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De-MARylation reaction is 16-folder quicker than de-PARylation. ADP-ribose hydrolase activity allows the virus to interfere with the host immune defenses involving poly-ADP-ribose polymerases (PARPs)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045149"}],"value":"Methyltransferase: Displays a capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP. Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m(7)GTP or m(7)GDP. GDP is a better substrate than GTP. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m(7)GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00059569"}],"value":"NTPase/helicase: Multi-functional protein that exhibits NTPase and RNA unwinding activities. Hydrolyzes all NTPs efficiently and unwinds RNA duplexes containing 5' overhangs. Possesses a sequence independent RNA-5'-triphosphatase (RTPase) activity suggestive of its role in forming viral cap structure. Also participates in viral genome replication, RNA translocation and genome packaging/unpackaging"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055240"}],"value":"Putative protease: The putative protease domain although necessary for replication of the virus may not be a protease but rather a structural Zn(2+)-binding domain. Inhibits induction of IFN-beta by MDA5 and RIG-I pathways and down-regulates the expression of MDA5"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046095"}],"value":"RNA-directed RNA polymerase: Plays an essential role in the virus replication. 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