DAPB_TALSN
ID DAPB_TALSN Reviewed; 900 AA.
AC B8MTH6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=dapB; ORFNames=TSTA_003660;
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
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; EQ962660; EED12308.1; -; Genomic_DNA.
DR RefSeq; XP_002487962.1; XM_002487917.1.
DR AlphaFoldDB; B8MTH6; -.
DR SMR; B8MTH6; -.
DR STRING; 441959.B8MTH6; -.
DR ESTHER; penmq-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR PRIDE; B8MTH6; -.
DR EnsemblFungi; EED12308; EED12308; TSTA_003660.
DR GeneID; 8098062; -.
DR VEuPathDB; FungiDB:TSTA_003660; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; B8MTH6; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; B8MTH6; -.
DR Proteomes; UP000001745; 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..900
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412164"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..900
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 753
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 830
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 863
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 812
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 900 AA; 101025 MW; 178445E1C9D9EAD4 CRC64;
MARTDQGLGA ESEPLTNQSH RHSNSFSSTD SLSTDGSLFG DDMNATQFQK STQLPEETPY
RDIEEGVEGE PESDILSHPR DKSKRSRGSR WIWVIGLLCL GGWILAFILF WGRRNNNSDI
SSSVAAVHDA ESATGATSYG KPLTLDSVLN GSWGRRKHSI SWVAGPDGED GLLLERGEDG
KKGYLRVESI LSRQNETDAD DGLILMESGT IEANGKYLQP SETWPSPNFK SVLVAVDAVS
NWRYSFTATY WLFDVKTQTA QPLDPDAPKG RIQLASWSPN SDAVVFTRDN NLYLRRLDST
TVTQITKDGG KDVFNGIPDW VYEEEVYGSD TATWWSNDGK YVAFLRTNES MVPEFPIEYY
MSRLSGKHPS PGLEKYPDVR KIKYPKAGAP NPVVTLQFYD VESTDVFSVN VSGGFADDDR
LITEVVWASE TKVLVKEFNR ESDVVRTVLI DVGSRSGDVI RVDNFAQDDG GWAEVTQSTT
FIPADPANGR PDDGYLDIVV HDGYDHWGYF TPVNNSQPIL LTSGPWEVVD TQPAVDLRNG
IVYLVATKES PTQRHVYSVK LDGSDFQAMT DTSKAGYYDV SFSIGGGYAL LSYEGPHIPW
QKLVNTPSNQ QHFEEVIEQN EHLFSMIEKY ALPAEIYQNI TIDNITLQVV ERRPPHFNPI
KKYPVLFWLY GGPGSQSVDR KFMVDFQSYV SSTLGYIVVT VDGRGTGHIG RIARTIVRGN
LGFWEARDQI ETAKAWAKKP YVDKDHIAIW GWSYGGFMTL KTLEQDAGQT FQYGMAVSPV
TDWRFYDSIY TERYMHTPEH NPTGYEHSAI SNMTALQQNV RFLIMHGTAD DNVHFQNTLS
LIDKLDMGGV ENYDVHVYPD SDHSIYFHNA HKMVYDRLSS WLVNAFTDEW HHVGSALAAT
