ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
252-337
2.16e-12
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
:
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 62.93 E-value: 2.16e-12
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
162-239
2.06e-10
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
:
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 57.54 E-value: 2.06e-10
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per ...
411-704
3.52e-78
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General]
Pssm-ID: 274252 [Multi-domain] Cd Length: 267 Bit Score: 250.83 E-value: 3.52e-78
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. ...
412-488
5.24e-27
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. SpoIID is necessary for membrane migration as well as for some of the earlier steps in engulfment during bacterial endospore formation. The domain is also found in amidase enhancer proteins. Amidases, like SpoIID, are cell wall hydrolases.
Pssm-ID: 462491 [Multi-domain] Cd Length: 100 Bit Score: 105.38 E-value: 5.24e-27
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
64-149
6.99e-16
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 72.95 E-value: 6.99e-16
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
252-337
2.16e-12
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 62.93 E-value: 2.16e-12
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
162-239
2.06e-10
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 57.54 E-value: 2.06e-10
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per ...
411-704
3.52e-78
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General]
Pssm-ID: 274252 [Multi-domain] Cd Length: 267 Bit Score: 250.83 E-value: 3.52e-78
stage II sporulation protein D; Stage II sporulation protein D (SpoIID) is a protein of the ...
414-705
1.69e-50
stage II sporulation protein D; Stage II sporulation protein D (SpoIID) is a protein of the endospore formation program in a number of lineages in the Firmicutes (low-GC Gram-positive bacteria). It is expressed in the mother cell compartment, under control of Sigma-E. SpoIID, along with SpoIIM and SpoIIP, is one of three major proteins involved in engulfment of the forespore by the mother cell. [Cellular processes, Sporulation and germination]
Pssm-ID: 274332 [Multi-domain] Cd Length: 338 Bit Score: 179.53 E-value: 1.69e-50
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. ...
412-488
5.24e-27
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. SpoIID is necessary for membrane migration as well as for some of the earlier steps in engulfment during bacterial endospore formation. The domain is also found in amidase enhancer proteins. Amidases, like SpoIID, are cell wall hydrolases.
Pssm-ID: 462491 [Multi-domain] Cd Length: 100 Bit Score: 105.38 E-value: 5.24e-27
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
64-149
6.99e-16
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 72.95 E-value: 6.99e-16
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
252-337
2.16e-12
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 62.93 E-value: 2.16e-12
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
162-239
2.06e-10
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 57.54 E-value: 2.06e-10
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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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.
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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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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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