| First Author | Roussigne M | Year | 2003 |
| Journal | Trends Biochem Sci | Volume | 28 |
| Issue | 2 | Pages | 66-9 |
| PubMed ID | 12575992 | Mgi Jnum | J:235859 |
| Mgi Id | MGI:5803834 | Doi | 10.1016/S0968-0004(02)00013-0 |
| Citation | Roussigne M, et al. (2003) The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase. Trends Biochem Sci 28(2):66-9 |
| abstractText | 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. |
