The domain within your query sequence starts at position 1 and ends at position 176; the E-value for the A_deamin domain shown below is 1.3e-49.



PFAM accession number:PF02137
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, 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)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry A_deamin