DAPB_PARBD
ID DAPB_PARBD Reviewed; 912 AA.
AC C1FZL3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=DAPB; ORFNames=PADG_00053;
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10084};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN275957; EEH43764.1; -; Genomic_DNA.
DR RefSeq; XP_010756181.1; XM_010757879.1.
DR AlphaFoldDB; C1FZL3; -.
DR SMR; C1FZL3; -.
DR STRING; 121759.XP_010756181.1; -.
DR ESTHER; parba-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; EEH43764; EEH43764; PADG_00053.
DR GeneID; 22579951; -.
DR KEGG; pbn:PADG_00053; -.
DR VEuPathDB; FungiDB:PADG_00053; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; MRTPQEN; -.
DR Proteomes; UP000001628; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
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.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 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..912
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412154"
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..912
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 751
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 828
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 861
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 912 AA; 102308 MW; 7BF8C0744459EAA0 CRC64;
MAAEKGGSSD EERKPLTRGS MEYRDSSNSL HYSSSAASLS LAVIDRINGS THDTGPDEIG
RGDRDYSDDG EYDLEEADYI PSGGKPVQKK VKIVLGFLLF LCLSGWSLAF VLFLFGGHES
SKTSIVYEDN ISDTGSQGIK ITLDEVFDGT WSPNSRDISW IPGPNGEDGL LLEKGASISN
GYLRVEDIVS RKDPKSSKKP IVLMQKAYFN VSGEAVFPSR VWPSPDLKTV LVLSNEEKNW
RHSFTGKYWL FDVESQTGQP LDPAAKDQRV QLASWSPRSD AVVFTRDNNM FLRKLSSNEV
IKITTNGGVN LFYGVPDWVY EEEVFSGNSV TWWADDGEYI AFLRTNESSV PEYPVQYFVS
RPNGEIPKPG GESYPETRKI KYPKAGAPNP IVDLQFFDVG KDEVFSVDIK GDFADSNRLI
IEVVWASNGK VIVRSTNRES DVLHVAVIDV LSRTGKIVRK EDINALDGGW VEPSQTTRFI
PADPDNGRLN DGYIDTVIYE GRDQLAYYTP IDNPKPIVLT NGHSEVVQAP SGVDLKRGLV
YFVVAGNEPW ERHIYSVNFD GTSLQPVTNV SESSYYDVSF SNGAGYAFLK YAGPQVPWQK
VISTPANEVT FEETIEENNH LSERLRQYTL ESKIYQYIDI DGFSLPVLER RPPNFNQTKK
YPVLFYLYGG PGSQTVKKKF NVDFQSYVAA NLGYIVVTVD GRGTGFIGRK ARCIIRGNLG
HFESLDQIQA AKIWAAKPYV DESRISIWGW SYGGFMALKT IEQDGGRTFK YGIAVAPVTD
WRYYDSIYTE RYMHTPQRNP GGYDNAAISN TTALANNIRF LVMHGTADDN VHIQNSLTFI
DKLDVNNVHN YDVHFFPDSD HSIYFHNAHK IVYSRLADWL VNAFNGEWLK TYDPTPNDSI
LRRAATWVGM SI
