ribose uptake protein RbsU and similar proteins; This group includes ribose uptake protein ...
19-293
2.40e-156
ribose uptake protein RbsU and similar proteins; This group includes ribose uptake protein RbsU and similar proteins. RbsU is encoded on the rbsUDK gene cluster, which encodes proteins involved in ribose uptake and phosphorylation. RbsR has been annotated as the repressor of the rbsUDK operon, based on its homology with RbsR repressors. RbsU belongs to the glucose/ribose porter (GRP) family (TC 2.A.7.5) and probably functions by H(+) symport. GRP family proteins have a distinctive topology: 10 putative transmembrane (TM) alpha-helical spanning domains per polypeptide chain, which apparently arose by intragenic duplication of an element encoding a primordial five-TM polypeptide. The GRP family belongs to the Drug/Metabolite Transporter (DMT) superfamily (TC 2.A.7).
:
Pssm-ID: 438514 [Multi-domain] Cd Length: 285 Bit Score: 437.30 E-value: 2.40e-156
ribose uptake protein RbsU and similar proteins; This group includes ribose uptake protein ...
19-293
2.40e-156
ribose uptake protein RbsU and similar proteins; This group includes ribose uptake protein RbsU and similar proteins. RbsU is encoded on the rbsUDK gene cluster, which encodes proteins involved in ribose uptake and phosphorylation. RbsR has been annotated as the repressor of the rbsUDK operon, based on its homology with RbsR repressors. RbsU belongs to the glucose/ribose porter (GRP) family (TC 2.A.7.5) and probably functions by H(+) symport. GRP family proteins have a distinctive topology: 10 putative transmembrane (TM) alpha-helical spanning domains per polypeptide chain, which apparently arose by intragenic duplication of an element encoding a primordial five-TM polypeptide. The GRP family belongs to the Drug/Metabolite Transporter (DMT) superfamily (TC 2.A.7).
Pssm-ID: 438514 [Multi-domain] Cd Length: 285 Bit Score: 437.30 E-value: 2.40e-156
Sugar transport protein; This is a family of bacterial sugar transporters approximately 300 ...
19-296
4.30e-102
Sugar transport protein; This is a family of bacterial sugar transporters approximately 300 residues long. Members include glucose uptake proteins, ribose transport proteins, and several putative and hypothetical membrane proteins probably involved in sugar transport across bacterial membranes. These members are transmembrane proteins which are usually 5+5 duplications. This model recognizes a set of five TMs,
Pssm-ID: 429127 [Multi-domain] Cd Length: 280 Bit Score: 299.95 E-value: 4.30e-102
RhaT L-rhamnose-proton symporter family protein; These proteins are members of the L-Rhamnose ...
19-296
3.06e-63
RhaT L-rhamnose-proton symporter family protein; These proteins are members of the L-Rhamnose Symporter (RhaT) Family (TC 2.A.7). This family includes two characterized members, both of which function as L-rhamnose:H+ symporters and have 10 GES predicted transmembrane domains. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273265 Cd Length: 290 Bit Score: 201.06 E-value: 3.06e-63
ribose uptake protein RbsU and similar proteins; This group includes ribose uptake protein ...
19-293
2.40e-156
ribose uptake protein RbsU and similar proteins; This group includes ribose uptake protein RbsU and similar proteins. RbsU is encoded on the rbsUDK gene cluster, which encodes proteins involved in ribose uptake and phosphorylation. RbsR has been annotated as the repressor of the rbsUDK operon, based on its homology with RbsR repressors. RbsU belongs to the glucose/ribose porter (GRP) family (TC 2.A.7.5) and probably functions by H(+) symport. GRP family proteins have a distinctive topology: 10 putative transmembrane (TM) alpha-helical spanning domains per polypeptide chain, which apparently arose by intragenic duplication of an element encoding a primordial five-TM polypeptide. The GRP family belongs to the Drug/Metabolite Transporter (DMT) superfamily (TC 2.A.7).
Pssm-ID: 438514 [Multi-domain] Cd Length: 285 Bit Score: 437.30 E-value: 2.40e-156
Sugar transport protein; This is a family of bacterial sugar transporters approximately 300 ...
