ID A0A067MY21_9AGAM Unreviewed; 316 AA.
AC A0A067MY21;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=dolichyl-phosphate beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012583};
DE EC=2.4.1.117 {ECO:0000256|ARBA:ARBA00012583};
GN ORFNames=BOTBODRAFT_28169 {ECO:0000313|EMBL:KDQ19600.1};
OS Botryobasidium botryosum FD-172 SS1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Botryobasidiaceae; Botryobasidium.
OX NCBI_TaxID=930990 {ECO:0000313|EMBL:KDQ19600.1, ECO:0000313|Proteomes:UP000027195};
RN [1] {ECO:0000313|Proteomes:UP000027195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-172 SS1 {ECO:0000313|Proteomes:UP000027195};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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}.
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DR EMBL; KL198019; KDQ19600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067MY21; -.
DR STRING; 930990.A0A067MY21; -.
DR HOGENOM; CLU_033536_9_1_1; -.
DR InParanoid; A0A067MY21; -.
DR OrthoDB; 179325at2759; -.
DR Proteomes; UP000027195; 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:UP000027195};
KW Transferase {ECO:0000313|EMBL:KDQ19600.1}.
FT DOMAIN 61..232
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT REGION 34..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 316 AA; 34645 MW; 3EF3CB743AE20987 CRC64;
MLVAVLAAGI ALYITAHIAL IILSPKPMTP TAEEKTFLSA SSPTKPQPLP SLSDPASVQL
SVVVPAYNES TRLPPMLRTT LAHLASVRPA RTYEVLIVDD GSSDSTSAVA LTLASAHPKE
DIRVVRLRRN RGKGAAVKHG FLHARGERIL MVDADGASRF EDLEKLWEEM DKIEKDGQGV
VVGSRAHLVG TEAVVKRSLV RNILMHGFHF LLRTFGVGHI RDTQCGFKLF TRTTSQSLFP
SLHITNWIFD VELLLLARML RVPVAEVPVA WEEVAGSKIR LLWDSLGMLT DLIVIRGNYA
LGRWRPVSVG AGKKVD
//
