ID   DAPB_ASPFC              Reviewed;         919 AA.
AC   B0XYK8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=dapB; ORFNames=AFUB_041260;
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 [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: Type IV 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: Vacuole membrane {ECO:0000250}; Single-pass type
CC       II membrane protein {ECO:0000250}. Note=Lysosome-like vacuoles.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; DS499596; EDP52954.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XYK8; -.
DR   SMR; B0XYK8; -.
DR   ESTHER; aspfu-q4wx13; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   GlyCosmos; B0XYK8; 4 sites, No reported glycans.
DR   EnsemblFungi; EDP52954; EDP52954; AFUB_041260.
DR   VEuPathDB; FungiDB:AFUB_041260; -.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   PhylomeDB; B0XYK8; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
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:SF200; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 2; 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; Membrane; Protease;
KW   Serine protease; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Vacuole.
FT   CHAIN           1..919
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412133"
FT   TOPO_DOM        1..92
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..919
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        757
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        834
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        867
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        643
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        811
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   919 AA;  103089 MW;  FF38600F2230B801 CRC64;
     MRRSDGHEET SEFLPMTHSR SVSAASQTST DSSLSTESLF PREQKPFPNA MGGMALADDD
     KYRDLEDGEA ELSEPFLSSS KKAATGGGRA RRIFWILVLL CLGGWLLAFV LFLTGGRANY
     QTASDALQAH GADSALGSTS TSSGKPVTLQ QVLGGQWNPR YHAIGWVAGP NNEDGLLVEK
     GGDEKQGYLR VDDIRSRKGN NTGRESRVLM RKPIVHVDGQ AIVPSNVWPS PDLKKVLLIS
     EQQKNWRHSF TGKYWVFDVD SQTAQPLDPS APDGRVQLAL WSPASDAVVF VRDNNLYLRR
     LSSDSVVAIT KDGGENLFYG VPDWVYEEEV ISGNSVTWWS NDAKYIAFFR TNETSVPEFP
     VQYYISRPSG KKPLPGLENY PDVREIKYPK PGAPNPVVDL QFYDVEKNEV FSVQVADDFA
     DDDRIIIEVL WASEGKILVR STNRESDILK VYLIDTQSRT GKLVRSEDVA GLDGGWVEPS
     QSTRFVPADP NNGRPHDGYI DTVPYNGYDH LAYFSPLDNP NALMLTSGEW EVVDAPAAVD
     LQRGLVYFVG TKEAPTQRHV YRVQLDGSNL NPLTDTSKPG YYDVSFSHGT GYALLTYKGP
     SIPWQAIINT HGDEITYEDR IEDNAQLTKM VEAYALPTEV YQNVTVDGYT LQVVERRPPH
     FNPAKKYPVL FYLYGGPGSQ TVDRKFTVDF QSYVASSLGY IVVTVDGRGT GFIGRKARCI
     VRGNLGFYEA HDQIATAKMW AAKSYVDETR MAIWGWSFGG FMTLKTLEQD AGRTFQYGMA
     VAPVTDWRFY DSIYTERYMH TPQHNPNGYD NSTITDMAAL SESVRFLVMH GASDDNVHLQ
     NTLVLIDKLD LSNVENYDVQ FYPDSDHSIY FHNAHMMVYH RLSDWLVNAF NGEWHLIAKP
     VPDESMWERM KRSLRLLSP
//