19-296
4.30e-102
Sugar transport protein; This is a family of bacterial sugar transporters approximately 300 residues long. Members include glucose uptake proteins, ribose transport proteins, and several putative and hypothetical membrane proteins probably involved in sugar transport across bacterial membranes. These members are transmembrane proteins which are usually 5+5 duplications. This model recognizes a set of five TMs,
Pssm-ID: 429127 [Multi-domain] Cd Length: 280 Bit Score: 299.95 E-value: 4.30e-102
glucose/ribose porter family; The glucose/ribose porter (GRP) family (TC 2.A.7.5) includes two ...
20-293
8.77e-91
glucose/ribose porter family; The glucose/ribose porter (GRP) family (TC 2.A.7.5) includes two functionally characterized members, a glucose uptake permease from Staphylococcus xylosus, and a probable ribose uptake permease from Lactobacillus sakei. Both proteins probably function by H(+) symport. This family also includes several putative and hypothetical membrane proteins that are probably involved in sugar transport across bacterial membranes. GRP family proteins have a distinctive topology: 10 putative transmembrane (TM) alpha-helical spanning domains per polypeptide chain, which apparently arose by intragenic duplication of an element encoding a primordial five-TM polypeptide. In Lactococcus lactis, GlcU was identified as the sole non-PTS (phosphoenolpyruvate:phosphotransferase systems) permease involved in the transport of glucose, which is driven by the proton-motive force. A gene from Bacillus subtilis, ycxE, that is homologous to glcU, could substitute for glcU in Escherichia coli glucose growth experiments and restored glucose repression in Staphylococcus xylosus glcU mutants. RbsU is encoded on the rbsUDK gene cluster, which encodes proteins involved in ribose uptake and phosphorylation. RbsR has been annotated as the repressor of the rbsUDK operon, based on its homology with RbsR repressors. The GRP family belongs to the Drug/Metabolite Transporter (DMT) superfamily (TC 2.A.7).
Pssm-ID: 438513 [Multi-domain] Cd Length: 279 Bit Score: 270.87 E-value: 8.77e-91
glucose uptake protein GlcU; Glucose uptake protein GlcU is part of the glucose/ribose porter ...
20-292
2.01e-63
glucose uptake protein GlcU; Glucose uptake protein GlcU is part of the glucose/ribose porter (GRP) family (TC 2.A.7.5), which also includes ribose transport proteins, and several putative and hypothetical membrane proteins probably involved in sugar transport across bacterial membranes. GRP family proteins have a distinctive topology: 10 putative transmembrane (TM) alpha-helical spanning domains per polypeptide chain, which apparently arose by intragenic duplication of an element encoding a primordial five-TM polypeptide. In Lactococcus lactis, GlcU was identified as the sole non-PTS (phosphoenolpyruvate:phosphotransferase systems) permease involved in the transport of glucose, which is driven by the proton-motive force. A gene from Bacillus subtilis, ycxE, that is homologous to glcU, could substitute for glcU in Escherichia coli glucose growth experiments and restored glucose repression in Staphylococcus xylosus glcU mutants. The GRP family belongs to the Drug/Metabolite Transporter (DMT) superfamily (TC 2.A.7).
Pssm-ID: 438515 [Multi-domain] Cd Length: 277 Bit Score: 201.24 E-value: 2.01e-63
RhaT L-rhamnose-proton symporter family protein; These proteins are members of the L-Rhamnose ...
19-296
3.06e-63
RhaT L-rhamnose-proton symporter family protein; These proteins are members of the L-Rhamnose Symporter (RhaT) Family (TC 2.A.7). This family includes two characterized members, both of which function as L-rhamnose:H+ symporters and have 10 GES predicted transmembrane domains. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273265 Cd Length: 290 Bit Score: 201.06 E-value: 3.06e-63
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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
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.
Click here to see more details.
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
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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)
mapped to the query sequence.
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
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
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
(CDART).
Modify your query to search against a different database and/or use advanced search options
