DAPB_TALMQ
ID DAPB_TALMQ Reviewed; 899 AA.
AC B6QVW4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=dapB; ORFNames=PMAA_013400;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995906; EEA19077.1; -; Genomic_DNA.
DR RefSeq; XP_002153462.1; XM_002153426.1.
DR AlphaFoldDB; B6QVW4; -.
DR SMR; B6QVW4; -.
DR STRING; 441960.B6QVW4; -.
DR ESTHER; penmq-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; EEA19077; EEA19077; PMAA_013400.
DR GeneID; 7030827; -.
DR KEGG; tmf:PMAA_013400; -.
DR VEuPathDB; FungiDB:PMAA_013400; -.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; B6QVW4; -.
DR Proteomes; UP000001294; 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..899
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412157"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..899
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 752
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 829
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 862
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
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 899 AA; 100866 MW; D2920B066695CD62 CRC64;
MARKDKDNGP EFVPLTNRSH RSSASFSSTD SLSSDGSLFG DDDVNALHSQ KITRTQLPEE
NPYRDDDVEL ERGDNIFSRP TENSKRNRGS RLIWVVGLLC LGGWILAFVL FWGRRNSELS
SSIAAVHGAD SATGSTSYGK PLTLDGVLNG SWGRRRHSIS WVAGPNGQDG LLLERDEDEK
KAYLRVESIH SRQNQTDARE GWVLMESGAF AVNGKSLQPS ATWPSPDFKS VLVAANAVSN
WRHSFTATYW LFDVDTQTAQ PLDPDEPKGR IQLASWSPQS DAVVFTRDNN LYLRKLDSDK
VSQLTKDGGK DVFNGVPDWV YEEEVFGTDS TTWWSKDGKY VAFLRTNESM VPEFPIEYYM
SRPSGKKPPA GLDKYPDVRK IKYPKAGSPN PVVTLQFYDI ENAEVFSVNV SGGFADDDRL
ITEVVWASSG KVLVKEFNRE SDVIRTVLID VPSRTGELVR VDNFAQDDGG WAEVTQSTTF
IPADPANGRP DDGYIDIIVH DGYDHWGYFT PVNNSVPVLL TSGPWEVVDT EPAVDLANNI
VYFVASKESP TQRHVYSVKL DGSDLQPLTD VTKAGYYDAS FSIGGGYVLL SYDGPRVPWQ
KVINTPSNQN PFEEIIEQNE QLSKMIEKYA LPAEIYQNIT IDNVTLQVVE RRPPHFNPVK
KYPVLFWLYG GPGSQSVDRR FSVDFQSYVA STLGYIVVTV DGRGTGHIGR AARTIVRGNL
GYWEARDQIE TAKAWAKKPY VDKDHIAIWG WSYGGFMTLK TLEQDAGQTF QYGMAVSPVT
DWRFYDSIYT ERYMHTPEHN PTGYEHSAIS NMTALQQNVR FLVMHGTADD NVHFQNTLSL
IDKLDMAGVE NYDVHVYPDS DHSIYFHNAH KMVYDRLSSW LVTAFTDGWQ QGNSVLPVT
