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Database: UniProt
Entry: A0A0W0G743_9AGAR
LinkDB: A0A0W0G743_9AGAR
Original site: A0A0W0G743_9AGAR 
ID   A0A0W0G743_9AGAR        Unreviewed;       240 AA.
AC   A0A0W0G743;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=dolichyl-phosphate beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012583};
DE            EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN   ORFNames=WG66_3156 {ECO:0000313|EMBL:KTB44261.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB44261.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB44261.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB44261.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT   pod rot of cacao.";
RL   Submitted (DEC-2015) 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:KTB44261.1}.
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DR   EMBL; LATX01000961; KTB44261.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0G743; -.
DR   eggNOG; KOG2977; Eukaryota.
DR   Proteomes; UP000054988; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW   Transferase {ECO:0000313|EMBL:KTB44261.1}.
FT   DOMAIN          2..165
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
SQ   SEQUENCE   240 AA;  26347 MW;  2E3EDB6D0CC95753 CRC64;
     MLAAAIDHLT SLKEKRTFEV LIVDDGSSDD TTAASIKLAG KYPKCDIRVV TLEKNLGKGG
     AVRHGMLFSG GERLLMVDAD GASRFNDLEL LWEAMDKIAP DHAPGVVVGS RAHLVKSEAV
     VKRSFVRNVL MYGLHTVLRI VGVGHIRDTQ CGFKLFSRSA ARQIFPAQHL PTWIFDVELL
     LLAKQLGIPV AEIPIEWHEV AGSKLNVMTA SLQMLRDLLI VRANHLLGRW SAVPSKGKIE
//
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