KH_TYPE_2. DR InterPro; IPR001351; Ribosomal_S3_C. DR InterPro; IPR008282; Ribosomal_S3_N. DR InterPro; IPR005704; S3_bact. DR Pfam; PF00189; Ribosomal_S3_C; 1. DR Pfam; PF00417; Ribosomal_S3_N; 1. DR TIGRFAMs; TIGR01009; rpsC_bact; 1. DR PROSITE; PS50823; KH_TYPE_2; FALSE_NEG. DR PROSITE; PS00548; RIBOSOMAL_S3; 1. KW Ribosomal protein; Chloroplast. FT DOMAIN 43 124 KH type-2. SQ SEQUENCE 224 AA; 25916 MW; B6B86BE4A8AF70DA CRC64; MGQKINPLGF RLGTTQNHHS FWFAQPKNYS EGLQEDKKIR NCIKNYIQKN RKKGSNRKME SDSSSEVITH IEIQKEIDTI HVIIHIGFPN LLKKKGAIEE LEKDLQKEVN SVNQRLNIAI EKVKEPYRQP NILAEYIAFQ LKNRVSFRKA MKKAIELTKK ADIKGIKIQI AGRLAGKEIA RAECIKKGRL PLQTIRAKID YCCYPIRTIY GVLGVKIWIF VEEE // ID RR4_MAIZE STANDARD; PRT; 201 AA. AC P02355; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Chloroplast 30S ribosomal protein S4 (Basic protein). GN RPS4. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83272969; PubMed=6308577; RA Subramanian A.R., Steinmetz A., Bogorad L.; RT "Maize chloroplast DNA encodes a protein sequence homologous to the RT bacterial ribosome assembly protein S4."; RL Nucleic Acids Res. 11:5277-5286(1983). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA where it nucleates assembly of the body of CC the 30S subunit (By similarity). CC -!- FUNCTION: With S5 and S12 plays an important role in translational CC accuracy (By similarity). CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. CC The interaction surface between S4 and S5 is involved in control CC of translational fidelity (By similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the S4P family of ribosomal proteins. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X01608; CAA25754.1; -. DR EMBL; X86563; CAA60288.1; -. DR PIR; A02706; R3ZM4. DR HSSP; P81288; 1C05. DR Gramene; P02355; -. DR MaizeDB; 66415; -. DR HAMAP; MF_01306; -; 1. DR InterPro; IPR001912; Ribosomal_S4. DR InterPro; IPR005709; Ribosomal_S4_b/o. DR InterPro; IPR002942; S4. DR Pfam; PF00163; Ribosomal_S4; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM00363; S4; 1. DR TIGRFAMs; TIGR01017; rpsD_bact; 1. DR PROSITE; PS00632; RIBOSOMAL_S4; 1. DR PROSITE; PS50889; S4; 1. KW Ribosomal protein; RNA-binding; rRNA-binding; Chloroplast. FT DOMAIN 89 150 S4 RNA-binding. SQ SEQUENCE 201 AA; 23463 MW; 8D796F1499057BB5 CRC64; MSRYRGPRLK KIRRLGALPG LTRKTPKSGS NQKKKFHSGK KEQYRIRLQE KQKLRFHYGL TERQLLRYVH IAGKAKRSTG QVLLQLLEMR LDNILFRLGM ASTIPGARQL VNHRHILVNG RIVDIPSFRC KPRDIITTKD NQRSKRLVQN YIASSDPGKL PKHLTVDTLQ YKGLVKKILD RKWVGLKINE LLVVEYYSRQ T // ID RR7_MAIZE STANDARD; PRT; 156 AA. AC P12339; DT 01-OCT-1989 (Rel. 12, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast 30S ribosomal protein S7. GN RPS7-A AND RPS7-B. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. FR9CMSSR37; TISSUE=Leaf; RX MEDLINE=88033114; PubMed=2822717; RA Giese K., Subramanian A.R., Larrinua I.M., Bogorad L.; RT "Nucleotide sequence, promoter analysis, and linkage mapping of the RT unusually organized operon encoding ribosomal proteins S7 and S12 in RT maize chloroplast."; RL J. Biol. Chem. 262:15251-15255(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA where it nucleates assembly of the head CC domain of the 30S subunit (By similarity). CC -!- SUBUNIT: Part of the 30S ribosomal subunit. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the S7P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M17841; AAA85360.1; -. DR EMBL; X86563; CAA60339.1; -. DR EMBL; X86563; CAA60362.1; -. DR PIR; S58630; S58630. DR HSSP; P17291; 1RSS. DR Gramene; P12339; -. DR MaizeDB; 66081; -. DR HAMAP; MF_00480; -; 1. DR InterPro; IPR000235; Ribosomal_S7. DR InterPro; IPR005717; Ribosomal_S7_b/o. DR Pfam; PF00177; Ribosomal_S7; 1. DR ProDom; PD000817; Ribosomal_S7; 1. DR TIGRFAMs; TIGR01029; rpsG_bact; 1. DR PROSITE; PS00052; RIBOSOMAL_S7; 1. KW Ribosomal protein; RNA-binding; rRNA-binding; Chloroplast. FT CONFLICT 90 90 I -> M (in Ref. 1). SQ SEQUENCE 156 AA; 17659 MW; DC2E149ADC8E5115 CRC64; MSRRGTAEKR TAKSDPIFRN RLVNMVVNRI MKDGKKSLAY QILYRAVKKI QQKTETNPLL VLRQAIRRVT PNIGVKTRRN KKGSTRKVPI EIGSKQGRAL AIRWLLEASQ KRPGRNMAFK LSSELVDAAK GSGGAIRKKE ATHRMAEANR ALAHFR // ID RR8_MAIZE STANDARD; PRT; 136 AA. AC P08530; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Chloroplast 30S ribosomal protein S8. GN RPS8. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88111635; PubMed=2828044; RA Markmann-Mulisch U., Subramanian A.R.; RT "Nucleotide sequence and linkage map position of the genes for RT ribosomal proteins L14 and S8 in the maize chloroplast genome."; RL Eur. J. Biochem. 170:507-514(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA central domain where it helps coordinate CC assembly of the platform of the 30S subunit (By similarity). CC -!- SUBUNIT: Part of the 30S ribosomal subunit. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: Belongs to the S8P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06734; CAA29913.1; -. DR EMBL; X86563; CAA60321.1; -. DR PIR; S00280; R3ZMBC. DR HSSP; P56209; 1SEI. DR Gramene; P08530; -. DR MaizeDB; 67052; -. DR HAMAP; MF_01302; -; 1. DR InterPro; IPR000630; Ribosomal_S8. DR Pfam; PF00410; Ribosomal_S8; 1. DR ProDom; PD001098; Ribosomal_S8; 1. DR PROSITE; PS00053; RIBOSOMAL_S8; 1. KW Ribosomal protein; RNA-binding; rRNA-binding; Chloroplast. SQ SEQUENCE 136 AA; 15638 MW; B90CC85C8F7222FD CRC64; MGKDTIADLL TSIRNADMNK KGTVRVVSTN ITENIVKILL REGFIESVRK HQESNRYFLV STLRHQRRKT RKGIYRTRTF LKRISRPGLR IYANYQGIPK VLGGMGIAIL STSRGIMTDR EARLNRIGGE VLCYIW // ID RS11_MAIZE STANDARD; PRT; 159 AA. AC P25460; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 40S ribosomal protein S11. GN RPS11. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; TISSUE=Seedling; RX MEDLINE=91322524; PubMed=1840689; RA Lebrun M., Freyssinet G.; RT "Nucleotide sequence and characterization of a maize cytoplasmic RT ribosomal protein S11 cDNA."; RL Plant Mol. Biol. 17:265-268(1991). CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the S17P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55967; CAA39438.1; -. DR PIR; S16577; S16577. DR HSSP; P23828; 1RIP. DR MaizeDB; 69569; -. DR InterPro; IPR008994; Nucleic_acid_OB. DR InterPro; IPR000266; Ribosomal_S17. DR Pfam; PF00366; Ribosomal_S17; 1. DR PRINTS; PR00973; RIBOSOMALS17. DR ProDom; PD001295; Ribosomal_S17; 1. DR PROSITE; PS00056; RIBOSOMAL_S17; 1. KW Ribosomal protein; rRNA-binding. SQ SEQUENCE 159 AA; 17690 MW; 650279BBFEB32855 CRC64; MAEQTEKAFL KQPKVFLSSK KSGKGKKPGK GGNRFWKSIG LGFKTPREAI EGTYIDKKCP FTGTVSIRGR IIAGTCHSAK MNRTIIVRRN YLHFVKKYQR YEKRHSNIPA HISPCFRVKE GDHVIIGQCR PLSKTVRFNV VKVIPAGSAA AGKKAFTAA // ID RS13_MAIZE STANDARD; PRT; 151 AA. AC Q05761; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 40S ribosomal protein S13. GN RPS13. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93192530; PubMed=8448368; RA Joanin P., Gigot C., Philipps G.; RT "cDNA nucleotide sequence and expression of a maize cytoplasmic RT ribosomal protein S13 gene."; RL Plant Mol. Biol. 21:701-704(1993). CC -!- SIMILARITY: Belongs to the S15P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62455; CAA44311.1; -. DR PIR; S30146; S30146. DR MaizeDB; 65480; -. DR InterPro; IPR000589; Ribosomal_S15. DR Pfam; PF00312; Ribosomal_S15; 1. DR PROSITE; PS00362; RIBOSOMAL_S15; 1. KW Ribosomal protein. SQ SEQUENCE 151 AA; 17058 MW; BBE3A9126748F629 CRC64; MGAMHSRGKG ISSSALPYKR TPPTWLKTAA SDVEEMITKA AKKGQMPSQI GVLLRDQHGI PLVKSVTGSK ILRILKAHGL APEIPEDLYF LIKKAVAIRK HLERNRKDKD SKFRLILVES RIHRLARYYK RTKKLPPTWK YESTTASTLV A // ID RS20_MAIZE STANDARD; PRT; 60 AA. AC Q08068; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 40S ribosomal protein S20 (S22) (Fragment). GN RPS20. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94105294; PubMed=8278499; RA Keith C.S., Hoang D.O., Barrett B.M., Feigelman B., Nelson M.C., RA Thai H., Baysdorfer C.; RT "Partial sequence analysis of 130 randomly selected maize cDNA RT clones."; RL Plant Physiol. 101:329-332(1993). CC -!- SIMILARITY: Belongs to the S10P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95062; AAA18549.2; -. DR PIR; T03646; T03646. DR MaizeDB; 25438; -. DR InterPro; IPR001848; Ribosomal_S10. DR Pfam; PF00338; Ribosomal_S10; 1. DR PRINTS; PR00971; RIBOSOMALS10. DR ProDom; PD001272; Ribosomal_S10; 1. DR PROSITE; PS00361; RIBOSOMAL_S10; PARTIAL. KW Ribosomal protein. FT NON_TER 1 1 FT NON_TER 60 60 SQ SEQUENCE 60 AA; 6908 MW; C6DD37D88B8525B9 CRC64; EKVCADLVKG AKDKHLRVKG PVRIPTKVLH ITTRKSPCGE GTNTWDRFEF RIHKRVIDLI // ID RS21_MAIZE STANDARD; PRT; 81 AA. AC Q41852; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 40S ribosomal protein S21. GN RPS21. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; RA Dresselhaus T., Cordts S., Heuer S., Loerz H., Kranz E.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the S21E family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X98656; CAA67225.1; -. DR PIR; T03945; T03945. DR MaizeDB; 82786; -. DR InterPro; IPR001931; Ribosomal_S21E. DR Pfam; PF01249; Ribosomal_S21e; 1. DR ProDom; PD006584; Ribosomal_S21E; 1. DR PROSITE; PS00996; RIBOSOMAL_S21E; 1. KW Ribosomal protein. SQ SEQUENCE 81 AA; 9020 MW; 922F17E331BA9739 CRC64; MQNEEGKTVD LYVPRKCSAT NRIITAKDHA SVQINIGHLD ANGLYDGHFT TFALSGFVRA QGDADSSLDR LWQKKKAEIK Q // ID RS28_MAIZE STANDARD; PRT; 65 AA. AC P46302; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 40S ribosomal protein S28. GN RPS28. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. DEA; TISSUE=Root meristem; RA Chevalier C., le Querrec F., Raymond P.; RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the S28E family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X82124; CAA57636.1; -. DR PIR; S49035; S49035. DR MaizeDB; 82916; -. DR InterPro; IPR000289; Ribosomal_S28e. DR Pfam; PF01200; Ribosomal_S28e; 1. DR ProDom; PD005541; Ribosomal_S28e; 1. DR PROSITE; PS00961; RIBOSOMAL_S28E; 1. KW Ribosomal protein. SQ SEQUENCE 65 AA; 7411 MW; 3B0ECE7A4948B52E CRC64; MDTQVKLAVV VKVMGRTGSR GQVTQVRVKF LDDQNRLIMR NVKGPVCEGD ILTLLESERE ARRLR // ID RS8_MAIZE STANDARD; PRT; 221 AA. AC Q08069; DT 01-FEB-1996 (Rel. 33, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 40S ribosomal protein S8. GN RPS8. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RA Betawar N.M., Baysdorfer C.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 1-41 FROM N.A. RX MEDLINE=94105294; PubMed=8278499; RA Keith C.S., Hoang D.O., Barrett B.M., Feigelman B., Nelson M.C., RA Thai H., Baysdorfer C.; RT "Partial sequence analysis of 130 randomly selected maize cDNA RT clones."; RL Plant Physiol. 101:329-332(1993). CC -!- SIMILARITY: Belongs to the S8E family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U64436; AAB06330.1; -. DR EMBL; M95064; AAA18551.2; -. DR PIR; T03647; T03647. DR PIR; T04088; T04088. DR MaizeDB; 25471; -. DR InterPro; IPR001047; Ribosomal_S8E. DR Pfam; PF01201; Ribosomal_S8e; 1. DR ProDom; PD005658; Ribosomal_S8E; 1. DR TIGRFAMs; TIGR00307; S8e; 1. DR PROSITE; PS01193; RIBOSOMAL_S8E; 1. KW Ribosomal protein. SQ SEQUENCE 221 AA; 25057 MW; 6D53A6F49F78ABC0 CRC64; MGISRDSMHK RRATGGKQKA WRKKRKYELG RQPANTKLSS NKTVRRVRVR GGNVKWRALR LDTGNYSWGS EAVTRKTRIL DVVYNASNNE LVRTQTLVKS AIVQVDAAPF KQWYLTHYGV DIGRKKKTPA AKKDNAEGQE VEAAAEETKK SNHVTRKLEK RKEGRTLDPH IEEQFGSGRL LACISSRPGQ CGRADGYILE GKELEFYMKK LQRKKGKSAV A // ID RT03_MAIZE STANDARD; PRT; 559 AA. AC P27928; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Mitochondrial ribosomal protein S3. GN RPS3. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91216097; PubMed=1708720; RA Hunt M.D., Newton K.J.; RT "The NCS3 mutation: genetic evidence for the expression of ribosomal RT protein genes in Zea mays mitochondria."; RL EMBO J. 10:1045-1052(1991). CC -!- SUBCELLULAR LOCATION: Mitochondrial. CC -!- SIMILARITY: Belongs to the S3P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57445; CAA40690.1; -. DR PIR; S15025; R3ZMS3. DR MaizeDB; 69576; -. DR InterPro; IPR009019; KH_prok. DR InterPro; IPR001351; Ribosomal_S3_C. DR InterPro; IPR008282; Ribosomal_S3_N. DR Pfam; PF00189; Ribosomal_S3_C; 1. DR Pfam; PF00417; Ribosomal_S3_N; 1. DR PROSITE; PS00548; RIBOSOMAL_S3; 1. KW Ribosomal protein; Mitochondrion. SQ SEQUENCE 559 AA; 64233 MW; 09A52ED8A3AC6075 CRC64; MARKGNPISV RLDLNRSSDP SRFSDYYYGK SLYQDVNLRS YFSSIRPPTR LTFGFRLGRC IILHFPKRTF IHFFLPRRPL RLKRRDKSRP GKDKGRWWAF GKVGPIGCLH SSEGTEEERN EVRGRGAGKR VESIDREKQN EIRIWPKKMQ RYGYHDRTPS RKKNFSKSLR VSGAFKHPKY AGVVNDIAFL IENDDSFIKT KLFKFFFLPK KSRSDGPTSH LLKRTLPAVR PSLNYSVMQY FFNTKNKMHF DPVVVLNHFV APGVAEPSTM GGAKGGSLDK RIRSRIAFFV ESSTSDKKCL ARAKKRLIHF IRQANDLRFA GTTKTTISLF PFFGATFFFS RDGVGVYNNP FYEYAREQLL GQLRIKCRNL MGKDKVMELI EKFIDLGRIG KLIKGIEMMI EIILRKRRIP YGYNSYLNEV QKMRSFLSNR TNTNTLIESV KIKSVYQSAS LIAQDISFQL RNNPISFRSI FSKIVKDIPL IMPKGVEGIR ICCSGRLGGA EIARTECGKY GKTSCNVFNQ KIDYAPAEVS TRDGISGVKV RISYSQNKKG RAISETYEI // ID RT12_MAIZE STANDARD; PRT; 125 AA. AC P60099; P10851; DT 01-JUL-1989 (Rel. 11, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Mitochondrial ribosomal protein S12. GN RPS12. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WF9-N; TISSUE=Hypocotyl; RX MEDLINE=89201232; PubMed=2853827; RA Gualberto J.M., Wintz H., Weil J.-H., Grienenberger J.-M.; RT "The genes coding for subunit 3 of NADH dehydrogenase and for RT ribosomal protein S12 are present in the wheat and maize RT mitochondrial genomes and are co-transcribed."; RL Mol. Gen. Genet. 215:118-127(1988). CC -!- FUNCTION: Protein S12 is involved in the translation initiation CC step. CC -!- SUBCELLULAR LOCATION: Mitochondrial. CC -!- RNA EDITING: Modified_positions=24, 66, 74, 90, 95, 97. CC -!- SIMILARITY: Belongs to the S12P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14709; CAA32834.1; ALT_SEQ. DR MaizeDB; 69570; -. DR InterPro; IPR008994; Nucleic_acid_OB. DR InterPro; IPR006032; Ribosomal_S12_23. DR InterPro; IPR005679; Ribosomal_S12b/c. DR Pfam; PF00164; Ribosomal_S12; 1. DR PRINTS; PR01034; RIBOSOMALS12. DR ProDom; PD000576; Ribosomal_S12_23; 1. DR TIGRFAMs; TIGR00981; rpsL_bact; 1. DR PROSITE; PS00055; RIBOSOMAL_S12; 1. KW Ribosomal protein; Mitochondrion; RNA editing. SQ SEQUENCE 125 AA; 14309 MW; AE5061CB6FDBF49F CRC64; MPTKNQLIRH GREEKRRTDR TRALDQCPQK QGVCLRVSTR TPKKPNSALR KIAKVRLSNR HDIFAYIPGE GHNLQEHSIV LVRGGRVKDL PGVKFHCIRG VKDLLGIPDR RKGRSKYGAE RPKSK // ID RT13_MAIZE STANDARD; PRT; 129 AA. AC P08977; Q36281; DT 01-NOV-1988 (Rel. 09, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Mitochondrial ribosomal protein S13. GN RPS13. OS Zea mays (Maize). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; RX MEDLINE=86310310; PubMed=2875379; RA Bland M.M., Levings C.S. III, Matzinger D.F.; RT "The tobacco mitochondrial ATPase subunit 9 gene is closely linked to RT an open reading frame for a ribosomal protein."; RL Mol. Gen. Genet. 204:8-16(1986). CC -!- FUNCTION: Located at the top of the head of the small subunit, it CC contacts several helices of the 18S rRNA (By similarity). CC -!- SUBUNIT: Part of the small ribosomal subunit. CC -!- SUBCELLULAR LOCATION: Mitochondrial. CC -!- SIMILARITY: Belongs to the S13P family of ribosomal proteins. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18339; AAA70274.1; -. DR PIR; S01428; R3MZ13. DR MaizeDB; 69575; -. DR InterPro; IPR001892; Ribosomal_S13. DR Pfam; PF00416; Ribosomal_S13; 1. DR ProDom; PD001363; Ribosomal_S13; 1. DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1. DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1. KW Ribosomal protein; RNA-binding; rRNA-binding; Mitochondrion. SQ SEQUENCE 129 AA; 14938 MW; 178D633F3BF1622F CRC64; MSYISGARSL PDEQVRIAST KMDGIGPKKA IQLRYRLGIS GNIKIHELTK YQIDQIEQMI AQDHVVHWEL KRGERADIER LISISRYRGI RHQDGSPLRG QRTHTNARTA RKQIRKGNER RLPKEQATD // ID S1FA_MAIZE STANDARD; PRT; 63 AA. AC P42554; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE DNA binding protein S1FA (Fragment). GN S1FA. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A2; RX MEDLINE=95111093; PubMed=7811968; RA Shen B., Carneiro N., Torres-Jerez I., Stevenson R., McCreery T., RA Helentjaris T., Baysdorfer C., Almira E., Ferl R., Habben J., RA Larkins B.; RT "Partial sequencing and mapping of clones from two maize cDNA RT libraries."; RL Plant Mol. Biol. 26:1085-1101(1994). CC -!- FUNCTION: DNA-binding protein that specifically recognizes a CC negative element (S1F) within the RPS1 promoter (By similarity). CC -!- SUBCELLULAR LOCATION: Nuclear (Probable). CC -!- SIMILARITY: STRONG, TO S1FA IN OTHER PLANTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; T23392; -; NOT_ANNOTATED_CDS. DR MaizeDB; 102210; -. DR InterPro; IPR006779; S1FA. DR Pfam; PF04689; S1FA; 1. KW Transcription regulation; Repressor; DNA-binding; Nuclear protein. FT NON_TER 1 1 SQ SEQUENCE 63 AA; 6953 MW; F481EEEBB762F795 CRC64; NKGLNPGMVV XLVVASFLLI FFVGNYALYX YAQKTLPPKK KKPVSKKKLK KEKLKQGVSA PGE // ID SOD4_MAIZE STANDARD; PRT; 151 AA. AC P23345; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Superoxide dismutase [Cu-Zn] 4A (EC 1.15.1.1). GN SODCC.3 OR SOD4A. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90136495; PubMed=2482436; RA Cannon R.E., Scandalios J.G.; RT "Two cDNAs encode two nearly identical Cu/Zn superoxide dismutase RT proteins in maize."; RL Mol. Gen. Genet. 219:1-8(1989). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 copper ion and 1 zinc ion per subunit (By CC similarity). CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17564; -; NOT_ANNOTATED_CDS. DR PIR; S07007; S07007. DR HSSP; P07505; 1SRD. DR MaizeDB; 47586; -. DR InterPro; IPR001424; SOD_CU_ZN. DR Pfam; PF00080; sodcu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR ProDom; PD000469; SOD_CU_ZN; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. KW Antioxidant; Oxidoreductase; Metal-binding; Copper; Zinc; KW Multigene family. FT INIT_MET 0 0 By similarity. FT METAL 44 44 Copper (By similarity). FT METAL 46 46 Copper (By similarity). FT METAL 61 61 Copper and zinc (By similarity). FT METAL 69 69 Zinc (By similarity). FT METAL 78 78 Zinc (By similarity). FT METAL 81 81 Zinc (By similarity). FT METAL 118 118 Copper (By similarity). FT DISULFID 55 144 By similarity. SQ SEQUENCE 151 AA; 14983 MW; 9C6226F86C919E58 CRC64; VKAVAVLGSS EGVKGTIFFT QEGDGPTTVT GSVSGLKPGL HGFHVHALGD TTNGCMSTGP HYNPASKEHG APEDENRHAG DLGNVTAGAD GVANINVTDS QIPLTGPNSI IGRAVVVHAD PDDLGKGGHE LSKSTGNAGG RVACGIIGLQ G // ID SOD5_MAIZE STANDARD; PRT; 151 AA. AC P23346; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Superoxide dismutase [Cu-Zn] 4AP (EC 1.15.1.1). GN SODCC.2 OR SOD4AP. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90136495; PubMed=2482436; RA Cannon R.E., Scandalios J.G.; RT "Two cDNAs encode two nearly identical Cu/Zn superoxide dismutase RT proteins in maize."; RL Mol. Gen. Genet. 219:1-8(1989). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 copper ion and 1 zinc ion per subunit (By CC similarity). CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X17565; CAB57992.1; ALT_SEQ. DR HSSP; P07505; 1SRD. DR MaizeDB; 47586; -. DR InterPro; IPR001424; SOD_CU_ZN. DR Pfam; PF00080; sodcu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR ProDom; PD000469; SOD_CU_ZN; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. KW Antioxidant; Oxidoreductase; Metal-binding; Copper; Zinc; KW Multigene family. FT INIT_MET 0 0 By similarity. FT METAL 44 44 Copper (By similarity). FT METAL 46 46 Copper (By similarity). FT METAL 61 61 Copper and zinc (By similarity). FT METAL 69 69 Zinc (By similarity). FT METAL 78 78 Zinc (By similarity). FT METAL 81 81 Zinc (By similarity). FT METAL 118 118 Copper (By similarity). FT DISULFID 55 144 By similarity. SQ SEQUENCE 151 AA; 14939 MW; 9C7E572A6C1AEF1D CRC64; VKAVAVLGSS DGVKGTIFFT QEGDGPTAVT GSVSGLKPGL HGFHVHALGD TTNGCMSTGP HYNPASKEHG APEDENRHAG DLGNVTAGAD GVANINVTDS QIPLTGPNSI IGRAVVVHAD PDDLGKGGHE LSKSTGNAGG RVACGIIGLQ G // ID SODC_MAIZE STANDARD; PRT; 150 AA. AC P11428; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Superoxide dismutase [Cu-Zn] 2 (EC 1.15.1.1). GN SODCC.1 OR SOD2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87092359; PubMed=3467349; RA Cannon R.E., White J.A., Scandalios J.G.; RT "Cloning of cDNA for maize superoxide dismutase 2 (SOD2)."; RL Proc. Natl. Acad. Sci. U.S.A. 84:179-183(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87249683; PubMed=3597043; RA Cannon R.E., Scandalios J.G.; RT "The superoxide dismutase-2 gene of maize."; RL Isozymes Curr. Top. Biol. Med. Res. 14:73-81(1987). