ID A0A0W0FGC7_9AGAR Unreviewed; 428 AA.
AC A0A0W0FGC7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative acid protease {ECO:0000313|EMBL:KTB35334.1};
GN ORFNames=WG66_11932 {ECO:0000313|EMBL:KTB35334.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB35334.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB35334.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB35334.1,
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:KTB35334.1}.
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DR EMBL; LATX01001990; KTB35334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0FGC7; -.
DR eggNOG; KOG1339; Eukaryota.
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; cd05471; pepsin_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; 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:SF87; SACCHAROPEPSIN; 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};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KTB35334.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..428
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006901673"
FT DOMAIN 118..425
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 136
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 315
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 149..154
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 428 AA; 46143 MW; 3AE2AC558005A07C CRC64;
MFSKAALFIA ITIALLSSAN PIIDPILRHD IGRPIPLRKR KSLTKDDGVF DIDNAVVQAV
ITKNKHRQNL INLKKNTGHL LNENAVIRPV AVLPKDILDK LHKRQSEPLE DVRNDLEWIG
PVSIGTPGQS FLINFDTGSA DLWIPSEDCR SSACASKTLY EPGTSSTSKK ERGQFGIQYG
DGSMVSGPIY SDTVSIGGVN VTGQHFSAVT ALSRSFDTDP IDGILGLAYP VLSNIDPSPF
FNTAIEQGAV PNKSFGFYLA ANNSELFLGG TNPKLYTGEI EYHQIDTSTG FWQIPGASAL
IGSTEVVSDF ATIIDSGTTI MYGPPSDVKK LYSKIEGARL VDQVNGFYAF PCNNIPSVAF
SWGGKAWPIT EENFNLGLVE AGSTECVGAI SAQDLGLGDV WLLGDSFMKN AYTAFDYDKN
AVGFAQLA
//
