Vaccinia virus, the prototypic poxvirus, possesses a double-stranded DNA genome of 191,686 base pairs
capable of encoding approximately 200 proteins. Virion enzymes produce mature viral mRNA with eukaryotic features,
including a 5' cap and a 3' poly(A) tail. V. virus mRNA capping enzyme is a multifunctional protein with RNA triphosphatase, RNA guanylyltransferase, RNA
(guanine-7) methyltransferase, and transcription termination factor activities. The protein is a heterodimer of 95kDa and 33kDa
subunits encoded by the v.virus D1 and D12 genes, respectively. The capping reaction entails transfer of GMP from
GTP to the 5'-diphosphate end of mRNA via a covalent enzyme-(lysyl-GMP) intermediate.
Higman MA, Christen LA, Niles EG.
The mRNA (guanine-7-)methyltransferase domain of the vaccinia virus mRNA capping enzyme. Expression in Escherichia coli and structural and kinetic comparison to the intact capping enzyme.
J. Biol. Chem. 269 1994 14974-81
[PubMed: 8195132] http://intl.jbc.org/cgi/content/abstract/269/21/14974