Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ...
1256-1523
0e+00
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT). This domain belongs to glucosyltransferase 24 family (GT24) A-type domain. The GT domain displays the expected glycosyltransferase type A (GT-A) fold.
:
Pssm-ID: 436473 Cd Length: 268 Bit Score: 613.08 E-value: 0e+00
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1116-1222
4.17e-47
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded beta-sandwiches found in UDP-glucose-glycoprotein glucosyltransferase-like proteins. UDP-g_GGTase is an important, central component of the QC system in the ER for checking that glycoproteins are folded correctly. This QC prevents incorrectly folded glycoproteins from leaving the ER.
:
Pssm-ID: 461910 Cd Length: 109 Bit Score: 164.20 E-value: 4.17e-47
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ...
1256-1523
0e+00
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT). This domain belongs to glucosyltransferase 24 family (GT24) A-type domain. The GT domain displays the expected glycosyltransferase type A (GT-A) fold.
Pssm-ID: 436473 Cd Length: 268 Bit Score: 613.08 E-value: 0e+00
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain ...
1256-1503
0e+00
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain of glycoprotein glucosyltransferase (UGT). UGT is a large glycoprotein whose C-terminus contains the catalytic activity. This catalytic C-terminal domain is highly homologous to Glycosyltransferase Family 8 (GT 8) and contains the DXD motif that coordinates donor sugar binding, characteristic for Family 8 glycosyltransferases. GT 8 proteins are retaining enzymes based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. The non-catalytic N-terminal portion of the human UTG1 (HUGT1) has been shown to monitor the protein folding status and activate its glucosyltransferase activity.
Pssm-ID: 133054 Cd Length: 248 Bit Score: 562.40 E-value: 0e+00
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1116-1222
4.17e-47
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded beta-sandwiches found in UDP-glucose-glycoprotein glucosyltransferase-like proteins. UDP-g_GGTase is an important, central component of the QC system in the ER for checking that glycoproteins are folded correctly. This QC prevents incorrectly folded glycoproteins from leaving the ER.
Pssm-ID: 461910 Cd Length: 109 Bit Score: 164.20 E-value: 4.17e-47
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein ...
1256-1523
0e+00
Glucosyltransferase 24; This is the catalytic domain found in UDP-glucose:glycoprotein glucosyltransferase (UGGT). This domain belongs to glucosyltransferase 24 family (GT24) A-type domain. The GT domain displays the expected glycosyltransferase type A (GT-A) fold.
Pssm-ID: 436473 Cd Length: 268 Bit Score: 613.08 E-value: 0e+00
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain ...
1256-1503
0e+00
The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family; C-terminal domain of glycoprotein glucosyltransferase (UGT). UGT is a large glycoprotein whose C-terminus contains the catalytic activity. This catalytic C-terminal domain is highly homologous to Glycosyltransferase Family 8 (GT 8) and contains the DXD motif that coordinates donor sugar binding, characteristic for Family 8 glycosyltransferases. GT 8 proteins are retaining enzymes based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. The non-catalytic N-terminal portion of the human UTG1 (HUGT1) has been shown to monitor the protein folding status and activate its glucosyltransferase activity.
Pssm-ID: 133054 Cd Length: 248 Bit Score: 562.40 E-value: 0e+00
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
1256-1503
2.10e-82
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.
Pssm-ID: 132996 [Multi-domain] Cd Length: 246 Bit Score: 270.85 E-value: 2.10e-82
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded ...
1116-1222
4.17e-47
UDP-glucose:Glycoprotein Glucosyltransferase; This domain consists of 7 stranded beta-sandwiches found in UDP-glucose-glycoprotein glucosyltransferase-like proteins. UDP-g_GGTase is an important, central component of the QC system in the ER for checking that glycoproteins are folded correctly. This QC prevents incorrectly folded glycoproteins from leaving the ER.
Pssm-ID: 461910 Cd Length: 109 Bit Score: 164.20 E-value: 4.17e-47
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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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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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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