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 copper ion and 1 zinc ion per subunit (By CC similarity). CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M15175; AAA33511.1; -. DR EMBL; M54936; AAA33510.1; -. DR PIR; A29077; A29077. DR HSSP; P07505; 1SRD. DR MaizeDB; 47586; -. DR InterPro; IPR001424; SOD_CU_ZN. DR Pfam; PF00080; sodcu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR ProDom; PD000469; SOD_CU_ZN; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. KW Antioxidant; Oxidoreductase; Metal-binding; Copper; Zinc; KW Multigene family. FT INIT_MET 0 0 By similarity. FT METAL 43 43 Copper (By similarity). FT METAL 45 45 Copper (By similarity). FT METAL 60 60 Copper and zinc (By similarity). FT METAL 68 68 Zinc (By similarity). FT METAL 77 77 Zinc (By similarity). FT METAL 80 80 Zinc (By similarity). FT METAL 117 117 Copper (By similarity). FT DISULFID 54 143 By similarity. SQ SEQUENCE 150 AA; 14973 MW; C63A117072C37873 CRC64; VKAVAVLAGT DVKGTIFFSQ EGDGPTTVTG SISGLKPGLH GFHVHALGDT TNGCMSTGPH FNPVGKEHGA PEDEDRHAGD LGNVTAGEDG VVNVNITDSQ IPLAGPHSII GRAVVVHADP DDLGKGGHEL SKSTGNAGGR VACGIIGLQG // ID SODM_MAIZE STANDARD; PRT; 235 AA. AC P09233; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Superoxide dismutase [Mn] 3.1, mitochondrial precursor (EC 1.15.1.1). GN SODA.4 OR SOD3.1 OR SOD3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; RX MEDLINE=89051020; PubMed=2461225; RA Redinbaugh M.G., Wadsworth G.T., Scandalios J.G.; RT "Isolation and characterization of a cDNA for mitochondrial manganese RT superoxide dismutase (SOD-3) of maize and its relation to other RT manganese superoxide dismutases."; RL Biochim. Biophys. Acta 951:61-70(1988). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity). CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X12540; CAA31058.1; -. DR HSSP; P04179; 1ABM. DR MaizeDB; 47587; -. DR InterPro; IPR001189; SODismutase. DR Pfam; PF00081; sodfe; 1. DR Pfam; PF02777; sodfe_C; 1. DR PRINTS; PR01703; MNSODISMTASE. DR ProDom; PD000475; SODismutase; 1. DR PROSITE; PS00088; SOD_MN; 1. KW Oxidoreductase; Metal-binding; Manganese; Mitochondrion; KW Transit peptide; Multigene family. FT TRANSIT 1 31 Mitochondrion. FT CHAIN 32 235 Superoxide dismutase [Mn] 3.1. FT METAL 59 59 Manganese (By similarity). FT METAL 107 107 Manganese (By similarity). FT METAL 196 196 Manganese (By similarity). FT METAL 200 200 Manganese (By similarity). SQ SEQUENCE 235 AA; 25545 MW; AD51BAD0F44FDE56 CRC64; MALRTLASKK VLSFPFGGAG RPLAAAASAR GVTTVTLPDL SYDFGALEPA ISGEIMRLHH QKHHATYVAN YNKALEQLET AVSKGDASAV VQLQAAIKFN GGGHVNHSIF WKNLKPISEG GGEPPHGKLG WAIDEDFGSF EALVKKMNAE GAALQGSGWV WLALDKEAKK VSVETTANQD PLVTKGASLV PLLGIDVWEH AYYLQYKNVR PDYLNNIWKV MNWKYAGEVY ENVLA // ID SODN_MAIZE STANDARD; PRT; 232 AA. AC P41978; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Superoxide dismutase [Mn] 3.2, mitochondrial precursor (EC 1.15.1.1). GN SODA.1 OR SOD3.2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94022365; PubMed=8415698; RA Zhu D., Scandalios J.G.; RT "Maize mitochondrial manganese superoxide dismutases are encoded by a RT differentially expressed multigene family."; RL Proc. Natl. Acad. Sci. U.S.A. 90:9310-9314(1993). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L19461; AAA72020.2; -. DR PIR; C48684; C48684. DR HSSP; P04179; 1AP6. DR MaizeDB; 47587; -. DR InterPro; IPR001189; SODismutase. DR Pfam; PF00081; sodfe; 1. DR Pfam; PF02777; sodfe_C; 1. DR PRINTS; PR01703; MNSODISMTASE. DR ProDom; PD000475; SODismutase; 1. DR PROSITE; PS00088; SOD_MN; 1. KW Oxidoreductase; Metal-binding; Manganese; Mitochondrion; KW Transit peptide; Multigene family. FT TRANSIT 1 29 Mitochondrion (By similarity). FT CHAIN 30 232 Superoxide dismutase [Mn] 3.2. FT METAL 57 57 Manganese (By similarity). FT METAL 105 105 Manganese (By similarity). FT METAL 193 193 Manganese (By similarity). FT METAL 197 197 Manganese (By similarity). SQ SEQUENCE 232 AA; 25357 MW; 6A08B981281DB488 CRC64; MALRTLASKN ALSFALGGAA RPSAASARGV TTVALPDLSY DFGALEPVIS GEIMRLHHQK HHATYVVNYN KALEQLDAVV VKGDASAVVQ LQGAIKFNGG GHFNHSIFWE NLKPISEGGE PPHGKLGWAI DEDFGSFEAL VKRMNAEGAA LQGSGWVWLA LDKEPKKLSV ETTANQDPLV TKGASLVPLL GIDVWEHAYY LQYKNVRPDY LNNIWKVMNW KYAGEVYENV LA // ID SODO_MAIZE STANDARD; PRT; 233 AA. AC P41979; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Superoxide dismutase [Mn] 3.3, mitochondrial precursor (EC 1.15.1.1). GN SODA.2 OR SOD3.3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94022365; PubMed=8415698; RA Zhu D., Scandalios J.G.; RT "Maize mitochondrial manganese superoxide dismutases are encoded by a RT differentially expressed multigene family."; RL Proc. Natl. Acad. Sci. U.S.A. 90:9310-9314(1993). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix. CC -!- TISSUE SPECIFICITY: Predominantly expressed in the embryo late in CC embryogenesis. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L19462; AAA72021.2; -. DR PIR; A48684; A48684. DR HSSP; P04179; 1ABM. DR MaizeDB; 47587; -. DR InterPro; IPR001189; SODismutase. DR Pfam; PF00081; sodfe; 1. DR Pfam; PF02777; sodfe_C; 1. DR PRINTS; PR01703; MNSODISMTASE. DR ProDom; PD000475; SODismutase; 1. DR PROSITE; PS00088; SOD_MN; 1. KW Oxidoreductase; Metal-binding; Manganese; Mitochondrion; KW Transit peptide; Multigene family. FT TRANSIT 1 29 Mitochondrion (By similarity). FT CHAIN 30 233 Superoxide dismutase [Mn] 3.3. FT METAL 57 57 Manganese (By similarity). FT METAL 105 105 Manganese (By similarity). FT METAL 194 194 Manganese (By similarity). FT METAL 198 198 Manganese (By similarity). SQ SEQUENCE 233 AA; 25448 MW; 061160B89B195A96 CRC64; MALRTLASKN ALSFALGGAA RPSAESARGV TTVALPDLSY DFGALEPVIS GEIMRLHHQK NHATYVVNYN KALEQIDDVV VKGDDSAVVQ LQGAIKFNGG GHVNHSIFWK NLKPISEGGG EPPHGKLGWA IDEDFGSFEA LVKRMNAEGA ALQGSGWVWL ALDKEAKKVS VETTANQDPL VTKGASLVPL LGIDVWEHAY YLQYKNVRPD YLNNIWKVMN WKYAGEVYEN VLA // ID SODP_MAIZE STANDARD; PRT; 233 AA. AC P41980; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Superoxide dismutase [Mn] 3.4, mitochondrial precursor (EC 1.15.1.1). GN SODA.3 OR SOD3.4. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94022365; PubMed=8415698; RA Zhu D., Scandalios J.G.; RT "Maize mitochondrial manganese superoxide dismutases are encoded by a RT differentially expressed multigene family."; RL Proc. Natl. Acad. Sci. U.S.A. 90:9310-9314(1993). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L19463; AAA72022.2; -. DR PIR; B48684; B48684. DR HSSP; P04179; 1AP6. DR MaizeDB; 47587; -. DR InterPro; IPR001189; SODismutase. DR Pfam; PF00081; sodfe; 1. DR Pfam; PF02777; sodfe_C; 1. DR PRINTS; PR01703; MNSODISMTASE. DR ProDom; PD000475; SODismutase; 1. DR PROSITE; PS00088; SOD_MN; 1. KW Oxidoreductase; Metal-binding; Manganese; Mitochondrion; KW Transit peptide; Multigene family. FT TRANSIT 1 29 Mitochondrion (By similarity). FT CHAIN 30 233 Superoxide dismutase [Mn] 3.4. FT METAL 57 57 Manganese (By similarity). FT METAL 105 105 Manganese (By similarity). FT METAL 194 194 Manganese (By similarity). FT METAL 198 198 Manganese (By similarity). SQ SEQUENCE 233 AA; 25239 MW; 214626404EB742A3 CRC64; MALRTLASKN ALSFALGGAA RPSAASARGV TTVALPDLSY DFGALEPAIS GEIMRLHHQK HHATYVGNYN KALEQLDAAV AKGDASAVVQ LQGAIKFNGG GHVNHSIFWK NLKPISEGGG EPPHGKLGWA IDEDFGSFEA LVKRMNAEGA ALQGSGWVWL ALDKEPKKLS VETTANQDPL VTKGASLVPL LGIDVWEHAY YLQYKNVRPD YLNNIWKVMN WKYAGEVYEN VLA // ID SPS_MAIZE STANDARD; PRT; 1068 AA. AC P31927; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Sucrose-phosphate synthase (EC 2.4.1.14) (UDP-glucose-fructose- DE phosphate glucosyltransferase). GN SPS. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 71-74; 206-212; 471-481 AND RP 872-892. RC STRAIN=cv. Pioneer 3184; TISSUE=Leaf; RX MEDLINE=92338837; PubMed=1840396; RA Worrell A.C., Bruneau J.-M., Summerfelt K., Boersig M., Voelker T.A.; RT "Expression of a maize sucrose phosphate synthase in tomato alters RT leaf carbohydrate partitioning."; RL Plant Cell 3:1121-1130(1991). CC -!- FUNCTION: Involved in the regulation of carbon partitioning in the CC leaves of plants. May regulate the synthesis of sucrose and CC therefore play a major role as a limiting factor in the export of CC photoassimilates out of the leaf. CC -!- CATALYTIC ACTIVITY: UDP-glucose + D-fructose 6-phosphate = UDP + CC sucrose 6-phosphate. CC -!- ENZYME REGULATION: Activity regulated by phosphorylation and CC moderated by concentration of metabolites and light. CC -!- PATHWAY: Sucrose synthesis. CC -!- SUBUNIT: Homodimer or homotetramer. CC -!- DEVELOPMENTAL STAGE: Germinating seeds or mature leaves. CC -!- PTM: Phosphorylated. However, phosphorylation is not essential for CC enzyme function. CC -!- SIMILARITY: Belongs to the glycosyltransferase family 1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M97550; AAA33513.1; -. DR PIR; JQ1329; JQ1329. DR MaizeDB; 25294; -. DR InterPro; IPR001296; Glyco_trans_1. DR Pfam; PF00534; Glycos_transf_1; 1. KW Transferase; Glycosyltransferase; Phosphorylation. FT DOMAIN 25 31 Poly-Gly. SQ SEQUENCE 1068 AA; 118575 MW; 074679B5E9A1D282 CRC64; MAGNEWINGY LEAILDSHTS SRGAGGGGGG GDPRSPTKAA SPRGAHMNFN PSHYFVEEVV KGVDESDLHR TWIKVVATRN ARERSTRLEN MCWRIWHLAR KKKQLELEGI QRISARRKEQ EQVRREATED LAEDLSEGEK GDTIGELAPV ETTKKKFQRN FSDLTVWSDD NKEKKLYIVL ISVHGLVRGE NMELGRDSDT GGQVKYVVEL ARAMSMMPGV YRVDLFTRQV SSPDVDWSYG EPTEMLCAGS NDGEGMGESG GAYIVRIPCG PRDKYLKKEA LWPYLQEFVD GALAHILNMS KALGEQVGNG RPVLPYVIHG HYADAGDVAA LLSGALNVPM VLTGHSLGRN KLEQLLKQGR MSKEEIDSTY KIMRRIEGEE LALDASELVI TSTRQEIDEQ WGLYDGFDVK LEKVLRARAR RGVSCHGRYM PRMVVIPPGM DFSNVVVHED IDGDGDVKDD IVGLEGASPK SMPPIWAEVM RFLTNPHKPM ILALSRPDPK KNITTLVKAF GECRPLRELA NLTLIMGNRD DIDDMSAGNA SVLTTVLKLI DKYDLYGSVA FPKHHNQADV PEIYRLAAKM KGVFINPALV EPFGLTLIEA AAHGLPIVAT KNGGPVDITN ALNNGLLVDP HDQNAIADAL LKLVADKNLW QECRRNGLRN IHLYSWPEHC RTYLTRVAGC RLRNPRWLKD TPADAGADEE EFLEDSMDAQ DLSLRLSIDG EKSSLNTNDP LWFDPQDQVQ KIMNNIKQSS ALPPSMSSVA AEGTGSTMNK YPLLRRRRRL FVIAVDCYQD DGRASKKMLQ VIQEVFRAVR SDSQMFKISG FTLSTAMPLS ETLQLLQLGK IPATDFDALI CGSGSEVYYP GTANCMDAEG KLRPDQDYLM HISHRWSHDG ARQTIAKLMG AQDGSGDAVE QDVASSNAHC VAFLIKDPQK VKTVDEMRER LRMRGLRCHI MYCRNSTRLQ VVPLLASRSQ ALRYLSVRWG VSVGNMYLIT GEHGDTDLEE MLSGLHKTVI VRGVTEKGSE ALVRSPGSYK RDDVVPSETP LAAYTTGELK ADEIMRALKQ VSKTSSGM // ID SSG1_MAIZE STANDARD; PRT; 605 AA. AC P04713; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Granule-bound starch synthase I, chloroplast precursor (EC 2.4.1.21). GN WAXY. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Kloesgen R.B., Gierl A., Schwarz-Sommer Z., Saedler H.; RT "Molecular analysis of the waxy locus of Zea mays."; RL Mol. Gen. Genet. 203:237-244(1986). CC -!- FUNCTION: Required for the synthesis of amylose in endosperm. CC -!- CATALYTIC ACTIVITY: ADP-glucose + {(1,4)-alpha-D-glucosyl}(N) = CC ADP + {(1,4)-alpha-D-glucosyl}(N+1). CC -!- PATHWAY: Starch biosynthesis. CC -!- SUBCELLULAR LOCATION: Chloroplast or amyloplast, granule-bound. CC -!- SIMILARITY: Belongs to the glycosyltransferase family 1. CC Bacterial/plant glycogen synthase subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03935; CAA27574.1; -. DR PIR; S07314; S07314. DR MaizeDB; 15806; -. DR InterPro; IPR001296; Glyco_trans_1. DR Pfam; PF00534; Glycos_transf_1; 1. KW Transferase; Glycosyltransferase; Transit peptide; Chloroplast; KW Amyloplast; Starch biosynthesis. FT TRANSIT 1 72 Chloroplast. FT CHAIN 73 605 Granule-bound starch synthase I. FT BINDING 91 91 ADP-glucose (By similarity). SQ SEQUENCE 605 AA; 65966 MW; 137F15207DBFC189 CRC64; MAALATSQLV ATRAGLGVPD ASTFRRGAAQ GLRGARASAA ADTLSMRTSA RAAPRHQQQA RRGGRFPSLV VCASAGMNVV FVGAEMAPWS KTGGLGDVLG GLPPAMAANG HRVMVVSPRY DQYKDAWDTS VVSEIKMGDG YETVRFFHCY KRGVDRVFVD HPLFLERVWG KTEEKIYGPV AGTDYRDNQL RFSLLCQAAL EAPRILSLNN NPYFSGPYGE DVVFVCNDWH TGPLSCYLKS NYQSHGIYRD AKTAFCIHNI SYQGRFAFSD YPELNLPERF KSSFDFIDGY EKPVEGRKIN WMKAGILEAD RVLTVSPYYA EELISGIARG CELDNIMRLT GITGIVNGMD VSEWDPSRDK YIAVKYDVST AVEAKALNKE ALQAEVGLPV DRNIPLVAFI GRLEEQKGPD VMAAAIPQLM EMVEDVQIVL LGTGKKKFER MLMSAEEKFP GKVRAVVKFN AALAHHIMAG ADVLAVTSRF EPCGLIQLQG MRYGTPCACA STGGLVDTII EGKTGFHMGR LSVDCNVVEP ADVKKVATTL QRAIKVVGTP AYEEMVRNCM IQDLSWKGPA KNWENVLLSL GVAGGEPGVE GEEIAPLAKE NVAAP // ID SUS1_MAIZE STANDARD; PRT; 802 AA. AC P04712; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Sucrose synthase 1 (EC 2.4.1.13) (Sucrose-UDP glucosyltransferase 1) DE (Shrunken-1). GN SH-1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Werr W., Frommer W.-B., Maas C., Starlinger P.; RT "Structure of the sucrose synthase gene on chromosome 9 of Zea mays RT L."; RL EMBO J. 4:1373-1380(1985). CC -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and CC fructose for various metabolic pathways. Most active in the sink CC tissues where it is responsible for the breakdown of the arriving CC sucrose. CC -!- CATALYTIC ACTIVITY: NDP-glucose + D-fructose = NDP + sucrose. CC -!- SIMILARITY: Belongs to the glycosyltransferase family 1. Plant CC sucrose synthase subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02400; CAA26247.1; -. DR EMBL; X02382; CAA26229.1; -. DR PIR; S07184; YUZMS. DR MaizeDB; 13861; -. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR000368; Sucrose_synth. DR Pfam; PF00534; Glycos_transf_1; 1. DR Pfam; PF00862; Sucrose_synth; 1. KW Transferase; Glycosyltransferase; Multigene family. SQ SEQUENCE 802 AA; 91731 MW; BF1BE860598B680A CRC64; MAAKLTRLHS LRERLGATFS SHPNELIALF SRYVHQGKGM LQRHQLLAEF DALFDSDKEK YAPFEDILRA AQEAIVLPPW VALAIRPRPG VWDYIRVNVS ELAVEELSVS EYLAFKEQLV DGQSNSNFVL ELDFEPFNAS FPRPSMSKSI GNGVQFLNRH LSSKLFQDKE SLYPLLNFLK AHNYKGTTMM LNDRIQSLRG LQSSLRKAEE YLLSVPQDTP YSEFNHRFQE LGLEKGWGDT AKRVLDTLHL LLDLLEAPDP ANLEKFLGTI PMMFNVVILS PHGYFAQSNV LGYPDTGGQV VYILDQVRAL ENEMLLRIKQ QGLDITPKIL IVTRLLPDAA GTTCGQRLEK VIGTEHTDII RVPFRNENGI LRKWISRFDV WPYLETYTED VSSEIMKEMQ AKPDLIIGNY SDGNLVATLL AHKLGVTQCT IAHALEKTKY PNSDIYLDKF DSQYHFSCQF TADLIAMNHT DFIITSTFQE IAGSKDTVGQ YESHIAFTLP GLYRVVHGID VFDPKFNIVS PGADMSVYYP YTETDKRLTA FHPEIEELIY SDVENSEHKF VLKDKKKPII FSMARLDRVK NMTGLVEMYG KNARLRELAN LVIVAGDHGK ESKDREEQAE FKKMYSLIDE YKLKGHIRWI SAQMNRVRNG ELYRYICDTK GAFVQPAFYE AFGLTVIESM TCGLPTIATC HGGPAEIIVD GVSGLHIDPY HSDKAADILV NFFDKCKADP SYWDEISQGG LQRIYEKYTW KLYSERLMTL TGVYGFWKYV SNLERRETRR YIEMFYALKY RSLASQVPLS FD // ID SUS2_MAIZE STANDARD; PRT; 816 AA. AC P49036; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Sucrose synthase 2 (EC 2.4.1.13) (Sucrose-UDP glucosyltransferase 2). GN SUS1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94159796; PubMed=8115551; RA Huang X.-F., Nguyen-Quoc B., Chourey P.S., Yelle S.; RT "Complete nucleotide sequence of the maize (Zea mays L.) sucrose RT synthase 2 cDNA."; RL Plant Physiol. 104:293-294(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RA Nguyen-Quoc B., Huang X.-F., Krivitzky M., Yelle S., Lecharny A.; RT "Maize sucrose synthase 2: gene eequence and expression in the RT developing leaf."; RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP PHOSPHORYLATION. RC TISSUE=Leaf; RX MEDLINE=97037743; PubMed=8883390; RA Huber S.C., Huber J.L., Liao P.-C., Gage D.A., McMichael R.W. Jr., RA Chourey P.S., Hannah L.C., Koch K.; RT "Phosphorylation of serine-15 of maize leaf sucrose synthase. RT Occurrence in vivo and possible regulatory significance."; RL Plant Physiol. 112:793-802(1996). CC -!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and CC fructose for various metabolic pathways. CC -!- CATALYTIC ACTIVITY: NDP-glucose + D-fructose = NDP + sucrose. CC -!- SIMILARITY: Belongs to the glycosyltransferase family 1. Plant CC sucrose synthase subfamily. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L22296; AAA33514.1; -. DR EMBL; L33244; AAA33515.1; -. DR MaizeDB; 13861; -. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR000368; Sucrose_synth. DR Pfam; PF00534; Glycos_transf_1; 1. DR Pfam; PF00862; Sucrose_synth; 1. KW Transferase; Glycosyltransferase; Multigene family; Phosphorylation. FT MOD_RES 15 15 PHOSPHORYLATION. SQ SEQUENCE 816 AA; 92939 MW; E4DF863BE7AFC4C8 CRC64; MGEGAGDRVL SRLHSVRERI GDSLSAHPNE LVAVFTRLKN LGKGMLQPHQ IIAEYNNAIP EAEREKLKDG AFEDVLRAAQ EAIVIPPWVA LAIRPRPGVW EYVRVNVSEL AVEELRVPEY LQFKEQLVEE GPNNNFVLEL DFEPFNASFP RPSLSKSIGN GVQFLNRHLS SKLFHDKESM YPLLNFLRAH NYKGMTMMLN DRIRSLSALQ GALRKAEEHL STLQADTPYS EFHHRFQELG LEKGWGDCAK RAQETIHLLL DLLEAPDPST LEKFLGTIPM VFNVVILSPH GYFAQANVLG YPDTGGQVVY ILDQVRAMEN EMLLRIKQCG LDITPKILIV TRLLPDATGT TCGQRLEKVL GTEHCHILRV PFRTENGIVR KWISRFEVWP YLETYTDDVA HEIAGELQAN PDLIIGNYSD GNLVACLLAH KMGVTHCTIA HALEKTKYPN SDLYWKKFED HYHFSCQFTT DLIAMNHADF IITSTFQEIA GNKDTVGQYE SHMAFTMPGL YRVVHGIDVF DPKFNIVSPG ADLSIYFPYT ESHKRLTSLH PEIEELLYSQ TENTEHKFVL NDRNKPIIFS MARLDRVKNL TGLVELYGRN KRLQELVNLV VVCGDHGNPS KDKEEQAEFK KMFDLIEQYN LNGHIRWISA QMNRVRNGEL YRYICDTKGA FVQPAFYEAF GLTVVEAMTC GLPTFATAYG GPAEIIVHGV SGYHIDPYQG DKASALLVDF FDKCQAEPSH WSKISQGGLQ RIEEKYTWKL YSERLMTLTG VYGFWKYVSN LERRETRRYL EMLYALKYRT MASTVPLAVE GEPSSK // ID TBA1_MAIZE STANDARD; PRT; 451 AA. AC P14640; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tubulin alpha-1 chain (Alpha-1 tubulin). GN TUBA1 OR TUA1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; TISSUE=Root; RX MEDLINE=91322482; PubMed=1713800; RA Montoliu L., Rigau J., Puigdomenech P.; RT "A tandem of alpha-tubulin genes preferentially expressed in RT radicular tissues from Zea mays."; RL Plant Mol. Biol. 14:1-15(1990). CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It CC binds two moles of GTP, one at an exchangeable site on the beta CC chain and one at a nonexchangeable site on the alpha-chain. CC -!- SUBUNIT: Dimer of alpha and beta chains. CC -!- SIMILARITY: Belongs to the tubulin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15704; CAA33734.1; -. DR PIR; S15773; S15773. DR MaizeDB; 17141; -. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (Potential). FT SITE 451 451 Involved in polymerization. SQ SEQUENCE 451 AA; 49731 MW; 32815A2055702414 CRC64; MRECISIHIG QAGIQVGNAC WELYCLEHGI QADGQMPGDK TIGGGDDAFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD RIRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT VYPSPQVSTS VVEPYNSVLS THSLLEHTDV AILLDNEAIY DICRRSLDIE RPTYTNLNRL VSQVISSLTA SLRFDGALNV DVNEFQTNLV PYPRIHFMLS SYAPVISAEK AYHEQLSVAE ITNSAFEPSS MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP SVVPGGDLAK VQRAVCMISN STSVVEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGAEFD EGEDGDEGDE Y // ID TBA2_MAIZE STANDARD; PRT; 451 AA. AC P14641; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tubulin alpha-2 chain (Alpha-2 tubulin). GN TUBA2 OR TUA2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; TISSUE=Root; RX MEDLINE=91322482; PubMed=1713800; RA Montoliu L., Rigau J., Puigdomenech P.; RT "A tandem of alpha-tubulin genes preferentially expressed in RT radicular tissues from Zea mays."; RL Plant Mol. Biol. 14:1-15(1990). CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It CC binds two moles of GTP, one at an exchangeable site on the beta CC chain and one at a nonexchangeable site on the alpha-chain. CC -!