| Primary Identifier | IPR011145 | Type | Homologous_superfamily |
| Short Name | Scavenger_mRNA_decap_enz_N |
| description | This superfamily represents the N-terminal domain of 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) []. 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. DcpS exists as a dimer and each monomer is comprised of an N-terminal and a C-terminal region. The two N-termini form into a domain-swapped dimer and carry out substrate binding, cap dinucleotide, and hydrolysis []. |
