DCPS (gene)
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| Scavenger mRNA decapping enzyme (DcpS) N-terminal | |||||||||
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| File:PDB 1vlr EBI.jpg
crystal structure of mrna decapping enzyme (dcps) from mus musculus at 1.83 a resolution
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| Identifiers | |||||||||
| Symbol | DcpS | ||||||||
| Pfam | PF05652 | ||||||||
| InterPro | IPR008594 | ||||||||
| SCOP | 1st4 | ||||||||
| SUPERFAMILY | 1st4 | ||||||||
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| Scavenger mRNA decapping enzyme C-term binding | |||||||||
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| Identifiers | |||||||||
| Symbol | DcpS_C | ||||||||
| Pfam | PF11969 | ||||||||
| Pfam clan | CL0265 | ||||||||
| SCOP | 1st4 | ||||||||
| SUPERFAMILY | 1st4 | ||||||||
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Scavenger mRNA-decapping enzyme DcpS is a protein that in humans is encoded by the DCPS gene.[1][2][3]
The scavenger mRNA decapping enzymes include 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 substrates to release m(7)GMP (N7-methyl GMP), while Dcp2 uses capped mRNA as a substrate in order to hydrolyse the cap to release m(7)GDP (N7-methyl GDP).[4] 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 in its C-terminal domain, with three histidines separated by hydrophobic residues.[5] 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.
References
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Further reading
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This article incorporates text from the public domain Pfam and InterPro IPR008594
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