ID   M7TPK1_BOTF1            Unreviewed;       399 AA.
AC   M7TPK1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   08-NOV-2023, entry version 41.
DE   SubName: Full=Putative pepsinogen c protein {ECO:0000313|EMBL:EMR85491.1};
GN   ORFNames=BcDW1_5871 {ECO:0000313|EMBL:EMR85491.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR85491.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KB707897; EMR85491.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7TPK1; -.
DR   STRING; 1290391.M7TPK1; -.
DR   MEROPS; A01.081; -.
DR   HOGENOM; CLU_062498_0_0_1; -.
DR   Proteomes; UP000012045; 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:SF68; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00026; Asp; 2.
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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..399
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012271774"
FT   DOMAIN          29..382
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        306..345
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   399 AA;  43881 MW;  8F62BB19E9C5481A CRC64;
     MSTFTLLALT AAASAAVLEL PVHIQNTYSS VEFEVGTPAK PYRFLFDTGS TTSWVNGRNC
     TDTSCPNISG FVRTQYNELN SSTSVDLDQY ASIPYIDGDV LAGNVFSDVF SDEKGTLSWN
     QTFMAADDSS WRFITADGFL GLGFSSIAEN KTSSLVETLL WEDKLDETRF ALFYGTNLNN
     TGVQDGVLTI GGSHEDVYVD GEVVYMPLRV ESPYELWRAP LRSVNVLAAH ENSTVTVHNG
     KLPSTDAPAN TWPKANTTWP MYGAGTAVFD TGAGRISLPS SMIGAFYFNL GWNITKLMNG
     EERMQCEHLN STWAVSLTFG ESNDESNDVT FSVRGDEFLT PGEQCMPPVD DSGSSSFSLL
     GADFLRRHYS VFDFGGSRVE DYQPKIGFGK LKEEYDYLK
//