DAPB_PARBA
ID DAPB_PARBA Reviewed; 912 AA.
AC C1GT79;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=DAPB; ORFNames=PAAG_01724;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
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}.
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DR EMBL; KN293994; EEH39262.1; -; Genomic_DNA.
DR RefSeq; XP_002796716.1; XM_002796670.2.
DR AlphaFoldDB; C1GT79; -.
DR SMR; C1GT79; -.
DR STRING; 502779.C1GT79; -.
DR ESTHER; parba-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; EEH39262; EEH39262; PAAG_01724.
DR GeneID; 9099681; -.
DR KEGG; pbl:PAAG_01724; -.
DR VEuPathDB; FungiDB:PAAG_01724; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000002059; Partially assembled 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_0000412153"
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..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
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; 102461 MW; 018B5421BC256D62 CRC64;
MAAEKGESSD EERKPLTRDS MEYRDSSNSL HYSSSAASLS LAVIDRINGS THDTGPNEIG
RGDRDYSDDG EYDLEEADYI PSGGKPVQKK VKIVLGFLLF LCLSGWSLSF VLFLFGGHES
SKTSNVYDDN ISDTGSQGNK ITLDEVLDGT WSPAFHDISW IPGPNGEDGL LLERGASISN
GYLRVEDIVS RKDPKSSKKP IVLMQKAYFN VSGEAVFPSR VWPSPDLKTV LVLSNEEKNW
RHSFTGKYWL FDVESQTGQP LDPAAKDQRV QLASWSPRSD AVVFTRDNNM FLRKLSSNEV
MKITTNGGVN LFYGVPDWVY EEEVYSGNSV TWWADDGEYI AFLRTNESSV PEYPVQYFVS
LPNGEISKPG EESYPETRKI KYPKAGAPNP IVDLQFFDVG KDEVFSVDIK GDFADSNRLI
TEVVWASNGK VIVRSTNRES DVLHVAVIDV LSRTGKIVRK EDINALDGGW VEPSQTARFI
PADPDNGRLN DGYIDTVIYE GRDQLAYYTP VDNPNPIVLT KGHSEVVQAP SGVDLKRGLV
YFVVAGNEPW ERHIYSVNFD GTSIQPVTNV SESSYYDVSF SNGAGYAFLK YAGPQVPWQK
VISTPANEVT FEETIEENNR LSERLRQYTL ESKIYQYIDI DGFSLPVLER RPPNFNQTKK
YPVLFYLYGG PGSQTVNKKF NVDFQSYVAA NLGYIVVTVD GRGTGFIGRK ARCVIRGNLG
HFESRDQIQA AKIWAAKPYV DESRISIWGW SYGGFMALKT IEQDGGRTFK YGIAVAPVTD
WRYYDSIYTE RYMHTPQRNP GGYDNAAISN TTALANNIRF LVMHGTADDN VHIQNSLTFI
DKLDVNNVHN YDVHFFPDSD HSIYFHNAHK IVYSRLADWL VNAFNGEWLK TYNPAPNDSI
FRRAAIWVGL SI