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   27-MAR-2024, entry version 47.
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   GlyCosmos; E9CUF4; 3 sites, No reported glycans.
DR   VEuPathDB; FungiDB:CPSG_00188; -.
DR   VEuPathDB; FungiDB:D8B26_001003; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   OMA; MRTPQEN; -.
DR   Proteomes; UP000002497; Unassembled 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: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   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
//