- SUBUNIT: Dimer of alpha and beta chains. CC -!- SIMILARITY: Belongs to the tubulin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15704; CAA33733.1; -. DR PIR; S15772; S15772. DR MaizeDB; 17141; -. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (Potential). FT SITE 451 451 Involved in polymerization. SQ SEQUENCE 451 AA; 49731 MW; C7815A2054C02415 CRC64; MRECISIHIG QAGIQVGNAC WELYCLEHGI QADGQMPGDK TIGGGDDAFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD RIRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT VYPSPQVSTS VVEPYNSVLS THSLLEHTDV AILLDNEAIY DICRRSLDIE RPTYTNLNRL VSQVISSLTA SLRFDGALNV DVNEFQTNLV PYPRIHFMLS SYAPVISAEK AYHEQLSVAE ITNSAFEPSS MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP SVVPGGDLAK VQRAVCMISN STSVVEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGAEFD EGEEGDDGDE Y // ID TBA3_MAIZE STANDARD; PRT; 450 AA. AC P22275; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tubulin alpha-3 chain (Alpha-3 tubulin). GN TUBA3 OR TUA3. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91078640; PubMed=1701749; RA Montoliu L., Puigdomenech P., Rigau J.; RT "The Tub alpha 3 gene from Zea mays: structure and expression in RT dividing plant tissues."; RL Gene 94:201-207(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Shoot; RX MEDLINE=92395680; PubMed=1522603; RA Villemur R., Joyce C.M., Haas N.A., Goddard R.H., Kopczak S.D., RA Hussey P.J., Snustad D.P., Silflow C.D.; RT "Alpha-tubulin gene family of maize (Zea mays L.). Evidence for two RT ancient alpha-tubulin genes in plants."; RL J. Mol. Biol. 227:81-96(1992). CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It CC binds two moles of GTP, one at an exchangeable site on the beta CC chain and one at a nonexchangeable site on the alpha-chain. CC -!- SUBUNIT: Dimer of alpha and beta chains. CC -!- SIMILARITY: Belongs to the tubulin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M60171; AAA33518.1; -. DR EMBL; X63176; CAA44861.1; -. DR PIR; JN0105; JN0105. DR MaizeDB; 17141; -. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (Potential). FT SITE 450 450 Involved in polymerization. SQ SEQUENCE 450 AA; 49561 MW; 1BAB7E7C16615224 CRC64; MRECISVHIG QAGIQVGNAC WELYCLEHGI QPDGQVPGDK TAGHHDDAFS TFFSQTGAGK HVPRAIFVDL EPTVIDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD RIRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVE YGKKSKLGFT VYPSPQVSTS VVEPYNSVLS THSLLEHTDV SILLDNEAIY DICRRSLDIE RPNYSNLNRL VSQVISSLTA SLRFDGALNV DVNEFQTNLV PYPRIHFMLS SYAPVISSAK AFHEQLSVAE ITSSAFEPAS MMVKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQAP TVVPGADLAK VQRAVCMISN STSVVEVFSR INSKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVAAEGG SDDGDEEEEY // ID TBA4_MAIZE STANDARD; PRT; 61 AA. AC P33626; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tubulin alpha-4 chain (Alpha-4 tubulin) (Fragments). GN TUBA4 OR TUA4. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Shoot; RX MEDLINE=92395680; PubMed=1522603; RA Villemur R., Joyce C.M., Haas N.A., Goddard R.H., Kopczak S.D., RA Hussey P.J., Snustad D.P., Silflow C.D.; RT "Alpha-tubulin gene family of maize (Zea mays L.). Evidence for two RT ancient alpha-tubulin genes in plants."; RL J. Mol. Biol. 227:81-96(1992). CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It CC binds two moles of GTP, one at an exchangeable site on the beta CC chain and one at a nonexchangeable site on the alpha-chain. CC -!- SUBUNIT: Dimer of alpha and beta chains. CC -!- SIMILARITY: Belongs to the tubulin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63179; CAA44864.1; -. DR EMBL; X63180; CAA44865.1; -. DR MaizeDB; 17141; -. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR PROSITE; PS00227; TUBULIN; PARTIAL. KW Microtubule; GTP-binding; Multigene family. FT NON_CONS 46 47 FT SITE 61 61 Involved in polymerization. SQ SEQUENCE 61 AA; 6532 MW; C607503FE066E128 CRC64; MRECISIHIG QAGIQVGNAC WELYCLEHGI QADGQMPGDK TIGGGDAEFD EGEDGDEGDE Y // ID TBA5_MAIZE STANDARD; PRT; 450 AA. AC Q02245; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tubulin alpha-5 chain (Alpha-5 tubulin). GN TUBA5 OR TUA5. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Shoot; RX MEDLINE=92395680; PubMed=1522603; RA Villemur R., Joyce C.M., Haas N.A., Goddard R.H., Kopczak S.D., RA Hussey P.J., Snustad D.P., Silflow C.D.; RT "Alpha-tubulin gene family of maize (Zea mays L.). Evidence for two RT ancient alpha-tubulin genes in plants."; RL J. Mol. Biol. 227:81-96(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. Black Mexican Sweet; RA Morejohn L.C., Huang C.Y., Hunsperger J.P., Rubenstein I., Solomon F.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It CC binds two moles of GTP, one at an exchangeable site on the beta CC chain and one at a nonexchangeable site on the alpha-chain. CC -!- SUBUNIT: Dimer of alpha and beta chains. CC -!- SIMILARITY: Belongs to the tubulin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63177; CAA44862.1; -. DR EMBL; U05258; AAA16225.1; -. DR EMBL; L27815; AAA33437.1; -. DR PIR; S28982; S28982. DR MaizeDB; 17141; -. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (By similarity). FT SITE 450 450 Involved in polymerization. SQ SEQUENCE 450 AA; 49625 MW; E41B3F5F5683F02D CRC64; MREIISIHIG QAGIQVGNAC WELYCLEHGI EHDGTMPSDS SVGVAHDAFN TFFSETGSGK HVPRAIFVDL EPTVIDEVRT GSYRQLFHPE QLISGKEDAA NNFARGHYTV GKEIVDLCLD RVRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT IYPSPQVSTA VVEPYNSVLS THSLLEHTDV AVLLDNEAIY DICRRSLDIE RPTYTNLNRL ISQIISSLTT SLRFDGAINV DVTEFQTNLV PYPRIHFMLS SYAPVISAEK AYHEQLSVPE ITNAVFEPSS MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT VQFVDWCPTG FKCGINYQPP SVVPGGDLAK VQRAVCMISN NTAVAEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGAEGA DDEGDEGDDY // ID TBA6_MAIZE STANDARD; PRT; 450 AA. AC P33627; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tubulin alpha-6 chain (Alpha-6 tubulin). GN TUBA6 OR TUA6. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Shoot; RX MEDLINE=92395680; PubMed=1522603; RA Villemur R., Joyce C.M., Haas N.A., Goddard R.H., Kopczak S.D., RA Hussey P.J., Snustad D.P., Silflow C.D.; RT "Alpha-tubulin gene family of maize (Zea mays L.). Evidence for two RT ancient alpha-tubulin genes in plants."; RL J. Mol. Biol. 227:81-96(1992). CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It CC binds two moles of GTP, one at an exchangeable site on the beta CC chain and one at a nonexchangeable site on the alpha-chain. CC -!- SUBUNIT: Dimer of alpha and beta chains. CC -!- SIMILARITY: Belongs to the tubulin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63178; CAA44863.1; -. DR PIR; S28983; S28983. DR MaizeDB; 17141; -. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (By similarity). FT SITE 450 450 Involved in polymerization. SQ SEQUENCE 450 AA; 49599 MW; 114BC37E166F0931 CRC64; MREIISIHIG QAGIQVGNAC WELYCLEHGI EPDGTMPSDT SVGVAHDAFN TFFSETGSGK HVPRAIFVDL EPTVIDEVRT GSYRQLFHPE QLISGKEDAA NNFARGHYTV GKEIVDLCLD RVRKLADNCT GLQGFLVFNA VGGGTGSGLG SLLLERLSVD YGKKSKLGFT IYPSPQVSTA VVEPYNSVLS THSLLEHTDV AVLLDNEAIY DICRRSLDIE RPTYTNLNRL ISQIISSLTT SLRFDGAINV DVTEFQTNLV PYPRIHFMLS SYAPVISAEK AYHEQLSVPE ITNAVFEPSS MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT VQFVDWCPTG FKCGINYQPP SVVPGGDLAK VQRAVCMISN NTAVAEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGAEGA DDEGDEGDDY // ID TBB1_MAIZE STANDARD; PRT; 446 AA. AC P18025; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tubulin beta-1 chain (Beta-1 tubulin). GN TUBB1 OR TUB1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=91355923; PubMed=2103487; RA Hussey P.J., Haas N., Hunsperger J., Larkin J., Snustad D.P., RA Silflow C.D.; RT "The beta-tubulin gene family in Zea mays: two differentially RT expressed beta-tubulin genes."; RL Plant Mol. Biol. 15:957-972(1990). CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It CC binds two moles of GTP, one at an exchangeable site on the beta CC chain and one at a nonexchangeable site on the alpha-chain. CC -!- SUBUNIT: Dimer of alpha and beta chains. CC -!- TISSUE SPECIFICITY: Found in areas of rapidly dividing tissues. CC -!- SIMILARITY: Belongs to the tubulin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52878; CAA37060.1; -. DR PIR; S14701; S14701. DR MaizeDB; 24940; -. DR InterPro; IPR002453; Beta_tubulin. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; FALSE_NEG. DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 140 146 GTP (Potential). SQ SEQUENCE 446 AA; 49962 MW; 9A32D43927A21297 CRC64; MREILHIQGG QCGNQIGAKF WEVVCAEHGI DATGRYGGDS DLQLERVNVY YNEASCGRFV PRAVLMDLEP GTMDSVRSGP YGHIFRPDNF VFGQSGAGNN SAKGHYTEGA ELIDSVLDVV RKEAENCDCL QGFQVCHSLG GGTGSAMGTL LISKIREEYP DRMMLTFSVF PSPKVSDTVV EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLTTP SFGDLNHLIS ATMSGVTCCL RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YRALTVPELT QQMWDAKNMM CAADPRHGRY LTASAMFRGK MSTKEVDEQM LNVQNKNSSY FVEWIPNNVK STVCDIPPHG LKMASTFIGN STSIQEMFRR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEEGEYEDEE EGDLQD // ID TBB2_MAIZE STANDARD; PRT; 444 AA. AC P18026; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tubulin beta-2 chain (Beta-2 tubulin). GN TUBB2 OR TUB2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; TISSUE=Endosperm; RX MEDLINE=91355923; PubMed=2103487; RA Hussey P.J., Haas N., Hunsperger J., Larkin J., Snustad D.P., RA Silflow C.D.; RT "The beta-tubulin gene family in Zea mays: two differentially RT expressed beta-tubulin genes."; RL Plant Mol. Biol. 15:957-972(1990). CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It CC binds two moles of GTP, one at an exchangeable site on the beta CC chain and one at a nonexchangeable site on the alpha-chain. CC -!- SUBUNIT: Dimer of alpha and beta chains. CC -!- SIMILARITY: Belongs to the tubulin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52879; CAA37061.1; -. DR PIR; S14702; S14702. DR MaizeDB; 24940; -. DR InterPro; IPR002453; Beta_tubulin. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 140 146 GTP (Potential). SQ SEQUENCE 444 AA; 49883 MW; 0EBF0632A9081006 CRC64; MREILHIQGG QCGNQIGSKF WEVVCDEHGI DPTGRYMGTS DVQLERVNVY YNEASCGRFV PRAVLMDLEP GTMDAVRTGP YGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVLDVV RKEAENCDCL QGFQVCHSLG GGTGSGMGTL LISKIREEYP DRMMMTFSVF PSPKVSDTVV EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLTTP SFGDLNHLIS ATMSGVTCCL RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YRSLTVPELT QQMWDSKNMM CAADPRHGRY LTASAMFRGK MSTKEVDEQM INVQNKNSSY FVEWIPNNVK SSVCDIPPRG LSMSSTFVGN STSIQEMFRR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEEADYEEEE AAAE // ID TBG2_MAIZE STANDARD; PRT; 469 AA. AC Q41808; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Tubulin gamma-2 chain (Gamma-2 tubulin). GN TUBG2 OR TUBG OR TUBC. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Black Mexican Sweet; RA Canaday J., Stoppin V., Endle M.C., Lambert A.M.; RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Tubulin is the major constituent of microtubules. Gamma CC tubulin is found at microtubule organizing centers (MTOC) such as CC the spindle poles or the centrosome, suggesting that it is CC involved in the minus-end nucleation of microtubule assembly. CC -!- SIMILARITY: Belongs to the tubulin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X78891; CAA55488.1; -. DR PIR; S44193; S44193. DR MaizeDB; 113512; -. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR003008; Tubulin_FtsZ. DR Pfam; PF00091; tubulin; 1. DR Pfam; PF03953; tubulin_C; 1. DR PRINTS; PR01161; TUBULIN. DR PROSITE; PS00227; TUBULIN; 1. KW Microtubule; GTP-binding; Multigene family. FT NP_BIND 142 148 GTP (Potential). SQ SEQUENCE 469 AA; 52841 MW; 3F06E5848FA2B5D1 CRC64; MPREIITIQV GQCGNQIGME FWKQLCLEHG IGKDGLLEDF ATQGGDRKDV FFYQADDQHF IPRSLLIDLE PRVINGIQNS EYRNLYNHEN IFVAEHGGGA GNNWASGYHQ GEQVVDDIMD MVDREADGSD SLEGFVLCHS IAGGTGSGMG SYLLETLNDR YSKKLVQTYS VFPNQMETSD VVVQPYNSLL TLKRLTLNAD CVVVLDNTAL NRIAVERLHL SNPTFAQTNS LVSTVMSAST TTLRYPGYMN NDLVGLLASL IPTPRCHFLM TGYTPLTVER QVNMIRKTTV LDVMRRLLQT KNVMVSSYAR TKEASQAKYI SILNIIQGEV DPTQVHESLQ RIRERKLVNF IDWAPASIQV ALSRKSPYVQ TTHRVSGLML ANHTSIRHLF GKCLGQYEKL RKKQAFLDNY RKFPMFADND LSEFDESREI IESLVDEYKA CESPDYIKWG MEDPGEANVA ADLDSKLVV // ID TBP1_MAIZE STANDARD; PRT; 200 AA. AC P50158; Q43865; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE TATA-box binding protein 1 (TATA-box factor 1) (TATA binding factor 1) DE (TATA sequence-binding protein 1) (TBP-1) (Transcription initiation DE factor TFIID TBP-1 subunit). GN TBP1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73 Inbred; TISSUE=Leaf blade, and Sheath; RX MEDLINE=94146556; PubMed=8312743; RA Vogel J.M., Roth B., Cigan M., Freeling M.; RT "Expression of the two maize TATA binding protein genes and function RT of the encoded TBP proteins by complementation in yeast."; RL Plant Cell 5:1627-1638(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. RTCS 2; TISSUE=Endosperm; RX MEDLINE=97017135; PubMed=8863736; RA Goddemeier M.L., Feix G.; RT "Genomic structure of the maize TATA-box binding protein 1 (TBP-1): RT conserved exon/intron structure in eukaryotic TBP genes."; RL Gene 174:111-114(1996). CC -!- FUNCTION: General transcription factor that functions at the CC core of the DNA-binding multiprotein factor TFIID. Binding of CC TFIID to the TATA box is the initial transcriptional step of the CC pre-initiation complex (PIC), playing a role in the activation of CC eukaryotic genes transcribed by RNA polymerase II. CC -!- SUBUNIT: Belongs to the TFIID complex together with the TBP- CC associated factors (TAFs). Binds DNA as monomer. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Belongs to the TBP family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L13301; AAA65941.1; -. DR EMBL; X90652; CAA62224.1; ALT_SEQ. DR PIR; S21140; S21140. DR HSSP; P28148; 1VOL. DR MaizeDB; 25978; -. DR InterPro; IPR000814; TFIID. DR Pfam; PF00352; TBP; 2. DR PRINTS; PR00686; TIFACTORIID. DR PROSITE; PS00351; TFIID; 2. KW Transcription; Nuclear protein; DNA-binding; Repeat. FT REPEAT 25 101 1. FT REPEAT 115 192 2. FT VARIANT 5 5 G -> R (in Ref. 2). SQ SEQUENCE 200 AA; 22323 MW; 75B9E6D511024A41 CRC64; MAEPGLEDSQ PVDLSKHPSG IVPTLQNIVS TVNLDCKLDL KAIALQARNA EYNPKRFAAV IMRIREPKTT ALIFASGKMV CTGAKSEQQS KLAARKYARI IQKLGFPAKF KDFKIQNIVG SCDVKFPIRL EGLAYSHGAF SSYEPELFPG LIYRMKQPKI VLLIFVSGKI VLTGAKVREE TYTAFENIYP VLAEFRKVQQ // ID TBP2_MAIZE STANDARD; PRT; 200 AA. AC P50159; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE TATA-box binding protein 2 (TATA-box factor 2) (TATA binding factor 2) DE (TATA sequence-binding protein 2) (TBP-2) (Transcription initiation DE factor TFIID TBP-2 subunit). GN TBP2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73 Inbred; TISSUE=Leaf blade, and Sheath; RX MEDLINE=94146556; PubMed=8312743; RA Vogel J.M., Roth B., Cigan M., Freeling M.; RT "Expression of the two maize TATA binding protein genes and function RT of the encoded TBP proteins by complementation in yeast."; RL Plant Cell 5:1627-1638(1993). CC -!- FUNCTION: General transcription factor that functions at the CC core of the DNA-binding multiprotein factor TFIID. Binding of CC TFIID to the TATA box is the initial transcriptional step of the CC pre-initiation complex (PIC), playing a role in the activation of CC eukaryotic genes transcribed by RNA polymerase II. CC -!- SUBUNIT: Belongs to the TFIID complex together with the TBP- CC associated factors (TAFs). Binds DNA as monomer. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Belongs to the TBP family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L13302; AAA65942.1; -. DR PIR; S61088; S61088. DR HSSP; P28148; 1VOL. DR MaizeDB; 25978; -. DR InterPro; IPR000814; TFIID. DR Pfam; PF00352; TBP; 2. DR PRINTS; PR00686; TIFACTORIID. DR PROSITE; PS00351; TFIID; 2. KW Transcription; Nuclear protein; DNA-binding; Repeat. FT REPEAT 25 101 1. FT REPEAT 115 192 2. SQ SEQUENCE 200 AA; 22295 MW; 81A42559DF1F9A5B CRC64; MAEPGLEGSQ PVDLSKHPSG IVPTLQNIVS TVNLDCKLDL KAIALQARNA EYNPKRFAAV IMRIREPKTT ALIFASGKMV CTGAKSEQQS KLAARKYARI IQKLGFPAKF KDFKIQNIVG SCDVKFPIRL EGLAYSHGAF SSYEPELFPG LIYRMKQPKI VLLIFVSGKI VLTGAKVREE TYTAFENIYP VLSEFRKIQQ // ID TH41_MAIZE STANDARD; PRT; 354 AA. AC Q41738; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Thiazole biosynthetic enzyme 1-1, chloroplast precursor. GN THI1-1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seedling; RX MEDLINE=96128022; PubMed=8541506; RA Belanger F.C., Leustek T., Chu B., Kriz A.L.; RT "Evidence for the thiamine biosynthetic pathway in higher-plant RT plastids and its developmental regulation."; RL Plant Mol. Biol. 29:809-821(1995). CC -!- FUNCTION: Involved in biosynthesis of the thiamine precursor CC thiazole. CC -!- PATHWAY: Thiamine biosynthesis. CC -!- SUBCELLULAR LOCATION: Chloroplast; membrane associated. CC -!- TISSUE SPECIFICITY: Highest expression in developing embryos and CC green leaves and a very low level expression seen in endosperm, CC roots, etiolated shoots and immature ears. CC -!- DEVELOPMENTAL STAGE: During embryo development, expression CC increases from 15-21 days after pollination and decreases slightly CC at day 24 and this level is maintained until day 36. CC -!- SIMILARITY: Belongs to the THI4 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U17350; AAA96738.1; -. DR PIR; S61419; S61419. DR MaizeDB; 128724; -. DR InterPro; IPR002922; Thi4. DR Pfam; PF01946; Thi4; 1. DR TIGRFAMs; TIGR00292; TIGR00292; 1. KW Thiamine biosynthesis; Transit peptide; Chloroplast; Multigene family; KW FAD; NAD. FT TRANSIT 1 46 Chloroplast (Potential). FT CHAIN 47 354 Thiazole biosynthetic enzyme 1-1. FT NP_BIND 91 120 FAD or NAD (Potential). SQ SEQUENCE 354 AA; 37104 MW; 1D27B449CB9294DE CRC64; MATAAASSLL KSSFAGSRLP AATRTTPASL VVATGPRGAG AGPICASMSM SSSNPPYDLT SFRFSPIKES IVSREMTRRY MTDMITYADT DVVIVGAGSA GLSCAYELSK DPAVSIAIVE QSVSPGGGAW LGGQLFSAMV VRKPAHLFLD ELGVAYDEAE DYVVIKHAAL FTSTVMSLLL ARPNVKLFNA VAVEDLIVRG GRVGGVVTNW ALVSMNHDTQ SCMDPNVMEA KVVVSSCGHD GPFGATGVKR LQDIGMISAV PGMKALDMNT AEDEIVRLTR EVVPGMIVTG MEVAEIDGAP RMGPTFGAMM ISGQKAAHLA LKALGRPNAV DGTMSPPLRE ELMIAYKDDE VVDA // ID TH42_MAIZE STANDARD; PRT; 354 AA. AC Q41739; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Thiazole biosynthetic enzyme 1-2, chloroplast precursor. GN THI1-2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Seedling; RX MEDLINE=96128022; PubMed=8541506; RA Belanger F.C., Leustek T., Chu B., Kriz A.L.; RT "Evidence for the thiamine biosynthetic pathway in higher-plant RT plastids and its developmental regulation."; RL Plant Mol. Biol. 29:809-821(1995). CC -!- FUNCTION: Involved in biosynthesis of the thiamine precursor CC thiazole. CC -!- PATHWAY: Thiamine biosynthesis. CC -!- SUBCELLULAR LOCATION: Chloroplast; membrane associated. CC -!- TISSUE SPECIFICITY: Highest expression in developing embryos and CC green leaves and a very low level expression seen in endosperm, CC roots, etiolated shoots and immature ears. CC -!- DEVELOPMENTAL STAGE: During embryo development, expression CC increases from 15-21 days after pollination and decreases slightly CC at day 24 and this level is maintained until day 36. CC -!