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Conserved domains on  [gi|1486421620|ref|WP_119957511|]
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MULTISPECIES: excisionase [Bacillati]

Protein Classification

MerR family transcriptional regulator( domain architecture ID 323)

MerR family transcriptional regulator activates transcription through protein-dependent DNA distortion and the majority of regulators in the family respond to environmental stimuli, such as oxidative stress, heavy metals or antibiotics

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HTH_MerR-SF super family cl02600
Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; ...
6-67 1.57e-15

Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; Helix-turn-helix (HTH) transcription regulator MerR superfamily, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.


The actual alignment was detected with superfamily member pfam09035:

Pssm-ID: 470628  Cd Length: 62  Bit Score: 63.48  E-value: 1.57e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1486421620  6 VPIWERYTLTIEEASKYFRIGEKKLRKLAEENINSGWVIMNGNRVQIKRKQFEKIVDTLDVI 67
Cdd:pfam09035  1 IPIHKKMSLNTKEAAEYSGIGEKKIDQIAGENEGADFILEVGSHILFKRKEFEDFIDEALTI 62
 
Name Accession Description Interval E-value
Tn916-Xis pfam09035
Excisionase from transposon Tn916; The phage-encoded excisionase protein Tn916-Xis adopts a ...
6-67 1.57e-15

Excisionase from transposon Tn916; The phage-encoded excisionase protein Tn916-Xis adopts a winged-helix structure that consists of a three-stranded anti-parallel beta-sheet that packs against a helix-turn-helix (HTH) motif and a third C-terminal alpha-helix. It is encoded for by Tn916, which also codes for the integrase Tn916-Int. The protein interacts with DNA by the insertion of helix alpha-2 into the major groove and the contact of the hairpin that connects strands beta-2 and beta-3 with the adjacent phosphodiester backbone and/or minor groove. Tn916-Xis stimulates phage excision and inhibits viral integration by stabilising distorted DNA structures.


Pssm-ID: 286167  Cd Length: 62  Bit Score: 63.48  E-value: 1.57e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1486421620  6 VPIWERYTLTIEEASKYFRIGEKKLRKLAEENINSGWVIMNGNRVQIKRKQFEKIVDTLDVI 67
Cdd:pfam09035  1 IPIHKKMSLNTKEAAEYSGIGEKKIDQIAGENEGADFILEVGSHILFKRKEFEDFIDEALTI 62
 
Name Accession Description Interval E-value
Tn916-Xis pfam09035
Excisionase from transposon Tn916; The phage-encoded excisionase protein Tn916-Xis adopts a ...
6-67 1.57e-15

Excisionase from transposon Tn916; The phage-encoded excisionase protein Tn916-Xis adopts a winged-helix structure that consists of a three-stranded anti-parallel beta-sheet that packs against a helix-turn-helix (HTH) motif and a third C-terminal alpha-helix. It is encoded for by Tn916, which also codes for the integrase Tn916-Int. The protein interacts with DNA by the insertion of helix alpha-2 into the major groove and the contact of the hairpin that connects strands beta-2 and beta-3 with the adjacent phosphodiester backbone and/or minor groove. Tn916-Xis stimulates phage excision and inhibits viral integration by stabilising distorted DNA structures.


Pssm-ID: 286167  Cd Length: 62  Bit Score: 63.48  E-value: 1.57e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1486421620  6 VPIWERYTLTIEEASKYFRIGEKKLRKLAEENINSGWVIMNGNRVQIKRKQFEKIVDTLDVI 67
Cdd:pfam09035  1 IPIHKKMSLNTKEAAEYSGIGEKKIDQIAGENEGADFILEVGSHILFKRKEFEDFIDEALTI 62
 
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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