glycosyltransferase family 18 protein may act as alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase that contributes to the creation of branches in complex-type N-glycans
Glycosyltransferase family 18; Enzymes belonging to glycosyltransferase family 18 (alpha-1, ...
184-430
3.32e-157
Glycosyltransferase family 18; Enzymes belonging to glycosyltransferase family 18 (alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase) contribute to the creation of branches in complex-type N-glycans. This domain is responsible for the catalytic activity of the enzyme.
The actual alignment was detected with superfamily member pfam15024:
Pssm-ID: 434401 Cd Length: 557 Bit Score: 457.13 E-value: 3.32e-157
Glycosyltransferase family 18; Enzymes belonging to glycosyltransferase family 18 (alpha-1, ...
184-430
3.32e-157
Glycosyltransferase family 18; Enzymes belonging to glycosyltransferase family 18 (alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase) contribute to the creation of branches in complex-type N-glycans. This domain is responsible for the catalytic activity of the enzyme.
Pssm-ID: 434401 Cd Length: 557 Bit Score: 457.13 E-value: 3.32e-157
Glycosyltransferase family 18; Enzymes belonging to glycosyltransferase family 18 (alpha-1, ...
184-430
3.32e-157
Glycosyltransferase family 18; Enzymes belonging to glycosyltransferase family 18 (alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase) contribute to the creation of branches in complex-type N-glycans. This domain is responsible for the catalytic activity of the enzyme.
Pssm-ID: 434401 Cd Length: 557 Bit Score: 457.13 E-value: 3.32e-157
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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