Double-stranded RNA-specific adenosine deaminase converts multiple adenosines to inosinesand creates I/U mismatched base pairs in double-helical RNA substrates without apparent sequencespecificity. DRADA has been found to modify adenosines in AU-rich regions more frequently, probablydue to the relative ease of melting A/U base pairs compared to G/C base pairs. The protein functions tomodify 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. TheDRADA repeat is also found in viral E3 proteins, which contain a double-stranded RNA-binding domain.