ID A7ECF7_SCLS1 Unreviewed; 381 AA.
AC A7ECF7;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase {ECO:0000256|ARBA:ARBA00015841};
DE EC=2.4.1.142 {ECO:0000256|ARBA:ARBA00012611};
GN ORFNames=SS1G_02996 {ECO:0000313|EMBL:EDO00136.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDO00136.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: Participates in the formation of the lipid-linked precursor
CC oligosaccharide for N-glycosylation. Involved in assembling the
CC dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic
CC surface of the ER. {ECO:0000256|ARBA:ARBA00024899}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl
CC diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:13865,
CC Rhea:RHEA-COMP:9520, Rhea:RHEA-COMP:11044, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472; EC=2.4.1.142;
CC Evidence={ECO:0000256|ARBA:ARBA00001259};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
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DR EMBL; CH476623; EDO00136.1; -; Genomic_DNA.
DR RefSeq; XP_001596773.1; XM_001596723.1.
DR AlphaFoldDB; A7ECF7; -.
DR STRING; 665079.A7ECF7; -.
DR EnsemblFungi; EDO00136; EDO00136; SS1G_02996.
DR GeneID; 5493048; -.
DR KEGG; ssl:SS1G_02996; -.
DR eggNOG; KOG2941; Eukaryota.
DR HOGENOM; CLU_012079_2_0_1; -.
DR InParanoid; A7ECF7; -.
DR OMA; CKLIIDW; -.
DR OrthoDB; 1219598at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004578; F:chitobiosyldiphosphodolichol beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR026051; ALG1-like.
DR PANTHER; PTHR13036; BETA1,4 MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR13036:SF0; CHITOBIOSYLDIPHOSPHODOLICHOL BETA-MANNOSYLTRANSFERASE; 1.
DR Pfam; PF13692; Glyco_trans_1_4; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 381 AA; 42851 MW; 7757E51A99EE68DB CRC64;
MATRNGEHVE PKISVQVLVL GDIGRSPRMQ YHAMSIAKHG GRVDLIGYQE SELPSGLTDN
PLITINPPSI PTFFVAYLVC IVRNTHLIID WHNYGWTILA GTRGSKHIFV RLYKWYEAFL
GSWAPTVSFT VSRAMERQLR DSPYKIKSPI FTLHDRPASI FQPITDQEKR RAFLQRLPET
KDHVDSIMNG DVRLLVSSTS WTPDEDFNLL LDALVKYGPF AEFDCPPILA IITGKGPQKQ
MYLDRIAELT ESYDLVNVTI KTAWLDIEDY ASLLACADLG VCLHKSSSGV DLPMKVVDMF
GAGLPVVGYD QYFSWPELVK EGINGWGFTT ADDLADILEE VFKDTSGKEL ARLKKGAIEE
GRKRWDEEWD GVAGRLLGLI D
//
