InterPro domain: IPR032867

This entry represents a highly conserved C-terminal DYW domain found in some plant pentatricopeptide repeat (PPR) proteins [ 1 ]. This domain contains a characteristic zinc binding motif (CXXC, HXE), which has been shown to bind zinc ions. The glutamate residue of the HXE motif is catalytically required in the reaction catalysed by cytidine deaminase [ 2 ]. This domain is required for RNA editing, a process that deaminates specific cytidines (C) to uridines (U) [ 3 , 4 , 4 ].

1. A conserved DYW domain of the pentatricopeptide repeat protein possesses a novel endoribonuclease activity. FEBS Lett. 582, 4163-8
2. A conserved glutamate residue in the C-terminal deaminase domain of pentatricopeptide repeat proteins is required for RNA editing activity. J. Biol. Chem. 290, 10136-42
3. Cytidine deaminase motifs within the DYW domain of two pentatricopeptide repeat-containing proteins are required for site-specific chloroplast RNA editing. J. Biol. Chem. 290, 2957-68
4. RNA editing in plants: Machinery and flexibility of site recognition. Biochim. Biophys. Acta 1847, 779-85