- SIMILARITY: Belongs to the THI4 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U17351; AAA96739.1; -. DR PIR; S61420; S61420. DR MaizeDB; 128724; -. DR InterPro; IPR002922; Thi4. DR Pfam; PF01946; Thi4; 1. DR TIGRFAMs; TIGR00292; TIGR00292; 1. KW Thiamine biosynthesis; Transit peptide; Chloroplast; Multigene family; KW FAD; NAD. FT TRANSIT 1 45 Chloroplast (Potential). FT CHAIN 46 354 Thiazole biosynthetic enzyme 1-2. FT NP_BIND 88 117 FAD or NAD (Potential). SQ SEQUENCE 354 AA; 37233 MW; 452E905B46B6AF13 CRC64; MATTAASSLL KSSFAGSRLP SATRTTTPSS VAVATPRAGG GPIRASISSP NPPYDLTSFR FSPIKESIVS REMTRRYMTD MITHADTDVV IVGAGSAGLS CAYELSKDPT VSVAIVEQSV SPGGGAWLGG QLFSAMVVRR PAHLFLDELG VGYDEAEDYV VVKHAALFTS TVMSRLLARP NVKLFNAVAV EDLIVRRGRV GGVVTNWALV SMNHDTQSCM DPNVMEAKVV VSSCGHDGPF GATGVKRLQD IGMISAVPGM KALDMNAAED EIVRLTREVV PGMIVTGMEV AEIDGAPRMG PTFGAMMISG QKAAHLALKA LGRPNAVDGT IPEVSPALRE EFVIASKDDE VVDA // ID THG1_MAIZE STANDARD; PRT; 47 AA. AC P81008; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Gamma-zeathionin 1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Seed; RA Castro M.S., Fontes W., Morhy L., Bloch C. Jr.; RT "Complete amino acid sequences of two gamma-thionins from maize (Zea RT mays L.) seeds."; RL Protein Pept. Lett. 3:267-274(1996). CC -!- FUNCTION: Thionins are small plant proteins which are toxic CC to animal cells. CC -!- SIMILARITY: Belongs to the plant defensin family. DR PIR; A58319; A58319. DR HSSP; P20158; 1GPS. DR MaizeDB; 139775; -. DR InterPro; IPR008176; Gamma-thionin. DR InterPro; IPR003614; Knot1. DR Pfam; PF00304; Gamma-thionin; 1. DR ProDom; PD002594; G_Purothionin; 1. DR SMART; SM00505; Knot1; 1. DR PROSITE; PS00940; GAMMA_THIONIN; 1. KW Plant defense; Plant toxin. FT DISULFID 3 47 By similarity. FT DISULFID 14 34 By similarity. FT DISULFID 20 41 By similarity. FT DISULFID 24 43 By similarity. SQ SEQUENCE 47 AA; 5199 MW; 0F3A74A58C3BBDFE CRC64; RVCRRRSAGF KGVCMSDHNC AQVCLQEGYG GGNCDGIMRQ CKCIRQC // ID THIM_MAIZE STANDARD; PRT; 167 AA. AC Q41864; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Thioredoxin M-type, chloroplast precursor (TRX-M). GN TRM1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B23; TISSUE=Leaf; RA Trevanion S.J., Ashton A.R.; RT "Isolation of a full-length cDNA clone for thioredoxin-m from maize."; RL (In) Plant Gene Register PGR95-129. CC -!- FUNCTION: Participates in various redox reactions through the CC reversible oxidation of the active center dithiol to a disulfide. CC The M form is known to activate NADP-malate dehydrogenase (By CC similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast (By similarity). CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L40957; AAA92464.1; -. DR PIR; T03957; T03957. DR HSSP; P80579; 1QUW. DR MaizeDB; 114054; -. DR InterPro; IPR006662; Thiored. DR InterPro; IPR006663; Thioredox_dom2. DR InterPro; IPR005746; Thioredoxin. DR Pfam; PF00085; thiored; 1. DR PRINTS; PR00421; THIOREDOXIN. DR TIGRFAMs; TIGR01068; thioredoxin; 1. DR PROSITE; PS00194; THIOREDOXIN; 1. KW Redox-active center; Electron transport; Chloroplast; Transit peptide. FT TRANSIT 1 53 Chloroplast (Potential). FT CHAIN 54 167 Thioredoxin M-type. FT DISULFID 89 92 Redox-active (By similarity). SQ SEQUENCE 167 AA; 18073 MW; 30679958A20C005E CRC64; MAMETCFRAW ALHAPAGSKD RLLVGNLVLP SKRALAPLSV GRVATRRPRH VCQSKNAVDE VVVADEKNWD GLVMACETPV LVEFWAPWCG PCRMIAPVID ELAKDYAGKI TCCKVNTDDS PNVASTYGIR SIPTVLIFKG GEKKESVIGA VPKSTLTTLI DKYIGSS // ID THZ2_MAIZE STANDARD; PRT; 47 AA. AC P81009; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Gamma-zeathionin 2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Seed; RA Castro M.S., Fontes W., Morhy L., Bloch C. Jr.; RT "Complete amino acid sequences of two gamma-thionins from maize (Zea RT mays L.) seeds."; RL Protein Pept. Lett. 3:267-274(1996). CC -!- FUNCTION: Thionins are small plant proteins which are toxic to CC animal cells. CC -!- SIMILARITY: Belongs to the plant defensin family. DR PIR; B58319; B58319. DR HSSP; P20230; 1GPT. DR MaizeDB; 139775; -. DR InterPro; IPR008176; Gamma-thionin. DR InterPro; IPR003614; Knot1. DR Pfam; PF00304; Gamma-thionin; 1. DR ProDom; PD002594; G_Purothionin; 1. DR SMART; SM00505; Knot1; 1. DR PROSITE; PS00940; GAMMA_THIONIN; 1. KW Plant defense; Plant toxin. FT DISULFID 3 47 By similarity. FT DISULFID 14 36 By similarity. FT DISULFID 20 41 By similarity. FT DISULFID 24 43 By similarity. SQ SEQUENCE 47 AA; 5368 MW; 4F0810A6D9532A0E CRC64; RVCMGKSQHH SFPCISDRLC SNECVKEDGG WTAGYCHLRY CRCQKAC // ID TOCC_MAIZE STANDARD; PRT; 474 AA. AC Q94FY8; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Probable tocopherol cyclase, chloroplast precursor (Sucrose export DE defective 1). GN SDX1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21238660; PubMed=11340186; RA Provencher L.M., Miao L., Sinha N., Lucas W.J.; RT "Sucrose export defective 1 encodes a novel protein implicated in RT chloroplast-to-nucleus signaling."; RL Plant Cell 13:1127-1141(2001). CC -!- FUNCTION: May be involved in the synthesis of tocopherols, which CC presumably protect photosynthetic complexes from oxidative stress. CC May prevent activation of a cell death pathway or may be invloved CC in the signaling between the chloroplast and the nucleus in CC bundle sheath cells (By similarity). CC -!- PATHWAY: Vitamin E biosynthesis. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- TISSUE SPECIFICITY: Present in all green tissues, both in bundle CC sheath and in mesophyll cells. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF302187; AAK60502.1; -. DR MaizeDB; 60529; -. KW Chloroplast; Transit peptide. FT TRANSIT 1 65 Chloroplast (Potential). FT CHAIN 66 474 Probable tocopherol cyclase. SQ SEQUENCE 474 AA; 52671 MW; 35204655F9942CD6 CRC64; MNLAVAAALP SVTPRTGVVL PRSSRRHCPR GVVPRAASSS VSSFTSPSAA AAPIYTPTPQ DRSLRTPHSG YHFDGTARPF FEGWYFKVSI PECRQSFCFM YSVENPLFRD GMSDLDKLLY RPRFTGVGAQ ILGADDKYIC QFSEKSNNFW GSRHELMLGN TFISNKESTP PQGEVPPQDF SRRVLEGLQV TPIWHQGFIR DDGRSNYVPN VQTARWEYST RPVYGWGDVK SKQLSTAGWL AAFPFFEPHW QICMARGLST GWIEWDGERF EFENAPSYSE KNWGGGFPRK WYWIQCNVFP GASGEVSLTA AGGLRKIGLG DTYESPSLIG IHYEGQFFEF VPWTGTVSWD IGLWGLWKMS GENKTHLVEI EATTAESGTA LRAPTIEAGL VPACKDTCYG DLRLQLWEKK YDGSKGEMIL DATSNMAALE VGGGPWFNGW KGTTVVNEVV NNIVGTPVDV ESLLPIPFLK PPGL // ID TPIS_MAIZE STANDARD; PRT; 252 AA. AC P12863; DT 01-OCT-1989 (Rel. 12, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE Triosephosphate isomerase, cytosolic (EC 5.3.1.1) (TIM). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86245049; PubMed=3755078; RA Marchionni M., Gilbert W.; RT "The triosephosphate isomerase gene from maize: introns antedate the RT plant-animal divergence."; RL Cell 46:133-141(1986). CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone CC phosphate. CC -!- PATHWAY: Plays an important role in several metabolic pathways. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic (Probable). CC -!- MISCELLANEOUS: In plants, there are two types of TPIS, cytosolic CC and plastid. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D00012; BAA00009.1; -. DR EMBL; L00371; AAB81110.1; -. DR PIR; A25501; ISZMT. DR HSSP; P00940; 1TPH. DR MaizeDB; 65619; -. DR InterPro; IPR000652; Triophos_ismrse. DR Pfam; PF00121; TIM; 1. DR ProDom; PD001005; Triophos_ismrse; 1. DR TIGRFAMs; TIGR00419; tim; 1. DR PROSITE; PS00171; TIM; 1. KW Isomerase; Glycolysis; Gluconeogenesis; Fatty acid biosynthesis; KW Pentose shunt. FT INIT_MET 0 0 FT ACT_SITE 95 95 By similarity. FT ACT_SITE 165 165 By similarity. SQ SEQUENCE 252 AA; 26894 MW; FC35EC8DA7A20543 CRC64; GRKFFVGGNW KCNGTTDQVE KIVKTLNEGQ VPPSDVVEVV VSPPYVFLPV VKSQLRQEFH VAAQNCWVKK GGAFTGEVSA EMLVNLGVPW VILGHSERRA LLGESNEFVG DKVAYALSQG LKVIACVGET LEQREAGSTM DVVAAQTKAI AEKIKDWSNV VVAYEPVWAI GTGKVATPAQ AQEVHASLRD WLKTNASPEV AESTRIIYGG SVTAANCKEL AAQPDVDGFL VGGASLKPEF IDIINAATVK SA // ID TRA1_MAIZE STANDARD; PRT; 806 AA. AC P08770; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Putative AC transposase (ORFA). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Kunze R., Stochaj U., Laufs J., Starlinger P.; RT "Transcription of transposable element Activator (Ac) of Zea mays L."; RL EMBO J. 6:1555-1563(1987). CC -!- MISCELLANEOUS: This protein is coded by the transposable maize CC controlling element "activator" (Ac), which is able to activate CC chromosome breakage at a specific location; it may be the CC structural gene for a trans-acting function required for CC transposition. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05424; CAA29005.1; -. DR PIR; T02916; T02916. DR MaizeDB; 65747; -. DR InterPro; IPR003656; BED_finger. DR InterPro; IPR008906; HATC. DR Pfam; PF05699; hATC; 1. DR Pfam; PF02892; zf-BED; 1. DR SMART; SM00614; ZnF_BED; 1. KW Transposable element; Transposition; DNA-binding; DNA recombination; KW Repeat. FT INIT_MET 0 0 FT DOMAIN 108 127 10 X 2 AA tandem repeats of P-[QE]. FT REPEAT 108 109 1. FT REPEAT 110 111 2. FT REPEAT 112 113 3. FT REPEAT 114 115 4. FT REPEAT 116 117 5. FT REPEAT 118 119 6. FT REPEAT 120 121 7. FT REPEAT 122 123 8. FT REPEAT 124 125 9. FT REPEAT 126 127 10. SQ SEQUENCE 806 AA; 91890 MW; B3B2B5BE79D53DED CRC64; TPPVGNNPPS GSAIRLAKLM STTRAPSTRK TNSVFSAYAQ GLKRKAEASS SRIQNVRARA RGHGCGRTSP SSSTAEAERH FIQSVSSSNA NGTATDPSQD DMAIVHEPQP QPQPQPEPQP QPQPEPEEEA PQKRAKKCTS DVWQHFTKKE IEVEVDGKKY VQVWGHCNFP NCKAKYRAEG HHGTSGFRNH LRTSHSLVKG QLCLKSEKDH GKDINLIEPY KYDEVVSLKK LHLAIIMHEY PFNIVEHEYF VEFVKSLRPH FPIKSRVTAR KYIMDLYLEE KEKLYGKLKD VQSRFSTTMD MWTSCQNKSY MCVTIHWIDD DWCLQKRIVG FFHVEGRHTG QRLSQTFTAI MVKWNIEKKL FALSLDNASA NEVAVHDIIE DLQDTDSNLV CDGAFFHVRC ACHILNLVAK DGLAVIAGTI EKIKAIVLAV KSSPLQWEEL MKCASECDLD KSKGISYDVS TRWNSTYLML RDALYYKPAL IRLKTSDPRR YDAICPKAEE WKMALTLFKC LKKFFDLTEL LSGTQYSTAN LFYKGFCEIK DLIDQWCVHE KFVIRRMAVA MSEKFEKYWK VSNIALAVAC FLDPRYKKIL IEFYMKKFHG DSYKVHVDDF VRVIRKLYQF YSSCSPSAPK TKTTTNDSMD DTLMENEDDE FQNYLHELKD YDQVESNELD KYMSEPLLKH SGQFDILSWW RGRVAEYPIL TQIARDVLAI QVSTVASESA FSAGGRVVDP YRNRLGSEIV EALICTKDWV AASRKGATYF PTMIGDLEVL DSVIAAATNH ENHMDEDEDA IEFSKNNEDV ASGSSP // ID TRA9_MAIZE STANDARD; PRT; 839 AA. AC P03010; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Putative AC9 transposase. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=84205699; PubMed=6327080; RA Pohlman R.F., Fedoroff N.V., Messing J.; RT "The nucleotide sequence of the maize controlling element Activator."; RL Cell 37:635-643(1984). CC -!- MISCELLANEOUS: This protein is coded by the transposable maize CC controlling element "activator" (Ac), which is able to activate CC chromosome breakage at a specific location; it may be the CC structural gene for a trans-acting function required for CC transposition. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; K01964; -; NOT_ANNOTATED_CDS. DR PIR; A03540; TQZMCA. DR MaizeDB; 65747; -. DR InterPro; IPR003656; BED_finger. DR InterPro; IPR008906; HATC. DR Pfam; PF05699; hATC; 1. DR Pfam; PF02892; zf-BED; 1. DR SMART; SM00614; ZnF_BED; 1. KW Transposable element; Transposition; DNA-binding; DNA recombination. SQ SEQUENCE 839 AA; 97068 MW; 803606AA325EA042 CRC64; MYVHVRVGMD VAAHHHHHQQ LRRERHFIQS VSSSNANGTA TDPSQDDMAI VHEPQPQPQP QPEPQPQPQP EPEEEAPQKR AKKCTSDVWQ HFTKKEIEVE VDGKKYVQVW GHCNFPNCKA KYRAEGHHGT SGFRNHLRTS HSLVKGQLCL KSEKDHGKDI NLIEPYKYDE VVSLKKLHLA IIMHEYPFNI VEHEYFVEFV KSLRPHFPIK SRVTARKYIM DLYLEEKEKL YGKLKDVQSR FSTTMDMWTS CQNKSYMCVT IHWIDDDWCL QKRIVGFFHV EGRHTGQRLS QTFTAIMVKW NIEKKLFALS LDNASANEVA VHDIIEDLQD TDSNLVCDGA FFHVRCACHI LNLVAKDGLA VIAGTIEKIK AIVLAVKSSP LQWEELMKCA SECDLDKSKG ISYDVSTRWN STYLMLRDAL YYKPALIRLK TSDPRRYVCL NCCTCHHYKF SINQMSIIVG TMQFVLKPRS GRWHLTLFKC LKKFFDLTEL LSGTQYSTAN LFYKGFCEIK DLIDQWCCHE KFVIRRMAVA MSEKFEKYWK VSNIALAVAC FLDPRYKKIL IEFYMKKFHG DSYKVHVDDF VRVIRKLYQF YSSCSPSAPK TKTTTNDSMD DTLMENEDDE FQNYLHELKD YDQVESNELD KYMSEPLLKH SGQFDILSWW RGRVAEYPIL TQIARDVLAI QVSTVASESA FSAGGRVVDP YRNRLGSEIV EALICTKDWV AASRKGEWHI CYNEVPIYSY STIILLILMH ICVIQGATYF PTMIGDLEVL DSVIAAATNH ENHMDEVFKD YYLLRAWAIN LLLFTTVLMH GLFLSPCFDA CALLPSRVIL PAWLALTDF // ID TRP1_MAIZE STANDARD; PRT; 389 AA. AC P43283; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Tryptophan synthase beta chain 1 (EC 4.2.1.20) (Orange pericarp 1) DE (Fragment). GN TSB1 OR ORP1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93005720; PubMed=1356534; RA Wright A.D., Moehlenkamp C.A., Perrot G.H., Neuffer M.G., RA Cone K.C.; RT "The maize auxotrophic mutant orange pericarp is defective in RT duplicate genes for tryptophan synthase beta."; RL Plant Cell 4:711-719(1992). CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L- CC tryptophan from indole and L-serine. CC -!- CATALYTIC ACTIVITY: L-serine + 1-(indol-3-yl)glycerol 3-phosphate CC = L-tryptophan + glyceraldehyde 3-phosphate. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Tryptophan biosynthesis; fifth (last) step. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. CC -!- SUBCELLULAR LOCATION: Chloroplast (Probable). CC -!- SIMILARITY: Belongs to the trpB family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M76684; AAA33490.1; -. DR PIR; PQ0449; PQ0449. DR HSSP; P00933; 2WSY. DR MaizeDB; 15412; -. DR InterPro; IPR001926; B6_enzyme_beta. DR InterPro; IPR006653; Trp_synth_b_rel. DR InterPro; IPR006654; Trp_synth_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR00263; trpB; 1. DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1. KW Tryptophan biosynthesis; Pyridoxal phosphate; Lyase; Chloroplast; KW Multigene family. FT NON_TER 1 1 FT BINDING 84 84 Pyridoxal phosphate (By similarity). SQ SEQUENCE 389 AA; 42519 MW; 64DB87D3CAC918EB CRC64; GRFGGKYVPE TLMHALTELE NAFHALATDD EFQKELDGIL KDYVGRESPL YFAERLTEHY KRADGTGPLI YLKREDLNHR GAHKINNAVA QALLAKRLGK QRIIAETGAG QHGVATATVC ARFGLQCIIY MGAQDMERQA LNVFRMKLLG AEVRAVHSGT ATLKDATSEA IRDWVTNVET THYILGSVAG PHPYPMMVRE FHKVIGKETR RQAMHKWGGK PDVLVACVGG GSNAMGLFHE FVEDQDVRLI GVEAAGHGVD TDKHAATLTK GQVGVLHGSM SYLLQDDDGQ VIEPHSISAG LDYPGVGPEH SFLKDIGRAE YDSVTDQEAL DAFKRVSRLE GIIPALETSH ALAYLEKLCP TLPDGVRVVL NCSGRGDKDV HTASKYLDV // ID TRP2_MAIZE STANDARD; PRT; 443 AA. AC P43284; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Tryptophan synthase beta chain 2, chloroplast precursor (EC 4.2.1.20) DE (Orange pericarp 2) (Fragment). GN TSB2 OR ORP2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93005720; PubMed=1356534; RA Wright A.D., Moehlenkamp C.A., Perrot G.H., Neuffer M.G., RA Cone K.C.; RT "The maize auxotrophic mutant orange pericarp is defective in RT duplicate genes for tryptophan synthase beta."; RL Plant Cell 4:711-719(1992). CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L- CC tryptophan from indole and L-serine. CC -!- CATALYTIC ACTIVITY: L-serine + 1-(indol-3-yl)glycerol 3-phosphate CC = L-tryptophan + glyceraldehyde 3-phosphate. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: Tryptophan biosynthesis; fifth (last) step. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. CC -!- SUBCELLULAR LOCATION: Chloroplast (Probable). CC -!- SIMILARITY: Belongs to the trpB family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M76685; AAA33491.1; -. DR PIR; PQ0450; PQ0450. DR HSSP; P00933; 2WSY. DR MaizeDB; 15412; -. DR InterPro; IPR001926; B6_enzyme_beta. DR InterPro; IPR006653; Trp_synth_b_rel. DR InterPro; IPR006654; Trp_synth_beta. DR Pfam; PF00291; PALP; 1. DR TIGRFAMs; TIGR00263; trpB; 1. DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1. KW Tryptophan biosynthesis; Pyridoxal phosphate; Lyase; Chloroplast; KW Transit peptide; Multigene family. FT NON_TER 1 1 FT TRANSIT <1 45 Chloroplast (Potential). FT CHAIN 46 443 Tryptophan synthase beta chain 2. FT BINDING 138 138 Pyridoxal phosphate (By similarity). SQ SEQUENCE 443 AA; 47844 MW; FC11A64D0761C9EC CRC64; PGPPPPAPEG RRRRGRGRNA AGQAVAAEAS PAAVEMGNGA AAPGLQRPDA MGRFGRFGGK YVPETLMHAL TELESAFHAL ATDDEFQKEL DGILKDYVGR ESPLYFAERL TEHYKRADGT GPLIYLKRED LNHTGAHKIN NAVAQALLAK RLGKQRIIAE TGAGQHGVAT ATVCRRFGLQ CIIYMGAQDM ERQALNVFRM RLLGAEVRAV HSGTATLKDA TSEAIRDWVT NVETTHYILG SVAGPHPYPM MVREFHKVIG KETRRQAMDK WGGKPDVLVA CVGGGSNAMG LFHEFVEDQD VRLVGLEAAG HGVDTDKHAA TLTKGQVGVL HGSMSYLLQD DDGQVIEPHS ISAGLDYPGV GPEHSFLKDI GRAEYDSVTD QEALDAFKRV SRLEGIIPAL ETSHALAYLE KLCPTLADGV RVVVNCSGRG DKDVHTASKY LDV // ID TRPA_MAIZE STANDARD; PRT; 346 AA. AC P42390; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Tryptophan synthase alpha chain, chloroplast precursor (EC 4.2.1.20). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. CG000237; RX MEDLINE=95284367; PubMed=7766899; RA Kramer V.C., Koziel M.G.; RT "Structure of a maize tryptophan synthase alpha subunit gene with RT pith enhanced expression."; RL Plant Mol. Biol. 27:1183-1188(1995). CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage CC of indoleglycerol phosphate to indole and glyceraldehyde 3- CC phosphate. CC -!- CATALYTIC ACTIVITY: L-serine + 1-(indol-3-yl)glycerol 3-phosphate CC = L-tryptophan + glyceraldehyde 3-phosphate. CC -!- PATHWAY: Tryptophan biosynthesis; fifth (last) step. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. CC -!- SUBCELLULAR LOCATION: Chloroplast (Probable). CC -!- SIMILARITY: Belongs to the trpA family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X76713; CAA54131.1; -. DR PIR; S56665; S56665. DR HSSP; P00929; 1A5B. DR MaizeDB; 102199; -. DR InterPro; IPR003009; FMN_enzyme. DR InterPro; IPR002028; Trp_synthaseA. DR Pfam; PF00290; trp_syntA; 1. DR ProDom; PD001535; Trp_synthaseA; 1. DR TIGRFAMs; TIGR00262; trpA; 1. DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1. KW Tryptophan biosynthesis; Lyase; Chloroplast; Transit peptide. FT TRANSIT 1 ? Chloroplast (Potential). FT CHAIN ? 346 Tryptophan synthase alpha chain. SQ SEQUENCE 346 AA; 36967 MW; 05F8FC2635071F3E CRC64; MAFAPKTSSS SSLSSALQAA QSPPLLLRRM SSTATPRRRY DAAVVVTTTT TARAAAAAVT VPAAPPQAGR RRRCHQSKRR HPQRRSRPVS DTMAALMAKG KTAFIPYITA GDPDLATTAE ALRLLDGCGA DVIELGVPCS DPYIDGPIIQ ASVARALASG TTMDAVLEML REVTPELSCP VVLLSYYKPI MSRSLAEMKE AGVHGLIVPD LPYVAAHSLW SEAKNNNLEL VLLTTPAIPE DRMKEITKAS EGFVYLVSVN GVTGPRANVN PRVESLIQEV KKVTNKPVAV GFGISKPEHV KQIAQWGADG VIIGSAMVRQ LGEAASPKQG LRRLEEYARG MKNALP // ID TS2_MAIZE STANDARD; PRT; 336 AA. AC P50160; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Sex determination protein tasselseed 2. GN TS2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=93364991; PubMed=8358795; RA Delong A., Calderon-Urrea A., Dellaporta S.L.; RT "Sex determination gene TASSELSEED2 of maize encodes a short-chain RT alcohol dehydrogenase required for stage-specific floral organ RT abortion."; RL Cell 74:757-768(1993). CC -!- FUNCTION: Required for stage-specific floral organ abortion. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L20621; AAC37345.1; -. DR PIR; A47542; A47542. DR HSSP; P19992; 1HDC. DR MaizeDB; 56963; -. DR InterPro; IPR002198; ADH_short. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. KW Oxidoreductase; Developmental protein. FT NP_BIND 59 83 NAD or NADP (By similarity). FT ACT_SITE 207 207 By similarity. SQ SEQUENCE 336 AA; 35204 MW; 4E273D6152B0BB99 CRC64; MHASLASYAA AAMPALDLRP EIAHAHQPVM SPSHHGWDGN GATAVPTPMP KRLDGKVAIV TGGARGIGEA IVRLFAKHGA RVVIADIDDA AGEALASALG PQVSFVRCDV SVEDDVRRAV DWALSRHGGR LDVYCNNAGV LGRQTRAARS ILSFDAAEFD RVLRVNALGA ALGMKHAARA MAPRRAGSIV SVASVAAVLG GLGPHAYTAS KHAIVGLTKN AACELRAHGV RVNCVSPFGV ATPMLINAWR QGHDDATADA DRDLDLDLDV TVPSDQEVEK MEEVVRGLAT LKGPTLRPRD IAEAVLFLAS DEARYISGHN LVVDGGVTTS RNLIGL // ID UBIQ_SOYBN STANDARD; PRT; 76 AA. AC P03993; O82079; DT 23-OCT-1986 (Rel. 02, Created) DT 23-OCT-1986 (Rel. 02, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Ubiquitin. OS Glycine max (Soybean), OS Pisum sativum (Garden pea), OS Avena sativa (Oat), OS Avena fatua (Wild oats), OS Hordeum vulgare (Barley), OS Triticum aestivum (Wheat), OS Zea mays (Maize), OS Helianthus annuus (Common sunflower), OS Lupinus albus (White lupine), OS Lupinus polyphyllus (Large-leaved lupine), OS Lycopersicon esculentum (Tomato), OS Solanum tuberosum (Potato), OS Linum usitatissimum (Flax) (Linseed), OS Nicotiana sylvestris (Wood tobacco), OS Asparagus officinalis (Garden asparagus), OS Oryza sativa (Rice), OS Petroselinum crispum (Parsley) (Petroselinum hortense), OS Brassica rapa (Turnip), and OS Daucus carota (Carrot). