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Conserved domains on  [gi|1781484223|gb|QGT54007|]
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anti-sigma 70 protein [Acinetobacter phage vB_AbaM_Konradin]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AsiA super family cl07572
Anti-Sigma Factor A; Anti-sigma factor A is a transcriptional inhibitor that inhibits sigma ...
4-77 3.55e-13

Anti-Sigma Factor A; Anti-sigma factor A is a transcriptional inhibitor that inhibits sigma 70-directed transcription by weakening its interaction with the core of the host's RNA polymerase. It is an all-helical protein, composed of six helical segments and intervening loops and turns, as well as a helix-turn-helix DNA binding motif, although neither free anti-sigma factor nor anti-sigma factor bound to sigma-70 has been shown to interact directly with DNA. In solution, the protein forms a symmetric dimer of small (10.59 kDa) protomers, which are composed of helix and coil regions and are devoid of beta-strand/sheet secondary structural elements.


The actual alignment was detected with superfamily member pfam09010:

Pssm-ID: 401090  Cd Length: 85  Bit Score: 59.26  E-value: 3.55e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1781484223  4 ETLAEIIAVVSILIKFGHDDILEDKNLFIAFLNELGI-TINDKKVTAAGLFNLTQDITTRQKEQLIAEFNIGHAP 77
Cdd:pfam09010  5 DLALDIAAVASILIKFGRDDCVENQALFIAFCNEAGFrTHEGKEFNQMSFRKIFAELPQEDKKELIDEFNEGFVP 79
 
Name Accession Description Interval E-value
AsiA pfam09010
Anti-Sigma Factor A; Anti-sigma factor A is a transcriptional inhibitor that inhibits sigma ...
4-77 3.55e-13

Anti-Sigma Factor A; Anti-sigma factor A is a transcriptional inhibitor that inhibits sigma 70-directed transcription by weakening its interaction with the core of the host's RNA polymerase. It is an all-helical protein, composed of six helical segments and intervening loops and turns, as well as a helix-turn-helix DNA binding motif, although neither free anti-sigma factor nor anti-sigma factor bound to sigma-70 has been shown to interact directly with DNA. In solution, the protein forms a symmetric dimer of small (10.59 kDa) protomers, which are composed of helix and coil regions and are devoid of beta-strand/sheet secondary structural elements.


Pssm-ID: 401090  Cd Length: 85  Bit Score: 59.26  E-value: 3.55e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1781484223  4 ETLAEIIAVVSILIKFGHDDILEDKNLFIAFLNELGI-TINDKKVTAAGLFNLTQDITTRQKEQLIAEFNIGHAP 77
Cdd:pfam09010  5 DLALDIAAVASILIKFGRDDCVENQALFIAFCNEAGFrTHEGKEFNQMSFRKIFAELPQEDKKELIDEFNEGFVP 79
 
Name Accession Description Interval E-value
AsiA pfam09010
Anti-Sigma Factor A; Anti-sigma factor A is a transcriptional inhibitor that inhibits sigma ...
4-77 3.55e-13

Anti-Sigma Factor A; Anti-sigma factor A is a transcriptional inhibitor that inhibits sigma 70-directed transcription by weakening its interaction with the core of the host's RNA polymerase. It is an all-helical protein, composed of six helical segments and intervening loops and turns, as well as a helix-turn-helix DNA binding motif, although neither free anti-sigma factor nor anti-sigma factor bound to sigma-70 has been shown to interact directly with DNA. In solution, the protein forms a symmetric dimer of small (10.59 kDa) protomers, which are composed of helix and coil regions and are devoid of beta-strand/sheet secondary structural elements.


Pssm-ID: 401090  Cd Length: 85  Bit Score: 59.26  E-value: 3.55e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1781484223  4 ETLAEIIAVVSILIKFGHDDILEDKNLFIAFLNELGI-TINDKKVTAAGLFNLTQDITTRQKEQLIAEFNIGHAP 77
Cdd:pfam09010  5 DLALDIAAVASILIKFGRDDCVENQALFIAFCNEAGFrTHEGKEFNQMSFRKIFAELPQEDKKELIDEFNEGFVP 79
 
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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