DAPB_COCPS
ID DAPB_COCPS Reviewed; 917 AA.
AC E9CUF4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=DAPB; ORFNames=CPSG_00188;
OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=443226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Coccidioides posadasii strain Silveira.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; GL636486; EFW22289.1; -; Genomic_DNA.
DR AlphaFoldDB; E9CUF4; -.
DR SMR; E9CUF4; -.
DR STRING; 443226.E9CUF4; -.
DR ESTHER; cocp7-dapb; DPP4N_Peptidase_S9.
DR EnsemblFungi; EFW22289; EFW22289; CPSG_00188.
DR VEuPathDB; FungiDB:CPSG_00188; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR Proteomes; UP000002497; 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..917
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412143"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..917
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
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 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 917 AA; 102500 MW; 3986DB9EBD68189D CRC64;
MGVEKRINDE EMQPLAERDD KSRDSIDSTS TASISLALLG GANGSAHGSR AARTRKSENQ
EKYHDDEEEG DLEEGFVPPA GGWSAPRKVS VIFTLIVTLC IAGWLVAFFV LLGRHKDSSK
DAAVSQGESN IIPGIYSGGR GGKKLDLDGV LFGNWSPKSH DISWFPGPNG ADGLLLEQGG
DRNKAYLRVE DIRSRNPGNK ADDTIVLMRE SSFMVGKRLV RPSKVWPSPD LKTVLVMSDQ
RKNWRHSYTG NYWIFDVETQ TGEPLDPESL DGGIQLASWS PNSDAIVFTR KNNMFIRRLP
SKNVKQITTD GGTNLFYGIP DWVYEEEVFS DSSATWWDGD GKFVAFLRTN ESRVPEYPVQ
YFIPNTNKPS RPSEENYPDI RKIKYPKAGA PNPVVNIQFF DVEKEEVFSV DVKDDLPDDD
RLVIGVTWAS NGNVLVRETN RESDRLSVVL IDAAKRAGKV VRSRNFSSLD GGWVEPSQTT
HFVPADPKNG RPHDGYIETI PHDGFEHLAY FTPMDNSEPT VLTSGDWEVV DAPSAVDLKR
GLVYFVAAKE NPTERHIYTV KLDGSDLQPI VDTKSAGYYS ISLSAGAGYA LLKYEGPDIP
WQKVISTPAN EEKYEESIEK NPGLADMARK YALPSLHYQT ITISGYELQV VERRPANFNP
DKKYPVLFHL YGGPGSQTVT KKFKVDFQSY VASNLGYIVV TVDGRGTGFI GRKARCAVRG
NLGHYEAIDQ IETAKAWGKR SYVDAGRMAI WGWSYGGFMT LKTLEQDAGQ TFQYGMAVAP
VTDWRFYDSI YTERYMHTPQ NNPEGYDRSA ISNVTALDQA VRFMIVHGSG DDNVHIQNTL
TLLDKLDLGS VKNFDVHVYP DSDHSIYFHN ANKMVYQRLS DWLVNAFNGE WVKTRDPIPH
KSLARRALGL INILRNG
