| Type: | Domain | Name: | Vaccinia virus D10, N-terminal |
| Description: | This domain is found on the N terminus of the viral protein D10 (VD10) and the related MutT motif proteins []. The VD10 protein is probably essential for virus replication [] and is often found to the N terminus of a NUDIX hydrolase domain. Previous studies indicated that the vaccinia virus D10 protein, which is conserved in all sequenced poxviruses, participates in the rapid turnover of host and viral mRNAs. D10 contains a motif present in the family of Nudix/MutT enzymes, a subset of which has been shown to enhance mRNA turnover in eukaryotic cells through cleavage of the 5' cap (m7GpppNm-). The D10 protein possesses an intrinsic activity that liberates m7GDP from capped RNA substrates. Furthermore, point mutations in the Nudix/MutT motif abolished decapping activity. D10 has a strong affinity for capped RNA substrates of lengths of 24-309 nt were decapped efficiently. The poxviruses represent the only virus family shown to encode a Nudix hydrolase-decapping enzyme. The activity of the decapping and capping enzymes, accelerate mRNA turnover and helps to eliminate competing host mRNAs allowing stage-specific synthesis of viral proteins []. | Short Name: | Vaccinia_D10_N |
