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Database: UniProt
Entry: A0A061FWE4_THECC
LinkDB: A0A061FWE4_THECC
Original site: A0A061FWE4_THECC 
ID   A0A061FWE4_THECC        Unreviewed;       520 AA.
AC   A0A061FWE4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   22-NOV-2017, entry version 21.
DE   SubName: Full=Zn-dependent exopeptidases superfamily protein isoform 1 {ECO:0000313|EMBL:EOY19139.1};
GN   ORFNames=TCM_043913 {ECO:0000313|EMBL:EOY19139.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Malvales; Malvaceae; Byttnerioideae;
OC   Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY19139.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY19139.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23731509;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C.,
RA   Feltus F.A., Mustiga G.M., Amores F., Phillips W., Marelli J.P.,
RA   May G.D., Shapiro H., Ma J., Bustamante C.D., Schnell R.J., Main D.,
RA   Gilbert D., Parida L., Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its
RT   use to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53-R53(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CM001888; EOY19139.1; -; Genomic_DNA.
DR   EnsemblPlants; EOY19139; EOY19139; TCM_043913.
DR   Gramene; EOY19139; EOY19139; TCM_043913.
DR   OMA; YQWVTIP; -.
DR   Proteomes; UP000026915; Chromosome 10.
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   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000026915};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   520 AA;  57022 MW;  5563568A020D880B CRC64;
     MAAISRVQLL HHPSSVFSRF PHSPSSSFAF SLCRRKFSSS APLLCSLSSS SSSSSTNASI
     VGDLLDYLNE SWTQFHATAE AKRQLIAAGF HLLNENDEWD LKPGGRYFFT RNMSCLVAFA
     IGEKYIVGNG FHVIAAHTDS PCLKLKPKSA SSKSNYLMLN VQTYGGGLWH TWFDRDLSVA
     GRVIVRANDG SFLHKLVKVK RPLLRVPTLA IHLNRTVNTD GFKPNLETHL VPLLATKPEE
     EAAEPKEKSS LSSKAVHHPL LMQILSDELC CDVDDIVNIE LNICDTQPSC LGGANNEFIF
     SGRLDNLASS YCALRALVDS CGSPGDLSSE HAIRMVALFD NEEVGSDSFQ GAGAPTMFQA
     MRRIVGSLAN SYGGGSAFDR AIRQSFLVSA DMAHGVHPNF MDKHEEHHRP EMRKGLVIKH
     NANQRYATSG VTAFLFKEVG KIHNLPTQDF VVRNDMGCGS TIGPILASGV GIRTVDCGIA
     QLSMHSVREV CGKDDIDIAY KHFKAFYQIF SSIDRKLIVD
//
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