ID   DPP5_TRIEQ              Reviewed;         726 AA.
AC   A7UKV4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Dipeptidyl-peptidase 5;
DE            EC=3.4.14.-;
DE   AltName: Full=Dipeptidyl-peptidase V;
DE            Short=DPP V;
DE            Short=DppV;
DE   Flags: Precursor;
GN   Name=DPP5;
OS   Trichophyton equinum (Horse ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=63418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Brown J.T., Preuett B.L., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT   and Trichophyton equinum.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal
CC       dipeptides sequentially from polypeptides having unsubstituted N-
CC       termini. Contributes to pathogenicity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR   EMBL; EU076569; ABU50379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7UKV4; -.
DR   SMR; A7UKV4; -.
DR   ESTHER; artbe-DPP5; Prolyl_oligopeptidase_S9.
DR   MEROPS; S09.012; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR011659; PD40.
DR   InterPro; IPR001375; Peptidase_S9.
DR   Pfam; PF07676; PD40; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..726
FT                   /note="Dipeptidyl-peptidase 5"
FT                   /id="PRO_0000384092"
FT   REGION          269..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        558
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        641
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        673
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        605
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        699
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   726 AA;  80073 MW;  42DE1FB42F4D740E CRC64;
     MAAAKWLIAS LAFASSGLAF TPEDFISAPR RGEAIPDPKG ELAVFHVSKY NFDKKDRPSG
     WNLLNLKNGD ISVLTTDSDI SEITWLGDGT KIVYVNGTDS VKGGVGIWIS DAKNFGNAYK
     AGSVNGAFSG LKLAKSGDKI NFVGYGQSTT KGDLYNEAAA KEAVSSARIY DSLFVRHWDT
     YVGTQFNAVF SGALTKSGDK YSFDGKLKNL VHPVKYAESP YPPFGGSGDY DLSSDGKTVA
     FMSKAPELPK ANLTTTYIFV VPHDGSRVAE PINKRNGPRT PQAIEGASSS PVFSPDGKRI
     AYLQMATKNY ESDRRVIHIA EVGSNKPVQR IASNWDRSPE VVKWSSDGRT LYVTAEDHAT
     GKLFTLPADA RDSHKPAVVK HDGSVSSFYF VGSSKSVLIS GNSLWSNALF QVATPGRPNR
     KLFYANEHDP ELKGLGPNDI EPLWVDGART KIHSWIVKPT GFDKNKVYPL AFLIHGGPQG
     SWGDSWSTRW NPRVWADQGY VVVAPNPTGS TGFGQKLTDD ITNDWGGAPY KDLVKIWEHV
     RDHIKYIDTD NGIAAGASFG GFMVNWIQGH DLGRKFKALV SHDGTFVGSS KIGTDELFFI
     EHDFNGTFFE ARQNYDRWDC SKPELVAKWS TPQLVIHNDF DFRLSVAEGV GLFNVLQEKG
     IPSRFLNFPD ETHWVTKPEN SLVWHQQVLG WINKWSGINK SNPKSIKLSD CPIEVVDHEA
     HSYFDY