ID   DAPB_ASPNG              Reviewed;         901 AA.
AC   Q96VT7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=dapB;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=15812650; DOI=10.1007/s00438-005-1134-9;
RA   Jalving R., Godefrooij J., Veen W.J., van Ooyen A.J., Schaap P.J.;
RT   "Characterisation of the Aspergillus niger dapB gene, which encodes a novel
RT   fungal type IV dipeptidyl aminopeptidase.";
RL   Mol. Genet. Genomics 273:319-325(2005).
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:0000269|PubMed:15812650}.
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; AJ278532; CAC41019.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96VT7; -.
DR   SMR; Q96VT7; -.
DR   ESTHER; aspng-DAPB; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   GlyCosmos; Q96VT7; 3 sites, No reported glycans.
DR   PaxDb; 5061-CADANGAP00002590; -.
DR   VEuPathDB; FungiDB:An02g11420; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1135973; -.
DR   VEuPathDB; FungiDB:ATCC64974_53600; -.
DR   VEuPathDB; FungiDB:M747DRAFT_255184; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   BRENDA; 3.4.14.5; 518.
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; 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..901
FT                   /note="Dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412137"
FT   TOPO_DOM        1..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..901
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        739
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        816
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        849
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        334
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        625
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        793
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   901 AA;  101256 MW;  3A519512C903D784 CRC64;
     MSSPRPSTSS TSSDSGLSVD TTAYPEESKY TSTAPGAGGL SDENRYRDVE EGEAGADEPF
     LPSAKKQAAS GSRTSRLIWG LVILCVAGWL WGLVLFVTQN RSAQQSVSEA LQSHESGAIS
     GSSSSGKPVT LEQVLTGQWL PRSHAVSWIA GPNGEDGLLV EQGEDQGKGY LRVDDIRSRK
     GDATSQESRV LMEKAIVQVD GRTIFPVSTW PSPNLNKVLL LSEREKNWRH SFTGKYWIFD
     VATQTAQPLD PSNPDGRVQL AIWSPTSDMV AFVRDNNLYL RRLSSKEVVP ITKDGGADLF
     YGIPDWVYEE EVFSGNSVTW WSGDGKYVAF LRTNETAVPE FPVQYYLSRP SGKRPPPGLE
     DYPEVREIKY PKAGAPNPVV SLQFYDVEKQ EVFSIEAPDD FEDDDRIVIE IVWGTEGKIL
     VRATNRESDV LKVFLFDTKA RTSKLVRTEN VADIDGGWVE PTQYTWFIPA DPSNGRPHDG
     YLDTVIHEGY EHLGYFTPLD NSEPILLTQG EWEVVDAPTA VDLRKGIVYF ISTKESPTER
     HLYQVNLDGS NLKPLTDTSK PGYYDVSFSH GTGYALLSYR GPSIPWQAIV NTETDELKYE
     ETIEDNAGLA RMVDSYALPT EIYQNVTIDG FTLQVVERRP PHFNPAKKYP VLFYLYNGPR
     SQTVDRKFSI DFQSYVASSL GYIVVTVDGR GTGFSGRKTR CIVRGNLGYY EAYDQITTAN
     LWGEKPYVDE TRMSIWGWSY GGFMTLKTLE QDAGQTFQYG MAVAPVTDWR HYDSIYTERY
     MHTPAHNPNG YDNTSITDMT ALQQTVRFLV IHGASDDNVH IQNTLVLVDK LDLAGVQNYD
     LHFYPDSDHS INFHNAHRMV YERLSSWLVN AFNDEWHRIA DPVPDDSMWE KVKRSLPMLV
     N
//