ID   DPP4_NEOFI              Reviewed;         765 AA.
AC   A1CX29;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=NFIA_106690;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
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.
CC       {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;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; DS027685; EAW25181.1; -; Genomic_DNA.
DR   RefSeq; XP_001267078.1; XM_001267077.1.
DR   AlphaFoldDB; A1CX29; -.
DR   SMR; A1CX29; -.
DR   STRING; 331117.A1CX29; -.
DR   ESTHER; aspfu-DPP4; DPP4N_Peptidase_S9.
DR   MEROPS; S09.008; -.
DR   GlyCosmos; A1CX29; 9 sites, No reported glycans.
DR   EnsemblFungi; EAW25181; EAW25181; NFIA_106690.
DR   GeneID; 4593808; -.
DR   KEGG; nfi:NFIA_106690; -.
DR   VEuPathDB; FungiDB:NFIA_106690; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_2_1; -.
DR   OMA; SLMFAKF; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000006702; 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   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..765
FT                   /note="Probable dipeptidyl peptidase 4"
FT                   /id="PRO_0000397814"
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"
SQ   SEQUENCE   765 AA;  85823 MW;  490FAB631D986EA1 CRC64;
     MKWSILLLVG CAAAIDVPRQ PYAPTGSGKK RLTFNETVVK RAISPSAISV EWISTSEDGD
     YVYQDQDGSL KIQSIVTNNT QTLVPADKVP EDAYSYWIHP NLSSVLWATN YTKQYRHSYF
     ADYFIQDVQS MNLRPLAPDQ SGDIQYAQWS PTGDAIAFVR GNDVFVWTNA STSQITNDGG
     PDLFNGVPDW IYEEEILGDR FALWFSPDGA YLAFLRFNET GVPTFTVPYY MDNEEIAPPY
     PRELELRYPK VSQTNPTVEL NLLELRTGER TPVPIDAFDA KELIIGEVAW LTEKHDVVAV
     KAFNRVQDRQ KVVAVDVASL RTKTINERDG TDGWLDNLLS MAYIGPIGES KEEYYIDISD
     QSGWAHLWLF PVAGGEPIAL TKGEWEVTAI LSIDKPRQLV YFLSTKHHST ERHLYSVSWK
     TMEITPLVDD TVPAVWSASF SSQGGYYILS YRGPDVPYQD LYAINSTAPL RTITSNAAVL
     DGLKEYTLPN ITYFELALPS GETLNVMQRL PVKFSSKKKY PVLFTPYGGP GAQEVSKAWQ
     ALDFKAYIAS DPELEYITWT VDNRGTGYKG RAFRCQVTSR LGELEAADQV FAAQQAAKLP
     YVDADHIAIW GWSYGGYLTG KVIETDSGAF SLGVQTAPVS DWRFYDSMYT ERYMKTLESN
     AAGYNASAIR KVAGYKNVRG GVLIQHGTGD DNVHFQNAAA LVDTLVGAGV TPEKLQVQWF
     TDSDHGIRYH GGNVFLYRQL SKRLYEEKKR KEKGEAHQWS KKSVL
//