{PDOC50141} {PS50141; A_DEAMIN_EDITASE} {BEGIN} *********************************************** * Adenosine to inosine editase domain profile * *********************************************** Editase (EC 3.5.4.-) are enzymes that catalyze the site-selective deamination of adenosine residue into inosine within double stranded regions of mRNA. In mRNA inosine is read as guanosine by the translation apparatus, resulting in codon changes within the synthesized protein. The editase domain contains the active site and binds three zinc atoms [1]. Several editases share a common global arrangement of domains. Hence, the DRADA proteins contain two DRADA repeats (see ), three double stranded RNA-binding domains (dsRBD) (see ), and one editase domain from N- to C-terminus, while the RED1 and RED2 editases have a simplified domains structure with no DRADA repeat and only two dsRBD [2]. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Note: Editases that deaminate cytidine are not detected by this profile (see ). -Last update: December 2001 / First entry. [ 1] Maas S., Melcher T., Seeburg P.H. "Mammalian RNA-dependent deaminases and edited mRNAs." Curr. Opin. Cell Biol. 9:343-349(1997). PubMed=9159072 [ 2] Slavov D., Crnogorac-Jurcevic T., Clark M., Gardiner K. "Comparative analysis of the DRADA A-to-I RNA editing gene from mammals, pufferfish and zebrafish." Gene 250:53-60(2000). PubMed=10854778 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}