Roussigne, M., Kossida, S., Lavigne, A.C., Clouaire, T., Ecochard, V., Glories, A., Amalric, F., Girard, J.P. (2003). The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase.  Trends Biochem. Sci. 28(2): 66--69.

FBrf0156066

Review

We have identified a novel evolutionarily conserved protein motif - designated the THAP domain - that defines a new family of cellular factors. We have found that the THAP domain presents striking similarities with the site-specific DNA-binding domain (DBD) of Drosophila P element transposase, including a similar size, N-terminal location, and conservation of the residues that define the THAP motif, such as the C2CH signature (Cys-Xaa(2-4)-Cys-Xaa(35-50)-Cys-Xaa(2)-His). Our results suggest that the THAP domain is a novel example of a DBD that is shared between cellular proteins and transposases from mobile genomic parasites.