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Conserved domains on  [gi|447177133|ref|WP_001254389|]
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conjugal transfer relaxosome protein TraY [Escherichia coli]

Protein Classification

similar to relaxosome protein TraY( domain architecture ID 11486828)

protein similar to relaxosome protein TraY

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13740 PRK13740
conjugal transfer relaxosome protein TraY;
1-70 2.77e-31

conjugal transfer relaxosome protein TraY;


:

Pssm-ID: 184292  Cd Length: 70  Bit Score: 103.71  E-value: 2.77e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447177133  1 MRRRNARGGISRTVSVYLDEDTNNRLIRAKDRSGRSKTIEVQIRLRDHLKRFPDFYNEEIFREVIEESES 70
Cdd:PRK13740  1 MKRRNTRPAPGRKVSLKLDEDTNNKLIEAKERSGRSKTNEVQIRLRDHLKRFPDFYNSEIFREVAEETES 70
 
Name Accession Description Interval E-value
PRK13740 PRK13740
conjugal transfer relaxosome protein TraY;
1-70 2.77e-31

conjugal transfer relaxosome protein TraY;


Pssm-ID: 184292  Cd Length: 70  Bit Score: 103.71  E-value: 2.77e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447177133  1 MRRRNARGGISRTVSVYLDEDTNNRLIRAKDRSGRSKTIEVQIRLRDHLKRFPDFYNEEIFREVIEESES 70
Cdd:PRK13740  1 MKRRNTRPAPGRKVSLKLDEDTNNKLIEAKERSGRSKTNEVQIRLRDHLKRFPDFYNSEIFREVAEETES 70
TraY pfam05509
TraY domain; This family consists of several enterobacterial TraY proteins. TraY is involved ...
 14-62 3.20e-18

TraY domain; This family consists of several enterobacterial TraY proteins. TraY is involved in bacterial conjugation where it is required for efficient nick formation in the F plasmid. These proteins have a ribbon-helix-helix fold and are likely to be DNA-binding proteins.


Pssm-ID: 428502  Cd Length: 49  Bit Score: 69.97  E-value: 3.20e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 447177133  14 VSVYLDEDTNNRLIRAKDRSGRSKTIEVQIRLRDHLKRFPDFYNEEIFR 62
Cdd:pfam05509  1 VTLQLDEETNKLLEEAAERSGRSKRKEAALRLKDHLDRFPDIYESEKRE 49
 
Name Accession Description Interval E-value
PRK13740 PRK13740
conjugal transfer relaxosome protein TraY;
1-70 2.77e-31

conjugal transfer relaxosome protein TraY;


Pssm-ID: 184292  Cd Length: 70  Bit Score: 103.71  E-value: 2.77e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447177133  1 MRRRNARGGISRTVSVYLDEDTNNRLIRAKDRSGRSKTIEVQIRLRDHLKRFPDFYNEEIFREVIEESES 70
Cdd:PRK13740  1 MKRRNTRPAPGRKVSLKLDEDTNNKLIEAKERSGRSKTNEVQIRLRDHLKRFPDFYNSEIFREVAEETES 70
TraY pfam05509
TraY domain; This family consists of several enterobacterial TraY proteins. TraY is involved ...
 14-62 3.20e-18

TraY domain; This family consists of several enterobacterial TraY proteins. TraY is involved in bacterial conjugation where it is required for efficient nick formation in the F plasmid. These proteins have a ribbon-helix-helix fold and are likely to be DNA-binding proteins.


Pssm-ID: 428502  Cd Length: 49  Bit Score: 69.97  E-value: 3.20e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 447177133  14 VSVYLDEDTNNRLIRAKDRSGRSKTIEVQIRLRDHLKRFPDFYNEEIFR 62
Cdd:pfam05509  1 VTLQLDEETNKLLEEAAERSGRSKRKEAALRLKDHLDRFPDIYESEKRE 49
 
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.
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