ID   M7U376_BOTF1            Unreviewed;       723 AA.
AC   M7U376;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN   ORFNames=BcDW1_3387 {ECO:0000313|EMBL:EMR88024.1};
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:EMR88024.1, 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 S9C family.
CC       {ECO:0000256|ARBA:ARBA00010040}.
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DR   EMBL; KB707803; EMR88024.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7U376; -.
DR   STRING; 1290391.M7U376; -.
DR   MEROPS; S09.012; -.
DR   HOGENOM; CLU_008615_0_1_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF69322; Tricorn protease domain 2; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..723
FT                   /note="Dipeptidyl-peptidase V"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004086302"
FT   DOMAIN          492..701
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   723 AA;  79186 MW;  5A3A9232B295F02C CRC64;
     MLFTMRSSLS LVALLSAGLA NGTYTNSTPT FTPQAMLSSP RRGSAIPNAD GTLALYTVAT
     YSFEEHHNAH ELRVMNLANG TSWLFSNSSG ISNVNWLGDG SKIIWFVSEE DGSTSFVVGD
     ATAPSAEPIS AGSVPGAVDN LKLVSIGEGT LGVAFSGQAL PNGTLYNSEL APTPYSTGRA
     YTKIFVRHWD TYVTPQRNSI WYAALSTTGN NYTLSEPINA LNGSGLESPV PPFGATNRQD
     ITLNQATTTK SDVYYVPLTT FTETSPELKV ISTPNLEGAS DAVVFSPSGS SLAFVRMAHI
     SYESDKNRVL QVADVTSDLT AIEFFASEDG KGAWDRSPST LLYSQDGESI YAVAEDFARV
     RLFTFTSDPT NTTLPSIIFK DGGVTDLHYQ GEDKLLISSS SYLDNSVFSS VDPIVSAATN
     ASSGITTISA NLNSLKAYGL SRDFISDVFY QGDGDYLVHA WIIKPSTFVE GQKYPLAFYI
     HGGPQGATED LWSTRWNMAV FAEQGYVVVA FNPTGSTGFG QNITDGIQNQ WGGRPYNDLV
     KGWEYIEENL SYVDTDRAIA LGASYGGYMV NWIQGQPLGR KFKALFTHDG CFSTLAQYSS
     EELWFMQHDF NGTLWENFDN YARWNPANHT DAWSTPHLIN HNELDYRLPI AEGLAAFNVL
     QAKGIESKFL SFPDENHWVL NQENSLVWHK TVIDWLNEHV GLPVYSSPDD TDYRAVLQNG
     PWI
//