The domain within your query sequence starts at position 244 and ends at position 627; the E-value for the ADEAMc domain shown below is 3.74e-205.

TFHDQIAMLSHRCFNALTNSFQPSLLGRKILAAIIMKRDPEDMGVVVSLGTGNRCVKGDS
LSLKGETVNDCHAEIISRRGFIRFLYSELMKYNHHTAKNSIFELARGGEKLQIKKTVSFH
LYISTAPCGDGALFDKSCSDRAVESTESRHYPVFENPKQGKLRTKVENGEGTIPVESSDI
VPTWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFLQPVYLKSVTLGYLFSQGHLTR
AICCRVTRDGKAFEDGLRYPFIVNHPKVGRVSVYDSKRQSGKTKETSVNWCMADGYDLEI
LDGTRGTVDGPGKELSRVSKKNIFLQFKKLCSFRARRDLLQLSYGEAKKAARDYDLAKNY
FKKSLRDMGYGNWISKPQEEKNFY

ADEAMc

tRNA-specific and double-stranded RNA adenosine deaminase (RNA-specific editase)
ADEAMc
SMART accession number:SM00552
Description: -
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:adenosine deaminase activity (GO:0004000), RNA binding (GO:0003723)
Family alignment:
View or

There are 1742 ADEAMc domains in 1742 proteins in SMART's nrdb database.

Click on the following links for more information.