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Database: UniProt
Entry: F9GA67_FUSOF
LinkDB: F9GA67_FUSOF
Original site: F9GA67_FUSOF 
ID   F9GA67_FUSOF            Unreviewed;       461 AA.
AC   F9GA67;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=FOXB_15549 {ECO:0000313|EMBL:EGU73939.1};
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:EGU73939.1};
RN   [1] {ECO:0000313|EMBL:EGU73939.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU73939.1};
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:EGU73939.1}.
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DR   EMBL; AFQF01003985; EGU73939.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9GA67; -.
DR   STRING; 660025.F9GA67; -.
DR   MEROPS; A01.080; -.
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}.
FT   DOMAIN          114..446
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        337
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   461 AA;  51219 MW;  0826F3F3AC062D1C CRC64;
     MEAIYQVQHQ FRLDRGLTRI SVKRNPHYQP HGTKSYVHLL NRFGFKPTKP GPYFQDRQIQ
     QRGLAHPRFH AAVGGRVYQT KILRKKLGTD GTLDADGTQI GEVTAEDLPF DSMYLCEVSI
     GTPPQKFNLD FDTGSADLWV NIPNEALKQR VKNTDQKGHN VFNPLSSSSF NELTDKTWKI
     SYGDGSSASG DCGSDDVTIG GLTIKNQTVE LASQLDQQFA RGKGDGLLGL AFPQINTVKT
     NWDSDPADTP VVNMINQHDI PKEAELFTSA FYSQRDANSP ESFYTFGFID TDLVARSGEE
     ISWTRIDSSD GFWKFPSARF SVKGKIIDLS GNKAIADTGT TLVLVSDEVC EALYDAIPGA
     RYSPTQQGYV FPRSTNVEDL PEFKVAIGDK QFDIQPQDLV FAPADKDNWY GGIQSRGNLP
     FDIFGDAFLK SVYAIWDQGN KRFGVVPKIE ETQNLDPTPI A
//
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