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Database: UniProt
Entry: A0A166PUK3_9PEZI
LinkDB: A0A166PUK3_9PEZI
Original site: A0A166PUK3_9PEZI 
ID   A0A166PUK3_9PEZI        Unreviewed;       699 AA.
AC   A0A166PUK3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN   ORFNames=CT0861_04866 {ECO:0000313|EMBL:KZL67180.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL67180.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL67180.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL67180.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family.
CC       {ECO:0000256|ARBA:ARBA00010040}.
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:KZL67180.1}.
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DR   EMBL; LFIV01000151; KZL67180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166PUK3; -.
DR   STRING; 708197.A0A166PUK3; -.
DR   OrthoDB; 5471261at2759; -.
DR   Proteomes; UP000076552; 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   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; SSF82171; DPP6 N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT   DOMAIN          477..692
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   699 AA;  77507 MW;  364D515CC3219D8B CRC64;
     MRVAKEFTPE VLLSAPRRGA AVPSPDGTLI LYTQSTHSFD DKKTLNEVRV MDVESGASDQ
     LTDDDKVHDA LWVPGTASHV IYLKSGDKGT TQIWVADAAS PAKEHYVAAE YDAPIRALKV
     KALADGSVAF VVAGLVGPDG SLFNDEAEEK ATTGRIFDDH HVRFWNTLYK PHKYALWYST
     LVNAHGKWGV AGELHNAIKD TRLEAPFGMY GEVDSGGSFD ISDRGIAFIA EDVGLSPEKA
     GMAHVYYVPL QSFTAAATVK PRPIVMGISE TRAYYTNVRC SPDGAKVAFL QSLSSDFSDT
     RLYIGHTTSF GAYDVHKMVF GQGPRLPPRA FEFAGDSDAI FLLTEDCGRV KLSHLELRHH
     AEATPLVQSG VVTAFYPLRE ASYDKVLVTS NSMVDSSLWQ IVDVSLNTAP RVVSSATKHG
     AKYGLSHRMV SEFWYEGEND AVVHSFIIKP TNFDETKKYP WVLLPHGGPV SSSLDSWSTR
     WNMALWAQKG YVLVAPNIAG STGYGAEFAA RVYRSWGGAP YQDLVALMDH LKQLPYLDHA
     RAIVAGASYG GYMISWMMGH DLIRRFSCAV WHDGIFNLPA FMIQTDFVDG GPNFGGPPFI
     WNNSEELERW NPARPELLRN WTHAPPTLVI HSEKDYRCPI TEGIAAYNTL QCQGVKSRFL
     TFSDECHWVL NPENSLVWHK TVFDWMAKYA GETQVARRD
//
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