InterPro domain: IPR044099

Dcp2 is the catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay [ 1 , 2 ]. Dcp2 contains an all-alpha N-terminal helical domain and a domain which has the Nudix fold. It has been shown that the Nudix domain of both Saccharomyces cerevisiae and S. pombe Dcp2 proteins is sufficient for decapping activity. While decapping is not dependent on the N-terminal of Dcp2, it does affect its efficiency. Dcp1 binds the N-terminal domain of Dcp2 stimulating the decapping activity of Dcp2 [ 3 ].

This entry represents the NUDIX hydrolase domain found in Dcp2. This domain catalyses the mRNA decapping reaction [ 4 ].

1. Decapping reaction of mRNA requires Dcp1 in fission yeast: its characterization in different species from yeast to human. J. Biochem. 136, 805-12
2. Functional characterization of the mammalian mRNA decapping enzyme hDcp2. RNA 9, 1138-47
3. Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe. Nat. Struct. Mol. Biol. 13, 63-70
4. Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J. 21, 6915-24