ID A0A165C5A1_EXIGL Unreviewed; 281 AA.
AC A0A165C5A1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Hexosyltransferase {ECO:0000256|RuleBase:RU363063};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363063};
GN ORFNames=EXIGLDRAFT_730529 {ECO:0000313|EMBL:KZV81846.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV81846.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV81846.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV81846.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein
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; KV426363; KZV81846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165C5A1; -.
DR STRING; 1314781.A0A165C5A1; -.
DR InParanoid; A0A165C5A1; -.
DR OrthoDB; 1611647at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
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:InterPro.
DR Gene3D; 3.90.550.50; -; 1.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
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}.
SQ SEQUENCE 281 AA; 32605 MW; FEC0F8B84401F30B CRC64;
MSIADELDLR AFLRENVYSR VSTDEVQFEL KFFVARQPSA YGDLLPWRLS AGDVNRLVRE
EHARFGDIHF VDAVENKWTL CLKRFLALKW AASVPQSEYD FFFTADSDSF VRLAALSRRM
HHKRPDLLDP RRTFSMWGDM KANWLHWRKA NDSSAPDEQY DGEWYDFPIG MGYLMSSALT
ARLNDVSDRL PHNVPYYSDD VLIGSWVAEY APETLLMSDK GGFHDPPLHG TQPFPVDYST
VLIHHIDINE MRQLRAMPEW NGEWLPAPQS DESTTSAWRK P
//
