NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489061537|ref|WP_002971568|]
View 

MULTISPECIES: CopG family ribbon-helix-helix protein [Brucella]

Protein Classification

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PutA1 COG3905
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ...
 1-62 2.54e-09

Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];


:

Pssm-ID: 443111  Cd Length: 69  Bit Score: 48.28  E-value: 2.54e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489061537  1 MRIPRDLLAEIEEIASLTERSRSWVIVRAMKAYLAAEGREIRDIAKARCAIENGEGIDLDTV 62
Cdd:COG3905   7 VRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWREALIQEGLAAADAGEFVSHEEV 68
 
Name Accession Description Interval E-value
PutA1 COG3905
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ...
 1-62 2.54e-09

Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];


Pssm-ID: 443111  Cd Length: 69  Bit Score: 48.28  E-value: 2.54e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489061537  1 MRIPRDLLAEIEEIASLTERSRSWVIVRAMKAYLAAEGREIRDIAKARCAIENGEGIDLDTV 62
Cdd:COG3905   7 VRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWREALIQEGLAAADAGEFVSHEEV 68
RHH_CopAso-like cd22233
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ...
 2-37 1.28e-04

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: 35.42  E-value: 1.28e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 489061537  2 RIPRDLLAEIEEIASLTERSRSWVIVRAMKAYLAAE 37
Cdd:cd22233   6 RLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLERE 41
 
Name Accession Description Interval E-value
PutA1 COG3905
Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription] ...
 1-62 2.54e-09

Predicted transcriptional regulator, contains ribbon-helix-helix (RHH_1) domain [Transcription];


Pssm-ID: 443111  Cd Length: 69  Bit Score: 48.28  E-value: 2.54e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489061537  1 MRIPRDLLAEIEEIASLTERSRSWVIVRAMKAYLAAEGREIRDIAKARCAIENGEGIDLDTV 62
Cdd:COG3905   7 VRLDDELKERLDALAAALDRSRSWLIKEAIAQYVEREEWREALIQEGLAAADAGEFVSHEEV 68
RHH_CopAso-like cd22233
ribbon-helix-helix domain of Shewanella oneidensis type II antitoxin CopA(SO), and similar ...
 2-37 1.28e-04

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: 35.42  E-value: 1.28e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 489061537  2 RIPRDLLAEIEEIASLTERSRSWVIVRAMKAYLAAE 37
Cdd:cd22233   6 RLDDDLKERLDRLAAATDRSRSWIIKEAIEEYLERE 41
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH