ID   DPP4_TRIVH              Reviewed;         753 AA.
AC   D4CZ59;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Probable dipeptidyl peptidase 4;
DE            EC=3.4.14.5;
DE   AltName: Full=Dipeptidyl peptidase IV;
DE            Short=DPP IV;
DE            Short=DppIV;
DE   Flags: Precursor;
GN   Name=DPP4; ORFNames=TRV_00096;
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 provided that the penultimate residue is proline. Contributes
CC       to pathogenicity (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC         polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC         Pro nor hydroxyproline.; EC=3.4.14.5; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10084};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; ACYE01000004; EFE45114.1; -; Genomic_DNA.
DR   RefSeq; XP_003025725.1; XM_003025679.1.
DR   AlphaFoldDB; D4CZ59; -.
DR   SMR; D4CZ59; -.
DR   ESTHER; artbc-dpp4; DPP4N_Peptidase_S9.
DR   EnsemblFungi; EFE45114; EFE45114; TRV_00096.
DR   GeneID; 9581968; -.
DR   KEGG; tve:TRV_00096; -.
DR   HOGENOM; CLU_006105_0_2_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:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Virulence.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..753
FT                   /note="Probable dipeptidyl peptidase 4"
FT                   /id="PRO_0000397815"
FT   ACT_SITE        616
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        668
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        703
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   753 AA;  85635 MW;  02B1752AB9C6F26E CRC64;
     MKTSQFLSLL LLAGIAQAIV PPREPRPPTG GGNKLLTYKE CVPRATISPR STSLAWINSD
     EDGQYISQSD DGALILQNIV TNTNKTLVAA DKVPKGYYDY WFKPDLSAVL WATNYTKQYR
     HSYFANYFIL DIEKGSLTPL AQDQAGDIQY AQWSPMDNSI AYVRGNDLYI WNNGKTKRIT
     ENGGPDIFNG VPDWVYEEEI FGDRFALWFS PDGEYLAYLR FNETGVPTYT IPYYKNKQKI
     APAYPRELEI RYPKVSAKNP TVQFHLLNIA SSQETTIPVT AFPENDLVIG EVAWLSSGHD
     SVAYRAFNRV QDREKIVSVK VESKESKVIR ERDGTDGWID NLLSMSYIGD VNGKEYYVDI
     SDASGWAHIY LYPVDGGKEI ALTTGEWEVV AILKVDTMKK LIYFTSTKYH STTRHVYSVS
     YDTKVMTPLV NDKEAAYYTA SFSAKGGYYI LSYQGPNVPY QELYSTKDSK KPLKTITSND
     ALLEKLKEYK LPKVSFFEIK LPSGETLNVK QRLPPNFNPH KKYPVLFTPY GGPGAQEVSQ
     AWNSLDFKSY ITSDPELEYV TWTVDNRGTG YKGRKFRSAV AKRLGFLEPQ DQVFAAKELL
     KNRWADKDHI GIWGWSYGGF LTAKTLETDS GVFTFGISTA PVSDFRLYDS MYTERYMKTV
     ELNADGCDDN VHFQNAAVLS NTLMNGGVTA DKLTTQWFTD SDHGIRYDMD STYQYKQLAK
     MVYDQKQRRP ERPPMHQWSK RVLAALFGER AEE