ID   DAPB_AJEDR              Reviewed;         915 AA.
AC   C5GVF3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=BDCG_08583;
OS   Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ER-3 / ATCC MYA-2586;
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(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; EQ999983; EEQ85314.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5GVF3; -.
DR   SMR; C5GVF3; -.
DR   STRING; 559297.C5GVF3; -.
DR   ESTHER; ajedr-dapb; DPP4N_Peptidase_S9.
DR   GlyCosmos; C5GVF3; 6 sites, No reported glycans.
DR   VEuPathDB; FungiDB:BDCG_08583; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 2876738at2759; -.
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; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Membrane; Protease;
KW   Serine protease; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Vacuole.
FT   CHAIN           1..915
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412127"
FT   TOPO_DOM        1..95
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        117..915
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        754
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        831
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        864
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        572
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        813
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        900
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   915 AA;  102912 MW;  396FF2E496FA8454 CRC64;
     MAGEKGGSRD EEREPLTRGS IEFRDSINSF DYSSSTASLS LAVIDRINGS TQDSRLGEKD
     QRDDDHDQYR NEEEYDVEDA DYIPSGGKTV QKTTKIVLWA LLFLCVGGWS LAFVIFLFRG
     HDTPQTSIAS EENISSGGAR GNRITLDEVL GGEWAPRAHS ISWFPGPNGE DGLILEKDNL
     SATAYLRVED IVGRKDPKAS KKSIVLMQKK MFTVGRETVY SAQAWPSPDL KTVLVLSDQQ
     KNWRHSFTGK YWLFDVETQT GQPLDPGAPD RRIQLASWSP QSDAVVFTRD NNMFLRKLTS
     NEVATITTDG GVDLFYGVPD WVYEEEVFSG NSATWWASDG DYIAFLRTNE SSVPDYPIQY
     FASRPSGENP KPGEENYPEV REVKYPKAGA PNPIVDLQFY DVGKGEVFSV DVTSEFADDD
     RLIIEVLWAS NGKALVRETN RESDILSIAI IDVLSRTGRI VRREDVNALD GGWVEPTQST
     RFIPADPDHG RLDDGYIDTV IYEGRDQLAY FTPLDNPKPI MLTKGHSEVV NAPSGVDLKR
     GLVYFVVAGN EPWERHIYSV NFDGTSLQPL TNVTESSYYD VSFSNGAGYA LLNYRGPKVP
     WQKVINTPAN ENSFEAIIEQ NDHLSRKLRL FSLESKVYQH VTVDGFSLPV MERRPPNFDP
     AKKYPVLFHL YGGPGSQTVS KKFSVDFQSY VASTLGYIVV TVDGRGTGHI GRKARCIIRG
     NLGHYEARDQ IETAKKWAAK PYVDESRMAI WGWSYGGFMT LKTLEQDGGR TFQYGMAVAP
     VTDWRYYDSI YTERYMRTPQ HNQGGYDTSA ISNTTALASN IRFLLMHGTA DDNVHIQNSL
     TLLDKLDLDD VDNYDVHVFP DSDHSIYFHN AHKMVYNRLG DWLINAFNGE WLKVHKPTPN
     NSLFRRAETW GGLPV
//