ID   W6ZLI4_COCMI            Unreviewed;       718 AA.
AC   W6ZLI4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN   ORFNames=COCMIDRAFT_81051 {ECO:0000313|EMBL:EUC50818.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC50818.1};
RN   [1] {ECO:0000313|EMBL:EUC50818.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC50818.1};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S9C family.
CC       {ECO:0000256|ARBA:ARBA00010040}.
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DR   EMBL; KI963921; EUC50818.1; -; Genomic_DNA.
DR   RefSeq; XP_007682774.1; XM_007684584.1.
DR   AlphaFoldDB; W6ZLI4; -.
DR   GeneID; 19125792; -.
DR   KEGG; bor:COCMIDRAFT_81051; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_008615_0_1_1; -.
DR   OrthoDB; 5471261at2759; -.
DR   Proteomes; UP000054032; 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:SF11; DIPEPTIDYL-PEPTIDASE 5-RELATED; 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; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..718
FT                   /note="Dipeptidyl-peptidase V"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004886969"
FT   DOMAIN          496..705
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   718 AA;  79471 MW;  6B90D64D3181992E CRC64;
     MAIKTAFLAA SLVLQSARAI DVEGLLAAPR RSNGILSPKG DRALFSETKF NWTTEKASTA
     WYFLDTETGD VKKAPFGSAA SEVVWVGDTD DSILYINSTN EQIPGGVTLY TADLSKDSFE
     PTLVASLHAP LSGLKAVKTD SGINFVGNCL AYEHNGSAYN PELVTAPKTS GQLYDANFVR
     HWNYYITAER VSVFSGVLSN LNGTYSYDGK LTNLLLGINY TITRPESPVQ ASSSDAGDYD
     LSPNGKLVAF RTKSPDLPKA NYTASYIYVV PFDGSEIAVP VNGPGTTAPE TAQGASGAPV
     WSHDSSKLAY TQQDGIDYES DKYKLYVAEI DGTNSKVRSV AEDWDSSPTG LKWSHDDADL
     WVTSELHASV RLWLVPQDAP ADFKPTNFTG PDTSIAGFGI LPDGSALVSA SASWTSRIWY
     KQHPGQDKEV LFTANEVDPE LEGLKPDSVS NFWITNEDGD DIQTFVFYPT DFDPSKKYPL
     AFIIHGGPQS TQGDTWSTRW NLRTWADQGF IVTTTQFTGS PSYSQAFTDK IQANWGGSPY
     RDLVQVFEHL RDNVDYVDTD RAIAAGASFG CYMINWIQGH ALGREFKALV CHDGKINQVA
     SYGTDELWFI QRDNNGTVWE NRENYEKWEP LAHFANASTP EFVIHNDLDY RVLQGEGLQT
     FNILQSLGVP SRFLHFPDEG HWVTNRHNSL LWHKSIFNWI RYWTGLDEEL STDGVITQ
//