InterPro domain: IPR033925

This domain is found at the C terminus of the DNA repair and recombination protein Rad51 and some Rad51-like proteins. It is critical for DNA binding [ 1 ]. Rad51 is a homologue of the bacterial RecA protein. Rad51 and RecA share a core ATPase domain.

Rad51-like genes form two separate groups (RAD-alpha and RAD-beta), each of which contains both archaeal and eukaryotic members [ 2 ]. This group of recombinases includes the eukaryotic proteins Rad51, Rad57, the meiosis-specific protein DMC1, and the archaeal protein RadA. They are closely related to the bacterial RecA group [ 3 ]. Rad51 proteins catalyze a similar recombination reaction as RecA, using ATP-dependent DNA binding activity and a DNA-dependent ATPase. However, this reaction is less efficient and requires accessory proteins such as Rad55/57 [ 4 , 5 ].

1. Gly-103 in the N-terminal domain of Saccharomyces cerevisiae Rad51 protein is critical for DNA binding. J. Biol. Chem. 280, 26303-11
2. Origins and evolution of the recA/RAD51 gene family: evidence for ancient gene duplication and endosymbiotic gene transfer. Proc. Natl. Acad. Sci. U.S.A. 103, 10328-33
3. DNA repair systems in archaea: mementos from the last universal common ancestor? J. Mol. Evol. 49, 474-84
4. Assembly of RecA-like recombinases: distinct roles for mediator proteins in mitosis and meiosis. Proc. Natl. Acad. Sci. U.S.A. 98, 8411-8
5. Rad51/RecA protein families and the associated proteins in eukaryotes. Mutat. Res. 435, 13-21