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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//