(data stored in ACNUC7421 zone)

SWISSPROT: Q4WNL2_ASPFU

ID   Q4WNL2_ASPFU            Unreviewed;       780 AA.
AC   Q4WNL2;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 79.
DE   RecName: Full=Dipeptidyl peptidase 3 {ECO:0000256|PIRNR:PIRNR007828};
DE            EC=3.4.14.4 {ECO:0000256|PIRNR:PIRNR007828};
DE   AltName: Full=Dipeptidyl aminopeptidase III {ECO:0000256|PIRNR:PIRNR007828};
DE   AltName: Full=Dipeptidyl peptidase III {ECO:0000256|PIRNR:PIRNR007828};
GN   ORFNames=AFUA_4G06140 {ECO:0000313|EMBL:EAL90172.1};
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.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90172.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL90172.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
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., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide from a peptide comprising
CC         four or more residues, with broad specificity. Also acts on
CC         dipeptidyl 2-naphthylamides.; EC=3.4.14.4;
CC         Evidence={ECO:0000256|PIRNR:PIRNR007828};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR007828,
CC         ECO:0000256|PIRSR:PIRSR007828-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR007828,
CC       ECO:0000256|PIRSR:PIRSR007828-2};
CC   -!- SIMILARITY: Belongs to the peptidase M49 family.
CC       {ECO:0000256|PIRNR:PIRNR007828}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL90172.1}.
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DR   EMBL; AAHF01000005; EAL90172.1; -; Genomic_DNA.
DR   RefSeq; XP_752210.1; XM_747117.1.
DR   STRING; 746128.CADAFUBP00006151; -.
DR   MEROPS; M49.004; -.
DR   EnsemblFungi; EAL90172; EAL90172; AFUA_4G06140.
DR   GeneID; 3509646; -.
DR   KEGG; afm:AFUA_4G06140; -.
DR   EuPathDB; FungiDB:Afu4g06140; -.
DR   HOGENOM; HOG000187784; -.
DR   InParanoid; Q4WNL2; -.
DR   KO; K01277; -.
DR   OMA; KSQKWGQ; -.
DR   OrthoDB; 1448344at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   InterPro; IPR005317; Dipeptidyl-peptase3.
DR   InterPro; IPR039461; Peptidase_M49.
DR   PANTHER; PTHR23422; PTHR23422; 1.
DR   Pfam; PF03571; Peptidase_M49; 1.
DR   PIRSF; PIRSF007828; Dipeptidyl-peptidase_III; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WNL2.
DR   SWISS-2DPAGE; Q4WNL2.
KW   Aminopeptidase {ECO:0000256|PIRNR:PIRNR007828};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR007828};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR007828, ECO:0000313|EMBL:EAL90172.1};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR007828,
KW   ECO:0000256|PIRSR:PIRSR007828-2};
KW   Metalloprotease {ECO:0000256|PIRNR:PIRNR007828};
KW   Protease {ECO:0000256|PIRNR:PIRNR007828};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Zinc {ECO:0000256|PIRNR:PIRNR007828, ECO:0000256|PIRSR:PIRSR007828-2}.
FT   ACT_SITE        524
FT                   /evidence="ECO:0000256|PIRSR:PIRSR007828-1"
FT   METAL           523
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR007828-2"
FT   METAL           528
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR007828-2"
FT   METAL           582
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR007828-2"
SQ   SEQUENCE   780 AA;  87275 MW;  91DB87344A1CF8C6 CRC64;
     MLPLLAALRR LPSNHRLLSI HRPSTTTITS LLPLSCLPRS SLLTQRFNFS SSTPSFASFI
     PLSTSSEAAS NTIMDDKIKQ HYLADSPPTV VRLEIKSHFD ALKDGKLRKY AHYLSRAAFE
     GTRITLRQVS PESEPIYDLI IALYNACNGD WVSLARKTKV SDEHLRFFLE YAAQFLGNCG
     NYKGFGDSKF IPRLPVAAFE ALASITPDAK AAFEKANRTG GGIYETSNQS LMHLGYTEGG
     HMTTYYPDSP SITKDEITAI GDLMEQKGLP LENTRLKKLP SGDFELLIAS GVSSPPSRDR
     DLGDVESLDL DGKLKGKKVQ LVFGDHREEM AKIAHSVKQA SLYSANENQK RMLNAYALSF
     GAGSIEAFKE AQRIWVKDQK PILETNLGFV ETYRDPHGVR GEWEGFVALV NLERTRAFGK
     LVDSAESMIP KLPWSKDFEK DKFLSPDFTS LEVLSFQSSG VPAGINLPNY DDIRQNLGFK
     NVSLGNVLSA KAPNEPVPFI PEKDLEVYRR YRDPAFEVQV GIHELLGHGT GKLLQETAPG
     KYNFDVSNPP VSPITNKPVT TWYKPGQTWS SVFGAIASSY EECRAECVAM VLSCDFEILK
     IFGFGDGQVD LNNEAGDVLF VAYLQMARAG LVALEFWDPK TQKWGQAHMQ ARYSILRTFL
     DAGDDFVRLV YTKEDLSDLE IHLDRSKILT HGRPAVERYL QQLHIYKSTA DIDAGKKLYS
     DITFVDEWWG TKVRDIVLKN KIPRKIFVQG NTILNGDEVT LKEYEPTLEG MIQSFVERNV
//

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