ID A0A0W0FW32_9AGAR Unreviewed; 960 AA.
AC A0A0W0FW32;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 08-NOV-2023, entry version 32.
DE SubName: Full=Putative acid protease {ECO:0000313|EMBL:KTB40514.1};
GN ORFNames=WG66_6897 {ECO:0000313|EMBL:KTB40514.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB40514.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB40514.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB40514.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTB40514.1}.
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; LATX01001573; KTB40514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0FW32; -.
DR Proteomes; UP000054988; 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; cd09917; F-box_SF; 1.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
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:SF74; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF00646; F-box; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS50181; FBOX; 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, ECO:0000313|EMBL:KTB40514.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT DOMAIN 81..399
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 416..465
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 45..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 99
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 279
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 960 AA; 107183 MW; 69EE19CF36ADEB72 CRC64;
MPSTVSFKSS LSPMAKDADL QPVVGNHMKH IVNRDRARAQ KLMSGMHPHG PLEFRKKHGH
QAPPTPAGKN SVDVTDSAVT YVMPVAIGNP ATTYNLLIDT GSSNTWVGAN KEYKPSKQSQ
TERKEVSVTY GSGSFIGTEY TDCVALSDNL MIEEQSIGIA RETKGFGNDG IDGILGIGPV
DLTHGTVQGM ESVPTVTDSL LKQGTIQTES IGIFYAPTTG ESLPNGEMTF GGVDETKTTT
SIKYVPITKT SPACQYWGVD QVIKYDGQQI LNNCAGIVDT GTTLIMLATD CFEKYMKMTG
AVMDDATGLL TVTKEQFKNM KSMMFHIGDM SCELTPNAQI WPRKMNTMFG GQTDKIYLVF
ADMGQPSGTG LDFINGFTFL QRFYTLMRAV ITSFTRQLEQ QLNAIKNVLH IQTVPQDHLF
RLPHKIIIRI VAELDITGVS RCLQVCTRLR DIIKSTRLHE YKARLALANL EDGTVDSSYD
IEARLAQLEA HQKAWKDFRW TKSVTISSDP KYPWNFAGGV FAQALEFPDG ICHVFTQLPS
SARGIEMKQW SLDCIQNDTF NYSPAQDLLV CLDSNHKIEQ SRPPILIRLL SLTDGKAHPL
ASYPSIRVAE LPAPLDSWEF TIQICGHTLA IMASPKTGLI LDLVPKLYIV NWKTGKIQEV
EFQLLDLIIV PERLCLKFLS NGTKGMTVRL ITERYLLVCK LYFAATHIAP GPGLSIVDLE
ARLTRCTAIT LLLPKVQGHE FMMLRVAPCH SLAHEPSHQP FLPFRASSQD DPVLVRMIVK
PRKTEESEKK EKTEASEKTK KPQCFALFIP RSLLLYHARK LAFLPRAVDE RVSATIPWES
WGPSNTKFLQ WGDGTTSCGM RMLARRSDTD PFASDRPKAE RQYRIFDFNP FPMRYGFQKD
SPIQLSHTIV VRSPLFSSPI VTSLPCRIID GELSEEASWY IWNEDTLALI KENEVKICSV
//