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   27-MAR-2024, entry version 65.
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   GlyCosmos; C1GT79; 7 sites, No reported glycans.
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; 2876738at2759; -.
DR   Proteomes; UP000002059; Partially assembled WGS sequence.
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; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
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.
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
//