DAPB_UNCRE
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 03-AUG-2022, entry version 57.
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 EnsemblFungi; EEP76561; EEP76561; UREG_01410.
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 OrthoDB; 269253at2759; -.
DR Proteomes; UP000002058; 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..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
