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Database: UniProt
Entry: A0A194WXR0_9HELO
LinkDB: A0A194WXR0_9HELO
Original site: A0A194WXR0_9HELO 
ID   A0A194WXR0_9HELO        Unreviewed;       516 AA.
AC   A0A194WXR0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   SubName: Full=Peptidase M18, aminopeptidase I {ECO:0000313|EMBL:KUJ12720.1};
GN   ORFNames=LY89DRAFT_687685 {ECO:0000313|EMBL:KUJ12720.1};
OS   Phialocephala scopiformis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Phialocephala.
OX   NCBI_TaxID=149040 {ECO:0000313|EMBL:KUJ12720.1, ECO:0000313|Proteomes:UP000070700};
RN   [1] {ECO:0000313|EMBL:KUJ12720.1, ECO:0000313|Proteomes:UP000070700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 120377 {ECO:0000313|EMBL:KUJ12720.1,
RC   ECO:0000313|Proteomes:UP000070700};
RG   DOE Joint Genome Institute;
RA   Walker A.K., Frasz S.L., Seifert K.A., Miller J.D., Mondo S.J.,
RA   Labutti K., Lipzen A., Dockter R., Kennedy M., Grigoriev I.V.,
RA   Spatafora J.W.;
RT   "Full genome of DAOMC 229536 Phialocephala scopiformis, a fungal
RT   endophyte of spruce producing the potent anti-insectan compound
RT   rugulosin.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KQ947423; KUJ12720.1; -; Genomic_DNA.
DR   RefSeq; XP_018067075.1; XM_018215559.1.
DR   EnsemblFungi; KUJ12720; KUJ12720; LY89DRAFT_687685.
DR   GeneID; 28825285; -.
DR   KEGG; psco:LY89DRAFT_687685; -.
DR   KO; K01267; -.
DR   Proteomes; UP000070700; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 2.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KUJ12720.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070700};
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:UP000070700};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   516 AA;  56610 MW;  F9C67BA4473EBEF1 CRC64;
     MASKKVSAAV AKANDFIDFV NASPTPYHAV QSAITRLTTA GFTEIRERDP WTSLLHPGGK
     YYLTRNASSI VAFTIGAKWK PGNPIAMVGA HTDSPCLRLK PVSKKSGAGF LQVGVETYGG
     GIWHTWFDRD LSVAGRAMVR DGKGGFVQRL FKVERPILRI PTLAVHLERQ DKFEPNKETE
     LFPIAGLVAA ELNRTGQKEG KDHSIEGLEK EGEGEFRPLK VLRDRHHPYL VEIIAEHAGV
     DVEDVIDFEM VLYDTQKSCI GGINNELIFS PRLDNLGMTY CAIEGLIESV SQKHALDDET
     GIRLSVCFDH EEIGSTSAHG AASNLLPAVL RRLSVLPAGH HDSGSEQSYE KIPREQDLDI
     ATAYEQTLSS SFLVSADMAH SVNPNYAHKY EADHRPEMNK GTVIKVNANQ RYATNSPGII
     LLQEVAKLAK PSEDSTTSHG VPLQLFVVRN DSSCGSTIGP MLSAALGTRT IDVGNPQLSM
     HSIRETGGVY DVEHGVRLFE SFFQHFSELE SKILVD
//
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