| Ensembl ID | Symbol | Entrez ID | RBD | RBPome | PRI | Expresion | Pathway | Phenotype | Paralog | Ortholog | GO |
|---|---|---|---|---|---|---|---|---|---|---|---|
This family consists of several scavenger mRNA decapping enzymes (DcpS) and is the N-terminal domain of these proteins. 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.
This entry represents scavenger mRNA decapping enzymes, such as Dcp2 and DcpS. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' mRNA degradation. DcpS uses cap dinucleotides or capped oligonucleotides as substrate to release m(7)GMP (N7-methyl GMP), while Dcp2 uses capped mRNA as substrate in order to hydrolyse the cap to release m(7)GDP (N7-methyl GDP) [PUBMED:16246173]. 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 family contains a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues [PUBMED:16001405]. 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. This family is related to INTERPRO
Liu H, Rodgers ND, Jiao X, Kiledjian M; , EMBO J 2002;21:4699-4708.: The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases. PUBMED:12198172 EPMC:12198172.
