Z-DNA-binding domain in adenosine deaminases.
SMART accession number:SM00550
Description: Helix-turn-helix-containing domain. Also known as Zab.
Interpro abstract (IPR000607): Double-stranded RNA-specific adenosine deaminase (EC 3.5) converts multiple adenosines to inosines and creates I/U mismatched base pairs in double-helical RNA substrates without apparent sequence specificity. DRADA has been found to modify adenosines in AU-rich regions more frequently, probably due to the relative ease of melting A/U base pairs compared to G/C base pairs. The protein functions to modify viral RNA genomes, and may be responsible for hypermutation of certain negative-stranded viruses. DRADA edits the mRNAs for the glutamate receptor subunits by site-selective adenosine deamination. The DRADA repeat is also found in viral E3 proteins, which contain a double-stranded RNA-binding domain.
GO function:double-stranded RNA adenosine deaminase activity (GO:0003726), RNA binding (GO:0003723)
Family alignment:
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There are 934 Zalpha domains in 478 proteins in SMART's nrdb database.

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