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Database: UniProt
Entry: W3WG39_9PEZI
LinkDB: W3WG39_9PEZI
Original site: W3WG39_9PEZI 
ID   W3WG39_9PEZI            Unreviewed;       495 AA.
AC   W3WG39;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   07-JUN-2017, entry version 15.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:ETS72885.1};
GN   ORFNames=PFICI_15392 {ECO:0000313|EMBL:ETS72885.1};
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:ETS72885.1, 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; KI912126; ETS72885.1; -; Genomic_DNA.
DR   RefSeq; XP_007842164.1; XM_007843973.1.
DR   EnsemblFungi; ETS72885; ETS72885; PFICI_15392.
DR   GeneID; 19280405; -.
DR   Proteomes; UP000030651; 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   ECO:0000313|EMBL:ETS72885.1};
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   495 AA;  54202 MW;  931A3F036BD5E738 CRC64;
     MAPPQSALDF LEFVNASPTP FHAVQSAIAR LDKAGFTKVK ERENWSATLK PGGKYYMTRN
     GSTIVAFAIG SKWRPGNPIA MVAAHTDSPC LRIKPVSKKS GVGFLQVGVE TYGGGIWHSW
     FDRDLSIAGR VLVKDGQGNF VQKLVKVDRP IIRIPTLAIH LDREPSFNPN KETELFPIAG
     MVAAELNRTG VEEVVKDDNT SNTTFQPLKD MSDRHHPYIL EIIAEHAGVS VENVVDFEMV
     LYDVQKSVLG GLNEEFIYSA RLDNLNMTYC SVMGLIESVQ SSSLDDETSI RLIACFDHEE
     IGSTSAHGAN SDLLPAVVRR LSVVAGDRHG DSASHRSWEH ISSDPDADLT TAFEQTASGS
     FLVSADMAHS VHPNYVGKYE SNHQPEMNKG TVIKVNANQR YATNSPGIVL IQEAAKRAGV
     PLQLFVVRND SSCGSTIGPM LSAQMGIRTL DLGNPQLSMH SIRETGGTYD VEHAIKLFDS
     FLSHYSELEA KIYVD
//
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