Thiol-disulfide interchange protein, contains DsbC and DsbD domains [Posttranslational ...
464-809
1.05e-03
Thiol-disulfide interchange protein, contains DsbC and DsbD domains [Posttranslational modification, protein turnover, chaperones, Energy production and conversion];
The actual alignment was detected with superfamily member COG4233:
Pssm-ID: 443377 [Multi-domain] Cd Length: 681 Bit Score: 42.96 E-value: 1.05e-03
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
70-286
1.11e-13
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133029 [Multi-domain] Cd Length: 166 Bit Score: 69.90 E-value: 1.11e-13
Thiol-disulfide interchange protein, contains DsbC and DsbD domains [Posttranslational ...
464-809
1.05e-03
Thiol-disulfide interchange protein, contains DsbC and DsbD domains [Posttranslational modification, protein turnover, chaperones, Energy production and conversion];
Pssm-ID: 443377 [Multi-domain] Cd Length: 681 Bit Score: 42.96 E-value: 1.05e-03
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
70-286
1.11e-13
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133029 [Multi-domain] Cd Length: 166 Bit Score: 69.90 E-value: 1.11e-13
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
134-286
1.15e-06
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.
Pssm-ID: 133017 [Multi-domain] Cd Length: 237 Bit Score: 51.13 E-value: 1.15e-06
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
69-276
8.95e-05
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
Pssm-ID: 132997 [Multi-domain] Cd Length: 156 Bit Score: 44.03 E-value: 8.95e-05
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
80-302
5.16e-04
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133028 [Multi-domain] Cd Length: 202 Bit Score: 42.62 E-value: 5.16e-04
Thiol-disulfide interchange protein, contains DsbC and DsbD domains [Posttranslational ...
464-809
1.05e-03
Thiol-disulfide interchange protein, contains DsbC and DsbD domains [Posttranslational modification, protein turnover, chaperones, Energy production and conversion];
Pssm-ID: 443377 [Multi-domain] Cd Length: 681 Bit Score: 42.96 E-value: 1.05e-03
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
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.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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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,
or click on the triangles, if present, that represent functional sites (conserved features)
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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,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
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
non-specific hits
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advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
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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