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Database: UniProt
Entry: A0A059BX51_EUCGR
LinkDB: A0A059BX51_EUCGR
Original site: A0A059BX51_EUCGR 
ID   A0A059BX51_EUCGR        Unreviewed;       356 AA.
AC   A0A059BX51;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Hexosyltransferase {ECO:0000256|RuleBase:RU363063};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363063};
GN   ORFNames=EUGRSUZ_F03738 {ECO:0000313|EMBL:KCW70544.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW70544.1};
RN   [1] {ECO:0000313|EMBL:KCW70544.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW70544.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936,
CC         ECO:0000256|RuleBase:RU363063};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323,
CC       ECO:0000256|RuleBase:RU363063}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000256|ARBA:ARBA00008661, ECO:0000256|RuleBase:RU363063}.
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DR   EMBL; KK198758; KCW70544.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059BX51; -.
DR   EnsemblPlants; KCW70544; KCW70544; EUGRSUZ_F03738.
DR   Gramene; KCW70544; KCW70544; EUGRSUZ_F03738.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.50; -; 1.
DR   InterPro; IPR025298; DUF4094.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214:SF226; BETA-1,3-GALACTOSYLTRANSFERASE 7; 1.
DR   PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   Pfam; PF13334; DUF4094; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363063};
KW   Golgi apparatus {ECO:0000256|RuleBase:RU363063};
KW   Manganese {ECO:0000256|RuleBase:RU363063};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          1..71
FT                   /note="DUF4094"
FT                   /evidence="ECO:0000259|Pfam:PF13334"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  40418 MW;  A51D0D5ADD248E03 CRC64;
     MWSPPESSGQ FVSRARREQE LRMVSEDCDS KKKPEDDKNV LKQVHKTHEA IQSLDKSIES
     LQMELAASRS AMELGNGSGN QKARKKMFMV MGINTAFSSR KRRDSVRETW MPQGEKLLQL
     EREKGIVVRF MIGHSATSNS ILDRAIDSED AQHKDFLRLE HVEGYHELSA KTKTFFSTAV
     AMWDADFYIK VDDDVHVNLG MLATTLARHR SKPRVYIGCM KSGPVLSSKN VKYHEPEYWK
     FGEEGNKYFR HATGQIYALS RDLATYISIN QPILHKYANE DVSLGAWFIG LEVEHIDDRN
     MCCGTPPDCE WKAQAGNVCI ASFDWSCSGI CKSVEKIKDV HRRCGEGDAA VWDALI
//
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