Abstract
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
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Binding Sites
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DNA-Binding Proteins / genetics*
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DNA-Binding Proteins / metabolism*
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Drosophila melanogaster / enzymology*
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Drosophila melanogaster / genetics*
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Humans
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Molecular Sequence Data
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Protein Binding
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Protein Structure, Tertiary
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Sequence Homology, Amino Acid
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Transposases / genetics*
Substances
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DNA-Binding Proteins
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Transposases
Associated data
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GENBANK/A24786
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GENBANK/AF081567
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GENBANK/AF258556
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GENBANK/AK057453
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GENBANK/AK091412
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GENBANK/AL360202
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GENBANK/BC004346
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GENBANK/BC008358
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GENBANK/BC021721
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GENBANK/BC022081
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GENBANK/BC022989
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RefSeq/XM_043054
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RefSeq/XM_095114