DAPB_NEOFI
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 03-AUG-2022, entry version 80.
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 / NRRL 181
RC / 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; 36630.CADNFIAP00005675; -.
DR ESTHER; aspfu-q4wx13; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
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; 269253at2759; -.
DR Proteomes; UP000006702; 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 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
