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XB-ART-24252
Biochem Biophys Res Commun 1991 Dec 31;1813:1231-7.
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Molecular cloning of human XPAC gene homologs from chicken, Xenopus laevis and Drosophila melanogaster.

Shimamoto T , Kohno K , Tanaka K , Okada Y .


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We cloned homologs of the human Xeroderma Pigmentosum Group A complementing (XPAC) gene from chicken, Xenopus laevis and Drosophila melanogaster. A comparison of the amino acid sequences of these homologs with that of the human XPAC protein revealed that in the NH2-terminal domain there are only two conserved regions, one of which is presumed to function as the nuclear localization signal, whereas the COOH-terminal domain is highly conserved, the frequency of identical amino acids in all four XPAC proteins being 50%, and the four cysteine residues predicted to form a zinc-finger motif, and three other cysteine residues are all conserved. These results strongly suggest that the COOH-terminal domain containing a zinc-finger motif plays an important role in the function of these proteins.

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