ID A0A0W0F0G2_9AGAR Unreviewed; 393 AA.
AC A0A0W0F0G2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Putative acid protease {ECO:0000313|EMBL:KTB29803.1};
GN ORFNames=WG66_17682 {ECO:0000313|EMBL:KTB29803.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB29803.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB29803.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB29803.1,
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}.
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:KTB29803.1}.
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DR EMBL; LATX01002412; KTB29803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0F0G2; -.
DR eggNOG; KOG1339; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
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:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KTB29803.1};
KW Protease {ECO:0000313|EMBL:KTB29803.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..393
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006901349"
FT DOMAIN 70..391
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 88
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 393 AA; 41338 MW; 2E66061AC9F7CCB8 CRC64;
MNVISAKARG GLMRLFLFSL FACQSFAADV PHKILLSSRA VPGPSPLRKR ALPPSDVPLD
VFFKGTDLQW FGNISIGTPP QEITVVFDTG SSSLEFSSTL CRSCLNEAPK FDPSKSVTFV
DGGRTSSITF GTGVGVDPVV GANYRLTLRS GTDTVTVGGL ESSSVPLFLI TDQTPTFNID
PFSGIQGMGA RASGFFANLI SQGLPSLFGM FLAPIEIGNA ELTIGGIDES KFSGPLLFAS
LPSGGSSTWR LNSPGISVNG RTTSGLMASR NLIFDSGTSN MVFDTATTEA IYALISPDIK
PNPDEPGTYG IACSRISSLP AVIDITFIAQ NGSPFNLTIP SSELSVGPFE SDPSLCQTLI
NAVDGLQIVG ASLLKHYYSV WDVGGQRMGF ASL
//