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Scavenger mRNA decapping enzyme C-term binding
This family consists of several scavenger mRNA decapping enzymes (DcpS) and is the C-terminal region. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' decay of an mRNA. The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. The C-terminal domain contains a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues. The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function. [1]. 12198172. The scavenger mRNA decapping enzyme DcpS is a member of the HIT. family of pyrophosphatases.. Liu H, Rodgers ND, Jiao X, Kiledjian M;. EMBO J 2002;21:4699-4708. (from Pfam)
HIT domain-containing protein
histidine triad nucleotide-binding protein
histidine triad nucleotide-binding protein of the histidine triad family of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides
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