ID W9HN32_FUSOX Unreviewed; 413 AA.
AC W9HN32;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 22-FEB-2023, entry version 38.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=FOYG_13788 {ECO:0000313|EMBL:EWY84008.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY84008.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY84008.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; JH717847; EWY84008.1; -; Genomic_DNA.
DR AlphaFoldDB; W9HN32; -.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000030753; Unassembled WGS sequence.
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:UP000030753};
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_5004923989"
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; 44007 MW; 8BA30076606654B9 CRC64;
MKFSSVVTSG LASFTLVAGL PTVTSSNEHS VQQVRNPVYK RNGIAALGKI YRKYHIDLPE
YLKNSVLARR DGTGTVANKP IENNSEWLTP VQIGNPPRTF QMDLDTGSSD LWVYGSKAAT
AGGSSNRYNA SSSKSCEEMA GAKWTIEYGD GSGASGHVVK DTVSIGGLSV EAQAVQVADK
VHESFAQQQD LDGLLGLGFS SINTVTPKKQ KTFFENAKTE HGTGVFTADL QHDAPGTYTF
GVINKTAYEG DITYTAVDSS TGMWTFTSTG YAVGKGNITK TPITAIADTG TSLMFLPEQV
NKAYYSQIDG ARVDTTAGGY VFPCDTKMPD FTFYMGETGI TVPGSYMNFA PLEGPVPGEK
EGKREVGTCY GGLQSSAGDI NIFGDIALKA AFVVFDAEKT RIGFAKKTLV GVE
//
