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Database: UniProt
Entry: A0A0D2TSZ5_GOSRA
LinkDB: A0A0D2TSZ5_GOSRA
Original site: A0A0D2TSZ5_GOSRA 
ID   A0A0D2TSZ5_GOSRA        Unreviewed;       521 AA.
AC   A0A0D2TSZ5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN   ORFNames=B456_013G012600 {ECO:0000313|EMBL:KJB78673.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB78673.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB78673.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal aspartate or glutamate from a
CC         peptide, with a preference for aspartate.; EC=3.4.11.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001335};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CM001752; KJB78672.1; -; Genomic_DNA.
DR   EMBL; CM001752; KJB78673.1; -; Genomic_DNA.
DR   RefSeq; XP_012464754.1; XM_012609300.1.
DR   AlphaFoldDB; A0A0D2TSZ5; -.
DR   STRING; 29730.A0A0D2TSZ5; -.
DR   MEROPS; M18.A02; -.
DR   EnsemblPlants; KJB78672; KJB78672; B456_013G012600.
DR   EnsemblPlants; KJB78673; KJB78673; B456_013G012600.
DR   GeneID; 105783707; -.
DR   Gramene; KJB78672; KJB78672; B456_013G012600.
DR   Gramene; KJB78673; KJB78673; B456_013G012600.
DR   KEGG; gra:105783707; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   OMA; DRTVNQD; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000032304; Chromosome 13.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   521 AA;  57323 MW;  73273ADB88FE136A CRC64;
     MATISRAQLL HHPSAYFSRL PHSHSSFSIN FRRRKFSVTP PLLCSSSSSS SSSSASTNPS
     IVGDLLNYLN ESWTQFHATA EAKRQLIAAG FHLLNENDEW DLRPGGRYFF TRNMSCLVAF
     AVGEKYISGN GFHVIAAHTD SPCLKLKPKS ASSKSNYLML NVQTYGGGLW HTWFDRDLSV
     AGRVIVRASD GSFLHKLVKV KRPLLRVPTL AIHLNRTVNT DGFKPNLETQ LVPLLATKPE
     EAFPESKEKS SSSPKAAHHP LLMQILSDEL GCDVDDIVNI ELNICDTQPS CLGGANNEFI
     FSGRLDNLAS SYCALRALVD SCGSPGDLSS EHAIRMIALF DNEEVGSDSY QGAGAPTMFQ
     AMRRIAGSLA NSYAGESAFD RAIRQSFLVS ADMAHGVHPN FMDKHEEHHR PEMHKGLVIK
     HNANQRYATS GVTAFLFKEV AKMHNLPTQE FVVRNDMGCG STIGPILASG VGIRTVDCGI
     AQLSMHSVRE VCGKEDIDIA YKHFKAFYQT FSSIDRKLIV D
//
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