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847, 3888, 4498, 4499, 4513, 4565, 4577, 4232, 3870, 3874, OX 4081, 4113, 4006, 4096, 4686, 4530, 4043, 51350, 4039; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Soybean; RX MEDLINE=89083578; PubMed=2849766; RA Fortin M.G., Purohit S.K., Verma D.P.S.; RT "The primary structure of soybean (Glycine max) ubiquitin is RT identical to other plant ubiquitins."; RL Nucleic Acids Res. 16:11377-11377(1988). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Soybean; RX MEDLINE=94211917; PubMed=8159798; RA Bao-Sen X., Waterhouse R.N., Watanabe Y., Kajiwara H., Komatsu S., RA Hirano H.; RT "Nucleotide sequence of a soybean (Glycine max L. Merr.) ubiquitin RT gene."; RL Plant Physiol. 104:805-806(1994). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=P.sativum; RA Watts F.Z., Moore A.L.; RT "Nucleotide sequence of a full length cDNA clone encoding a RT polyubiquitin gene from Pisum sativum."; RL Nucleic Acids Res. 17:10100-10100(1989). RN [4] RP SEQUENCE. RC SPECIES=A.sativa; RA Vierstra R.D., Langan S.M., Schaller G.E.; RT "Complete amino acid sequence of ubiquitin from the higher plant RT Avena sativa."; RL Biochemistry 25:3105-3108(1986). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=H.vulgare; STRAIN=cv. Bomi; RX MEDLINE=86274685; PubMed=2426105; RA Gausing K., Barkardottir R.; RT "Structure and expression of ubiquitin genes in higher plants."; RL Eur. J. Biochem. 158:57-62(1986). RN [6] RP SEQUENCE FROM N.A. (MUB1 AND MUB2). RC SPECIES=H.vulgare; STRAIN=cv. Bomi; RX MEDLINE=91078635; PubMed=1701748; RA Gausing K., Jensen C.B.; RT "Two ubiquitin-long-tail fusion genes arranged as closely spaced RT direct repeats in barley."; RL Gene 94:165-171(1990). RN [7] RP SEQUENCE FROM N.A. RC SPECIES=T.aestivum; STRAIN=cv. Mustang; TISSUE=Leaf; RX MEDLINE=91316227; PubMed=1650258; RA Joshi C.P., Weng J., Nguyen H.T.; RT "Wheat ubiquitin gene exhibits a conserved protein coding region and RT a diverged 3' non-coding region."; RL Plant Mol. Biol. 16:907-908(1991). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=H.annuus; STRAIN=cv. HA401B / Cargill; RX MEDLINE=89183614; PubMed=2538802; RA Binet M.N., Steinmetz A., Tessier L.H.; RT "The primary structure of sunflower (Helianthus annuus) ubiquitin."; RL Nucleic Acids Res. 17:2119-2119(1989). RN [9] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RA Christensen A.H., Quail P.H.; RT "Sequence analysis and transcriptional regulation by heat shock of RT polyubiquitin transcripts from maize."; RL Plant Mol. Biol. 12:619-632(1989). RN [10] RP SEQUENCE FROM N.A. RC SPECIES=Maize; RX MEDLINE=92084112; PubMed=1660830; RA Chen K., Rubenstein I.; RT "Characterization of the structure and transcription of a ubiquitin RT fusion gene from maize."; RL Gene 107:205-212(1991). RN [11] RP SEQUENCE FROM N.A. RC SPECIES=L.polyphyllus; RX MEDLINE=91057134; PubMed=2173830; RA Perrey R., Warskulat U., Wink M.; RT "Molecular cloning of a cDNA for the ubiquitin gene of Lupinus RT polyphyllus."; RL Nucleic Acids Res. 18:6428-6428(1990). RN [12] RP SEQUENCE FROM N.A. RC SPECIES=L.albus; RX MEDLINE=94156199; PubMed=8112604; RA Jacinto A., Neves A.M., Vassilevskaia T.D., Ricardo C.P., RA Rodrigues-Pousada C.; RT "Cloning and characterization of two ubiquitin::79-amino-acid RT extension protein-encoding fusion genes from Lupinus albus."; RL Gene 139:201-205(1994). RN [13] RP SEQUENCE FROM N.A. RC SPECIES=L.usitatissimum; RX MEDLINE=91216447; PubMed=1850710; RA Agarwal M.L., Cullis C.A.; RT "The ubiquitin-encoding multigene family of flax, Linum RT usitatissimum."; RL Gene 99:69-75(1991). RN [14] RP SEQUENCE FROM N.A. (UBI3). RC SPECIES=L.esculentum; TISSUE=Root; RX MEDLINE=92032784; PubMed=1657246; RA Hoffman N.E., Ko K., Milkowski D., Pichersky E.; RT "Isolation and characterization of tomato cDNA and genomic clones RT encoding the ubiquitin gene ubi3."; RL Plant Mol. Biol. 17:1189-1201(1991). RN [15] RP SEQUENCE FROM N.A. (UBI3). RC SPECIES=S.tuberosum; STRAIN=cv. Lemhi Russet; TISSUE=Tuber; RX MEDLINE=93004476; PubMed=1327270; RA Garbarino J.E., Rockhold D.R., Belknap W.R.; RT "Expression of stress-responsive ubiquitin genes in potato tubers."; RL Plant Mol. Biol. 20:235-244(1992). RN [16] RP SEQUENCE FROM N.A. (UBI3). RC SPECIES=S.tuberosum; STRAIN=cv. Lemhi Russet; TISSUE=Tuber; RX MEDLINE=94154225; PubMed=8111011; RA Garbarino J.E., Belknap W.R.; RT "Isolation of a ubiquitin-ribosomal protein gene (ubi3) from potato RT and expression of its promoter in transgenic plants."; RL Plant Mol. Biol. 24:119-127(1994). RN [17] RP SEQUENCE FROM N.A. RC SPECIES=N.sylvestris; TISSUE=Leaf; RX MEDLINE=93099242; PubMed=1281439; RA Genschik P., Parmentier Y., Durr A., Marbach J., Criqui M.C., RA Jamet E., Fleck J.; RT "Ubiquitin genes are differentially regulated in protoplast-derived RT cultures of Nicotiana sylvestris and in response to various RT stresses."; RL Plant Mol. Biol. 20:897-910(1992). RN [18] RP SEQUENCE FROM N.A. RC SPECIES=A.officinalis; STRAIN=cv. Limbras 10; TISSUE=Spear; RA Davies K.M., King G.A.; RT "Isolation and characterization of Asparagus officinalis L. cDNA RT clones encoding two forms of ubiquitin mRNA."; RL N. Z. J. Crop Hortic. Sci. 21:153-159(1993). RN [19] RP SEQUENCE FROM N.A. RC SPECIES=O.sativa; RX MEDLINE=93271454; PubMed=8388748; RA Nishi P., Hashimoto H., Kidou S.I., Uchimiya H., Kato A.; RT "Isolation and characterization of a rice cDNA which encodes a RT ubiquitin protein and a 52 amino acid extension protein."; RL Plant Mol. Biol. 22:159-161(1993). RN [20] RP SEQUENCE FROM N.A. RC SPECIES=A.fatua; RX MEDLINE=93081737; PubMed=1333296; RA Reynolds G.J., Hooley R.; RT "cDNA cloning of a tetraubiquitin gene, and expression of ubiquitin- RT containing transcripts, in aleurone layers of Avena fatua."; RL Plant Mol. Biol. 20:753-758(1992). RN [21] RP SEQUENCE FROM N.A. RC SPECIES=P.crispum; RX MEDLINE=93192527; PubMed=8383552; RA Kawalleck P., Somssich I.E., Hahlbrock K., Feldbruegge M., RA Weisshaar B.; RT "Polyubiquitin gene expression and structural properties of the RT ubi4-2 gene in Petroselinum crispum."; RL Plant Mol. Biol. 21:673-684(1993). RN [22] RP SEQUENCE FROM N.A. RC SPECIES=B.rapa; RA Song S., Choi Y.; RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases. RN [23] RP SEQUENCE FROM N.A. RC SPECIES=D.carota; STRAIN=cv. Lunga di Amsterdam; RA Balestrazzi A., Cella R., Carbonera D.; RT "Cloning and expression analysis of a cDNA for carrot ubiquitin RT carboxyl extension protein."; RL (In) Plant Gene Register PGR98-109. CC -!- FUNCTION: Involved in the ATP-dependent selective degradation of CC cellular proteins, the maintenance of chromatin structure, the CC regulation of gene expression, the stress response, and ribosome CC biogenesis. CC -!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic. CC -!- MISCELLANEOUS: Ubiquitin is generally synthesized as a CC polyubiquitin precursor. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13251; CAA31627.1; ALT_TERM. DR EMBL; D16248; BAA03764.1; ALT_TERM. DR EMBL; X17020; CAA34886.1; ALT_TERM. DR EMBL; X04133; CAA27751.1; ALT_TERM. DR EMBL; M60175; AAA62698.1; ALT_TERM. DR EMBL; M60176; AAA62699.1; ALT_TERM. DR EMBL; X56601; CAA39938.1; ALT_TERM. DR EMBL; X14333; CAA32511.1; ALT_TERM. DR EMBL; M68937; AAA33519.1; ALT_TERM. DR EMBL; Z22612; CAA80333.1; ALT_TERM. DR EMBL; Z22613; CAA80334.1; ALT_TERM. DR EMBL; X54381; CAA38256.1; ALT_TERM. DR EMBL; M57895; AAA33401.1; ALT_TERM. DR EMBL; X58253; CAA41207.1; ALT_TERM. DR EMBL; Z11669; CAA77735.1; ALT_TERM. DR EMBL; L22576; AAA19247.1; ALT_TERM. DR EMBL; M74100; AAA34064.1; ALT_TERM. DR EMBL; M74101; AAA34123.1; ALT_TERM. DR EMBL; M74156; AAA34124.1; ALT_TERM. DR EMBL; X66875; CAA47346.1; ALT_TERM. DR EMBL; D12629; BAA02154.1; ALT_TERM. DR EMBL; D12776; BAA02241.1; ALT_TERM. DR EMBL; X69422; CAA49200.1; ALT_TERM. DR EMBL; X64344; CAA45621.1; ALT_TERM. DR EMBL; X64345; CAA45622.1; ALT_TERM. DR EMBL; Z24738; CAA80863.1; ALT_TERM. DR EMBL; L21898; AAA33014.1; ALT_TERM. DR EMBL; U68751; AAC26159.1; ALT_TERM. DR PIR; A02576; UQOA. DR PIR; A25062; A25062. DR PIR; JH0226; JH0226. DR PIR; JH0227; JH0227. DR PIR; PS0428; PS0428. DR PIR; S03599; UQFS. DR PIR; S12161; S12161. DR PIR; S18351; UQTO7A. DR PIR; S25001; S25001. DR HSSP; P02248; 1UBI. DR MaizeDB; 26015; -. DR MaizeDB; 26021; -. DR MaizeDB; 65187; -. DR InterPro; IPR000626; Ubiquitin. DR Pfam; PF00240; ubiquitin; 1. DR PRINTS; PR00348; UBIQUITIN. DR SMART; SM00213; UBQ; 1. DR PROSITE; PS00299; UBIQUITIN_1; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. KW Nuclear protein; Polyprotein. FT SITE 48 48 Necessary for branched-chain FT multiubiquitin adducts. FT BINDING 76 76 Acceptor proteins. SQ SEQUENCE 76 AA; 8525 MW; 852936277CD8403E CRC64; MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN IQKESTLHLV LRLRGG // ID UC03_MAIZE STANDARD; PRT; 18 AA. AC P80609; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 146) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 5.1, its MW is: 29.3 kDa. CC -!- CAUTION: The order of the peptides shown is uncertain. DR Maize-2DPAGE; P80609; COLEOPTILE. DR MaizeDB; 123924; -. FT NON_TER 1 1 FT NON_CONS 9 10 FT NON_TER 18 18 SQ SEQUENCE 18 AA; 1938 MW; 6F513BEBC35881C0 CRC64; AAVSLLQNKL AYDGFLSK // ID UC04_MAIZE STANDARD; PRT; 14 AA. AC P80610; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 128) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.8, its MW is: 34.6 kDa. DR Maize-2DPAGE; P80610; COLEOPTILE. DR MaizeDB; 123926; -. FT NON_TER 1 1 FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1393 MW; C14451BA1116D4AD CRC64; ADEGFSATVR NGAV // ID UC05_MAIZE STANDARD; PRT; 28 AA. AC P80611; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 154) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.8, its MW is: 35.3 kDa. CC -!- CAUTION: The order of the peptides shown is uncertain. DR Maize-2DPAGE; P80611; COLEOPTILE. DR MaizeDB; 123928; -. FT NON_TER 1 1 FT NON_CONS 15 16 FT NON_TER 28 28 SQ SEQUENCE 28 AA; 2932 MW; 9A3E0D47B441BA0E CRC64; DHPGVRDGTN IVLXKILPWG DEAYAAGG // ID UC06_MAIZE STANDARD; PRT; 15 AA. AC P80612; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 1131) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.8, its MW is: 71.0 kDa. DR Maize-2DPAGE; P80612; COLEOPTILE. DR MaizeDB; 123930; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1390 MW; 7005E22830F23D61 CRC64; AAAAPPRRGP SGPDA // ID UC07_MAIZE STANDARD; PRT; 22 AA. AC P80613; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 168) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.3, its MW is: 48.9 kDa. CC -!- CAUTION: The order of the peptides shown is uncertain. DR Maize-2DPAGE; P80613; COLEOPTILE. DR MaizeDB; 123932; -. FT NON_TER 1 1 FT NON_CONS 14 15 FT NON_TER 22 22 SQ SEQUENCE 22 AA; 2287 MW; 27C17392942E6D09 CRC64; IILELAAVDS ASGKLLINGN FK // ID UC08_MAIZE STANDARD; PRT; 15 AA. AC P80614; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 159) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.4, its MW is: 38.8 kDa. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. DR Maize-2DPAGE; P80614; COLEOPTILE. DR MaizeDB; 123934; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1785 MW; 1978B1D6AB4DDF8D CRC64; NDWRNAMYPV VPGHE // ID UC09_MAIZE STANDARD; PRT; 32 AA. AC P80615; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 206) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.4, its MW is: 16.9 kDa. CC -!- CAUTION: The order of the peptides shown is uncertain. DR Maize-2DPAGE; P80615; COLEOPTILE. DR MaizeDB; 123936; -. FT NON_TER 1 1 FT NON_CONS 17 18 FT NON_CONS 24 25 FT NON_TER 32 32 SQ SEQUENCE 32 AA; 3249 MW; 8841DBE253F211D6 CRC64; ITEEVAAAAA VGAGGYVXXL GEAGHHHLFN HE // ID UC11_MAIZE STANDARD; PRT; 40 AA. AC P80617; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 207) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.2, its MW is: 27.1 kDa. CC -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family. CC -!- CAUTION: The order of the peptides shown is uncertain. DR Maize-2DPAGE; P80617; COLEOPTILE. DR MaizeDB; 123940; -. FT NON_TER 1 1 FT NON_CONS 13 14 FT NON_CONS 26 27 FT NON_CONS 35 36 FT NON_TER 40 40 SQ SEQUENCE 40 AA; 4475 MW; 2ACD4BF8F4908277 CRC64; GLAYEYLEQD LGKKSELLLA ANPVHKVYDF VXGMKPEVAK // ID UC12_MAIZE STANDARD; PRT; 40 AA. AC P80618; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 237) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.0, its MW is: 21.7 kDa. CC -!- SIMILARITY: TO THE TOMATO ABSCISIC STRESS RIPENING PROTEINS. CC -!- CAUTION: The order of the peptides shown is uncertain. DR Maize-2DPAGE; P80618; COLEOPTILE. DR MaizeDB; 123942; -. FT NON_TER 1 1 FT NON_CONS 15 16 FT NON_CONS 25 26 FT NON_TER 40 40 SQ SEQUENCE 40 AA; 4426 MW; 2E4B14B6B37B34C2 CRC64; IEEEVAAAAA VGSGGXHHHH LFHHKXPEHA HRHKIEEEVA // ID UC14_MAIZE STANDARD; PRT; 15 AA. AC P80620; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 258) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 5.9, its MW is: 34.6 kDa. DR Maize-2DPAGE; P80620; COLEOPTILE. DR MaizeDB; 123944; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1564 MW; CF0BBAA0B7DE6658 CRC64; AYGGDGGAYY EWSPA // ID UC15_MAIZE STANDARD; PRT; 14 AA. AC P80621; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 245) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 4.8, its MW is: 35.7 kDa. DR Maize-2DPAGE; P80621; COLEOPTILE. DR MaizeDB; 123947; -. FT NON_TER 1 1 FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1396 MW; C68949275F404CD2 CRC64; VSTLLPVVAA EEPA // ID UC16_MAIZE STANDARD; PRT; 15 AA. AC P80622; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 308) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 5.9, its MW is: 18.6 kDa. DR Maize-2DPAGE; P80622; COLEOPTILE. DR MaizeDB; 123948; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1796 MW; D331A518F7440BE7 CRC64; QVWYDREVTA FVEPG // ID UC17_MAIZE STANDARD; PRT; 15 AA. AC P80623; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 32) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 5.5, its MW is: 42.7 kDa. DR Maize-2DPAGE; P80623; COLEOPTILE. DR MaizeDB; 123949; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1554 MW; C0AFFF15FFECEEC8 CRC64; ALSVPVFAVA PLNKK // ID UC18_MAIZE STANDARD; PRT; 14 AA. AC P80624; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 263) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.1, its MW is: 50.3 kDa. DR Maize-2DPAGE; P80624; COLEOPTILE. DR MaizeDB; 123950; -. FT NON_TER 1 1 FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1485 MW; 2EF9116472A39458 CRC64; DVHSNTGIFG IHTS // ID UC19_MAIZE STANDARD; PRT; 15 AA. AC P80625; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 406) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 5.6, its MW is: 18.4 kDa. DR Maize-2DPAGE; P80625; COLEOPTILE. DR MaizeDB; 123951; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1672 MW; 1CF69D4DA8737F9D CRC64; NGRRYTTYGC SPPVT // ID UC20_MAIZE STANDARD; PRT; 15 AA. AC P80626; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 445) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.1, its MW is: 45.3 kDa. CC -!- SIMILARITY: TO ADOMET SYNTHETASES. DR Maize-2DPAGE; P80626; COLEOPTILE. DR MaizeDB; 123952; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1597 MW; D2EECE163EB10156 CRC64; TQVTVEYVNE GGAMV // ID UC21_MAIZE STANDARD; PRT; 18 AA. AC P80627; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 443) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 5.9, its MW is: 26.5 kDa. CC -!- SIMILARITY: TO L-ASCORBATE PEROXIDASES. DR Maize-2DPAGE; P80627; COLEOPTILE. DR MaizeDB; 123953; -. FT NON_TER 1 1 FT NON_TER 18 18 SQ SEQUENCE 18 AA; 1938 MW; F32F6FEF038BAB8A CRC64; AKNYPTVSAE YSXAVEKA // ID UC22_MAIZE STANDARD; PRT; 5 AA. AC P80628; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 474) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.1, its MW is: 30.4 kDa. DR Maize-2DPAGE; P80628; COLEOPTILE. DR MaizeDB; 123954; -. FT NON_TER 1 1 FT NON_TER 5 5 SQ SEQUENCE 5 AA; 654 MW; 72CB19C9C0300000 CRC64; IFFEV // ID UC23_MAIZE STANDARD; PRT; 15 AA. AC P80629; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 502) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.2, its MW is: 45.0 kDa. DR Maize-2DPAGE; P80629; COLEOPTILE. DR MaizeDB; 123955; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1557 MW; C974ED33E9A4EC28 CRC64; AGDKPGDALL DEWLG // ID UC24_MAIZE STANDARD; PRT; 7 AA. AC P80630; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 447) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.0, its MW is: 30.0 kDa. DR Maize-2DPAGE; P80630; COLEOPTILE. DR MaizeDB; 123956; -. FT NON_TER 1 1 FT NON_TER 7 7 SQ SEQUENCE 7 AA; 665 MW; 6DC1B5B33DC1B5D0 CRC64; STAKSTA // ID UC25_MAIZE STANDARD; PRT; 15 AA. AC P80631; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 77) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 4.9, its MW is: 31.6 kDa. DR Maize-2DPAGE; P80631; COLEOPTILE. DR MaizeDB; 123957; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1580 MW; 83C54CF0CE1614D0 CRC64; AIGGLSRSFP VEAFE // ID UC27_MAIZE STANDARD; PRT; 15 AA. AC P80633; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 688) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.4, its MW is: 48.4 kDa. CC -!- SIMILARITY: TO XENOPUS HISTONE-BINDING PROTEIN N1/N2 AND RABBIT CC AND HUMAN NUCLEAR AUTOANTIGENIC SPERM PROTEIN. DR Maize-2DPAGE; P80633; COLEOPTILE. DR MaizeDB; 123958; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1853 MW; CA0E12A5DAED8DC7 CRC64; EREQLRDQVY DAMAE // ID UC28_MAIZE STANDARD; PRT; 15 AA. AC P80634; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 984) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.2, its MW is: 27.7 kDa. DR Maize-2DPAGE; P80634; COLEOPTILE. DR MaizeDB; 123959; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1631 MW; 45C554E40BE9E77F CRC64; XLEGAFVLNQ SQDAE // ID UC29_MAIZE STANDARD; PRT; 15 AA. AC P80635; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 45) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 4.9, its MW is: 37.6 kDa. DR Maize-2DPAGE; P80635; COLEOPTILE. DR MaizeDB; 123960; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1679 MW; 3D53086B16018BC1 CRC64; NPNPVPIPLV DIDYL // ID UC30_MAIZE STANDARD; PRT; 15 AA. AC P80636; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 662) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 4.9, its MW is: 32.3 kDa. DR Maize-2DPAGE; P80636; COLEOPTILE. DR MaizeDB; 123961; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1545 MW; 3485190F4EF38018 CRC64; SGTSPLLPAI TFILD // ID UC31_MAIZE STANDARD; PRT; 19 AA. AC P80637; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 67) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 5.8, its MW is: 41.7 kDa. CC -!- CAUTION: The order of the peptides shown is uncertain. DR Maize-2DPAGE; P80637; COLEOPTILE. DR MaizeDB; 123962; -. FT NON_TER 1 1 FT NON_CONS 10 11 FT NON_TER 19 19 SQ SEQUENCE 19 AA; 2439 MW; DFB2A5C15E50E5F5 CRC64; WILHDWDEDK XXXPYYNTI // ID UC32_MAIZE STANDARD; PRT; 49 AA. AC P80638; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 75) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.0, its MW is: 38.0 kDa. CC -!- CAUTION: The order of the peptides shown is uncertain. DR Maize-2DPAGE; P80638; COLEOPTILE. DR MaizeDB; 123963; -. FT NON_TER 1 1 FT NON_CONS 11 12 FT NON_CONS 17 18 FT NON_CONS 23 24 FT NON_CONS 35 36 FT NON_CONS 41 42 FT NON_TER 49 49 SQ SEQUENCE 49 AA; 5577 MW; 4FF0389E13AD15BD CRC64; XADGAMINYV EAFPHIKCTV LAPEFGAYVA FEVYPGFSEY KEWSELFTK // ID UC34_MAIZE STANDARD; PRT; 14 AA. AC P80640; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 360) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 5.7, its MW is: 41.1 kDa. CC -!