type VI secretion protein, VC_A0110 family; This protein family is associated with type VI ...
5-607
0e+00
type VI secretion protein, VC_A0110 family; This protein family is associated with type VI secretion in a number of pathogenic bacteria. Mutation is associated with impaired virulence, such as impaired infection of plants by Rhizobium leguminosarum.
:
Pssm-ID: 274541 Cd Length: 598 Bit Score: 723.63 E-value: 0e+00
type VI secretion protein, VC_A0110 family; This protein family is associated with type VI ...
5-607
0e+00
type VI secretion protein, VC_A0110 family; This protein family is associated with type VI secretion in a number of pathogenic bacteria. Mutation is associated with impaired virulence, such as impaired infection of plants by Rhizobium leguminosarum.
Pssm-ID: 274541 Cd Length: 598 Bit Score: 723.63 E-value: 0e+00
Type VI secretion system, TssF; This is a family of Gram-negative bacterial proteins that form ...
1-604
0e+00
Type VI secretion system, TssF; This is a family of Gram-negative bacterial proteins that form part of the type VI pathogenicity secretion system (T6SS), including TssF. TssF is homologs to phage tail proteins and is required for proper assembly of the Hcp tube (the T6SS inner tube) in bacteria. T6SSs are toxin delivery systems. It is a multiprotein complex requiring numerous core proteins (Tss proteins) including cytoplasmic, transmembrane, and outer membrane components. The needle or tube apparatus is comprised of a phage-like complex, similar to the T4 contractile bacteriophage tail, which is thought to be anchored to the membrane by a trans-envelope complex. T6SSs contain 13 conserved components (TssA-TssM) which are thought to form the core apparatus and to enable effector proteins to be injected into target cells in a single cell-contact-dependent step. TssF one of the core components of T6SSs machinery, has been shown to be recruited by TssK into the membrane-associated T6SS complex, contributing to the dynamic mechanism of the system. Furthermore, it has been reported to interact with TssG proteins stabilizing each other while making contact with TssE, TssK and VgrG as well as with tube and sheath components. Bioinformatic analysis suggest that TssF and TssG share similarities with the J and I proteins of the bacteriophage P2 baseplate respectively. Further experimental studies show that functional TssF and TssK proteins assemble into static foci near the cell envelope. Moreover, biochemical and cytological approaches provide support to the role of TssE, TssF, TssG, TssK and VgrG as T6SS baseplate components and to a sequential recruitment hierarchy (membrane complex, baseplate, tail tube/sheath) during T6SS biogenesis.
Pssm-ID: 428685 Cd Length: 606 Bit Score: 641.56 E-value: 0e+00
type VI secretion protein, VC_A0110 family; This protein family is associated with type VI ...
5-607
0e+00
type VI secretion protein, VC_A0110 family; This protein family is associated with type VI secretion in a number of pathogenic bacteria. Mutation is associated with impaired virulence, such as impaired infection of plants by Rhizobium leguminosarum.
Pssm-ID: 274541 Cd Length: 598 Bit Score: 723.63 E-value: 0e+00
Type VI secretion system, TssF; This is a family of Gram-negative bacterial proteins that form ...
1-604
0e+00
Type VI secretion system, TssF; This is a family of Gram-negative bacterial proteins that form part of the type VI pathogenicity secretion system (T6SS), including TssF. TssF is homologs to phage tail proteins and is required for proper assembly of the Hcp tube (the T6SS inner tube) in bacteria. T6SSs are toxin delivery systems. It is a multiprotein complex requiring numerous core proteins (Tss proteins) including cytoplasmic, transmembrane, and outer membrane components. The needle or tube apparatus is comprised of a phage-like complex, similar to the T4 contractile bacteriophage tail, which is thought to be anchored to the membrane by a trans-envelope complex. T6SSs contain 13 conserved components (TssA-TssM) which are thought to form the core apparatus and to enable effector proteins to be injected into target cells in a single cell-contact-dependent step. TssF one of the core components of T6SSs machinery, has been shown to be recruited by TssK into the membrane-associated T6SS complex, contributing to the dynamic mechanism of the system. Furthermore, it has been reported to interact with TssG proteins stabilizing each other while making contact with TssE, TssK and VgrG as well as with tube and sheath components. Bioinformatic analysis suggest that TssF and TssG share similarities with the J and I proteins of the bacteriophage P2 baseplate respectively. Further experimental studies show that functional TssF and TssK proteins assemble into static foci near the cell envelope. Moreover, biochemical and cytological approaches provide support to the role of TssE, TssF, TssG, TssK and VgrG as T6SS baseplate components and to a sequential recruitment hierarchy (membrane complex, baseplate, tail tube/sheath) during T6SS biogenesis.
Pssm-ID: 428685 Cd Length: 606 Bit Score: 641.56 E-value: 0e+00
Protein of unknown function (DUF2397); Proteins in this entry are encoded within a conserved ...
1-51
5.43e-03
Protein of unknown function (DUF2397); Proteins in this entry are encoded within a conserved gene four-gene neighbourhood found sporadically in a phylogenetically broad range of bacteria including: Nocardia farcinica, Symbiobacterium thermophilum, and Streptomyces avermitilis (Actinobacteria), Geobacillus kaustophilus (Firmicutes), Azoarcus sp. EbN1 and Ralstonia solanacearum (Betaproteobacteria).
Pssm-ID: 430739 Cd Length: 483 Bit Score: 39.55 E-value: 5.43e-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.
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
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Domains are color coded according to superfamilies
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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
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Modify your query to search against a different database and/or use advanced search options
