GenomeNet

Database: UniProt
Entry: W9YBJ3_9EURO
LinkDB: W9YBJ3_9EURO
Original site: W9YBJ3_9EURO 
ID   W9YBJ3_9EURO            Unreviewed;       434 AA.
AC   W9YBJ3;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=dolichyl-phosphate beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012583};
DE            EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN   ORFNames=A1O3_08022 {ECO:0000313|EMBL:EXJ79739.1};
OS   Capronia epimyces CBS 606.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ79739.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ79739.1, ECO:0000313|Proteomes:UP000019478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ79739.1,
RC   ECO:0000313|Proteomes:UP000019478};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-
CC         D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA-
CC         COMP:9517, Rhea:RHEA-COMP:9528, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117;
CC         Evidence={ECO:0000256|ARBA:ARBA00034053};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004648}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC       {ECO:0000256|ARBA:ARBA00006739}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXJ79739.1}.
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DR   EMBL; AMGY01000007; EXJ79739.1; -; Genomic_DNA.
DR   RefSeq; XP_007736313.1; XM_007738123.1.
DR   AlphaFoldDB; W9YBJ3; -.
DR   STRING; 1182542.W9YBJ3; -.
DR   GeneID; 19172113; -.
DR   eggNOG; KOG2977; Eukaryota.
DR   HOGENOM; CLU_033536_9_1_1; -.
DR   OrthoDB; 179325at2759; -.
DR   Proteomes; UP000019478; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004581; F:dolichyl-phosphate beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0043934; P:sporulation; IEA:UniProt.
DR   CDD; cd04188; DPG_synthase; 1.
DR   InterPro; IPR035518; DPG_synthase.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR10859:SF91; DOLICHYL-PHOSPHATE BETA-GLUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10859; GLYCOSYL TRANSFERASE; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW   Transferase {ECO:0000313|EMBL:EXJ79739.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          244..328
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   REGION          148..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  48151 MW;  FDF41B97231E191A CRC64;
     MGVMGRHFVD LYPQDGSFNW RLIPFILIWV AFAIVVVIWL LVTLFVPFPR KPRPSEKKFT
     TVDKTGDVTE PEPLPCWYDD LLRRYGKATR EEQEIELETE IEPAELFMTL VVPAFNEEDR
     LTGMLEEAVN VLETEYGSAA AASLKTAAKD TSPSTTRAVD ADGDAKATTA IRRRKANGVK
     SSSSSSSSPP LRGWEILIVD DGSTDHTVLT AQTFSRVHIL PKHPRRLSGP WTHRSETGVK
     IPPGSVRVVS LEENRGKGGA VTHGMRHARG QYVVFADADG ATKFSDLDKL VRACQEIEDE
     QGRGVAVGSR AHLVGSEAVV KRSKLRNFLM HSFHLLLKFM TPPQTARIKD TQCGFKLFSR
     PALPYIVPHM HMDGWIFDVE MLMLAEFAGI PVVEVAVGWK EVTGSKLNVI RDSVGMAVGL
     AILRLCWGTG IYNR
//
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