DUF1471 family protein YdgH; YdgH is the rare paralog in the DUF1471 family (PF07338) with ...
1-316
0e+00
DUF1471 family protein YdgH; YdgH is the rare paralog in the DUF1471 family (PF07338) with three tandem copies of the DUF1471 domain instead of just one. Note that STM1478 from the Salmonella enterica model strain LT2 is also called SssB.
:
Pssm-ID: 439699 [Multi-domain] Cd Length: 317 Bit Score: 542.38 E-value: 0e+00
DUF1471 family protein YdgH; YdgH is the rare paralog in the DUF1471 family (PF07338) with ...
1-316
0e+00
DUF1471 family protein YdgH; YdgH is the rare paralog in the DUF1471 family (PF07338) with three tandem copies of the DUF1471 domain instead of just one. Note that STM1478 from the Salmonella enterica model strain LT2 is also called SssB.
Pssm-ID: 439699 [Multi-domain] Cd Length: 317 Bit Score: 542.38 E-value: 0e+00
YdgH/BhsA/McbA-like domain; This domain is found in several Enterobacterial proteins of around ...
34-89
2.31e-14
YdgH/BhsA/McbA-like domain; This domain is found in several Enterobacterial proteins of around 90 residues in length, including E. coli YdgH, YhcN, BhsA and McbA, which play a role in stress response, biofilm formation and pathogenesis. BhsA (also known as ComC) reduces the permeability of the outer membrane to copper and may decrease biofilm formation by repressing cell-cell interaction and cell surface interaction. Members of this entry have one copy of this domain with the exception of YdgH, which has three copies. The function of this domain is unknown, however, it is suggested to be directly involved in host-pathogen interaction.
Pssm-ID: 429417 [Multi-domain] Cd Length: 55 Bit Score: 66.39 E-value: 2.31e-14
DUF1471 family protein YdgH; YdgH is the rare paralog in the DUF1471 family (PF07338) with ...
1-316
0e+00
DUF1471 family protein YdgH; YdgH is the rare paralog in the DUF1471 family (PF07338) with three tandem copies of the DUF1471 domain instead of just one. Note that STM1478 from the Salmonella enterica model strain LT2 is also called SssB.
Pssm-ID: 439699 [Multi-domain] Cd Length: 317 Bit Score: 542.38 E-value: 0e+00
YdgH/BhsA/McbA-like domain; This domain is found in several Enterobacterial proteins of around ...
34-89
2.31e-14
YdgH/BhsA/McbA-like domain; This domain is found in several Enterobacterial proteins of around 90 residues in length, including E. coli YdgH, YhcN, BhsA and McbA, which play a role in stress response, biofilm formation and pathogenesis. BhsA (also known as ComC) reduces the permeability of the outer membrane to copper and may decrease biofilm formation by repressing cell-cell interaction and cell surface interaction. Members of this entry have one copy of this domain with the exception of YdgH, which has three copies. The function of this domain is unknown, however, it is suggested to be directly involved in host-pathogen interaction.
Pssm-ID: 429417 [Multi-domain] Cd Length: 55 Bit Score: 66.39 E-value: 2.31e-14
YdgH/BhsA/McbA-like domain; This domain is found in several Enterobacterial proteins of around ...
118-173
5.96e-08
YdgH/BhsA/McbA-like domain; This domain is found in several Enterobacterial proteins of around 90 residues in length, including E. coli YdgH, YhcN, BhsA and McbA, which play a role in stress response, biofilm formation and pathogenesis. BhsA (also known as ComC) reduces the permeability of the outer membrane to copper and may decrease biofilm formation by repressing cell-cell interaction and cell surface interaction. Members of this entry have one copy of this domain with the exception of YdgH, which has three copies. The function of this domain is unknown, however, it is suggested to be directly involved in host-pathogen interaction.
Pssm-ID: 429417 [Multi-domain] Cd Length: 55 Bit Score: 48.67 E-value: 5.96e-08
YdgH/BhsA/McbA-like domain; This domain is found in several Enterobacterial proteins of around ...
261-315
6.91e-08
YdgH/BhsA/McbA-like domain; This domain is found in several Enterobacterial proteins of around 90 residues in length, including E. coli YdgH, YhcN, BhsA and McbA, which play a role in stress response, biofilm formation and pathogenesis. BhsA (also known as ComC) reduces the permeability of the outer membrane to copper and may decrease biofilm formation by repressing cell-cell interaction and cell surface interaction. Members of this entry have one copy of this domain with the exception of YdgH, which has three copies. The function of this domain is unknown, however, it is suggested to be directly involved in host-pathogen interaction.
Pssm-ID: 429417 [Multi-domain] Cd Length: 55 Bit Score: 48.29 E-value: 6.91e-08
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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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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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.
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),
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)
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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
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
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