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PROSITE documentation PDOC50141

Adenosine to inosine editase domain profile





Description

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 <PDOC50139>), three double stranded RNA-binding domains (dsRBD) (see <PDOC50137>), 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].

Note:

Editases that deaminate cytidine are not detected by this profile (see <PDOC00702>).

Last update:

December 2001 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

A_DEAMIN_EDITASE, PS50141; Adenosine to inosine editase domain profile  (MATRIX)


References

1AuthorsMaas S. Melcher T. Seeburg P.H.
TitleMammalian RNA-dependent deaminases and edited mRNAs.
SourceCurr. Opin. Cell Biol. 9:343-349(1997).
PubMed ID9159072

2AuthorsSlavov D. Crnogorac-Jurcevic T. Clark M. Gardiner K.
TitleComparative analysis of the DRADA A-to-I RNA editing gene from mammals, pufferfish and zebrafish.
SourceGene 250:53-60(2000).
PubMed ID10854778



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