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Database: UniProt
Entry: W9C7W9_SCLBF
LinkDB: W9C7W9_SCLBF
Original site: W9C7W9_SCLBF 
ID   W9C7W9_SCLBF            Unreviewed;       404 AA.
AC   W9C7W9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Glycosyltransferase family 8 protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SBOR_7733 {ECO:0000313|EMBL:ESZ91868.1};
OS   Sclerotinia borealis (strain F-4128).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ91868.1, ECO:0000313|Proteomes:UP000019487};
RN   [1] {ECO:0000313|EMBL:ESZ91868.1, ECO:0000313|Proteomes:UP000019487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX   PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA   Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT   "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT   pathogenic fungus.";
RL   Genome Announc. 2:E0117513-E0117513(2014).
CC   -!- FUNCTION: N-acetylglucosaminyltransferase involved in the Golgi-
CC       specific modification of N-linked glycans.
CC       {ECO:0000256|ARBA:ARBA00002911}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Vacuole
CC       membrane {ECO:0000256|ARBA:ARBA00004576}; Single-pass type II membrane
CC       protein {ECO:0000256|ARBA:ARBA00004576}.
CC   -!- SIMILARITY: Belongs to the GNT1 family.
CC       {ECO:0000256|ARBA:ARBA00010259}.
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family.
CC       {ECO:0000256|ARBA:ARBA00009105}.
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:ESZ91868.1}.
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DR   EMBL; AYSA01000450; ESZ91868.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9C7W9; -.
DR   STRING; 1432307.W9C7W9; -.
DR   HOGENOM; CLU_034860_1_1_1; -.
DR   OrthoDB; 1662019at2759; -.
DR   Proteomes; UP000019487; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   InterPro; IPR022751; Alpha_mannosyltransferase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR11183:SF121; GLUCOSE N-ACETYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR11183; GLYCOGENIN SUBFAMILY MEMBER; 1.
DR   Pfam; PF11051; Mannosyl_trans3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019487};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        50..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   404 AA;  46274 MW;  63563CD847C62C15 CRC64;
     MSHQAQRDLP DFLQNSPYLP VINFDIDEPP PPKAAKPSIA QIFRSRPVRT AIPIVICGLI
     ILFLLPHGTR KAKSLHLQYK TPACLKQAPI LAESLTGKEV GIEWDKYAYI TYATSKDHLC
     NALMLFESLN HLGSKAGRVL LYPQLWKNEW VEDANGRGME AITKMLIQAR DDYKVKLVNV
     EVLQHRHYTA DEWAESYTKL LAFNQTSYEK LLVLDSDSTV LKPMDELFLA PMSDSTQLLA
     PRAYWLDAQG IPQLSSHIML IKPSAIEFER LEIEIQNAGV GTYDMDIINS VFTQQKDSCG
     LLDHQIYALL TGEFRRPVTK HKGFWGKGHE TDIWDPERVF KKSKFVHFSD WPMKKPWQLQ
     DMEWVGKGPK CVPVTEGDDC RGRDIWDGLY KDFRERRVAI CGLD
//
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