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Database: UniProt
Entry: W3X0W5_9PEZI
LinkDB: W3X0W5_9PEZI
Original site: W3X0W5_9PEZI 
ID   W3X0W5_9PEZI            Unreviewed;       523 AA.
AC   W3X0W5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   25-OCT-2017, entry version 14.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETS79743.1};
GN   ORFNames=PFICI_09596 {ECO:0000313|EMBL:ETS79743.1};
OS   Pestalotiopsis fici W106-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Xylariomycetidae; Xylariales; Sporocadaceae;
OC   Pestalotiopsis.
OX   NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS79743.1, ECO:0000313|Proteomes:UP000030651};
RN   [1] {ECO:0000313|Proteomes:UP000030651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 {ECO:0000313|Proteomes:UP000030651};
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for
RT   synthesis of natural products.";
RL   BMC Genomics 16:28-28(2015).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KI912114; ETS79743.1; -; Genomic_DNA.
DR   RefSeq; XP_007836368.1; XM_007838177.1.
DR   EnsemblFungi; ETS79743; ETS79743; PFICI_09596.
DR   GeneID; 19274609; -.
DR   KEGG; pfy:PFICI_09596; -.
DR   KO; K01268; -.
DR   Proteomes; UP000030651; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
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:UP000030651};
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:UP000030651};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   523 AA;  56445 MW;  510A238C982A241B CRC64;
     MTQHTPEFLR QRSSNMSLRM AAVANASSAT SPVPFEARFD AQERQNTVAA RDLKPEDYTK
     PFCEFLQENP TVFHAVDYFK SKAFKHGYTE LSAREDWSGK IVPGGKYFST RNGSTIIAWT
     VGKAYKPGNG VAMIAGHIDA LTAKLKPVSS KPNKQGYIQL GVAPYAGALN ETWWDRDLSI
     GGRVIVREES GKTSSKLVKL DWPIAKVPTL APHFGVGMLG SNNKETQAVP IIGLDNSDLY
     PTTNSAPAEA LGPAGSFVAT QPPKLVKVIA KQLGLTDYSQ IVNWELELFD LQPATVAGLD
     KEFITGGRID DKLCSWGAFE GLLASTQGED EGTVKLVALF DDEEIGSLLR QGAKGNFMPL
     VIERSVEALS EKAGKAFGPS TVGRTYANSF LVSADVTHAV NPNFLERYLA DHAPRLNVGI
     TICADSNGHM TTDSVSTAIL TRVCELSDCT PQVFMIRNDS RSGGTVGPTL SSMMGVRAAD
     AGMAQLSMHS VRATTGALDP GLGAKFFKGF LDHWEKVDGE WTQ
//
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