ID   DPP5_TRIVH              Reviewed;         726 AA.
AC   D4D5P5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Probable 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; ORFNames=TRV_02418;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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; ACYE01000126; EFE42816.1; -; Genomic_DNA.
DR   RefSeq; XP_003023434.1; XM_003023388.1.
DR   AlphaFoldDB; D4D5P5; -.
DR   SMR; D4D5P5; -.
DR   ESTHER; artbe-DPP5; Prolyl_oligopeptidase_S9.
DR   EnsemblFungi; EFE42816; EFE42816; TRV_02418.
DR   GeneID; 9583454; -.
DR   KEGG; tve:TRV_02418; -.
DR   HOGENOM; CLU_008615_0_1_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
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="Probable dipeptidyl-peptidase 5"
FT                   /id="PRO_0000397822"
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;  80011 MW;  270BB1E6DBA90712 CRC64;
     MAAAKWLIAS LAFASSGLAF TPEDFISAPR RGEAIPDPKG ELAVFHVSKY NFDKKDRPSG
     WNLLNLKNGD ISVLTTDSDV SEITWLGDGT KVVYVNGTDS VKGGVGIWIS DAKNFGNAYK
     AGSVNGAFSG LKLAKSGDKI NFVGYGQSTT KGDLYNEAAA KEAVSSARIY DSLFVRHWDT
     YVGTQFNAVF SGALTKNGDK YSFDGKLKNL VQPVKYAESP YPPFGGSGDY DLSSDGKTVA
     FMSKAPELPK ANLTTSYIFL VPHDGSRVAE PINKRNGPRT PQGIEGASSS PVFSPDGKRI
     AYLQMATKNY ESDRRVIHIA EVGSNKPVQR IASNWDRSPE AVKWSSDGRT LYVTAEDHAT
     GKLFTLPADA RDNHKPEVVK HDGSVSSFYF VGSSKSVLIS GNSLWSNALF QVATPGRPNR
     KLFYANEHDP ELKGLGPNDI EPLWVDGART KIHSWIVKPT GFDKNKVYPL AFLIHGGPQG
     SWGDSWSTRW NPRVWADQGY VVVAPNPTGS TGFGQKLTDD ITNDWGGAPY KDLVKIWEHV
     HNNIKYIDTD NGIAAGASFG GFMVNWIQGQ DLGRKFKALV SHDGTFVGSS KIGTDELFFI
     EHDFNGTFFE ARQNYDRWDC SKPELVAKWS TPQLVVHNDF DFRLSVAEGV GLFNVLQEKG
     VPSRFLNFPD ETHWVTKPEN SLVWHQQVLG WVNKWSGINK SNPKSIKLSD CPIEVVDHEA
     HSYFDY