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helix-hairpin-helix domain-containing protein
The HhH domain is a short DNA-binding domain [2]. [1]. 8692686. The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Doherty AJ, Serpell LC, Ponting CP;. Nucleic Acids Res 1996;24:2488-2497. [2]. 18439896. Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates. Witte G, Hartung S, Buttner K, Hopfner KP;. Mol Cell. 2008;30:167-178. (from Pfam)
Helix-hairpin-helix motif
The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA [2]. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain [5]. [1]. 8692686. The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Doherty AJ, Serpell LC, Ponting CP;. Nucleic Acids Res 1996;24:2488-2497. [2]. 8832889. Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction. Rafferty JB, Sedelnikova SE, Hargreaves D, Artymiuk PJ, Baker PJ, Sharples GJ, Mahdi AA, Lloyd RG, Rice DW;. Science 1996;274:415-421. [3]. 12832627. An evolutionary analysis of the helix-hairpin-helix superfamily of DNA repair glycosylases. Denver DR, Swenson SL, Lynch M;. Mol Biol Evol 2003;20:1603-1611. [4]. 10908318. Common fold in helix-hairpin-helix proteins. Shao X, Grishin NV;. Nucleic Acids Res 2000;28:2643-2650. [5]. 18439896. Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates. Witte G, Hartung S, Buttner K, Hopfner KP;. Mol Cell. 2008;30:167-178. (from Pfam)
ComEA family DNA-binding protein
ComEA family DNA-binding protein contains a helix-hairpin-helix (HhH) motif, similar to Bacillus subtilis ComE operon protein 1, an integral membrane protein required for both DNA binding and transport
competence protein ComEA helix-hairpin-helix repeat region
Members of the subfamily recognized by this model include competence protein ComEA and closely related proteins from a number of species that exhibit competence for transformation by exongenous DNA, including Streptococcus pneumoniae, Bacillus subtilis, Neisseria meningitidis, and Haemophilus influenzae. This model represents a region of two tandem copies of a helix-hairpin-helix domain (PF00633), each about 30 residues in length. Limited sequence similarity can be found among some members of this family N-terminal to the region covered by this model.
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