CopG family ribbon-helix-helix protein [Devosia lucknowensis]
CopG family ribbon-helix-helix protein( domain architecture ID 10008124)
CopG family ribbon-helix-helix protein may bind DNA and function as a transcriptional regulator, similar to Caulobacter vibrioides orphan antitoxin ParD2, the antitoxin component of a non-functional type II toxin-antitoxin
List of domain hits
Name | Accession | Description | Interval | E-value | ||
PutA1 | COG3905 | Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
3-70 | 1.84e-18 | ||
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription]; : Pssm-ID: 443111 Cd Length: 69 Bit Score: 71.78 E-value: 1.84e-18
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Name | Accession | Description | Interval | E-value | ||
PutA1 | COG3905 | Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
3-70 | 1.84e-18 | ||
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription]; Pssm-ID: 443111 Cd Length: 69 Bit Score: 71.78 E-value: 1.84e-18
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RHH_CopAso-like | cd22233 | ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
5-45 | 1.93e-09 | ||
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar proteins; This family includes the N-terminal ribbon-helix-helix (RHH) domain of Shewanella oneidensis CopA(SO), a newly identified type II antitoxin, as well as the N-terminal RHH domain of Escherichia coli PutA flavoprotein, among other similar proteins, many of which are as yet uncharacterized. CopA(SO) is a typical RHH antitoxin that includes an ordered N-terminal domain (CopA(SO)-N) and a disordered C-terminal domain (CopA(SO)-C). Biophysical investigation indicates allosteric effects of CopA(SO)-N on CopA(SO)-C; DNA binding of CopA(SO)-N appears to induce CopA(SO)-C to fold and self-associate the C-terminal domain. The multifunctional E. coli proline utilization A (PutA) flavoprotein functions as a membrane-associated proline catabolic enzyme as well as a transcriptional repressor of the proline utilization genes putA and putP. The N-terminal domain of PutA is a transcriptional regulator with an RHH fold; structure studies show that it forms a homodimer to bind one DNA duplex. This family also includes orphan antitoxin ParD2, an antitoxin component of a non-functional type II toxin-antitoxin (TA system); it does not neutralize the effect of any of the RelE or ParE toxins. Pssm-ID: 409023 Cd Length: 44 Bit Score: 48.14 E-value: 1.93e-09
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Name | Accession | Description | Interval | E-value | ||
PutA1 | COG3905 | Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ... |
3-70 | 1.84e-18 | ||
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription]; Pssm-ID: 443111 Cd Length: 69 Bit Score: 71.78 E-value: 1.84e-18
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RHH_CopAso-like | cd22233 | ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ... |
5-45 | 1.93e-09 | ||
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar proteins; This family includes the N-terminal ribbon-helix-helix (RHH) domain of Shewanella oneidensis CopA(SO), a newly identified type II antitoxin, as well as the N-terminal RHH domain of Escherichia coli PutA flavoprotein, among other similar proteins, many of which are as yet uncharacterized. CopA(SO) is a typical RHH antitoxin that includes an ordered N-terminal domain (CopA(SO)-N) and a disordered C-terminal domain (CopA(SO)-C). Biophysical investigation indicates allosteric effects of CopA(SO)-N on CopA(SO)-C; DNA binding of CopA(SO)-N appears to induce CopA(SO)-C to fold and self-associate the C-terminal domain. The multifunctional E. coli proline utilization A (PutA) flavoprotein functions as a membrane-associated proline catabolic enzyme as well as a transcriptional repressor of the proline utilization genes putA and putP. The N-terminal domain of PutA is a transcriptional regulator with an RHH fold; structure studies show that it forms a homodimer to bind one DNA duplex. This family also includes orphan antitoxin ParD2, an antitoxin component of a non-functional type II toxin-antitoxin (TA system); it does not neutralize the effect of any of the RelE or ParE toxins. Pssm-ID: 409023 Cd Length: 44 Bit Score: 48.14 E-value: 1.93e-09
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COG4710 | COG4710 | Predicted DNA-binding protein with an HTH domain [General function prediction only]; |
5-69 | 6.60e-07 | ||
Predicted DNA-binding protein with an HTH domain [General function prediction only]; Pssm-ID: 443745 Cd Length: 76 Bit Score: 42.58 E-value: 6.60e-07
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Blast search parameters | ||||
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