Figure 1

Domain structure of DExH/D helicases involved in viral replication. Upper rectangle: RNA helicases of the RIG-I-like receptor family are components of the innate antiviral response that attenuates viral replication. Lower rectangle: RNA helicases that promote viral replication. Protein sequences were retrieved from the NCBI conserved domains database and domains determined by annotation and query of the Uniprot database. The predicted molecular weight (kDa) and number of amino acid residues (aa) are indicated. Jagged edges indicate interruption by additional sequence or domains. Domains are: CARD, Caspase-activation and recruitment domain; DExDc, DEAD-like helicase superfamily ATP binding domain; HELICc, Helicase superfamily C-term domain associated with DExH/D box proteins; RIG-I_CRD, Regulatory domain of RIG-I; RS/GYR, Arginine/serine, glycine tyrosine-rich domain; dsRBD, Double-stranded RNA binding domain; HA2, Helicase-associated domain of unknown function; DUF, Domain of unknown function; RG-rich, arginine and glycine-rich domain; SPRY, SP1a and RYanodine receptor domain; p68HR, Characteristic of p68-like RNA helicase; Peptidase_S29, serine protease domain with trypsin-like fold; Poty_PP, Observed in polyproteins of the Potyviridae.