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Conserved domains on  [gi|16078910|ref|NP_389731|]
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replication terminator protein [Bacillus subtilis subsp. subtilis str. 168]

Protein Classification

MarR family transcriptional regulator; GntR family transcriptional regulator( domain architecture ID 10492049)

MarR family transcriptional regulator such as the multiple antibiotic resistance transcriptional regulator MarR, the repressor of the marRAB operon involved in the activation of both antibiotic resistance and oxidative stress genes| GntR-family transcriptional regulator is one of a group of transcriptional regulators with a conserved N-terminal helix-turn-helix DNA-binding domain and a diverse C-terminal effector-binding and oligomerization domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RTP pfam02334
Replication terminator protein; The bacterial replication terminator protein (RTP) plays a ...
 10-122 2.49e-57

Replication terminator protein; The bacterial replication terminator protein (RTP) plays a role in the termination of DNA replication by impeding replication fork movement. Two RTP dimers bind to the two inverted repeat regions at the termination site.


:

Pssm-ID: 426725  Cd Length: 113  Bit Score: 172.95  E-value: 2.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078910    10 GFLVKQRAFLKLYMITMTEQERLYGLKLLEVLRSEFKEIGFKPNHTEVYRSLHELLDDGILKQIKVKKEGAKLQEVVLYQ 89
Cdd:pfam02334   1 GFLIKQRAFLKLYLITMVEQKRLYGLQLLDELRAEFKPYGYSPNHSEIYRALHELIEDGILKRVKKKKEGAKLQEVVIYQ 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 16078910    90 FKDYEAAKLYKKQLKVELDRCKKLIEKALSDNF 122
Cdd:pfam02334  81 FTDYEKAKLYKKQVKADLDRCIGLLRKALEDNY 113
 
Name Accession Description Interval E-value
RTP pfam02334
Replication terminator protein; The bacterial replication terminator protein (RTP) plays a ...
 10-122 2.49e-57

Replication terminator protein; The bacterial replication terminator protein (RTP) plays a role in the termination of DNA replication by impeding replication fork movement. Two RTP dimers bind to the two inverted repeat regions at the termination site.


Pssm-ID: 426725  Cd Length: 113  Bit Score: 172.95  E-value: 2.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078910    10 GFLVKQRAFLKLYMITMTEQERLYGLKLLEVLRSEFKEIGFKPNHTEVYRSLHELLDDGILKQIKVKKEGAKLQEVVLYQ 89
Cdd:pfam02334   1 GFLIKQRAFLKLYLITMVEQKRLYGLQLLDELRAEFKPYGYSPNHSEIYRALHELIEDGILKRVKKKKEGAKLQEVVIYQ 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 16078910    90 FKDYEAAKLYKKQLKVELDRCKKLIEKALSDNF 122
Cdd:pfam02334  81 FTDYEKAKLYKKQVKADLDRCIGLLRKALEDNY 113
 
Name Accession Description Interval E-value
RTP pfam02334
Replication terminator protein; The bacterial replication terminator protein (RTP) plays a ...
 10-122 2.49e-57

Replication terminator protein; The bacterial replication terminator protein (RTP) plays a role in the termination of DNA replication by impeding replication fork movement. Two RTP dimers bind to the two inverted repeat regions at the termination site.


Pssm-ID: 426725  Cd Length: 113  Bit Score: 172.95  E-value: 2.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078910    10 GFLVKQRAFLKLYMITMTEQERLYGLKLLEVLRSEFKEIGFKPNHTEVYRSLHELLDDGILKQIKVKKEGAKLQEVVLYQ 89
Cdd:pfam02334   1 GFLIKQRAFLKLYLITMVEQKRLYGLQLLDELRAEFKPYGYSPNHSEIYRALHELIEDGILKRVKKKKEGAKLQEVVIYQ 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 16078910    90 FKDYEAAKLYKKQLKVELDRCKKLIEKALSDNF 122
Cdd:pfam02334  81 FTDYEKAKLYKKQVKADLDRCIGLLRKALEDNY 113
 
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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