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Database: UniProt
Entry: W6Y9G9_COCCA
LinkDB: W6Y9G9_COCCA
Original site: W6Y9G9_COCCA 
ID   W6Y9G9_COCCA            Unreviewed;       507 AA.
AC   W6Y9G9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   07-JUN-2017, entry version 14.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EUC34160.1};
GN   ORFNames=COCCADRAFT_36117 {ECO:0000313|EMBL:EUC34160.1};
OS   Bipolaris zeicola 26-R-13.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930089 {ECO:0000313|EMBL:EUC34160.1, ECO:0000313|Proteomes:UP000053841};
RN   [1] {ECO:0000313|EMBL:EUC34160.1, ECO:0000313|Proteomes:UP000053841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=26-R-13 {ECO:0000313|EMBL:EUC34160.1,
RC   ECO:0000313|Proteomes:UP000053841};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R.,
RA   Martin J., Schackwitz W., Grimwood J., MohdZainudin N., Xue C.,
RA   Wang R., Manning V.A., Dhillon B., Tu Z.J., Steffenson B.J.,
RA   Salamov A., Sun H., Lowry S., LaButti K., Han J., Copeland A.,
RA   Lindquist E., Barry K., Schmutz J., Baker S.E., Ciuffetti L.M.,
RA   Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector
RT   coding capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KI964596; EUC34160.1; -; Genomic_DNA.
DR   RefSeq; XP_007711530.1; XM_007713340.1.
DR   EnsemblFungi; EUC34160; EUC34160; COCCADRAFT_36117.
DR   GeneID; 19148207; -.
DR   KEGG; bze:COCCADRAFT_36117; -.
DR   KO; K01267; -.
DR   Proteomes; UP000053841; Unassembled WGS sequence.
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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053841};
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:UP000053841};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   507 AA;  55815 MW;  21263927931E2706 CRC64;
     MSSKPSLQAA EDFLSFVNAS PTPFHAVKSA KERLEKAGFK QIKERDSWAP TLQPGGKYYL
     TRNTSSIVAF AIGQKWKPGN PIAMIGAHTD SPCLRIKPVS KRQSDGFLQV ACETYGGGLW
     HTWFDRDLSI AGRAMVRTKD GNIEQRLVKV DRPILRIPTL AIHLDRQENF QFNKETQLFP
     ITGLVAAELN RQGKTEETKE ETKDADNEGS FEPLAAPTAR HHPYIVDIIA EEAGVEASDI
     VDFEMVLYDT QKSVIGGLNN ELIFSPRLDN LMMTYCSVEG LIKSLSSPSA LKKDSIIRLI
     ACFDHEEIGS QTAQGADSNL LPAVIRRLSV LPASESNSDK SYDKVEADTA TAFEQTLATS
     FLVSADMAHS VHPNYPAKYE SQHRPEMNKG TVIKINANAR YATNTPGIVL LQEAARRAKP
     ASYNLSSTKE GVPLQLFVVR NDSSCGSTIG PMLSAAMGAR TLDLGNPQLS MHSIRETGGA
     HDVEHAVNLF DSFFENYEEL EKKIIVD
//
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