GenomeNet

Database: UniProt
Entry: W7LVK8_GIBM7
LinkDB: W7LVK8_GIBM7
Original site: W7LVK8_GIBM7 
ID   W7LVK8_GIBM7            Unreviewed;       465 AA.
AC   W7LVK8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=FVEG_02268 {ECO:0000313|EMBL:EWG39444.1};
OS   Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS   fungus) (Fusarium verticillioides).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG39444.1, ECO:0000313|Proteomes:UP000009096};
RN   [1] {ECO:0000313|EMBL:EWG39444.1, ECO:0000313|Proteomes:UP000009096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA   Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA   Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA   Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA   Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS022243; EWG39444.1; -; Genomic_DNA.
DR   RefSeq; XP_018745635.1; XM_018889481.1.
DR   AlphaFoldDB; W7LVK8; -.
DR   GeneID; 30060490; -.
DR   KEGG; fvr:FVEG_02268; -.
DR   VEuPathDB; FungiDB:FVEG_02268; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000009096; Chromosome 6.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05474; SAP_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR033876; SAP-like.
DR   PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009096};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..465
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004898218"
FT   DOMAIN          53..403
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          425..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   465 AA;  50168 MW;  D44E4BF6E499A529 CRC64;
     MRTFTLLTSL AVGVSAGTVS APIVKQRFHH ESSLHSRDTL SLAALNNITG GGYYAEFQVG
     TPGQNISFQL DTGSSDTWLN SDETDLCNSR TKQEAIGPCM TTFKPDDSRT YKLVDPDGFD
     ITYLDTRSIS GDYFNDTVTI DGKSIKQQRL GLATKSVRPT GLMGLGFSAN VVANGTYPTI
     VENMVSQGLI DRAAFSLWLN DLSAEQGTIL FGGLDTEKFV GKLATLPLLP DPSTLNLTHF
     TVAFEGFEVK TPKGQEIKID SLKKDTTAIL DSGATVCLLP EAQVAPIYKA FNVLSVEDVA
     IPFVDCAYGK DKGKGVSFDF KFDGKTISVP MSEMVINAFP DKQEIFDDPQ VSSYFDDWDS
     VCMFGISPVS QYGLTGGVTL LGDTFLRSAY VVYDLANEQL GIAEANHNTD ESNIVELKEK
     DTKFPDVTGI EGTSSSEEDD NAAGHLSPSS MVTLIVAAGI TWALL
//
DBGET integrated database retrieval system