ADEAMctRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase)
|SMART accession number:||SM00552
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|Interpro abstract (IPR002466):
||Editase (EC 3.5) are enzymes that alter mRNA by catalyzing the site-selective deamination of adenosine residue into inosine residue. The editase domain contains the active site and binds three Zn atoms [(PUBMED:9159072)]. Several editases share a common global arrangement of domains, from N to C terminus: two 'double-stranded RNA-specific adenosine deaminase' (DRADA) repeat domains (IPR000607), followed by three 'double-stranded RNA binding' (DsRBD) domains (IPR001159), followed by the editase domain. Other editases have a simplified domains structure with no DRADA_REP and possibly fewer DSRBD domains. Editase that deaminate cytidine are not detected by this signature.
|GO process:||RNA processing (GO:0006396)|
|GO function:||RNA binding (GO:0003723), adenosine deaminase activity (GO:0004000)|
There are 596 ADEAMc domains in 594 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
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