ID W7N832_GIBM7 Unreviewed; 454 AA.
AC W7N832;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 08-NOV-2023, entry version 38.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=FVEG_11317 {ECO:0000313|EMBL:EWG52627.1};
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:EWG52627.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG52627.1, 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}.
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DR EMBL; DS022257; EWG52627.1; -; Genomic_DNA.
DR RefSeq; XP_018758818.1; XM_018900532.1.
DR AlphaFoldDB; W7N832; -.
DR GeneID; 30068840; -.
DR KEGG; fvr:FVEG_11317; -.
DR VEuPathDB; FungiDB:FVEG_11317; -.
DR eggNOG; KOG1339; Eukaryota.
DR OrthoDB; 4940213at2759; -.
DR Proteomes; UP000009096; Chromosome 9.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF47; ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01220)-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000009096};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..454
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004899313"
FT DOMAIN 110..452
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 343
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 454 AA; 49623 MW; 079AA9DAFEE73B36 CRC64;
MRSLHFIFVL LASIMCPSFA AVAGNQVAQA HWDLSTSLNG FSFERARAIS AKTIDRTGVR
MSRLKSLKHK TGSHPRSALS HLTRTHLATA GKGTVPHQNI SAVGSFSTAY AIQCTWDDTP
VWLIFDTGSS DTWAAKTGFT CEDASGNLRK TQSPCSFGQP HIENFLHDIS EVYFHRRYGS
GEDVSGPMGV SDIACGGILV PKQQVGLVSR AYWRGDNTTV GILGLAYPSL TSAYLGDPND
TSDESEWNNY PYSPWFTTAI SKGVVDPVFS VSIERNTSDG VLAWGGLPPM PWGPKSFAAT
DLIIAKLVER EKTGWEPSFY TIIPDGLQWG TTTDTAKYPY IVDTETTMMH IPPPLAEAIA
KAFQPPATWM FEWSAYFVDC KAIPPHFAVI IKGVRFWINP ADLIYQDFTE PVTGKCAIAI
STGGSGPYIL GDLFLQNVVA VFDVGGAEMR FYSK
//
