glycosyltransferase family 17 protein may act as a beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase that transfers the bisecting GlcNAc to the core mannose of complex N-glycans
Glycosyltransferase family 17; This family represents beta-1,4-mannosyl-glycoprotein beta-1, ...
38-385
0e+00
Glycosyltransferase family 17; This family represents beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase (EC:2.4.1.144). This enzyme transfers the bisecting GlcNAc to the core mannose of complex N-glycans. The addition of this residue is regulated during development and has functional consequences for receptor signalling, cell adhesion, and tumour progression.
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Pssm-ID: 428090 Cd Length: 349 Bit Score: 700.95 E-value: 0e+00
Glycosyltransferase family 17; This family represents beta-1,4-mannosyl-glycoprotein beta-1, ...
38-385
0e+00
Glycosyltransferase family 17; This family represents beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase (EC:2.4.1.144). This enzyme transfers the bisecting GlcNAc to the core mannose of complex N-glycans. The addition of this residue is regulated during development and has functional consequences for receptor signalling, cell adhesion, and tumour progression.
Pssm-ID: 428090 Cd Length: 349 Bit Score: 700.95 E-value: 0e+00
Glycosyltransferase family 17; This family represents beta-1,4-mannosyl-glycoprotein beta-1, ...
38-385
0e+00
Glycosyltransferase family 17; This family represents beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase (EC:2.4.1.144). This enzyme transfers the bisecting GlcNAc to the core mannose of complex N-glycans. The addition of this residue is regulated during development and has functional consequences for receptor signalling, cell adhesion, and tumour progression.
Pssm-ID: 428090 Cd Length: 349 Bit Score: 700.95 E-value: 0e+00
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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Functional characterization of the conserved domain architecture found on the query.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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