- CAUTION: The order of the peptides shown is uncertain. DR Maize-2DPAGE; P80640; COLEOPTILE. DR MaizeDB; 123965; -. FT NON_TER 1 1 FT NON_CONS 8 9 FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1527 MW; DC525FF7B0BE682D CRC64; SIXEPLALSV FDEP // ID UC35_MAIZE STANDARD; PRT; 30 AA. AC P80641; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 365) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.3, its MW is: 39.2 kDa. CC -!- SIMILARITY: TO THE ZINC-CONTAINING ALCOHOL DEHYDROGENASE FAMILY. CC -!- CAUTION: The order of the peptides shown is uncertain. DR Maize-2DPAGE; P80641; COLEOPTILE. DR MaizeDB; 123966; -. FT NON_TER 1 1 FT NON_CONS 15 16 FT NON_TER 30 30 SQ SEQUENCE 30 AA; 3092 MW; 9717DBF2630E37A6 CRC64; HLGVVGLGGL GHVAVXQEAI ENLXADEFLI // ID UC36_MAIZE STANDARD; PRT; 52 AA. AC P80642; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Unknown protein from 2D-PAGE of etiolated coleoptile (Spot 415) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this unknown CC protein is: 6.0, its MW is: 27.2 kDa. CC -!- SIMILARITY: TO THE L-ASCORBATE PEROXIDASES. CC -!- CAUTION: The order of the peptides shown is uncertain. DR Maize-2DPAGE; P80642; COLEOPTILE. DR MaizeDB; 123967; -. FT NON_TER 1 1 FT NON_CONS 8 9 FT NON_CONS 17 18 FT NON_CONS 24 25 FT NON_CONS 38 39 FT NON_CONS 45 46 FT NON_TER 52 52 SQ SEQUENCE 52 AA; 5840 MW; 70DE0034741CF335 CRC64; AKNYPTVSGS DHLRQVFXMG LSDQALLSDP VFRPLVEKXF FDDYAXRSGF EG // ID UCRI_MAIZE STANDARD; PRT; 273 AA. AC P49727; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial DE precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92073358; PubMed=1961737; RA Huang J.T., Struck F., Matzinger D.F., Levings C.S. III; RT "Functional analysis in yeast of cDNA coding for the mitochondrial RT Rieske iron-sulfur protein of higher plants."; RL Proc. Natl. Acad. Sci. U.S.A. 88:10716-10720(1991). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase CC complex (complex III or cytochrome b-c1 complex), which is a CC respiratory chain that generates an electrochemical potential CC coupled to ATP synthesis. CC -!- CATALYTIC ACTIVITY: QH(2) + 2 ferricytochrome c = Q + 2 CC ferrocytochrome c. CC -!- COFACTOR: Binds 1 2Fe-2S iron sulfur cluster per subunit (By CC similarity). CC -!- SUBUNIT: The bc1 complex contains 10 subunits; 3 respiratory CC subunits, 2 core proteins and 5 low-molecular weight proteins. CC -!- SUBCELLULAR LOCATION: Mitochondrial inner membrane. CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S CC protein. CC -!- SIMILARITY: Belongs to the Rieske family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77224; AAA33507.1; -. DR PIR; A41607; A41607. DR HSSP; P13272; 1RIE. DR MaizeDB; 30151; -. DR InterPro; IPR005805; Rieske. DR InterPro; IPR005806; Rieske_dom. DR InterPro; IPR006317; Rieske_proteo. DR InterPro; IPR004192; UCR_TM_region. DR Pfam; PF00355; Rieske; 1. DR Pfam; PF02921; UCR_TM; 1. DR PRINTS; PR00162; RIESKE. DR TIGRFAMs; TIGR01416; Rieske_proteo; 1. DR PROSITE; PS00199; RIESKE_1; 1. DR PROSITE; PS00200; RIESKE_2; 1. KW Mitochondrion; Electron transport; Respiratory chain; Metal-binding; KW Iron-sulfur; Iron; 2Fe-2S; Oxidoreductase; Inner membrane; KW Transmembrane; Transit peptide. FT TRANSIT 1 61 Mitochondrion (Potential). FT CHAIN 62 273 Ubiquinol-cytochrome c reductase iron- FT sulfur subunit. FT METAL 216 216 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 218 218 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 235 235 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 238 238 Iron-sulfur (2Fe-2S) (By similarity). FT DISULFID 221 237 By similarity. SQ SEQUENCE 273 AA; 29835 MW; 43B08C116E9B1A2C CRC64; MLRVAGRRLS SSLSWRPAAA VARGPLAGAG VPDRDDDSAR GRSQPRFSID SPFFVASRGF SSTETVVPRN QDAGLADLPA TVAAVKNPNP KVVYDEYNHE RYPPGDPSKR AFAYFVLSGG RFIYASLLRL LVLKFVLSMS ASKDVLALAS LEVDLSSIEP GTTVTVKWRG KPVFIRRRTE DDIKLANSVD VASLRHPEQD AERVKNPEWL VVIGVCTHLG CIPLPNAGDF GGWFCPCHGS HYDISGRIRK GPAPFNLEVP TYSFLEENKL LVG // ID UFO1_MAIZE STANDARD; PRT; 471 AA. AC P16166; Q9ATX0; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Flavonol 3-O-glucosyltransferase (EC 2.4.1.91) (UDP-glucose flavonoid DE 3-O-glucosyltransferase) (Bronze-1) (Bz-McC allele). GN BZ1 OR UGT71A1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Furtek D., Schiefelbein J.W., Johnston F., Nelson O.E. Jr.; RT "Sequence comparisons of 3 wild-type bronze-1 alleles from Zea mays."; RL Plant Mol. Biol. 11:473-481(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88284304; PubMed=3396861; RA Ralston E.J., English J.J., Dooner H.K.; RT "Sequence of three bronze alleles of maize and correlation with the RT genetic fine structure."; RL Genetics 119:185-197(1988). CC -!- FUNCTION: In the presence of other necessary color factors, this CC glycosylation reaction allows the accumulation of anthocyanin CC pigments. CC -!- CATALYTIC ACTIVITY: UDP-glucose + a flavonol = UDP + flavonol CC 3-O-D-glucoside. CC -!- PATHWAY: Anthocyanin biosynthesis. CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13500; CAA31855.1; -. DR EMBL; AF391808; AAK73112.1; -. DR PIR; S01052; S01052. DR MaizeDB; 13885; -. DR InterPro; IPR002213; UDP_gluco_trans. DR Pfam; PF00201; UDPGT; 1. DR PROSITE; PS00375; UDPGT; 1. KW Transferase; Glycosyltransferase. SQ SEQUENCE 471 AA; 48769 MW; 6234FD59219AF534 CRC64; MAPADGESSP PPHVAVVAFP FSSHAAVLLS IARALAAAAA PSGATLSFLS TASSLAQLRK ASSASAGHGL PGNLRFVEVP DGAPAAEETV PVPRQMQLFM EAAEAGGVKA WLEAARAAAG GARVTCVVGD AFVWPAADAA ASAGAPWVPV WTAASCALLA HIRTDALRED VGDQAANRVD GLLISHPGLA SYRVRDLPDG VVSGDFNYVI NLLVHRMGQC LPRSAAAVAL NTFPGLDPPD VTAALAEILP NCVPFGPYHL LLAEDDADTA APADPHGCLA WLGRQPARGV AYVSFGTVAC PRPDELRELA AGLEDSGAPF LWSLREDSWP HLPPGFLDRA AGTGSGLVVP WAPQVAVLRH PSVGAFVTHA GWASVLEGLS SGVPMACRPF FGDQRMNARS VAHVWGFGAA FEGAMTSAGV ATAVEELLRG EEGARMRARA KELQALVAEA FGPGGECRKN FDRFVEIVCR A // ID UFO2_MAIZE STANDARD; PRT; 471 AA. AC P16165; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Flavonol 3-O-glucosyltransferase (EC 2.4.1.91) (UDP-glucose flavonoid DE 3-O-glucosyltransferase) (Bronze-1) (Bz-Mc2 allele). GN BZ1 OR UGT71A1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Furtek D., Schiefelbein J.W., Johnston F., Nelson O.E. Jr.; RT "Sequence comparisons of 3 wild-type bronze-1 alleles from Zea mays."; RL Plant Mol. Biol. 11:473-481(1988). CC -!- FUNCTION: In the presence of other necessary color factors, this CC glycosylation reaction allows the accumulation of anthocyanin CC pigments. CC -!- CATALYTIC ACTIVITY: UDP-glucose + a flavonol = UDP + flavonol CC 3-O-D-glucoside. CC -!- PATHWAY: Anthocyanin biosynthesis. CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13501; CAA31856.1; -. DR PIR; S08325; S08325. DR MaizeDB; 13885; -. DR InterPro; IPR002213; UDP_gluco_trans. DR Pfam; PF00201; UDPGT; 1. DR PROSITE; PS00375; UDPGT; 1. KW Transferase; Glycosyltransferase. SQ SEQUENCE 471 AA; 48621 MW; 81B897410A361299 CRC64; MAPADGESSP PPHVAVVAFP FSSHAAVLLS IARALAAAAA PSGATLSFLS TASSLAQLRK ASSASAGHGL PGNLRFVEVP DGAPAAEETV PVPRQMQLFM EAAEAGGVKA WLEAARAAAG GARVTCVVGD AFVWPAADAA ASAGAPWVPV WTAASCALLA HIRTDSLRED VGDQAANRVD EPLISHPGLA SYRVRDLPDG VVSGDFNYVI SLLVHRMGQC LPRSAAAVAL NTFPGLDPPD VTAALAEILP NCVPFGPYHL LLAEDDADTA APADPHGCLA WLGRQPARGV AYVSFGTVAC PRPDELRELA AGLEASAAPF LWSLREDSWT LLPPGFLDRA AGTGSGLVVP WAPQVAVLRH PSVGAFVTHA GWASVLEGVS SGVPMACRPF FGDQRMNARS VAHVWGFGAA FEGAMTSAGV AAAVEELLRG EEGAGMRARA KELQALVAEA FGPGGECRKN FDRFVEIVCR A // ID UFO3_MAIZE STANDARD; PRT; 471 AA. AC P16167; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Flavonol 3-O-glucosyltransferase (EC 2.4.1.91) (UDP-glucose flavonoid DE 3-O-glucosyltransferase) (Bronze-1) (Bz-W22 allele). GN BZ1 OR UGT71A1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Furtek D., Schiefelbein J.W., Johnston F., Nelson O.E. Jr.; RT "Sequence comparisons of 3 wild-type bronze-1 alleles from Zea mays."; RL Plant Mol. Biol. 11:473-481(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88284304; PubMed=3396861; RA Ralston E.J., English J.J., Dooner H.K.; RT "Sequence of three bronze alleles of maize and correlation with the RT genetic fine structure."; RL Genetics 119:185-197(1988). CC -!- FUNCTION: In the presence of other necessary color factors, this CC glycosylation reaction allows the accumulation of anthocyanin CC pigments. CC -!- CATALYTIC ACTIVITY: UDP-glucose + a flavonol = UDP + flavonol CC 3-O-D-glucoside. CC -!- PATHWAY: Anthocyanin biosynthesis. CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13502; CAA31857.1; -. DR EMBL; X07937; CAA30760.1; -. DR PIR; S01037; S01037. DR MaizeDB; 13885; -. DR InterPro; IPR002213; UDP_gluco_trans. DR Pfam; PF00201; UDPGT; 1. DR PROSITE; PS00375; UDPGT; 1. KW Transferase; Glycosyltransferase. SQ SEQUENCE 471 AA; 48673 MW; F417020B78366C01 CRC64; MAPADGESSP PPHVAVVAFP FSSHAAVLLS IARALAAAAA PSGATLSFLS TASSLAQLRK ASSASAGHGL PGNLRFVEVP DGAPAAEESV PVPRQMQLFM EAAEAGGVKA WLEAARAAAG GARVTCVVGD AFVWPAADAA ASAGAPWVPV WTAASCALLA HIRTDALRED VGDQAANRVD EPLISHPGLA SYRVRDLPDG VVSGDFNYVI NLLVHRMGQC LPRSAAAVAL NTFPGLDPPD VTAALAEILP NCVPFGPYHL LLAEDDADTA APADPHGCLA WLGRQPARGV AYVSFGTVAC PRPDELRELA AGLEASGAPF LWSLREDSWT LLPPGFLDRA AGTGSGLVVP WAPQVAVLRH PSVGAFVTHA GWASVLEGVS SGVPMACRPF FGDQRMNARS VAHVWGFGAA FEGAMTSAGV AAAVEELLRG EEGARMRARA KVLQALVAEA FGPGGECRKN FDRFVEIVCR A // ID UPTG_MAIZE STANDARD; PRT; 364 AA. AC P80607; Q9SAQ2; DT 01-OCT-1996 (Rel. 34, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Alpha-1,4-glucan-protein synthase [UDP-forming] (EC 2.4.1.112) (UDP- DE glucose:protein transglucosylase) (UPTG) (Amylogenin) (Golgi DE associated protein se-wap41). GN UPTG. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Jubile; RA Katz A., Van Lent J.W.M., Kotlizky G., Yahalom A., Epel B.L.; RT "Isolation of a maize 41 kDa Golgi associated protein."; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 31-57; 133-193; 199-208; 244-254; 289-307 AND 337-359, AND RP GLYCOSYLATION. RX MEDLINE=96096788; PubMed=8521968; RA Singh D.G., Lomako J., Lomako W.M., Whelan W.J., Meyer H.E., Serwe M., RA Metzger J.W.; RT "Beta-glucosylarginine: a new glucose-protein bond in a self- RT glucosylating protein from sweet corn."; RL FEBS Lett. 376:61-64(1995). RN [3] RP SEQUENCE OF 61-75 FROM N.A. RC TISSUE=Coleoptile; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). RN [4] RP ENZYME ACTIVITY. RA Rothschild A., Tandecarz J.S.; RT "UDP-glucose:protein transglucosylase in developing maize endosperm."; RL Plant Sci. 97:119-127(1994). RN [5] RP SUBCELLULAR LOCATION. RA Epel B.L., Van Lent J.W.M., Cohen L., Kotlizky G., Katz A., RA Yahalom A.; RT "A 41kDa protein isolated from maize mesocotyl cell walls RT immunolocalizes to plasmodesmata."; RL Protoplasma 191:70-78(1996). RN [6] RP INHIBITION BY IP. RX MEDLINE=96428992; PubMed=8832094; RA Rothschild A., Wald F.A., Bocca S.N., Tandecarz J.S.; RT "Inhibition of UDP-glucose: protein transglucosylase by a maize RT endosperm protein factor."; RL Cell. Mol. Biol. 42:645-651(1996). RN [7] RP INHIBITION BY IP. RX MEDLINE=98281745; PubMed=9620435; RA Wald F.A., Rothschild A., Moreno S., Tandecarz J.S.; RT "Identification of a UPTG inhibitor protein from maize endosperm: high RT homology with sucrose synthase protein."; RL Cell. Mol. Biol. 44:397-406(1998). CC -!- FUNCTION: Possible role in the synthesis of cell wall CC polysaccharides (By similarity). CC -!- CATALYTIC ACTIVITY: UDP-glucose + protein = UDP + alpha-D- CC glucosyl-protein. CC -!- ENZYME REGULATION: Inhibited by inhibitor protein (IP) which may CC be a form of sucrose synthase. CC -!- SUBUNIT: Homopentamer or homohexamer (By similarity). CC -!- SUBCELLULAR LOCATION: Cell wall-associated, with highest CC concentrations on plasmodesmata. Also located in the Golgi CC apparatus. CC -!- PTM: Reversibly glycosylated by UDP-glucose, UDP-xylose and UDP- CC galactose, but not UDP-mannose. CC -!- SIMILARITY: Belongs to the RGP family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U89897; AAB49896.1; -. DR PIR; T04331; T04331. DR Maize-2DPAGE; P80607; COLEOPTILE. DR MaizeDB; 123920; -. DR MaizeDB; 131466; -. DR InterPro; IPR004901; RGP. DR Pfam; PF03214; RGP; 1. KW Cellulose biosynthesis; Transferase; Glycosyltransferase; Membrane; KW Golgi stack; Cell wall; Glycoprotein. FT CARBOHYD 158 158 N-linked (Glc...). FT CONFLICT 40 40 A -> P (in Ref. 2). SQ SEQUENCE 364 AA; 41204 MW; 00CEC4FD30378D0C CRC64; MAGTVTVPGS STPSTPLLKD ELDIVIPTIR NLDFLEMWRA FFQPYHLIIV QDGDPTKTIK VPEGFDYELY NRNDINRILG PKASCISFKD SACRCFGYMV SKKKYIYTID DDCFVAKDPS GKDINALEQH IKNLLSPSTP FFFNTLYDPY REGADFVRGY PFSLREGAHT AVSHGLWLNI PDYDAPTQLV KPKERNERYV DAVMTIPKGT LFPMCGMNLA FDRDLIGPAM YFGLMGDGQP IGRYDDMWAG WCVKVICDHL SLGVKTGLPY IWHSKASNPF VNLKKEYKGI FWQEDIIPFF QNVTIPKDCD TVQKCYIYLS GQVKEKLGTI DPYFVKLGDA MVTWIEAWDE LNPSTPAAAN GKAK // ID VATA_MAIZE STANDARD; PRT; 561 AA. AC P49087; Q41775; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Vacuolar ATP synthase catalytic subunit A (EC 3.6.3.14) (V-ATPase A DE subunit) (Vacuolar proton pump alpha subunit) (V-ATPase 69 kDa DE subunit) (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Perotti E., Gavin O., Chanson A., Fraichard A.; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 47-258 FROM N.A. RC STRAIN=cv. Lixis; TISSUE=Coleoptile; RX MEDLINE=96197807; PubMed=8617373; RA Viereck R., Kirsch M., Loew R., Rausch T.; RT "Down-regulation of plant V-type H+ -ATPase genes after light-induced RT inhibition of growth."; RL FEBS Lett. 384:285-288(1996). CC -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of CC vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for CC acidifying a variety of intracellular compartments in eukaryotic CC cells. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SUBUNIT: V-ATPase is an heteromultimeric enzyme composed of a CC peripheral catalytic V1 complex (main components: subunits A, B, CC C, D, E, and F) attached to an integral membrane V0 proton pore CC complex (main component: the proteolipid protein). CC -!- TISSUE SPECIFICITY: High expression in the mesocotyl tip of CC etiolated seedlings compared to the base. CC -!- DEVELOPMENTAL STAGE: Expression is strongly linked to extension CC growth. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U36436; AAA80346.1; -. DR EMBL; X92373; CAA63117.1; -. DR PIR; S65525; S65525. DR MaizeDB; 120463; -. DR InterPro; IPR005725; ATP_synthV_A. DR InterPro; IPR000793; ATPase_a/b_C. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR004100; ATPase_a/bN. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. KW ATP synthesis; Hydrogen ion transport; Hydrolase; ATP-binding. FT NON_TER 1 1 FT NP_BIND 190 197 ATP (By similarity). FT CONFLICT 187 187 A -> C (in Ref. 2). FT CONFLICT 237 239 TLP -> QFA (in Ref. 2). FT CONFLICT 243 243 E -> R (in Ref. 2). SQ SEQUENCE 561 AA; 61951 MW; F398AF2A614D9E0C CRC64; ARATIQVYEE TAGLMVNDPV LRTRKPLSVE LGPGILGNIF DGIQRPLKTI AIKSGDVYIP RGVSVPALDK DVLWEFQPTK LGVGDVITGG DLYATVFENT LMQHHVALPP GSMGKISYIA PAGQYNLQDT VLELEFQGIK KKFTMLQTWP VRSPRPVASK LAADTPLLTG QRVLDALFPS VLGGTCAIPG AFGCGKTVIS QALSKYSNSE AVVYVGCGER GNEMAEVLMD FPQLTMTLPD GREESVMKRT TLVANTSNMP VAAREASIYT GITIAEYFRD MGYNVSMMAD STSRWAEALR EISGRLAEMP ADSGYPAYLA ARLASFYERA GKVKCLGSPD RNGSVTIVGA VSPPGGDFSD PVTSATLSIV QVFWGLDKKL AQRKHFPSVN WLISYSKYSK ALESFYEKFD PDFIDIRTKA REVLQREDDL NEIVQLVGKD ALAESDKITL ETAKLLREDY LAQNAFTPYD KFCPFYKSVW MMRNIIHFNT LANQAVERAA GTDGHKITYS VIKHRLGDLF YRLVSQKFED PAEGEEALVG KFKKLYDDLT TGFRNLEDEA R // ID VIV1_MAIZE STANDARD; PRT; 691 AA. AC P26307; DT 01-MAY-1992 (Rel. 22, Created) DT 01-MAY-1992 (Rel. 22, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Regulatory protein viviparous-1. GN VP1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W22; RX MEDLINE=91364172; PubMed=1889090; RA McCarty D.R., Hattori T., Carson C.B., Vasil V., Lazar M., Vasil I.K.; RT "The Viviparous-1 developmental gene of maize encodes a novel RT transcriptional activator."; RL Cell 66:895-905(1991). CC -!- FUNCTION: Transcriptional activator specifically required for CC expression of the maturation program in the seed development. CC Probably potentiates the response to the seed-specific hormone CC abscisic acid (ABA). May bind to DNA indirectly. CC -!- SUBCELLULAR LOCATION: Cytoplasmic or nuclear. CC -!- TISSUE SPECIFICITY: Seed. CC -!- DEVELOPMENTAL STAGE: Between 10 and 30 days after pollination. CC -!- SIMILARITY: Contains 1 TF-B3 domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M60214; AAA33506.1; -. DR PIR; A40024; A40024. DR TRANSFAC; T01087; -. DR MaizeDB; 65585; -. DR InterPro; IPR003340; TF_B3. DR Pfam; PF02362; B3; 1. DR PROSITE; PS50863; B3; 1. KW Developmental protein; Transcription regulation; DNA-binding; KW Activator. FT DOMAIN 1 170 PRO/ASP/GLU/SER/THR-RICH (PEST DOMAIN) FT (ACIDIC). FT DOMAIN 1 121 Transcriptional activation. FT DNA_BIND 517 619 TF-B3. SQ SEQUENCE 691 AA; 73328 MW; 6B8AB5F8EDF775C3 CRC64; MEASSGSSPP HSQENPPEHG GDMGGAPAEE IGGEAADDFM FAEDTFPSLP DFPCLSSPSS STFSSNSSSN SSSAYTNTAG RAGGEPSEPA SAGEGFDALD DIDQLLDFAS LSMPWDSEPF PGVSMMLENA MSAPPQPVGD GMSEEKAVPE GTTGGEEACM DASEGEELPR FFMEWLTSNR ENISAEDLRG IRLRRSTIEA AAARLGGGRQ GTMQLLKLIL TWVQNHHLQR KRPRDVMEEE AGLHVQLPSP VANPPGYEFP AGGQDMAAGG GTSWMPHQQA FTPPAAYGGD AVYPSAAGQQ YSFHQGPSTS SVVVNSQPFS PPPVGDMHGA NMAWPQQYVP FPPPGASTGS YPMPQPFSPG FGGQYAGAGA GHLSVAPQRM AGVEASATKE ARKKRMARQR RLSCLQQQRS QQLSLGQIQT SVHLQEPSPR STHSGPVTPS AGGWGFWSPS SQQQVQNPLS KSNSSRAPPS SLEAAAAAPQ TKPAPAGARQ DDIHHRLAAA SDKRQGAKAD KNLRFLLQKV LKQSDVGSLG RIVLPKKEAE VHLPELKTRD GISIPMEDIG TSRVWNMRYR FWPNNKSRMY LLENTGEFVR SNELQEGDFI VIYSDVKSGK YLIRGVKVRP PPAQEQGSGS SGGGKHRPLC PAGPERAAAA GAPEDAVVDG VSGACKGRSP EGVRRVRQQG AGAMSQMAVS I // ID YAC1_MAIZE STANDARD; PRT; 102 AA. AC P08771; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Transposable element activator hypothetical 12 kDa protein (AC 12 kDa DE protein). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Kunze R., Stochaj U., Laufs J., Starlinger P.; RT "Transcription of transposable element Activator (Ac) of Zea mays L."; RL EMBO J. 6:1555-1563(1987). CC -!- MISCELLANEOUS: This protein is coded by the transposable maize CC controlling element "Activator" (Ac), which is able to activate CC chromosome breakage at a specific location. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05424; CAA29006.1; -. DR PIR; T02917; T02917. DR MaizeDB; 69192; -. KW Transposable element; Hypothetical protein. SQ SEQUENCE 102 AA; 12406 MW; 0A7B6ED2251F97E1 CRC64; MQMVQLQIRV KMIWLLFMNH NHNHNHNQNH NHSHNLNPKK KHHRRGQRSA HRMYGSISPR RKLKWRSMER NTFRYGDIAT FLIARLSIGL RVIMEQADFE IT // ID YAC9_MAIZE STANDARD; PRT; 210 AA. AC P03936; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Transposable element activator hypothetical 23 kDa protein (AC 23 kDa DE protein). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=84205699; PubMed=6327080; RA Pohlman R.F., Fedoroff N.V., Messing J.; RT "The nucleotide sequence of the maize controlling element Activator."; RL Cell 37:635-643(1984). CC -!- MISCELLANEOUS: This protein is coded by the transposable maize CC controlling element "Activator" (Ac), which is able to activate CC chromosome breakage at a specific location. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; K01964; -; NOT_ANNOTATED_CDS. DR PIR; A04522; QQZMCA. DR MaizeDB; 69193; -. KW Transposable element; Hypothetical protein. SQ SEQUENCE 210 AA; 23009 MW; 4806B3BDE55185FE CRC64; MTQQLGAMVL TCCTAKCCEP VSSRGDRETA DGRMGERRAV EVWRTADRRW RMADGRTADG RAVEWRSGRM GGPRRDGRVA SSGVEGGPWM AASASGVPRH GRHRVWCLVQ PSGRPAGRQG ESERAGESET RVGVGVRLAA SGLRRGRVAA CECVMLLLVW CLPPGREAEQ RSLGISYMGW ASVVMDGSWS WPYCSHPELE NTVTKRDHPD // ID YC15_MAIZE STANDARD; PRT; 99 AA. AC P46666; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Hypothetical 11.6 kDa protein ycf15 (ORF 99). GN YCF15. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SIMILARITY: Belongs to the ycf15 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60336.1; -. DR EMBL; X86563; CAA60365.1; -. DR PIR; S58633; S58633. DR Gramene; P46666; -. DR MaizeDB; 121982; -. KW Chloroplast; Hypothetical protein. SQ SEQUENCE 99 AA; 11571 MW; EA5F3F41BBDEDA06 CRC64; MLIVLFRSKD IRGGRFVRPI LIFRTKRSWI LFRIGPERRR EAEMPTDLCL FSNSPDPIVP VFGTSSAKVT EWVSHQSNPF DKSGVILDII FYIYRNIIE // ID YC68_MAIZE STANDARD; PRT; 134 AA. AC P03938; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Hypothetical 14 kDa protein ycf68 (ORF 134). GN YCF68. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=82002211; PubMed=7023695; RA Koch W., Edwards K., Koessel H.; RT "Sequencing of the 16S-23S spacer in a ribosomal RNA operon of Zea RT mays chloroplast DNA reveals two split tRNA genes."; RL Cell 25:203-213(1981). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- SIMILARITY: Belongs to the ycf68 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z00028; CAB77704.1; -. DR EMBL; X86563; CAA60341.1; -. DR EMBL; X86563; CAA60359.1; -. DR PIR; A04524; QIZMI. DR PIR; S58626; S58626. DR Gramene; P03938; -. DR MaizeDB; 69587; -. KW Chloroplast; Hypothetical protein. FT CONFLICT 50 50 G -> R (in Ref. 1). FT CONFLICT 118 134 GGLEKAVINRTSLILPS -> AVWRKQ (in Ref. 1). SQ SEQUENCE 134 AA; 14874 MW; 17A52285347C054D CRC64; MAYSSCLNRS LKPNKLLLRR IDGAIQVRSH VDRTFYSLVG SGRSGGGPPG LLSSRESIHP LSVYGELSLE HRLRFVLNGK MEHLTTHLHR PRTTRSPLSF WGDGGIVPFE PFFHAFPGGL EKAVINRTSL ILPS // ID YCF3_MAIZE STANDARD; PRT; 170 AA. AC P27324; Q36720; Q36858; DT 01-AUG-1992 (Rel. 23, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Photosystem I assembly protein ycf3 (IRF170). GN YCF3. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73N Inbred; TISSUE=Seedling leaf; RX MEDLINE=91355944; PubMed=1884003; RA Kangasjaervi J., McCullough A., Gengenbach B.G.; RT "Nucleotide sequence and transcription of maize plastid genome Bam HI RT fragment 14 containing ORF170."; RL Plant Mol. Biol. 17:513-515(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). RN [3] RP SEQUENCE FROM N.A., AND RNA EDITING. RX MEDLINE=94181579; PubMed=7545915; RA Ruf S., Zeltz P., Kossel H.; RT "Complete RNA editing of unspliced and dicistronic transcripts of the RT intron-containing reading frame IRF170 from maize chloroplasts."; RL Proc. Natl. Acad. Sci. U.S.A. 91:2295-2299(1994). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=cv. A188; RA Kangasjaervi J., Gengenbach B.; RT "Differential transcription and processing of an intron-containing RT maize plastid gene leads to mRNAs potentially translatable into RT three distinct proteins containing a conserved tetratricopeptide RT repeat motif."; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Seems to be required for the assembly of the photosystem CC I complex (By similarity). CC -!- SUBCELLULAR LOCATION: Thylakoid membrane-associated (By CC similarity). CC -!- RNA EDITING: Modified_positions=15, 62; Note=Editing is CC independent of both splicing and processing of the primary CC transcript. CC -!- SIMILARITY: Belongs to the ycf3 family. CC -!- SIMILARITY: Contains 3 TPR repeats. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58080; CAA41108.1; ALT_SEQ. DR EMBL; X86563; CAA60287.1; ALT_SEQ. DR EMBL; S69196; AAB30283.2; -. DR EMBL; S69194; AAB30283.2; JOINED. DR EMBL; S69195; AAB30283.2; JOINED. DR EMBL; X62424; CAA44290.1; ALT_SEQ. DR PIR; S60189; S60189. DR Gramene; P27324; -. DR MaizeDB; 69194; -. DR HAMAP; MF_00439; -; 1. DR InterPro; IPR008941; TPR-like. DR InterPro; IPR001440; TPR. DR Pfam; PF00515; TPR; 3. DR PROSITE; PS50005; TPR; 3. DR PROSITE; PS50293; TPR_REGION; 1. KW Photosynthesis; Thylakoid; Membrane; Repeat; TPR repeat; Chloroplast; KW RNA editing. FT REPEAT 35 68 TPR 1. FT REPEAT 72 105 TPR 2. FT REPEAT 120 153 TPR 3. FT CONFLICT 16 16 S -> L (in Ref. 4). SQ SEQUENCE 170 AA; 19816 MW; 37A3055F04DB73E1 CRC64; MPRSRINGNF IDKTFSIVAN ILLQIIPTTS GEKRAFTYYR DGMLAQSEGN YAEALQNYYE AMRLEIDPYD RSYILYNIGL IHTSNGEHTK ALEYYFRALE RNPFLPQAFN NMAVICHYRG EQAILQGDSE IAEAWFDQAA EYWKQAIALT PGNYIEAQNW LKITKRFEFE // ID YCF4_MAIZE STANDARD; PRT; 185 AA. AC P46642; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Photosystem I assembly protein ycf4. GN YCF4. OS Zea mays (Maize). OG Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95395841; PubMed=7666415; RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.; RT "Complete sequence of the maize chloroplast genome: gene content, RT hotspots of divergence and fine tuning of genetic information by RT transcript editing."; RL J. Mol. Biol. 251:614-628(1995). CC -!- FUNCTION: Seems to be required for the assembly of the photosystem CC I complex (By similarity). CC -!- SUBCELLULAR LOCATION: Thylakoid membrane-associated (By CC similarity). CC -!- SIMILARITY: Belongs to the ycf4 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X86563; CAA60296.1; -. DR PIR; S58562; S58562. DR Gramene; P46642; -. DR MaizeDB; 118233; -. DR HAMAP; MF_00437; -; 1. DR InterPro; IPR003359; PSI_Ycf4. DR Pfam; PF02392; Ycf4; 1. DR ProDom; PD003698; PSI_Ycf4; 1. KW Photosynthesis; Thylakoid; Transmembrane; Chloroplast. FT TRANSMEM 21 43 Potential. FT TRANSMEM 63 85 Potential. SQ SEQUENCE 185 AA; 21608 MW; 930252790C1E68DD CRC64; MNWRSEHIWI ELLKGSRKRG NFFWACILFL GSLGFLAVGA SSYLGKNMIS VLPSQQILFF PQGVVMSFYG IAGLFISSYL WCTILWNVGS GYDRFDRKEG IVCIFRWGFP GIKRRIFLQF LVRDIQSIRI QVKEGLYPRR ILYMEIRGQG VIPLTRTDEK FFTPREIEQK AAELAYFLRV PIEVF // ID YM23_MAIZE STANDARD; PRT; 294 AA. AC P33544; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Hypothetical 33.9 kDa protein in mitochondrial linear 2.3 KB plasmid. OS Zea mays (Maize). OG Mitochondrion. OG Plasmid 2.3 kb. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B37N; RX MEDLINE=89296459; PubMed=2472603; RA Leon P., Walbot V., Bedinger P.; RT "Molecular analysis of the linear 2.3 kb plasmid of maize RT mitochondria: apparent capture of tRNA genes."; RL Nucleic Acids Res. 17:4089-4099(1989). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13704; CAA31989.1; -. DR PIR; S04740; S04740. DR MaizeDB; 78801; -. KW Hypothetical protein; Mitochondrion; Plasmid. SQ SEQUENCE 294 AA; 33870 MW; F0CD49613228176A CRC64; MTKTYRISSG LLREAVKKIT IARDSAFFVD KEILSKSSEL KNSLINPCHN VVREFVRESR DCDSDDYKRE YRLNDYRLEL TQPPSNISRG VIVVKTVRRW ELINQKYNAD LWIPPAKKGV VITPDIIDKL YLFWDNFLGS YEKEGINRKQ NTDPVSKGKV FDLLASRSSN NTNQTPEELR EIQTQIEHLT IHFDEGSVHE SAGQLKGKFF NKDRQSARDY LLDKLKDDKD KDIVRGMGTY TLECVAIHVL SKLFNVFSLE KTSVLAAALI SELDITAKTE YNNALLAKMQ REKE // ID YMS2_MAIZE STANDARD; PRT; 339 AA. AC P10579; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Hypothetical 39 kDa protein in mitochondrial S-1 and S-2 DNA (URF 2). OS Zea mays (Maize). OG Mitochondrion. OG Plasmid S-1, and Plasmid S-2. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC PLASMID=S-1; RA Paillard M., Sederoff R.R., Levings C.S. III; RT "Nucleotide sequence of the S-1 mitochondrial DNA from the S cytoplasm RT of maize."; RL EMBO J. 4:1125-1128(1985). RN [2] RP SEQUENCE FROM N.A. RC PLASMID=S-2; RA Levings C.S. III, Sederoff R.R.; RT "Nucleotide sequence of the S-2 mitochondrial DNA from the S cytoplasm RT of maize."; RL Proc. Natl. Acad. Sci. U.S.A. 80:4055-4059(1983). CC -!- MISCELLANEOUS: The mitochondria from the S male-sterile cytoplasm CC of maize contain unique DNA-protein complexes, designated S-1 and CC S-2. These complexes consist of double-stranded linear DNAs with CC proteins covalently attached to the 5'termini. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02451; -; NOT_ANNOTATED_CDS. DR MaizeDB; 69617; -. KW Hypothetical protein; Mitochondrion; Plasmid. SQ SEQUENCE 339 AA; 39319 MW; A0FE7CF66A012BAF CRC64; IQPARRHTKN TNMAKHTTKG TGHSMFISPR KIAHIPQINC EKQKLVLEVR SIYNDSWRVR GVLPFMINDF INQLNLTGKY RFGPVVYYQI NIKEIPPLIY DVIRMEASKG YLWLDERNLD THSLIGVYKC RVPMDLLVLK GLSNVILTTV NKAQPNISKF KDLKAMHYAF LNRQENVVKV VSIDLSDCMD YIPTSRILTS QKFTKQYGLY YNLVEWIIDL PIYDFHNHSF FPSTGITPIG EITHVILHNF YQNTVDSLLE SWYPGITYSR YGHELFILCK QTDEFTIDDC DIDNILEVLD LYSVDINWSS DGLLMADNND KALILHEDGS LEVWNSEDI // ID YMS4_MAIZE STANDARD; PRT; 256 AA. AC P10580; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Hypothetical 29 kDa protein in mitochondrial S-1 DNA (URF 4). OS Zea mays (Maize). OG Mitochondrion. OG Plasmid S-1. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Paillard M., Sederoff R.R., Levings C.S. III; RT "Nucleotide sequence of the S-1 mitochondrial DNA from the S cytoplasm RT of maize."; RL EMBO J. 4:1125-1128(1985). CC -!- MISCELLANEOUS: The mitochondria from the S male-sterile cytoplasm CC of maize contain unique DNA-protein complexes, designated S-1 and CC S-2. These complexes consist of double-stranded linear DNAs with CC proteins covalently attached to the 5'termini. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02451; -; NOT_ANNOTATED_CDS. DR MaizeDB; 69620; -. KW Hypothetical protein; Mitochondrion; Plasmid. SQ SEQUENCE 256 AA; 29338 MW; B1D6DB31E402D175 CRC64; YVLIMRLKLK RKIYRADFSE YKGLWSLYNR ATDNLYSHLQ RALEKYENFG VSAKHKVLQC LVHVVTSQSD NSVRYVYGNI FALVRLGTYV TVWYCYTESA PDFISVDPHY LDIELIIDLF KVRKLFVWIP YEEVISTSIL EAYDAVVERT ALTDCLDRKL REEELSDKFE FWGKCSDGDH TIDSVEENAT IEYASSKEGS ACKEGVDSSC KEEGGGCEEE GSGSEEDSDD SDNPRYLAFG VVVLVGVLLY VWYCSR // ID YPT1_MAIZE STANDARD; PRT; 208 AA. AC P16976; DT 01-AUG-1990 (Rel. 15, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE GTP-binding protein YPTM1. GN YPTM1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Coleoptile; RX MEDLINE=92115746; PubMed=1731354; RA Palme K., Diefenthal T., Vingron M., Sander C., Schell J.; RT "Molecular cloning and structural analysis of genes from Zea mays RT (L.) coding for members of the ras-related ypt gene family."; RL Proc. Natl. Acad. Sci. U.S.A. 89:787-791(1992). RN [2] RP SEQUENCE FROM N.A. RA Palme K., Diefenthal T., Sander C., Vingron M., Schell J.; RT "Identification of guanine-nucleotide binding proteins in plants: RT structural analysis and evolutionary comparisons of the ras-related RT ypt-gene family from Zea mays."; RL (In) Bosch L., Kraal B., Parmeggiani A. (eds.); RL The guanine-nucleotide binding proteins: common structural and RL functional properties, pp.273-284, Plenum Press, New York (1989). CC -!- FUNCTION: Protein transport. Probably involved in vesicular CC traffic (By similarity). CC -!- TISSUE SPECIFICITY: Low levels in coleoptiles. CC -!- PTM: The palmitic acid is required for membrane attachment and CC biological function. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63277; CAA44918.1; -. DR PIR; A38202; A38202. DR HSSP; P01112; 1PLK. DR MaizeDB; 65854; -. DR InterPro; IPR003579; GTPase_Rab. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Lipoprotein; Palmitate; Prenylation; Protein transport. FT NP_BIND 15 22 GTP (By similarity). FT NP_BIND 63 67 GTP (By similarity). FT NP_BIND 121 124 GTP (By similarity). FT DOMAIN 37 45 Effector region (Probable). FT LIPID 205 205 S-palmitoyl cysteine (By similarity). FT LIPID 206 206 S-geranylgeranyl cysteine FT (By similarity). FT CONFLICT 116 117 KL -> NV (in Ref. 2). SQ SEQUENCE 208 AA; 23311 MW; 8FB1C766BE5768F9 CRC64; MSNEFDYLFK LLLIGDSSVG KSCFLLRFAD DSYVDSYIST IGVDFKIRTV EVEGKTVKLQ IWDTAGQERF RTITSSYYRG AHGIIIVYDI TDMESFNNVK QWLDEIDRYA NDSVRKLLVG NKCDLAENRA VDTSVAQAYA QEVGIPFLET SAKESINVEE AFLAMSAAIK KSKAGSQAAL ERKPSNVVQM KGRPIQQEQQ KSSRCCST // ID YPT2_MAIZE STANDARD; PRT; 203 AA. AC Q05737; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE GTP-binding protein YPTM2. GN YPTM2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Coleoptile; RX MEDLINE=92115746; PubMed=1731354; RA Palme K., Diefenthal T., Vingron M., Sander C., Schell J.; RT "Molecular cloning and structural analysis of genes from Zea mays RT (L.) coding for members of the ras-related ypt gene family."; RL Proc. Natl. Acad. Sci. U.S.A. 89:787-791(1992). CC -!- FUNCTION: Protein transport. Probably involved in vesicular CC traffic (By similarity). CC -!- TISSUE SPECIFICITY: Its expression is weak in stems, higher in CC roots, leaves and coleoptiles, but highest in flowers. CC -!- PTM: The palmitic acid is required for membrane attachment and CC biological function. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X63278; CAA44919.1; -. DR PIR; B38202; B38202. DR HSSP; P05713; 3RAB. DR MaizeDB; 78605; -. DR InterPro; IPR003579; GTPase_Rab. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. KW GTP-binding; Lipoprotein; Prenylation; Palmitate; Protein transport. FT NP_BIND 15 22 GTP (By similarity). FT NP_BIND 63 67 GTP (By similarity). FT NP_BIND 121 124 GTP (By similarity). FT DOMAIN 37 45 Effector region (Probable). FT LIPID 200 200 S-palmitoyl cysteine (By similarity). FT LIPID 201 201 S-geranylgeranyl cysteine FT (By similarity). SQ SEQUENCE 203 AA; 22475 MW; E241326E7ACD1B8A CRC64; MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DSYLDSYIST IGVDFKIRTV EQDGKTIKLQ IWDTAGQERF RTITSSYYRG AHGIIIVYDV TDQESFNNVK QWLNEIDRYA SDNVNKLLVG NKSDLTANKV VATETAKAFA DEMGIPFMET SAKNATNVQQ AFMAMAASIK DRMASQPAAA NARPATVQIR GQPVNQKTSC CSS // ID ZB14_MAIZE STANDARD; PRT; 128 AA. AC P42856; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 14 kDa zinc-binding protein (Protein kinase C inhibitor) (PKCI). GN ZBP14 OR PKCI. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A619; RX MEDLINE=94304958; PubMed=8031868; RA Simpson G.G., Clark G.P., Brown J.W.S.; RT "Isolation of a maize cDNA encoding a protein with extensive RT similarity to an inhibitor of protein kinase C and a cyanobacterial RT open reading frame."; RL Biochim. Biophys. Acta 1222:306-308(1994). RN [2] RP CRYSTALLIZATION. RA Xiao B., Robinson K., Aitken A., Hirshberg M.; RT "Crystallization and preliminary X-ray analysis of maize ZBP14 RT protein, a member of a new family of zinc-binding proteins."; RL Acta Crystallogr. D 51:848-849(1995). CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the HIT family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z29643; CAA82751.1; -. DR PIR; S45368; S45368. DR HSSP; P80912; 4RHN. DR MaizeDB; 104300; -. DR InterPro; IPR001310; HIT. DR Pfam; PF01230; HIT; 1. DR PRINTS; PR00332; HISTRIAD. DR PROSITE; PS00892; HIT; 1. SQ SEQUENCE 128 AA; 14300 MW; F05132D5513F0DB4 CRC64; MSSEKEAALR RLDDSPTIFD KIIKKEIPST VVYEDEKVLA FRDINPQAPT HILIIPKVKD GLTGLAKAEE RHIEILGYLL YVAKVVAKQE GLEDGYRVVI NDGPSGCQSV YHIHVHLLGG RQMNWPPG // ID ZEA1_MAIZE STANDARD; PRT; 234 AA. AC P02859; DT 21-JUL-1986 (Rel. 01, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone A30). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=82081837; PubMed=6895552; RA Geraghty D., Peifer M.A., Rubenstein I., Messing J.; RT "The primary structure of a plant storage protein: zein."; RL Nucleic Acids Res. 9:5163-5174(1981). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=84207882; PubMed=6233138; RA Hu N.T., Peifer M.A., Heidecker G., Messing J., Rubenstein I.; RT "Primary structure of a genomic zein sequence of maize."; RL EMBO J. 1:1337-1342(1982). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 19 kDa and 19 kDa zeins are composed CC of nine adjacent, topologically antiparallel helices clustered CC within a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V01481; CAA24728.1; -. DR PIR; A90967; ZIZM3. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 234 Zein-alpha. SQ SEQUENCE 234 AA; 25403 MW; 502A99D438CA5DAA CRC64; MAAKIFCLLM LLGLSASAAT ATIFPQCSQA PIASLLPPYL SPAVSSVCEN PILQPYRIQQ AIAAGILPLS PLFLQQSSAL LQQLPLVHLL AQNIRAQQLQ QLVLANLAAY SQQQQFLPFN QLAALNSASY LQQQQLPFSQ LPAAYPQQFL PFNQLAALNS PAYLQQQQLL PFSQLAGVSP ATFLTQPQLL PFYQHAAPNA GTLLQLQQLL PFNQLALTNL AAFYQQPIIG GALF // ID ZEA2_MAIZE STANDARD; PRT; 235 AA. AC P04704; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone ZG99). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=82265740; PubMed=6286660; RA Marks M.D., Larkins B.A.; RT "Analysis of sequence microheterogeneity among zein messenger RNAs."; RL J. Biol. Chem. 257:9976-9983(1982). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=83103094; PubMed=7151164; RA Pedersen K., Devereux J., Wilson D.R., Sheldon E., Larkins B.A.; RT "Cloning and sequence analysis reveal structural variation among RT related zein genes in maize."; RL Cell 29:1015-1026(1982). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V01470; CAA24717.1; -. DR EMBL; V01479; CAA24726.1; -. DR PIR; A29288; ZIZM99. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 235 Zein-alpha. SQ SEQUENCE 235 AA; 25575 MW; 9E23E6323659730C CRC64; MAAKIFCLIM LLGLSASAAT ASIFPQCSQA PIASLLPPYL SPAMSSVCEN PILLPYRIQQ AIAAGILPLS PLFLQQSSAL LQQLPLVHLL AQNIRAQQLQ QLVLANLAAY SQQQQFLPFN QLAALNSAAY LQQQQLLPFS QLAAAYPRQF LPFNQLAALN SHAYVQQQQL LPFSQLAAVS PAAFLTQQQL LPFYLHTAPN VGTLLQLQQL LPFDQLALTN PAAFYQQPII GGALF // ID ZEA3_MAIZE STANDARD; PRT; 230 AA. AC P06674; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone 19A2) (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86059563; PubMed=2999157; RA Marks M.D., Lindell J.S., Larkins B.A.; RT "Nucleotide sequence analysis of zein mRNAs from maize endosperm."; RL J. Biol. Chem. 260:16451-16459(1985). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12142; AAA33525.1; -. DR PIR; D24557; ZIZMA2. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT NON_TER 1 1 FT SIGNAL <1 18 FT CHAIN 19 230 Zein-alpha. SQ SEQUENCE 230 AA; 25032 MW; 53FF1A84BDCE5F8D CRC64; KIFCFLMLLG LSASAATATI FPQCSQAPIT SLLPPYLSPA VSSVCENPIL QPYRIQQAIA AGILPLSPLF LQQPSALLQQ LPLVHLLAQN IRAQQLQQLV LGNLAAYSQQ HQFLPFNQLA ALNSAAYLQQ QLPFSQLAAA YPQQFLPFNQ LAALNSAAYL QQQQLPPFSQ LADVSPAAFL TQQQLLPFYL HAAPNAGTVL QLQQLLPFDQ LALTNPTAFY QQPIIGGALF // ID ZEA4_MAIZE STANDARD; PRT; 234 AA. AC P06675; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone 19B1). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86059563; PubMed=2999157; RA Marks M.D., Lindell J.S., Larkins B.A.; RT "Nucleotide sequence analysis of zein mRNAs from maize endosperm."; RL J. Biol. Chem. 260:16451-16459(1985). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12143; AAA33527.1; -. DR PIR; E24557; ZIZMB1. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 234 Zein-alpha. SQ SEQUENCE 234 AA; 25435 MW; A641FE13961136A2 CRC64; MAAKIFCLLM LLGLSASAAT ATIFPQCSQA PIASLLPPYL SSAVSSVCEN PILQPYRIQQ AIAAGILPLS PLFLQQSSAL LQQLPLVHLL AQNIRAQQLQ QLVLANLAAY SQQQQFLPFN QLGSLNSASY LQQQQLPFSQ LPAAYPQQFL PFNQLAALNS PAYLQQQQLL PFSQLAGVSP ATFLTQPQLL PFYQHVAPNA GTLLQLQQLL PFNQLALTNP AVFYQQPIIG GALF // ID ZEA5_MAIZE STANDARD; PRT; 234 AA. AC P08416; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone GZ19AB11). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; RX MEDLINE=87257300; PubMed=3502710; RA Kriz A.L., Boston R.S., Larkins B.A.; RT "Structural and transcriptional analysis of DNA sequences flanking RT genes that encode 19 kilodalton zeins."; RL Mol. Gen. Genet. 207:90-98(1987). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X05911; CAA29340.1; -. DR PIR; S03417; S03417. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 234 Zein-alpha. SQ SEQUENCE 234 AA; 25439 MW; 160290F97FD6584B CRC64; MAAKIFCLLM LLGLSASAAT ATIFTQCSQA PIASLLPPYL SSAVSSVCEN PILQPYRIQQ AIAAGILPLS PLFLQQSSAL LQQLPLVHLL AQNIRAQQLQ QLVLANLAAY SQQQQFLPFN QLGSLNSASY LQQQQLPFSQ LPAAYPQQFL PFNQLAALNS PAYLQQQQLL PFSQLAGVSP ATFLTQPQLL PFYQHVAPNA GTLLQLQQLL PFNQLALTNP AVFYQQPIIG GALF // ID ZEA6_MAIZE STANDARD; PRT; 240 AA. AC P04702; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone M6). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Viotti A., Cairo G., Vitale A., Sala E.; RT "Each zein gene class can produce polypeptides of different sizes."; RL EMBO J. 4:1103-1110(1985). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02450; CAA26294.1; -. DR PIR; A22831; A22831. