ID   DAPB_UNCRE              Reviewed;         914 AA.
AC   C4JHY5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=UREG_01410;
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476615; EEP76561.1; -; Genomic_DNA.
DR   RefSeq; XP_002541894.1; XM_002541848.1.
DR   AlphaFoldDB; C4JHY5; -.
DR   SMR; C4JHY5; -.
DR   STRING; 336963.C4JHY5; -.
DR   ESTHER; uncre-dapb; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   GlyCosmos; C4JHY5; 6 sites, No reported glycans.
DR   GeneID; 8440664; -.
DR   KEGG; ure:UREG_01410; -.
DR   VEuPathDB; FungiDB:UREG_01410; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; C4JHY5; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000002058; 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..914
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412167"
FT   TOPO_DOM        1..88
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..914
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..82
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   COMPBIAS        26..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        751
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        828
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        861
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        617
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   914 AA;  102559 MW;  454062230C415045 CRC64;
     MGAEKRINDE EAQPLTGRDR SRDSIDSTST ASISLALIDQ ANRSTHAGRT TPPRNFGNGE
     KYRDNDDDNP EGGLPPPSGA QRTPKKVSII FWLVAALCVG GWLVAFFVFM GSPKKDSDKE
     VVVSGAENST VPGVVSTGGK KVDLDGVLTG FWSPRSHEIS WIPGPDGEDG LLLEQDGDEN
     AGYLRVENIR NQKSTNKKDD AVVLMKRETF KVGARRVRPS KVWPSPDLKT VLVMSDRLKN
     WRHSYTGNYW LFNVETQTGE PLDPGSPDGR IQLASWSPKS DSVVFTRDNN MFIRNLSSKD
     VKPITTDGGV NLFYGIPDWV YEEEVFSGNS ATWWDNDGKF VAFLRTNESR VPEYPVQYFI
     PTVGRVAHAG EEHYPNTRKI KYPKAGAPNP TVNIQFFDVE KGEVFSIEME DDLPDHDRLI
     IEVIWASNGK VLVRETNRES DRLSMVLVDA KDRTAKVIRS QDFSKLDGGW IEPSQSTYFI
     PADPGNGRPH DGYIETVPFE GFNHLAYFTP LDNPSPVFLT SGNWEVTDAP SAVDLKRGLV
     YFVAAKEQPT ERHVYTVRLD GSDLQPIVNT KAPAYYTISL STGAGYALLK YEGPEIPWQK
     VISTPANEER FEETIENNTE LAGRAKDYAL PSLYYQTITI DGYTLPVVER RPPNFNPDKK
     YPVLFHLYGG PGSQTVSKRF KVDFQSYVAS NLGYIVVTVD GRGTGFIGRK ARCVVRDNLG
     HYEAIDQIET AKAWGKRPYV DATRMAIWGW SYGGFMTLKT LERDAGQTFQ YGMAVAPVTD
     WQFYDSIYTE RYMHTPQNNP AGYANTAVSN VTALGQTVRF MVIHGTGDDN VHYQNTLTLL
     DKLDVDNVGN FDVHVYPDSD HGIYFHNAYK MLHERLSDWL VNAFNGEWVK IRNPVPNKSL
     MRRARSLLKR MSNA
//