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Conserved domains on  [gi|446360020|ref|WP_000437875|]
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MULTISPECIES: Cro/Cl family transcriptional regulator [Bacteria]

Protein Classification

Cro/CI family transcriptional regulator( domain architecture ID 10557249)

Cro/CI family transcriptional regulator similar to Escherichia virus Lambda regulatory protein cro that plays an essential role in the switch from lysogenic to lytic state and in fine-tuning the lytic phase activation; it mediates the de-repression of the lytic promoters from repression by cI at an early stage of prophage induction

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cro pfam09048
Cro; Members of this family are involved in the repression of transcription by binding as a ...
3-60 5.80e-31

Cro; Members of this family are involved in the repression of transcription by binding as a homodimer to palindromic DNA operator sites in phage lambda: they repress genes expressed in early phage development and are necessary for the late stage of lytic growth. These proteins have a secondary structure consisting of three alpha-helices and three beta-sheets, and dimerize through interactions between the two antiparallel beta-strands.


:

Pssm-ID: 430385  Cd Length: 59  Bit Score: 102.22  E-value: 5.80e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446360020   3 QRITLKDYAMRFGQTKTAKDLGVYQSAINKAIHAGRKIFLTINADGSVYAEEVKPFPS 60
Cdd:pfam09048  2 ERITLSDFVTRFGQAKTAKDLGVKQSAISKALLAGRNIYVSVDTDGSVEAEEVRPFPS 59
 
Name Accession Description Interval E-value
Cro pfam09048
Cro; Members of this family are involved in the repression of transcription by binding as a ...
3-60 5.80e-31

Cro; Members of this family are involved in the repression of transcription by binding as a homodimer to palindromic DNA operator sites in phage lambda: they repress genes expressed in early phage development and are necessary for the late stage of lytic growth. These proteins have a secondary structure consisting of three alpha-helices and three beta-sheets, and dimerize through interactions between the two antiparallel beta-strands.


Pssm-ID: 430385  Cd Length: 59  Bit Score: 102.22  E-value: 5.80e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446360020   3 QRITLKDYAMRFGQTKTAKDLGVYQSAINKAIHAGRKIFLTINADGSVYAEEVKPFPS 60
Cdd:pfam09048  2 ERITLSDFVTRFGQAKTAKDLGVKQSAISKALLAGRNIYVSVDTDGSVEAEEVRPFPS 59
 
Name Accession Description Interval E-value
Cro pfam09048
Cro; Members of this family are involved in the repression of transcription by binding as a ...
3-60 5.80e-31

Cro; Members of this family are involved in the repression of transcription by binding as a homodimer to palindromic DNA operator sites in phage lambda: they repress genes expressed in early phage development and are necessary for the late stage of lytic growth. These proteins have a secondary structure consisting of three alpha-helices and three beta-sheets, and dimerize through interactions between the two antiparallel beta-strands.


Pssm-ID: 430385  Cd Length: 59  Bit Score: 102.22  E-value: 5.80e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446360020   3 QRITLKDYAMRFGQTKTAKDLGVYQSAINKAIHAGRKIFLTINADGSVYAEEVKPFPS 60
Cdd:pfam09048  2 ERITLSDFVTRFGQAKTAKDLGVKQSAISKALLAGRNIYVSVDTDGSVEAEEVRPFPS 59
 
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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