ZalphaZ-DNA-binding domain in adenosine deaminases.
|SMART accession number:||SM00550
||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:||RNA binding (GO:0003723), double-stranded RNA adenosine deaminase activity (GO:0003726)|
There are 334 Zalpha domains in 183 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
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- Structure (3D structures containing this domain)
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