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Database: UniProt
Entry: K3VS66_FUSPC
LinkDB: K3VS66_FUSPC
Original site: K3VS66_FUSPC 
ID   K3VS66_FUSPC            Unreviewed;       493 AA.
AC   K3VS66;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   07-JUN-2017, entry version 27.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKJ78129.1};
GN   ORFNames=FPSE_01590 {ECO:0000313|EMBL:EKJ78129.1};
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:EKJ78129.1, ECO:0000313|Proteomes:UP000007978};
RN   [1] {ECO:0000313|EMBL:EKJ78129.1, ECO:0000313|Proteomes:UP000007978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096 {ECO:0000313|EMBL:EKJ78129.1,
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:EKJ78129.1}.
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DR   EMBL; AFNW01000051; EKJ78129.1; -; Genomic_DNA.
DR   RefSeq; XP_009252985.1; XM_009254710.1.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EKJ78129; EKJ78129; FPSE_01590.
DR   GeneID; 20360210; -.
DR   KEGG; fpu:FPSE_01590; -.
DR   InParanoid; K3VS66; -.
DR   KO; K01267; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000007978; Chromosome 4.
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: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   493 AA;  53922 MW;  03634E54B6143833 CRC64;
     MAPPQEALDF VDFVNASPTP YHAVQSASAR FEKAGFKLIR ERDSWASTLR PGGKYYLTRN
     ASTIVAFTIG RKWRPGNPVA IVGAHTDSPC LRLKPVSKKT NVGFLQIGVE TYGGGIWTSW
     FDRDLSIAGR VLVKEGDNFV QKLVKVDKPL VRIPTLAIHL HRQTNFDPNK ETELFPIAGL
     VAAELNKDVK EKSEEKKDDG EEDEEFKPLK VITERHHPQV LDVIAAEAGV EVSDIVDFEL
     VLYDTQKSCI GGLADEFIFS PRLDNLGMTY CSVEGLIESV KNESSLEEDG TIRLTVCFDH
     EEIGSTSAQG ANSNLLPSVI RRLSVLPGNR DASSEGSYEA VHHEGEDATA YEQTLSRSFL
     VSADMAHSVH PNYAGKYESS HQPAMNGGTV VKINANQRYA TNSPGIVLIE ECARTAGVPL
     QLFVVRNDSP CGSTIGPGLA AALGMRTLDL GNPQLSMHSI RETGGTADVG YGIRLFKEFF
     EKYGSLEPKI LID
//
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