ID   M7TZI9_BOTF1            Unreviewed;       398 AA.
AC   M7TZI9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Putative aspartic endopeptidase pep2 protein {ECO:0000313|EMBL:EMR86694.1};
GN   ORFNames=BcDW1_4703 {ECO:0000313|EMBL:EMR86694.1};
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:EMR86694.1, 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}.
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; KB707850; EMR86694.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7TZI9; -.
DR   STRING; 1290391.M7TZI9; -.
DR   MEROPS; A01.018; -.
DR   HOGENOM; CLU_013253_3_4_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   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF89; SACCHAROPEPSIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
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..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..398
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004086120"
FT   DOMAIN          85..394
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        116..121
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        320..353
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   398 AA;  42909 MW;  8E49BAF3150F9B88 CRC64;
     MKGAFLAAAS LLGSVSAGVH KMPLKKVSLS EQLATANMQE HAKHLGQKYM GVRPESHASE
     MFKETSVHDA GDHTVPVSNF LNAQYFSEIT IGTPPQSFKV VLDTGSSNLW VPSSQCGSIA
     CYLHTKYDSS SSSTYKQNGT SFEIRYGSGS LSGFTSKDVM TIGDLKIKDQ VFAEATEEPG
     LAFAFGRFDG ILGLGYDTIS VNSIVPPFYS MVDQGLLDEP VFAFYLGSND ESDPSEAIFG
     GVNKDHYDGK ITEIPLRRKA YWEVDLDSIA FGDSEAELEN TGVILDTGTS LIALPADLAG
     LLNAEIGAKK GWNGQYTVDC AKRDSLPELT FTLSGHKFPI GPYDYILEVQ GSCISAIMGM
     DFPEPVGPLA ILGDAFLRRY YSIYDLGKNT VGLAKAKA
//