ID   A0A0L6WMY7_9AGAR        Unreviewed;       729 AA.
AC   A0A0L6WMY7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN   ORFNames=J132_08789 {ECO:0000313|EMBL:KNZ76718.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ76718.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family.
CC       {ECO:0000256|ARBA:ARBA00010040}.
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DR   EMBL; KQ412569; KNZ76718.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6WMY7; -.
DR   STRING; 1306850.A0A0L6WMY7; -.
DR   OrthoDB; 5471261at2759; -.
DR   Proteomes; UP000053712; 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; SSF69304; Tricorn protease N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053712}.
FT   DOMAIN          514..728
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   729 AA;  82007 MW;  F93B039733979ECF CRC64;
     MSPNQKFGFK EGPGIFSPKN LVELRRPGAG VANQAGDLVL VSVSEYSFDD QKNKKSLIVA
     PIESSAKPLE IQLEKGGEAF WIQSRTIAHV VEGEVGLEIY ALDVALRTSS GGDTDVLATT
     NNPVLIAKLP NKSATNFRYS IESGVLVFSD YVYSDGNLTS VAEQDDAYES RGNSAYVYDT
     TFERHWDTWV GPKKSSLFSV SLYQDADRKW VFDGQFINLL QGTKHSSPVE PFGGTDDFDI
     SRDQVVYTTL DPGLKNEYAW HTKQNVYITD IRGKSEPREL TSSMQGATHS PVLNVQGTQV
     AWLELDEDGY ESDRAKIVIY DLEKNVRFTL TQDWDRSPDR LAFSKEGNFI YFTAGDEAKV
     KVFVLPVPPT PPETTTHPTL PNKYITPVAL TDSKAASGIQ PLFHGRLLFS QSSFTSPNDV
     FVIRNLRRLE TSILQNEEPV HFDGQIQQIT YLTESALHGM NLDSGESFWF KGALDKNVQG
     WILKPHGWKD GKTKKWPVVL LIHGGPQGAW EDQWSTRWNP NVFAQQGYFV ILINPTGSTT
     FGQEFTDAIA GDWGGNPFVD LQKGWNHVLN AYPEIDAERA VAAGASWGGY AINWIQGHPE
     YGFNFKALVC HDGVFDSNYN GYSTDELFFF NHEWGGRPWD ETSKALSQKF SPSNFVNNWS
     TPQLLIHGSK DYRLPETESI GAFHALQQRG IRSRLVVFPD ENHWVLKHGN SLKWHYEVFR
     WFDEFVGKD
//