ID   DPP5_ARTOC              Reviewed;         726 AA.
AC   C5FH88;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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; ORFNames=MCYG_01626;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS995702; EEQ28807.1; -; Genomic_DNA.
DR   RefSeq; XP_002848692.1; XM_002848646.1.
DR   AlphaFoldDB; C5FH88; -.
DR   SMR; C5FH88; -.
DR   STRING; 63405.XP_002848692.1; -.
DR   ESTHER; nanot-dpp5; Prolyl_oligopeptidase_S9.
DR   MEROPS; S09.012; -.
DR   EnsemblFungi; EEQ28807; EEQ28807; MCYG_01626.
DR   GeneID; 9222948; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_008615_0_1_1; -.
DR   OMA; IFNWIRY; -.
DR   OrthoDB; 265965at2759; -.
DR   Proteomes; UP000002035; 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; IPR001375; Peptidase_S9.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..726
FT                   /note="Dipeptidyl-peptidase 5"
FT                   /id="PRO_0000384091"
FT   REGION          268..292
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        485
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;  80075 MW;  9C6D98446B7413ED CRC64;
     MAPAKWLIAS LAFASTGLAF TPEDFISAPR RGEAIPDPKG QFAVFPVSKY NFDTKDRPSG
     WNLLNLKTGD ISVLTTDADV SEITWLGEGT NLLYVNGTDS VKGGVGIWIS DAKNFGNAYK
     AGSIPGAFQG FKLAKSGDKI NFVGYGQSTT KGDLYNEAAI EKPVSSARIY DSLFVRHWDA
     YVGTQFNAVF SGALTKNGNK YSFDGKLKNL VQPVKYAESP YPPFGGSGDY DLSPDGKTVA
     FMSKAPELPK ANLTTSYIFT VPHDGSKVAE PINKRNGPRT PHGIEGASSS PVFSPDSKRI
     AYLQMATKNY ESDRRVIHIA EVGSNKPAQR IASNWDRSPE SIKWSSDGRT LYVTAEEHAT
     GKLFTLPSDA RDNHMPSAVK HDGSVSAFSF VGSSKSVLIT GNSLWSNALY QIATPGRPNR
     KLFYANEHDP QLKGLGPNDI EPLWVDGART KIHSWIVKPT GFDKNKVYPL AFLIHGGPQG
     SWGDNWSTRW NPRVWADQGY VVIAPNPTGS TGFGQKLTDD ITNDWGGAPY KDLFKIWEHV
     RDNLKYVDTD NGIAAGASFG GFMINWIQGQ ELGRKFKALV SHDGTFVGSS KIGTDELFFI
     EHDFNGTFFE ARQNYDRWDC SKPEYVAKWS TPQLVVHSDY DFRLSVAEGV GLFNVLQEKG
     VPSRLLNFPD ESHWVTKPEN SLVWHQQVLG WINKFSGINK SNPKAIKLSD CKVEVIDHEA
     GSYFDY