type IV secretion system protein VirB10; Members of this family are VirB10, an outer ...
190-362
7.80e-75
type IV secretion system protein VirB10; Members of this family are VirB10, an outer membrane-associated protein from the apparatus of protein type IV secretion systems (T4SS). The model attempts to exclude related TraI proteins of conjugal transfer systems as well as the ComB10 protein of a DNA-translocating competence protein of Helicobacter pylori. Because the N-terminal regions of VirB10 proteins are highly variable, the model
The actual alignment was detected with superfamily member NF038091:
Pssm-ID: 468345 Cd Length: 197 Bit Score: 230.14 E-value: 7.80e-75
type IV secretion system protein VirB10; Members of this family are VirB10, an outer ...
190-362
7.80e-75
type IV secretion system protein VirB10; Members of this family are VirB10, an outer membrane-associated protein from the apparatus of protein type IV secretion systems (T4SS). The model attempts to exclude related TraI proteins of conjugal transfer systems as well as the ComB10 protein of a DNA-translocating competence protein of Helicobacter pylori. Because the N-terminal regions of VirB10 proteins are highly variable, the model
Pssm-ID: 468345 Cd Length: 197 Bit Score: 230.14 E-value: 7.80e-75
VirB10 forms part of core complex in Type IV secretion system (T4SS); This family contains ...
200-362
1.70e-67
VirB10 forms part of core complex in Type IV secretion system (T4SS); This family contains VirB10, a component of the type IV secretion system (T4SS), including homologs TrbI, TraF, TrwE and TraL. T4S system is employed by pathogenic bacteria to export virulence DNAs and/or proteins directly from the bacterial cytoplasm into the host cell. It forms a large multiprotein complex consisting of 12 proteins termed VirB1-11 and VirD4. VirB10, interacts with VirB7 and VirB9, forming the membrane-spanning 'core complex' (CC), around which all other components assemble. The CC is inserted in both, the outer and inner membranes, playing a fundamental role as a scaffold for the rest of the T4SS components and actively participating in T4S substrate transfer through the bacterial envelope via conformational changes regulating channel opening and closing. TrwE in R33 plasmid has been shown to be anchored to the inner membrane and its C-terminal is necessary for conjugation; the transmembrane domains of TrwB and TrwE are involved in TrwB-TrwE interactions. TraF protein of the RP4 plasmid is involved in circularization of pilin subunits of P-type pili. In gonococcal genetic island (GGI) of Neisseria gonorrhoeae, T4SS encodes TrbI and circularization occurs via a covalent intermediate between the C terminus of putative pilin protein TraA and TrbI.
Pssm-ID: 319755 Cd Length: 180 Bit Score: 210.82 E-value: 1.70e-67
type IV secretion system protein VirB10; Members of this family are VirB10, an outer ...
190-362
7.80e-75
type IV secretion system protein VirB10; Members of this family are VirB10, an outer membrane-associated protein from the apparatus of protein type IV secretion systems (T4SS). The model attempts to exclude related TraI proteins of conjugal transfer systems as well as the ComB10 protein of a DNA-translocating competence protein of Helicobacter pylori. Because the N-terminal regions of VirB10 proteins are highly variable, the model
Pssm-ID: 468345 Cd Length: 197 Bit Score: 230.14 E-value: 7.80e-75
VirB10 forms part of core complex in Type IV secretion system (T4SS); This family contains ...
200-362
1.70e-67
VirB10 forms part of core complex in Type IV secretion system (T4SS); This family contains VirB10, a component of the type IV secretion system (T4SS), including homologs TrbI, TraF, TrwE and TraL. T4S system is employed by pathogenic bacteria to export virulence DNAs and/or proteins directly from the bacterial cytoplasm into the host cell. It forms a large multiprotein complex consisting of 12 proteins termed VirB1-11 and VirD4. VirB10, interacts with VirB7 and VirB9, forming the membrane-spanning 'core complex' (CC), around which all other components assemble. The CC is inserted in both, the outer and inner membranes, playing a fundamental role as a scaffold for the rest of the T4SS components and actively participating in T4S substrate transfer through the bacterial envelope via conformational changes regulating channel opening and closing. TrwE in R33 plasmid has been shown to be anchored to the inner membrane and its C-terminal is necessary for conjugation; the transmembrane domains of TrwB and TrwE are involved in TrwB-TrwE interactions. TraF protein of the RP4 plasmid is involved in circularization of pilin subunits of P-type pili. In gonococcal genetic island (GGI) of Neisseria gonorrhoeae, T4SS encodes TrbI and circularization occurs via a covalent intermediate between the C terminus of putative pilin protein TraA and TrbI.
Pssm-ID: 319755 Cd Length: 180 Bit Score: 210.82 E-value: 1.70e-67
VirB10 and similar proteins form part of core complex in Type IV secretion system (T4SS); This ...
200-317
6.83e-44
VirB10 and similar proteins form part of core complex in Type IV secretion system (T4SS); This family contains VirB10, a component of the type IV secretion system (T4SS) and its homologs, including TraB, TraF, IcmE, and similar proteins. T4S system is employed by pathogenic bacteria to export virulence DNAs and/or proteins directly from the bacterial cytoplasm into the host cell. It forms a large multiprotein complex consisting of 12 proteins termed VirB1-11 and VirD4. VirB10 interacts with VirB7 and VirB9, forming the membrane-spanning 'core complex' (CC), around which all other components assemble. The CC is inserted in both the outer and inner membranes, playing a fundamental role as a scaffold for the rest of the T4SS components and actively participating in T4S substrate transfer through the bacterial envelope via conformational changes regulating channel opening and closing. In Gram-negative bacterial pathogen Helicobacter pylori, an important aetiological agent of gastroduodenal disease in humans, the comB3 gene encodes protein with best homologies to TraS/TraB from the Pseudomonas aeruginosa conjugative plasmid RP1 and TrbI of plasmid RP4 and VirB10 from the Ti plasmid of Agrobacterium tumefaciens, as well as DotG/IcmE of Legionella pneumophila.
Pssm-ID: 319754 [Multi-domain] Cd Length: 151 Bit Score: 148.84 E-value: 6.83e-44
DotG/IcmE is a homolog of VirB10 which forms part of core complex in Type IV secretion system; ...
199-324
1.58e-07
DotG/IcmE is a homolog of VirB10 which forms part of core complex in Type IV secretion system; This family contains DotG/IcmE (VirB10 homolog) and a component of the type IV secretion system (T4SS), and similar proteins. The Dot/Icm system is a T4SS found in the pathogens Legionella and Coxiella and the conjugative apparatus of IncI plasmids; T4SS is employed by pathogenic bacteria to export virulence DNAs and/or proteins directly from the bacterial cytoplasm into the host cell. Similar to T4SS VirB/D components, the Legionella Dot/Icm secretion apparatus contains a critical five-protein sub-assembly that forms the membrane-spanning 'core-complex' (CC), around which all other components assemble. This transmembrane connection is mediated by protein dimer pairs consisting of two inner membrane proteins, DotF and DotG, each independently associating with DotH/DotC/DotD in the outer membrane.
Pssm-ID: 319757 Cd Length: 179 Bit Score: 50.65 E-value: 1.58e-07
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
