The THAP domain: a novel protein motif with similarity to the DNA-binding domain of P element transposase

Trends Biochem Sci. 2003 Feb;28(2):66-9. doi: 10.1016/S0968-0004(02)00013-0.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • DNA-Binding Proteins / genetics*
  • DNA-Binding Proteins / metabolism*
  • Drosophila melanogaster / enzymology*
  • Drosophila melanogaster / genetics*
  • Humans
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Transposases / genetics*


  • DNA-Binding Proteins
  • Transposases

Associated data

  • GENBANK/A24786
  • GENBANK/AF081567
  • GENBANK/AF258556
  • GENBANK/AK057453
  • GENBANK/AK091412
  • GENBANK/AL360202
  • GENBANK/BC004346
  • GENBANK/BC008358
  • GENBANK/BC021721
  • GENBANK/BC022081
  • GENBANK/BC022989
  • RefSeq/XM_043054
  • RefSeq/XM_095114