DAPB_AJEDR
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 03-AUG-2022, entry version 50.
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}.
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; EQ999983; EEQ85314.1; -; Genomic_DNA.
DR AlphaFoldDB; C5GVF3; -.
DR SMR; C5GVF3; -.
DR STRING; 559297.C5GVF3; -.
DR ESTHER; ajedr-dapb; DPP4N_Peptidase_S9.
DR EnsemblFungi; EEQ85314; EEQ85314; BDCG_08583.
DR VEuPathDB; FungiDB:BDCG_08583; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; MRTPQEN; -.
DR Proteomes; UP000002039; 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..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
