RraA family protein such as regulator of ribonuclease activity A (RraA), which globally modulates RNA abundance by binding to RNase E and regulating its endonucleolytic activity, and 4-hydroxy-4-methyl-2-oxoglutarate (HMG) aldolase, which catalyzes the aldol cleavage of HMG into 2 molecules of pyruvate
regulator of ribonuclease activity A; This family includes a number of closely related ...
1-155
1.90e-89
regulator of ribonuclease activity A; This family includes a number of closely related sequences from certain enterobacteria. The E. coli member of this family has been characterized as a regulator of RNase E and its crystal structure has been analyzed. The broader subfamily which includes this equivalog, TIGR01935, was initially classified as a "hypothetical equivalog" with the name "regulator of ribonuclease activity A" based on the same evidence for this model. It now appears that, considering the second group of enterobacterial sequences within TIGR01935, the functional assignment is unsupported. THIS PROTEIN IS _NOT_ MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error. [Transcription, Degradation of RNA, Regulatory functions, Protein interactions]
Pssm-ID: 132043 Cd Length: 161 Bit Score: 257.81 E-value: 1.90e-89
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
6-154
1.10e-46
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator of ribonuclease activity A (RraA), a protein that binds to RNase E and inhibits RNase E endonucleolytic cleavages. Members also include proteins with other functions, like a 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate (HMG/CHA) aldolase from Pseudomonas putida, which catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway and the uncharacterized YER010Cp protein from yeast, an organism lacking RNAse E.
Pssm-ID: 319245 [Multi-domain] Cd Length: 150 Bit Score: 149.15 E-value: 1.10e-46
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
30-152
5.38e-39
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) and 4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy- 4-hydroxy-2-oxoadipate (CHA) aldolase, also known as RraA-like protein. RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing. RraA-like proteins seem to contain aldolase and/or decarboxylase activity either in place of or in addition to the RNase E inhibitor functions.
Pssm-ID: 427475 [Multi-domain] Cd Length: 148 Bit Score: 129.55 E-value: 5.38e-39
regulator of ribonuclease activity A; This family includes a number of closely related ...
1-155
1.90e-89
regulator of ribonuclease activity A; This family includes a number of closely related sequences from certain enterobacteria. The E. coli member of this family has been characterized as a regulator of RNase E and its crystal structure has been analyzed. The broader subfamily which includes this equivalog, TIGR01935, was initially classified as a "hypothetical equivalog" with the name "regulator of ribonuclease activity A" based on the same evidence for this model. It now appears that, considering the second group of enterobacterial sequences within TIGR01935, the functional assignment is unsupported. THIS PROTEIN IS _NOT_ MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error. [Transcription, Degradation of RNA, Regulatory functions, Protein interactions]
Pssm-ID: 132043 Cd Length: 161 Bit Score: 257.81 E-value: 1.90e-89
RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase ...
5-154
6.15e-72
RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase E and its crystal structure has been analyzed. This model was initially classified as a "hypothetical equivalog" expressing the tentative hypothesis that all members might have the same function as the E. coli enzyme. Considering the second clade of enterobacterial sequences within this family, that appears to be less tenable. The function of these sequences outside of the narrow RraA equivalog model (TIGR02998) remains obscure. All of these were initially annotated as MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error in the case of the E. coli protein. [Unknown function, General]
Pssm-ID: 130990 Cd Length: 150 Bit Score: 213.35 E-value: 6.15e-72
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
6-154
1.10e-46
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator of ribonuclease activity A (RraA), a protein that binds to RNase E and inhibits RNase E endonucleolytic cleavages. Members also include proteins with other functions, like a 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate (HMG/CHA) aldolase from Pseudomonas putida, which catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway and the uncharacterized YER010Cp protein from yeast, an organism lacking RNAse E.
Pssm-ID: 319245 [Multi-domain] Cd Length: 150 Bit Score: 149.15 E-value: 1.10e-46
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
30-152
5.38e-39
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) and 4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy- 4-hydroxy-2-oxoadipate (CHA) aldolase, also known as RraA-like protein. RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing. RraA-like proteins seem to contain aldolase and/or decarboxylase activity either in place of or in addition to the RNase E inhibitor functions.
Pssm-ID: 427475 [Multi-domain] Cd Length: 148 Bit Score: 129.55 E-value: 5.38e-39
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.
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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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(labeled illustration).
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
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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
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
