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DPP4_ASPFU
ID   DPP4_ASPFU              Reviewed;         765 AA.
AC   Q4WPH9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=AFUA_4G09320;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; AAHF01000005; EAL89855.1; -; Genomic_DNA.
DR   RefSeq; XP_751893.1; XM_746800.1.
DR   AlphaFoldDB; Q4WPH9; -.
DR   SMR; Q4WPH9; -.
DR   STRING; 746128.CADAFUBP00006467; -.
DR   ESTHER; aspfu-DPP4; DPP4N_Peptidase_S9.
DR   MEROPS; S09.008; -.
DR   EnsemblFungi; EAL89855; EAL89855; AFUA_4G09320.
DR   GeneID; 3509739; -.
DR   KEGG; afm:AFUA_4G09320; -.
DR   VEuPathDB; FungiDB:Afu4g09320; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_2_1; -.
DR   InParanoid; Q4WPH9; -.
DR   OMA; AYVWKND; -.
DR   OrthoDB; 269253at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
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; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; IDA:AspGD.
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; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; 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_0000397812"
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;  85864 MW;  DA7BF150DB0D686E CRC64;
     MKWSILLLVG CAAAIDVPRQ PYAPTGSGKK RLTFNETVVK RAISPSAISV EWISTSEDGD
     YVYQDQDGSL KIQSIVTNHT QTLVPADKVP EDAYSYWIHP NLSSVLWATN YTKQYRHSYF
     ADYFIQDVQS MKLRPLAPDQ SGDIQYAQWT 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
 
 
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