Adenosine deaminase/editase (IPR002466)

Short name: A_deamin

Overlapping homologous superfamilies


Domain relationships



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 [PMID: 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, 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 terms

Biological Process

GO:0006396 RNA processing

Molecular Function

GO:0003723 RNA binding
GO:0004000 adenosine deaminase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles