TIGR00159 family protein; These proteins have no detectable global or local homology to any ...
46-253
3.12e-84
TIGR00159 family protein; These proteins have no detectable global or local homology to any protein of known function. Members are restricted to the bacteria and found broadly in lineages other than the Proteobacteria. [Hypothetical proteins, Conserved]
Pssm-ID: 129263 [Multi-domain] Cd Length: 211 Bit Score: 250.89 E-value: 3.12e-84
DisA bacterial checkpoint controller nucleotide-binding; The DisA protein is a bacterial ...
121-234
1.95e-61
DisA bacterial checkpoint controller nucleotide-binding; The DisA protein is a bacterial checkpoint protein that dimerizes into an octameric complex. The protein consists of three distinct domains. This domain is the first and is a globular, nucleotide-binding region; the next 146-289 residues constitute the DisA-linker family, pfam10635, that consists of an elongated bundle of three alpha helices (alpha-6, alpha-10, and alpha-11), one side of which carries an additional three helices (alpha7-9), which thus forms a spine like-linker between domains 1 and 3. The C-terminal residues, of domain 3, are represented by family HHH, pfam00633, the specific DNA-binding domain. The octameric complex thus has structurally linked nucleotide-binding and DNA-binding HhH domains and the nucleotide-binding domains are bound to a cyclic di-adenosine phosphate such that DisA is a specific di-adenylate cyclase. This N-terminal domain has been identified as a diadenylate cyclase (DAC) responsible for producing c-di-AMP from two molecules of ATP. The di-adenylate cyclase activity is strongly suppressed by binding to branched DNA, but not to duplex or single-stranded DNA, suggesting a role for DisA as a monitor of the presence of stalled replication forks or recombination intermediates via DNA structure-modulated c-di-AMP synthesis.
Pssm-ID: 460563 [Multi-domain] Cd Length: 115 Bit Score: 189.56 E-value: 1.95e-61
diadenylate cyclase CdaM; CdaM is one of several classes of diadenylate cyclase (the cyclic ...
115-238
4.56e-29
diadenylate cyclase CdaM; CdaM is one of several classes of diadenylate cyclase (the cyclic di-AMP synthesizing enzyme), characterized originally in Mycoplasma pneumoniae.
Pssm-ID: 439622 Cd Length: 196 Bit Score: 109.00 E-value: 4.56e-29
TIGR00159 family protein; These proteins have no detectable global or local homology to any ...
46-253
3.12e-84
TIGR00159 family protein; These proteins have no detectable global or local homology to any protein of known function. Members are restricted to the bacteria and found broadly in lineages other than the Proteobacteria. [Hypothetical proteins, Conserved]
Pssm-ID: 129263 [Multi-domain] Cd Length: 211 Bit Score: 250.89 E-value: 3.12e-84
DisA bacterial checkpoint controller nucleotide-binding; The DisA protein is a bacterial ...
121-234
1.95e-61
DisA bacterial checkpoint controller nucleotide-binding; The DisA protein is a bacterial checkpoint protein that dimerizes into an octameric complex. The protein consists of three distinct domains. This domain is the first and is a globular, nucleotide-binding region; the next 146-289 residues constitute the DisA-linker family, pfam10635, that consists of an elongated bundle of three alpha helices (alpha-6, alpha-10, and alpha-11), one side of which carries an additional three helices (alpha7-9), which thus forms a spine like-linker between domains 1 and 3. The C-terminal residues, of domain 3, are represented by family HHH, pfam00633, the specific DNA-binding domain. The octameric complex thus has structurally linked nucleotide-binding and DNA-binding HhH domains and the nucleotide-binding domains are bound to a cyclic di-adenosine phosphate such that DisA is a specific di-adenylate cyclase. This N-terminal domain has been identified as a diadenylate cyclase (DAC) responsible for producing c-di-AMP from two molecules of ATP. The di-adenylate cyclase activity is strongly suppressed by binding to branched DNA, but not to duplex or single-stranded DNA, suggesting a role for DisA as a monitor of the presence of stalled replication forks or recombination intermediates via DNA structure-modulated c-di-AMP synthesis.
Pssm-ID: 460563 [Multi-domain] Cd Length: 115 Bit Score: 189.56 E-value: 1.95e-61
diadenylate cyclase CdaM; CdaM is one of several classes of diadenylate cyclase (the cyclic ...
115-238
4.56e-29
diadenylate cyclase CdaM; CdaM is one of several classes of diadenylate cyclase (the cyclic di-AMP synthesizing enzyme), characterized originally in Mycoplasma pneumoniae.
Pssm-ID: 439622 Cd Length: 196 Bit Score: 109.00 E-value: 4.56e-29
CdaA N-terminal transmembrane domain; This entry represents the amino terminal three helical ...
15-85
8.84e-05
CdaA N-terminal transmembrane domain; This entry represents the amino terminal three helical transmembrane region found in the CdaA diadenylate cyclase enzyme.
Pssm-ID: 437125 Cd Length: 81 Bit Score: 40.24 E-value: 8.84e-05
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.
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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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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
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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
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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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