Literature summary for 2.7.7.48 extracted from

Bakshi, A.; Savithri, H.S.
Functional insights into the role of C-terminal disordered domain of Sesbania mosaic virus RNA-dependent RNA polymerase and the coat protein in viral replication in vivo (2019), Virus Res., 267, 26-35 .

Search for more literature for 2.7.7.48

Activating Compound

Activating Compound	Comment	Organism	Structure
viral protein P10	requirement of the interaction between RNA-dependent RNA polymerase (RdRp) and viral protein P10 via the intrinsically disordered C-terminal domain of RdRp in viral replication and progression of infection in vivo	Sesbania mosaic virus

Protein Variants

Protein Variants	Comment	Organism
additional information	transfection of a mutant icDNA expressing an RdRp lacking the C-terminal disordered domain leads to a drastic reduction in the copy numbers of both forms of viral RNA. This could be due to the loss of interaction between the disordered domain of RdRp and P10 and possibly other viral/host proteins that might be required for the assembly of viral replicase	Sesbania mosaic virus

Organism

Organism	UniProt	Comment	Textmining
Sesbania mosaic virus	Q9EB07	-	-

Synonyms

Synonyms	Comment	Organism
RDRP	-	Sesbania mosaic virus
RNA-dependent RNA polymerase	-	Sesbania mosaic virus

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Release 2023.1 (January 2023)