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Database: UniProt
Entry: F9FHP2_FUSOF
LinkDB: F9FHP2_FUSOF
Original site: F9FHP2_FUSOF 
ID   F9FHP2_FUSOF            Unreviewed;       396 AA.
AC   F9FHP2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   08-NOV-2023, entry version 51.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=FOXB_05921 {ECO:0000313|EMBL:EGU83511.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU83511.1};
RN   [1] {ECO:0000313|EMBL:EGU83511.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU83511.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGU83511.1}.
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DR   EMBL; AFQF01001831; EGU83511.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FHP2; -.
DR   SMR; F9FHP2; -.
DR   STRING; 660025.F9FHP2; -.
DR   MEROPS; A01.018; -.
DR   PaxDb; 5507-FOXG_12714P0; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..396
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003383095"
FT   DOMAIN          86..393
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        285
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        117..122
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   396 AA;  42777 MW;  A9050D850C47A8A3 CRC64;
     MKGALLTAAA LLGSAQAGVH KMKLNKVPLA DQLATNSVED HLQSLGQKYL GASRPKNAAD
     YAFATNTVNV EGGHPVPVSN FMNAQYFSEI TIGTPPQSFK VVLDTGSSNL WVPSQQCGSI
     ACYLHSKYDS SASSTYKENG TEFEIHYGSG SLSGFVSNDV VSIGDLEIKD QDFAEATKEP
     GLAFAFGRFD GILGLGYDRI AVNGMVPPFY QMVNQKLLDE PVFAFYLDDQ EGESEATFGG
     IDKSKFTGDI EYIPLRRKAY WEVDLEAIAF GDEVAEQENT GAILDTGTSL NVLPSALAEL
     LNKEIGAKKG YNGQYTIECD KRASLPDITF NLAGSNYSLP ATDYILEVQG SCISTFQGMD
     FPEPVGPLVI LGDAFLRRYY SVYDLGKNAV GLARAK
//
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