Protein Family Models

The HHH domain is a short DNA-binding domain [1]. [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. (from Pfam)

Date:

2024-10-16

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)

Date:

2024-10-16

Members of this family are involved in the Type II protein secretion system. The T2SK family includes proteins such as ExeK, PulK, OutX and XcpX. They consist of two tandem SAM-like domains, this entry represents the second one. [1]. 15223057. The general secretory pathway: a general misnomer?. Desvaux M, Parham NJ, Scott-Tucker A, Henderson IR;. Trends Microbiol. 2004;12:306-309. [2]. 14600218. Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella. Peabody CR, Chung YJ, Yen MR, Vidal-Ingigliardi D, Pugsley AP, Saier MH Jr;. Microbiology. 2003;149:3051-3072. [3]. 19299134. Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Desvaux M, Hebraud M, Talon R, Henderson IR;. Trends Microbiol. 2009;17:139-145. (from Pfam)

Date:

2024-10-16

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)

Date:

2024-10-16

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

Date:

2024-12-18

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.

Date:

2019-09-10