ID   DAPB_NEOFI              Reviewed;         919 AA.
AC   A1D7R6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=dapB; ORFNames=NFIA_069310;
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: 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; DS027690; EAW21760.1; -; Genomic_DNA.
DR   RefSeq; XP_001263657.1; XM_001263656.1.
DR   AlphaFoldDB; A1D7R6; -.
DR   SMR; A1D7R6; -.
DR   STRING; 331117.A1D7R6; -.
DR   ESTHER; aspfu-q4wx13; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   GlyCosmos; A1D7R6; 4 sites, No reported glycans.
DR   EnsemblFungi; EAW21760; EAW21760; NFIA_069310.
DR   GeneID; 4590303; -.
DR   KEGG; nfi:NFIA_069310; -.
DR   VEuPathDB; FungiDB:NFIA_069310; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000006702; 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   Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Vacuole.
FT   CHAIN           1..919
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412151"
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..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..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;  102984 MW;  B37965B691918558 CRC64;
     MRPSDDHGET SEFLPITRSR SVSAASQTST DSSLSTESLF PGEQKPFPNV NGTMALADDD
     QYRDLEDGEV EQTEPFLASS KKAATGGGRA RRIFWILVLL CLGGWLLAFA LFLTGGRANY
     QTASDALQAH GADSALGSTS TSSGKPVTLQ QVLAGQWNPR YHAIGWVAGP NNEDGLLVEK
     GGDEKQGYLR VDDIRSRKGN DTGRESRVLM WKPIVHVDGK AIVPSNVWPS PDLKKVLLIS
     EQQKNWRHSF TGKYWVLDVD SQTAQPLDPS APDGRVQLAL WSPASDAVVF VRDNNLYLRR
     LSSDSVVVIT KDGGENLFYG VPDWVYEEEV ISGNSVTWWS NDAKYIAFFR TNETSVPEFP
     VQYYISRPSG KKPLPGLENY PDVREIKYPK PGAPNPVVDL QFYDVDKNEV FSVEVADDFA
     DDDRIIIEVL WASEGKVLVR STNRESDILK VYLIDTKSRT GKLVRSEDVA GLDGGWVEPS
     QSTRFIPADP NNGRPHDGYI DTVPYNGYDH LAYFSPLDSP NALMLTSGEW EVVDAPAAVD
     LQRGLVYFVG TREAPTQRHV YRVQLDGSNL KPLTDTSKPG YYDVSFSHGT GYALLTYKGP
     SIPWQAIIKT QGDEITYEDR IEDNAQLTKM VEAYALPTEI YQNVTVDGYT LQLVERRPPH
     FNPAKKYPVL FYLYGGPGSQ TVDRKFTVDF QSYVASSLGY IVVTVDGRGT GFIGRKARCI
     VRGNLGFYEA HDQIATAKMW AAKSYVDETR MAIWGWSFGG FMTLKTLEQD AGQTFQYGMA
     VAPVTDWRFY DSIYTERYMH TPQHNPSGYD NSTITDMAAL SESVRFLVMH GASDDNVHLQ
     NTLVLIDKLD LSNVENYDLQ FYPDSDHSIY FHNAHTMVYD RLSDWLVNAF NGEWHLIAKP
     VPDESMWERM KRSLPLLYP
//