ID   DPP4_ASPFC              Reviewed;         765 AA.
AC   B0Y6C5; O14425;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-MAY-2023, entry version 65.
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=AFUB_066450;
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9234752; DOI=10.1128/iai.65.8.3042-3047.1997;
RA   Beauvais A., Monod M., Wyniger J., Debeaupuis J.P., Grouzmann E.,
RA   Brakch N., Svab J., Hovanessian A.G., Latge J.P.;
RT   "Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus
RT   pathogenic to humans.";
RL   Infect. Immun. 65:3042-3047(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 144.89 / FGSC A1163 / CEA10;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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. {ECO:0000269|PubMed:9234752}.
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;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.38 mM for Gly-Pro pNA and Ala-Pro pNA
CC         {ECO:0000269|PubMed:9234752};
CC         KM=0.15 mM for Arg-Pro pNA {ECO:0000269|PubMed:9234752};
CC       pH dependence:
CC         Optimum pH is 6.7 to 7.0. {ECO:0000269|PubMed:9234752};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9234752}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; U87950; AAC34310.1; -; Genomic_DNA.
DR   EMBL; DS499598; EDP50310.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y6C5; -.
DR   SMR; B0Y6C5; -.
DR   ESTHER; aspfu-DPP4; DPP4N_Peptidase_S9.
DR   MEROPS; S09.008; -.
DR   GlyCosmos; B0Y6C5; 9 sites, No reported glycans.
DR   EnsemblFungi; EDP50310; EDP50310; AFUB_066450.
DR   VEuPathDB; FungiDB:AFUB_066450; -.
DR   HOGENOM; CLU_006105_0_2_1; -.
DR   PhylomeDB; B0Y6C5; -.
DR   Proteomes; UP000001699; 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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF162; DIPEPTIDYL PEPTIDASE 4-RELATED; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Virulence.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..765
FT                   /note="Probable dipeptidyl peptidase 4"
FT                   /id="PRO_0000397810"
FT   ACT_SITE        613
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        690
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        725
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        490
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        665
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        117
FT                   /note="Y -> H (in Ref. 1; AAC34310)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="D -> G (in Ref. 1; AAC34310)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        538
FT                   /note="A -> P (in Ref. 1; AAC34310)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   765 AA;  85876 MW;  544F27B6134F9B1B CRC64;
     MKWSILLLVG CAAAIDVPRQ PYAPTGSGKK RLTFNETVVK RAISPSAISV EWISTSEDGD
     YVYQDQDGSL KIQSIVTNHT QTLVPADKVP EDAYSYWIHP NLSSVLWATN YTKQYRYSYF
     ADYFIQDVQS MKLRPLAPDQ SGDIQYAQWS PTGDAIAFVR DNNVFVWTNA STSQITNDGG
     PDLFNGVPDW IYEEEILGDR FALWFSPDGA YLAFLRFNET GVPTFTVPYY MDNEEIAPPY
     PRELELRYPK VSQTNPTVEL NLLELRTGER TPVPIDAFDA KELIIGEVAW LTGKHDVVAV
     KAFNRVQDRQ KVVAVDVASL RSKTISERDG TDGWLDNLLS MAYIGPIGES KEEYYIDISD
     QSGWAHLWLF PVAGGEPIAL TKGEWEVTNI LSIDKPRQLV YFLSTKHHST ERHLYSVSWK
     TKEITPLVDD TVPAVWSASF SSQGGYYILS YRGPDVPYQD LYAINSTAPL RTITSNAAVL
     NALKEYTLPN ITYFELALPS GETLNVMQRL PVKFSPKKKY PVLFTPYGGP GAQEVSKAWQ
     ALDFKAYIAS DPELEYITWT VDNRGTGYKG RAFRCQVASR LGELEAADQV FAAQQAAKLP
     YVDAQHIAIW GWSYGGYLTG KVIETDSGAF SLGVQTAPVS DWRFYDSMYT ERYMKTLESN
     AAGYNASAIR KVAGYKNVRG GVLIQHGTGD DNVHFQNAAA LVDTLVGAGV TPEKLQVQWF
     TDSDHGIRYH GGNVFLYRQL SKRLYEEKKR KEKGEAHQWS KKSVL
//