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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)
HhH-GPD superfamily base excision DNA repair protein
This family contains a diverse range of structurally related DNA repair proteins. The superfamily is called the HhH-GPD family after its hallmark Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate [2]. This includes endonuclease III, EC:4.2.99.18 and MutY an A/G-specific adenine glycosylase, both have a C terminal 4Fe-4S cluster. The family also includes 8-oxoguanine DNA glycosylases such as Swiss:P53397. The methyl-CPG binding protein MBD4 Swiss:Q9Z2D7 also contains a related domain [1] that is a thymine DNA glycosylase. The family also includes DNA-3-methyladenine glycosylase II EC:3.2.2.21 and other members of the AlkA family. [1]. 10499592. The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites. Hendrich B, Hardeland U, Ng HH, Jiricny J, Bird A;. Nature 1999;401:301-304. [2]. 10706276. Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Bruner SD, Norman DP, Verdine GL;. Nature 2000;403:859-866. (from Pfam)
endonuclease III domain-containing protein
endonuclease III domain-containing protein such as endonuclease III, a DNA repair enzyme that has both DNA N-glycosylase and AP-lyase activities
endonuclease III
This equivalog HMM identifes nth members of the PF00730 superfamily (HhH-GPD: Helix-hairpin-helix and Gly/Pro rich loop followed by a conserved aspartate). The major members of the superfamily are nth and mutY.
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