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Database: UniProt
Entry: K3V166_FUSPC
LinkDB: K3V166_FUSPC
Original site: K3V166_FUSPC 
ID   K3V166_FUSPC            Unreviewed;       559 AA.
AC   K3V166;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   25-OCT-2017, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKJ78926.1};
GN   ORFNames=FPSE_00893 {ECO:0000313|EMBL:EKJ78926.1};
OS   Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium.
OX   NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ78926.1, ECO:0000313|Proteomes:UP000007978};
RN   [1] {ECO:0000313|EMBL:EKJ78926.1, ECO:0000313|Proteomes:UP000007978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096 {ECO:0000313|EMBL:EKJ78926.1,
RC   ECO:0000313|Proteomes:UP000007978};
RX   PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA   Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA   Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT   "Comparative pathogenomics reveals horizontally acquired novel
RT   virulence genes in fungi infecting cereal hosts.";
RL   PLoS Pathog. 8:E1002952-E1002952(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EKJ78926.1}.
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DR   EMBL; AFNW01000017; EKJ78926.1; -; Genomic_DNA.
DR   RefSeq; XP_009252288.1; XM_009254013.1.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; EKJ78926; EKJ78926; FPSE_00893.
DR   GeneID; 20359513; -.
DR   KEGG; fpu:FPSE_00893; -.
DR   InParanoid; K3V166; -.
DR   KO; K01268; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000007978; Chromosome 3.
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:UP000007978};
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   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   559 AA;  60555 MW;  7AD79E58CBFBD585 CRC64;
     MTQVTPAMLS ARASSLSLRQ QAMSSSAILN NNNAPAPTSV ENKESSKSFI LSDMKGRDTR
     DNRACASCIS KLAPGEVGQV NWHLETGQAC RLCQVEKLEP EAFTKPFCDF LQENPTIFHT
     VDYFEKKLKA LGYEHLSPRD SWAGKIQPGG KYWVTRNGSS LIAFKVGKAY KPGNGVAMIG
     GHIDALTAKL KPVSTKPVKA GFVQLGVAPY AGALNATWWD RDLSIGGRVV VRDEESGKTT
     TKLVKLDWPI ARIPTLAPHF GVGMMGENNK ETQAVPIIGL ESSQRAATKV LGPVGSFVNT
     QPPRLVELIA NELKIQSYSS IINWELELYD SQPAQTGGMD REFIFAGRID DKLCSWSALT
     ALLASNENSD DGVIKLVALF DDEEIGSLLR QGARGNFLPS VVERTVEALN PDTYGPELIG
     RTFSSSFLSS ADVSHAGSPN FLEKYLSEHV PELNVGVVIA ADSNGHMTTD SISTAIMQRA
     GELGDCRTQT FQIRNDSRSG GTIGPALSSM MGVRSADVGL PQLSMHSIRA TTGSLDPGLG
     VKFFKSFLDN WEKIDAEWH
//
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