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 240 Zein-alpha. SQ SEQUENCE 240 AA; 26254 MW; 17E555FC177D55CB CRC64; MATKIFSLLM LLALSTCVAN ATIFPQCSQA PIASLLPPYL PSIIASICEN PALQPYRLQQ AIAASNIPSS PLLFQQSPAL SLVQSLVQTI RAQQLQQLVL PLINQVVLAN LSPYSQQQQF LPFNQLSTLN PAAYLQQQLL PSSQLATAYC QQQQLLPFNQ LAALNPAAYL QQQILLPFSQ LAAANRASFL TQQQLLLFYQ QFAANPATLL QLQQLLPFVQ LALTDPAASY QQHIIGGALF // ID ZEA7_MAIZE STANDARD; PRT; 240 AA. AC P04703; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone A20). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=84207881; PubMed=6897917; RA Geraghty D.E., Messing J., Rubenstein I.; RT "Sequence analysis and comparison of cDNAs of the zein multigene RT family."; RL EMBO J. 1:1329-1335(1982). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V01476; CAA24723.1; -. DR PIR; A22762; ZIZM2. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 240 Zein-alpha. SQ SEQUENCE 240 AA; 26240 MW; 2C44D3574C2A3C2E CRC64; MATKIFSLLM LLALSACVAN ATIFPQCSQA PIASLLPPYL PSMIASVCEN PALQPYRLQQ AIAASNIPLS PLLFQQSPAL SLVQSLVQTI RAQQLQQLVL PVINQVALAN LSPYSQQQQF LPFNQLSTLN PAAYLQQQLL PFSQLATAYS QQQQLLPFNQ LAALNPAAYL QQQILLPFSQ LAAANRASFL TQQQLLPFYQ QFAANPATLL QLQQLLPFVQ LALTDPAASY QQHIIGGALF // ID ZEA8_MAIZE STANDARD; PRT; 240 AA. AC P06676; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone 19C1). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86059563; PubMed=2999157; RA Marks M.D., Lindell J.S., Larkins B.A.; RT "Nucleotide sequence analysis of zein mRNAs from maize endosperm."; RL J. Biol. Chem. 260:16451-16459(1985). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12146; AAA33529.1; -. DR PIR; I24557; ZIZM91. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 240 Zein-alpha. SQ SEQUENCE 240 AA; 26254 MW; 3C9EBF7F30D83C2E CRC64; MATKIFSLLM LLALSACVAN ATIFPQCSQA PIASLLPPYL PSMIASVCEN PALQPYRLQQ AIAASNIPLS PLLFQQSPAL SLVQSLVQTI RAQQLQQLVL PLINQVALAN LSPYSQQQQF LPFNQLSTLN PAAYLQQQLL PFSQLATAYS QQQQLLPFNQ LAALNPAAYL QQQILLPFSQ LAAANRASFL TQQQLLPFYQ QFAANPATLL QLQQLLPFVQ LALTDPAASY QQHIIGGALF // ID ZEA9_MAIZE STANDARD; PRT; 240 AA. AC P06677; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone 19C2). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86059563; PubMed=2999157; RA Marks M.D., Lindell J.S., Larkins B.A.; RT "Nucleotide sequence analysis of zein mRNAs from maize endosperm."; RL J. Biol. Chem. 260:16451-16459(1985). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12145; AAA33530.1; -. DR PIR; H24557; ZIZM92. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 240 Zein-alpha. SQ SEQUENCE 240 AA; 26280 MW; 3733522CB9ACB3DA CRC64; MATKIFSLLM LLALSTCVAN ATIFPQCSQA PIASLLPPYL PSIIASICEN PALQPYRLQQ AIAASNIPLS PLLFQQSPAL SLVQSLVQTI RAQQLQQLVL PLINQVALAN LSPYSQQQQF LPFNQLSTLN PAAYLQQQLL PFSQLATAYS QQQQLLPFNQ LAALNPAAYL QQQILLPFSQ LAAANRASFL TQQQLLPFYQ QFAANPATLL QLQQLLPFVQ LALTDPAASY QQHIIGGALF // ID ZEAA_MAIZE STANDARD; PRT; 240 AA. AC P06678; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone 19D1). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86059563; PubMed=2999157; RA Marks M.D., Lindell J.S., Larkins B.A.; RT "Nucleotide sequence analysis of zein mRNAs from maize endosperm."; RL J. Biol. Chem. 260:16451-16459(1985). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12144; AAA33531.1; -. DR PIR; G24557; ZIZMD1. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 240 Zein-alpha. SQ SEQUENCE 240 AA; 26633 MW; 6A6E543974F9A8CA CRC64; MAAKIFALLA LLALSANVAT ATIIPQCSQQ YLSPVTAARF EYPTIQSYRL QQAIAASILR SLALTVQQPY ALLQQPSLVN LYLQRIVAQQ LQQQLLPTIN QVVAANLDAY LQQQQFLPFN QLAGVNPAAY LQAQQLLPFN QLVRSPAAFL LQQQLLPFHL QVVANIAAFL QQQQLLPFYP QVVGNINAFL QQQQLLPFYP QDVANNVAFL QQQQLLPFSQ LALTNPTTLL QQPTIGGAIF // ID ZEAB_MAIZE STANDARD; PRT; 186 AA. AC P04705; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone PZ19.1) (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83103094; PubMed=7151164; RA Pedersen K., Devereux J., Wilson D.R., Sheldon E., Larkins B.A.; RT "Cloning and sequence analysis reveal structural variation among RT related zein genes in maize."; RL Cell 29:1015-1026(1982). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V01471; CAA24718.1; -. DR EMBL; J01244; AAA33526.1; -. DR PIR; T03407; T03407. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 >186 Zein-alpha. FT NON_TER 186 186 SQ SEQUENCE 186 AA; 20419 MW; C3999FAACD515E82 CRC64; MAAKIFCLIM LLGLSASAAT ASIFPQCSQA PIASLLPPYL SPAMSSVCEN PILLPYRIQQ AIAAGILPLS PLFLQQSSAL LQQLPLVHLL AQNIRAQQLQ QLVLANLAAY SQQQQLPLVH LLAQNIRAQQ LQQLVLANLA AYSQQQQFLP FNQQLAAAYP RQFLPFNQLA ALNSHAYVQQ QQLLPF // ID ZEAC_MAIZE STANDARD; PRT; 235 AA. AC P24449; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Zein-alpha precursor (19 kDa) (PMS1). GN ZMPMS1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A619; RX MEDLINE=90060774; PubMed=2583513; RA Quayle T.J.A., Brown J.W.S., Feix G.; RT "Analysis of distal flanking regions of maize 19-kDa zein genes."; RL Gene 80:249-257(1989). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X53582; CAA37651.1; -. DR PIR; S15655; S15655. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 By similarity. FT CHAIN 22 235 Zein-alpha. SQ SEQUENCE 235 AA; 25505 MW; 18F26B4739204CAE CRC64; MAAKIFCLLM LLGLSASAAT ATIFPQCSQA PIASLLPPYL SPAVSSVCEN PILQPYRIQQ AIAAGILPLS PLFLQQSSAL LQQLPLVHLL AQNIRAQQLQ QLVLANVAAY SQQQQFLPFN QLAALNSAAY LQQQQLLPFS QLTAAYPQQF LPFNQLAALN SAAYLQQQQL LPFSQLAVVS PAAFLTQQQL LPFYLHAVPN AGTLLQLQQL LPFNQLALTN PAAFYQQPII GGALF // ID ZEAD_MAIZE STANDARD; PRT; 233 AA. AC P24450; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Zein-alpha precursor (19 kDa) (PMS2). GN ZMPMS2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. A619; RX MEDLINE=90060774; PubMed=2583513; RA Quayle T.J.A., Brown J.W.S., Feix G.; RT "Analysis of distal flanking regions of maize 19-kDa zein genes."; RL Gene 80:249-257(1989). RN [2] RP SEQUENCE FROM N.A. RA Langridge P., Brown J.W.S., Pintor-Toro J.A., Feix G.; RT "Expression of zein genes in Acetabularia mediterranea."; RL Eur. J. Cell Biol. 39:257-264(1985). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X58700; CAA41543.1; -. DR EMBL; X59526; CAA42105.1; ALT_TERM. DR PIR; S15656; S15656. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 233 Zein-alpha. SQ SEQUENCE 233 AA; 25515 MW; 49F6FD614B588EFC CRC64; MAAKIFCFLM LLGLSASVAT ATIFPQCSQA PIASLLPPYL SPAVSSMCEN PIVQPYRIQQ AIATGILPLS PLFLQQPSAL LQQLPLVHLV AQNIRAQQLQ QLVLANLAAY SQQHQFLPFN QLAALNSAAY LQQQLPFSQL VAAYPRQFLP FNQLAALNSA AYLQQQQLLP FSQLADVSPA AFLTQQQLLP FYLHAMPNAG TLLQLQQLLP FNQLALTNST VFYQQPIIGG ALF // ID ZEAL_MAIZE STANDARD; PRT; 267 AA. AC P04701; DT 13-AUG-1987 (Rel. 05, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Zein-alpha precursor (Clone Z4). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=84207882; PubMed=6233138; RA Hu N.T., Peifer M.A., Heidecker G., Messing J., Rubenstein I.; RT "Primary structure of a genomic zein sequence of maize."; RL EMBO J. 1:1337-1342(1982). RN [2] RP REVISIONS TO C-TERMINUS. RA Hu N.T., Peifer M.A., Heidecker G., Messing J., Rubenstein I.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V01472; CAA24719.1; -. DR PIR; S07172; S07172. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 267 Zein-alpha. SQ SEQUENCE 267 AA; 29206 MW; E7CFCDED340ADD29 CRC64; MAAKIFCLIM LLGLSASAAT ASIFPQCSQA PIASLLPPYL SPAMSSVCEN PILLPYRIQQ AIAAGILPLS PLFLQQSSAL LQQLPLVHLL AQNIRAQQLQ QLVLANLAAY SQQQQLPLVH LLAQNIRAQQ LQQLVLANLA AYSQQQQFLP FNQLAALNSA AYLQQQQLLP FSQLAAAYPR QFLPFNQLAA LNSHAYVQQQ QLLPFSQLAA VSPAAFLTQQ HLLPFYLHTA PNVGTLLQLQ QLLPFDQLAL TNPAVFYQQP IIGGALF // ID ZEAM_MAIZE STANDARD; PRT; 227 AA. AC P33679; DT 01-FEB-1994 (Rel. 28, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Zeamatin precursor. GN ZLP. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. B73; TISSUE=Seed; RX MEDLINE=95148737; PubMed=7846159; RA Malehorn D.E., Borgmeyer J.R., Smith C.E., Shah D.M.; RT "Characterization and expression of an antifungal zeamatin-like RT protein (Zlp) gene from Zea mays."; RL Plant Physiol. 106:1471-1481(1994). RN [2] RP SEQUENCE OF 21-48. RA Roberts W.K., Selitrennikoff C.P.; RT "Zeamatin, an antifungal protein from maize with membrane- RT permeabilizing activity."; RL J. Gen. Microbiol. 136:1771-1778(1990). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=96133724; PubMed=8548448; RA Batalia M.A., Monzingo A.F., Ernst S., Roberts W., Robertus J.D.; RT "The crystal structure of the antifungal protein zeamatin, a member RT of the thaumatin-like, PR-5 protein family."; RL Nat. Struct. Biol. 3:19-23(1996). CC -!- FUNCTION: Has antifungal activity. Inhibits Candida albicans and CC Trichoderma reesei; marginal inhibition observed against CC Alternaria solani and Neurospora crassa. CC -!- SIMILARITY: Belongs to the thaumatin family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U06831; AAA92882.1; -. DR PIR; T02075; T02075. DR PDB; 1DU5; 02-FEB-00. DR MaizeDB; 78797; -. DR InterPro; IPR001938; Thaumatin. DR Pfam; PF00314; thaumatin; 1. DR PRINTS; PR00347; THAUMATIN. DR ProDom; PD001321; Thaumatin; 1. DR SMART; SM00205; THN; 1. DR PROSITE; PS00316; THAUMATIN; 1. KW Plant defense; Fungicide; Signal; 3D-structure. FT SIGNAL 1 20 FT CHAIN 21 227 Zeamatin. FT DISULFID 30 226 FT DISULFID 72 82 FT DISULFID 87 93 FT DISULFID 139 215 FT DISULFID 145 198 FT DISULFID 153 163 FT DISULFID 167 176 FT DISULFID 177 185 FT STRAND 23 28 FT STRAND 34 39 FT TURN 40 42 FT STRAND 43 47 FT TURN 49 50 FT STRAND 52 56 FT TURN 59 60 FT STRAND 64 69 FT STRAND 72 74 FT TURN 76 77 FT STRAND 79 82 FT TURN 88 89 FT STRAND 90 90 FT STRAND 103 110 FT HELIX 111 113 FT STRAND 114 120 FT TURN 122 123 FT STRAND 125 125 FT STRAND 129 133 FT STRAND 144 145 FT TURN 149 152 FT HELIX 155 157 FT STRAND 158 159 FT TURN 160 161 FT STRAND 162 163 FT HELIX 166 170 FT HELIX 173 176 FT HELIX 179 184 FT HELIX 189 197 FT TURN 199 200 FT STRAND 202 202 FT TURN 205 206 FT HELIX 208 211 FT STRAND 213 216 FT TURN 217 218 FT STRAND 221 225 SQ SEQUENCE 227 AA; 23999 MW; 33ABFE0B1EB781E4 CRC64; MAGSVAIVGI FVALLAVAGE AAVFTVVNQC PFTVWAASVP VGGGRQLNRG ESWRITAPAG TTAARIWART GCKFDASGRG SCRTGDCGGV LQCTGYGRAP NTLAEYALKQ FNNLDFFDIS LIDGFNVPMS FLPDGGSGCS RGPRCAVDVN ARCPAELRQD GVCNNACPVF KKDEYCCVGS AANDCHPTNY SRYFKGQCPD AYSYPKDDAT STFTCPAGTN YKVVFCP // ID ZEAV_MAIZE STANDARD; PRT; 122 AA. AC P05815; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Zein-alpha (22 kDa) (Clone B49) (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=84207881; PubMed=6897917; RA Geraghty D.E., Messing J., Rubenstein I.; RT "Sequence analysis and comparison of cDNAs of the zein multigene RT family."; RL EMBO J. 1:1329-1335(1982). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. DR PIR; B22762; ZIZM49. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family. FT NON_TER 1 1 SQ SEQUENCE 122 AA; 13424 MW; CADF45F2A3F08A7A CRC64; AMVNPAAYLQ QQQLISSSPL DVVNAPTYLQ QQLLQQIIPA LTQLAVANPA AYLQQLLPFN QLTVSNSAAY LQQRQQLLNP LVVANPLVAA FLQQQQLLPY NQFSLMNPAL SWQQPIVGGA IF // ID ZEAW_MAIZE STANDARD; PRT; 261 AA. AC P06679; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Zein-alpha precursor (22 kDa) (Clone 22C2) (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86059563; PubMed=2999157; RA Marks M.D., Lindell J.S., Larkins B.A.; RT "Nucleotide sequence analysis of zein mRNAs from maize endosperm."; RL J. Biol. Chem. 260:16451-16459(1985). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12141; AAA33534.1; -. DR PIR; C24557; ZIZMC2. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT NON_TER 1 1 FT SIGNAL <1 16 FT CHAIN 17 261 Zein-alpha. SQ SEQUENCE 261 AA; 28431 MW; BA560B722745AA1E CRC64; LALLALLALF VSATNAFIIP QCSLAPSAII PQFLPPVTSM GFEHLAVQAY RLQQALAASV LQQPINQLQQ QSLAHLTIQT IATQQQQQFL PSVSQLDVVN PVAYLQQQLL ASNPLALANV AAYQQQQQLQ QFLPALSQLA MVNPAAYLQQ QQLLSSSPLA VGNAPTYLQQ QLLQQIVPAL TQLAVANPAA YLQQLLPFNQ LTVSNSAAYL QQRQQLLNPL EVPNPLVAGF LQQQQLLPYS QFSLMNPALS WQQPIVGGAI F // ID ZEAX_MAIZE STANDARD; PRT; 263 AA. AC P04700; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Zein-alpha precursor (22 kDa) (Clones PZ22.1 and 22A1). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=82265740; PubMed=6286660; RA Marks M.D., Larkins B.A.; RT "Analysis of sequence microheterogeneity among zein messenger RNAs."; RL J. Biol. Chem. 257:9976-9983(1982). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=86059563; PubMed=2999157; RA Marks M.D., Lindell J.S., Larkins B.A.; RT "Nucleotide sequence analysis of zein mRNAs from maize endosperm."; RL J. Biol. Chem. 260:16451-16459(1985). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V01478; CAA24725.1; -. DR PIR; A26564; ZIZM21. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 263 Zein-alpha. SQ SEQUENCE 263 AA; 28484 MW; 4AF7D0E83480E486 CRC64; MATKILALLA LLALLVSATN AFIIPQCSLA PSASIPQFLP PVTSMGFEHP AVQAYRLQLA LAASALQQPI AQLQQQSLAH LTLQTIATQQ QQQQFLPSLS HLAMVNPVTY LQQQLLASNP LALANVAAYQ QQQQLQQFMP VLSQLAMVNP AVYLQLLSSS PLAVGNAPTY LQQQLLQQIV PALTQLAVAN PAAYLQQLLP FNQLAVSNSA AYLQQRQQLL NPLAVANPLV ATFLQQQQQL LPYNQFSLMN PALQQPIVGG AIF // ID ZEAY_MAIZE STANDARD; PRT; 266 AA. AC P04699; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Zein-alpha precursor (22 kDa) (Clones ZA1/M1). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RA Spena A., Viotti A., Pirrotta V.; RT "A homologous repetitive block structure underlies the heterogeneity RT of heavy and light chain zein genes."; RL EMBO J. 1:1589-1594(1982). RN [2] RP SEQUENCE FROM N.A. RA Spena A.; RL Submitted (APR-1983) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RA Viotti A., Cairo G., Vitale A., Sala E.; RT "Each zein gene class can produce polypeptides of different sizes."; RL EMBO J. 4:1103-1110(1985). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V01475; CAA24722.1; -. DR PIR; B22831; B22831. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 266 Zein-alpha. SQ SEQUENCE 266 AA; 28987 MW; 670227E05256C0D2 CRC64; MATKILALLA LLALFVSATN AFIIPQCSLA PSAIIPQFLP PVTSMGFEHL AVQAYRLQQA LAASVLQQPI NQLQQQSLAH LTIQTIATQQ QQQFLPALSQ LDVVNPVAYL QQQLLASNPL ALANVAAYQQ QQQLQQFLPA LSQLAMVNPA AYLQQQQLLS SSPLAVGNAP TYLQQQLLQQ IVPALTQLAV ANPAAYLQQL LPFNQLTVSN SAAYLQQRQQ LLNPLEVPNP LVAAFLQQQQ LLPYSQFSLM NPALSWQQPI VGGAIF // ID ZEAZ_MAIZE STANDARD; PRT; 267 AA. AC P04698; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Zein-alpha precursor (22 kDa) (Clone PZ22.3). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=82265740; PubMed=6286660; RA Marks M.D., Larkins B.A.; RT "Analysis of sequence microheterogeneity among zein messenger RNAs."; RL J. Biol. Chem. 257:9976-9983(1982). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 22K and 19K zeins are composed of CC nine adjacent, topologically antiparallel helices clustered within CC a distorted cylinder. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; V01480; CAA24727.1; -. DR EMBL; J01246; AAA33533.1; -. DR PIR; B26564; ZIZM23. DR MaizeDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Seed storage protein; Multigene family; Signal. FT SIGNAL 1 21 FT CHAIN 22 267 Zein-alpha. FT CONFLICT 94 94 Missing (in Ref. 1; AAA33533). SQ SEQUENCE 267 AA; 29063 MW; CF52BDA594A29302 CRC64; MATKILSLLA LLALFASATN ASIIPQCSLA PSSIIPQFLP PVTSMAFEHP AVQAYRLQQA IAASVLQQPI AQLQQQSLAH LTIQTIATQQ QQQQFLPALS HLAMVNPVAY LQQQLLASNP LALANVVANQ QQQQLQQFLP ALSQLAMVNP AAYLQQQQLL SSSPLAVANA PTYLQQELLQ QIVPALTQLA VANPVAYLQQ LLPFNQLTMS NSVAYLQQRQ QLLNPLAVAN PLVAAFLQQQ QLLPYNRFSL MNPVLSRQQP IVGGAIF // ID ZEB1_MAIZE STANDARD; PRT; 180 AA. AC P06673; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 01-NOV-1988 (Rel. 09, Last annotation update) DE Zein-beta precursor (16 kDa) (Zein 2) (Clone 15A3). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86059563; PubMed=2999157; RA Marks M.D., Lindell J.S., Larkins B.A.; RT "Nucleotide sequence analysis of zein mRNAs from maize endosperm."; RL J. Biol. Chem. 260:16451-16459(1985). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- SUBCELLULAR LOCATION: Endosperm protein bodies. CC -!- SIMILARITY: To glutenin 2. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M12147; AAA33521.1; -. DR MaizeDB; 58053; -. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 19 Potential. FT CHAIN 20 180 Zein-beta. SQ SEQUENCE 180 AA; 19531 MW; A420806633E85E51 CRC64; MKMVIVLVVW LALSAASASA MQMPCPCAGL QGLYGAGAGL TTMMGAGGLY PYAEYLRQPQ CSPLAAAPYY AGCGQTSAMY QPLRQQCCQQ QMRMMDVQSV AQQLQMMMQL ERAATASSSL YEPALMQQQQ QLLAAQGLNP MAMMMAQNMP AMGGLYQYQY QLPSYRTNPC GVSAAIPPYY // ID ZEB2_MAIZE STANDARD; PRT; 183 AA. AC P08031; DT 01-AUG-1988 (Rel. 08, Created) DT 01-AUG-1988 (Rel. 08, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE Zein-beta precursor (Zein 2) (16 kDa) (Zein ZC1). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87248094; PubMed=3596247; RA Prat S., Perez-Grau L., Puigdomenech P.; RT "Multiple variability in the sequence of a family of maize endosperm RT proteins."; RL Gene 52:41-49(1987). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=cv. W64A; TISSUE=Endosperm; RX MEDLINE=91057131; PubMed=2243787; RA Reina M., Guillen P., Ponte I., Boronat A., Palau J.; RT "DNA sequence of the gene encoding the Zc1 protein from Zea mays W64 RT A."; RL Nucleic Acids Res. 18:6425-6425(1990). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- SUBCELLULAR LOCATION: Endosperm protein bodies. CC -!- SIMILARITY: To glutenin 2. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M16460; AAA33523.1; -. DR EMBL; X53515; CAA37595.1; -. DR PIR; B29017; B29017. DR MaizeDB; 58053; -. DR InterPro; IPR003612; AAI. DR InterPro; IPR001954; Glia_glutenin. DR InterPro; IPR000480; Glutelin. DR Pfam; PF00234; tryp_alpha_amyl; 1. DR PRINTS; PR00208; GLIADGLUTEN. DR PRINTS; PR00211; GLUTELIN. DR SMART; SM00499; AAI; 1. KW Seed storage protein; Repeat; Multigene family; Signal. FT SIGNAL 1 19 FT CHAIN 20 183 Zein-beta. SQ SEQUENCE 183 AA; 19558 MW; 3965BEBC1151F45A CRC64; MKVLIVALAL LALAASAASS TSGGCGCQTP PFHLPPPFYM PPPFYLPPQQ QPQPWQYPTQ PPQLSPCQQF GSCGVGSVGS PFLGQCVEFL RHQCSPAATP YGSPQCQALQ QQCCHQIRQV EPLHRYQATY GVVLQSFLQQ QPQGELAALM AAQVAQQLTA MCGLQLQQPG PCPCNAAAGG VYY // ID ZRP4_MAIZE STANDARD; PRT; 364 AA. AC P47917; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE O-methyltransferase ZRP4 (EC 2.1.1.-) (OMT). GN ZRP4. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. NKH31; TISSUE=Root; RX MEDLINE=94105316; PubMed=8278520; RA Held B.M., Wang H., John I., Wurtele E.S., Colbert J.T.; RT "An mRNA putatively coding for an O-methyltransferase accumulates RT preferentially in maize roots and is located predominantly in the RT region of the endodermis."; RL Plant Physiol. 102:1001-1008(1993). CC -!- FUNCTION: May be involved in the O-methylation of suberin CC phenylpropanoid precursors. CC -!- TISSUE SPECIFICITY: Accumulates preferentially in the roots and is CC located predominantly in the region of the endodermis, low levels CC are seen in the leaves, stems, and other shoot organs. CC -!- SIMILARITY: To other O-methyltransferases requiring S-adenosyl-L- CC methionine as substrate. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L14063; AAA18532.1; -. DR PIR; JQ2268; JQ2268. DR MaizeDB; 63528; -. DR InterPro; IPR001601; Methyltransf. DR InterPro; IPR001077; O_Met_trans2. DR InterPro; IPR000051; SAM_bind. DR Pfam; PF00891; Methyltransf_2; 1. KW Transferase; Methyltransferase. SQ SEQUENCE 364 AA; 39583 MW; FB8AD93AD5A6611D CRC64; MELSPNNSTD QSLLDAQLEL WHTTFAFMKS MALKSAIHLR IADAIHLHGG AASLSQILSK VHLHPSRVSS LRRLMRVLTT TNVFGTQPLG GGSDDDSEPV YTLTPVSRLL IGSQSSQLAQ TPLAAMVLDP TIVSPFSELG AWFQHELPDP CIFKHTHGRG IWELTKDDAT FDALVNDGLA SDSQLIVDVA IKQSAEVFQG ISSLVDVGGG IGAAAQAISK AFPHVKCSVL DLAHVVAKAP THTDVQFIAG DMFESIPPAD AVLLKSVLHD WDHDDCVKIL KNCKKAIPPR EAGGKVIIIN MVVGAGPSDM KHKEMQAIFD VYIMFINGME RDEQEWSKIF SEAGYSDYRI IPVLGVRSII EVYP //