DAPB_ASPFC
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 03-AUG-2022, entry version 57.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=dapB; ORFNames=AFUB_041260;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
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=CEA10 / CBS 144.89 / FGSC A1163;
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 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; 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; -; 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; 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
