ID W7MWG2_GIBM7 Unreviewed; 413 AA.
AC W7MWG2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=FVEG_13605 {ECO:0000313|EMBL:EWG55631.1};
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:EWG55631.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG55631.1, 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}.
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DR EMBL; DS022265; EWG55631.1; -; Genomic_DNA.
DR RefSeq; XP_018761822.1; XM_018902965.1.
DR AlphaFoldDB; W7MWG2; -.
DR EnsemblFungi; FVEG_13605T0; FVEG_13605T0; FVEG_13605.
DR GeneID; 30070937; -.
DR KEGG; fvr:FVEG_13605; -.
DR VEuPathDB; FungiDB:FVEG_13605; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OMA; RNPVYKR; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000009096; Chromosome 10.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_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; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 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|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..413
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004896787"
FT DOMAIN 87..405
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 288
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 413 AA; 43795 MW; 821B38368F31159A CRC64;
MKFSSVLTSG LASFTLVAGL PTITSPSEHS IQQVRNPVHK RNGIAALGKI YRKYHIDLPE
YLKSSLLARR DSTSTVTNKP IENNAEWLTP VQIGNPPRTF QMDLDTGSSD LWVYGSKAAT
AGGSSNPYNA SNSKTCEEMA GAKWSIEYGD GSGASGHVVK DTVSIGGLSV EAQAVQVADK
VDESFATQQE LDGLLGLGFS SINTVTPKKQ KTFFDNAKAE HGTGVFTADL KHDAPGTYTF
GVINKTAYEG DITYTAVDSS TGMWTFTSTG YTVGKGNVTK TSITAIADTG TSLIFLPEAV
NKAYYSQIDG AKIDATAGGY VFPCDTKMPD FTFYVGETGI TVPGAYMNFA PLEGPVPGEK
EGKREVGTCY GGLQSSAGDI NIFGDIALKA AFVVFDAERT RIGFAKKTLA GVE
//
