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evolution
the enzyme belongs to the RDR gene family, phylogenetic analysis of RDR genes present in potato and in a range of other plant species, overview
drug target
MN908947
important target for design of antiviral drugs against 2019-nCoV
drug target
the high sequence conservation between SARS-CoV RNA-dependent RNA polymerase (RdRp) and SARS-CoV-2 RNA polymerase makes it very likely that any potent agents developed for the SARS-CoV RdRp will exhibit equal potency and efficacy on the SARS-CoV-2 enzyme
drug target
MN908947
the high sequence conservation between SARS-CoV RNA-dependent RNA polymerase (RdRp) and SARS-CoV-2 RNA polymerase makes it very likely that any potent agents developed for the SARS-CoV RdRp will exhibit equal potency and efficacy on the SARS-CoV-2 enzyme
drug target
analysis of the enzyme as a potential therapeutic drug target using a computational approach. Targeting the RdRpactive sites, ASP760 and ASP761, by antiviral drugs could be a potential therapeutic option for inhibition of coronavirus RdRp, and thus viral replication. Target-based virtual screening and molecular docking results show that the antiviral Galidesivir and its structurally similar compounds show promise against SARS-CoV-2. CID123624208 and CID11687749 may be considered for in vitro and in vivo clinical trials
drug target
cryo-electron microscopy structure of the SARS-CoV-2 RNA-dependent RNA polymerase provides insights into the mechanism of viral RNA replication and a rational template for drug design to combat the viral infection
drug target
drug target for COVID-19
drug target
FDA approved library of drugs are docked against the active site of the enzyme (RdRp) using Schrodinger's computer-aided drug discovery tools for in silico drug-repurposing. In molecular dynamics simulations, pitavastatin, ridogrel and rosoxacin displayed superior binding with the active site through Arg555 and Mg2+
drug target
inhibition of the viral RNA-dependent RNA polymerase (RdRp) to resolve chronic infection is a useful therapeutic strategy against Hepatitis C virus
drug target
RNA-dependent RNA polymerase inhibitors are prospective therapeutics against SARS-CoV-2
drug target
SARS-CoV-2 polymerase is a key drug target for COVID-19
drug target
search for drugs that target RNA-dependent RNA polymerase (RdRp) by in silico screening of the U.S. Food and Drug Administration approved drug library. Well-tolerated and widely used drugs are selected for molecular dynamics simulations to evaluate drug-protein interactions and their persistence under physiological conditions. Eltrombopag, tipranavir, ergotamine, and conivaptan bind to the enzyme with high binding free energies
drug target
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since virally-encoded RNA-dependent RNA polymerases of RNA viruses synthesizes new genomes in the infected host they are prime targets for antiviral therapy
drug target
systemic discussion of the pharmacological therapeutics targeting RNA-dependent RNA polymerase (RdRp)
drug target
target for antiviral drugs
drug target
the enzyme (RdRp) of the SARS-CoV-2 RNA virus represents the most optimal target for an antiviral drug. Linear amino acid sequence as well as molecule structure show the highest homology to RdRps of other positive-sense RNA viruses. It is highly predictable that an antiviral developed for an RNA virus with a genome of the same polarity (i.e. Sofosbuvir for Hepatitis C virus) could have a higher inhibitory efficacy against the SARS-CoV-2, compared to antiviral developed for negative-sense RNA viruses
drug target
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the enzyme is a key target for the development of antiviral agents against Norwalk virus gastroenteritis
drug target
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the enzyme is considered as a promising target for specific antiviral therapeutics
drug target
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the enzyme is considered as a promising target for specific antiviral therapeutics
drug target
the enzyme plays a crucial role in SARS-CoV-2 replication, and thus could be a potential drug target. Comprehensive computational approaches including drug repurposing and molecular docking are employed to predict an effective drug candidate targeting RdRp of SARS-CoV-2. This study reveales that Rifabutin, Rifapentine, Fidaxomicin, 7-methyl-guanosine-5'-triphosphate-5'-guanosine and Ivermectin have a potential inhibitory interaction with RNA-dependent RNA polymerase (RdRp) of SARS-CoV-2 and could be effective drugs for COVID-19. Virtual screening of the compounds from ZINC database allow the prediction of two compounds (ZINC09128258 and ZINC09883305) with pharmacophore features that interact effectively with RdRp of SARSCoV-2, indicating their potentiality as effective inhibitors of the enzyme. Comparative structural analysis of protein-inhibitor complexes reveals that the amino acids Y32, K47, Y122, Y129, H133, N138, D140, T141, S709 and N781 are crucial for drug surface hotspot in the RdRp of SARS-CoV-2
drug target
the structural characteristics of the catalytic domain of the RNA-dependent RNA polymerase are explored using a computational pharmacology method. Ligand-binding characteristics of the binding site are determined using a receptor-ligand function-site interaction fingerprint strategy. Binding characteristics determined by this method help to rationalize RNA-dependent RNA polymerase-targeted drug discovery and provide insights into the specific binding mechanisms important for containing the SARS-CoV-2 virus
drug target
the viral RNA-dependent-RNA-polymerase (RdRp) is a target with polymerase inhibitors successfully used for the treatment of several viral diseases
malfunction
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D-elp1 depletion inhibits RNAi in S2 cells but does not affect micro RNA function. In D-elp1 null third instar larvae transposon RNA levels are also increased and the corresponding transposon antisense RNAs are reduced
malfunction
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impairing the nuclear import of PB2 by mutating its nuclear localization signal leads to abnormal formation of the trimeric polymerase in the cytoplasm
malfunction
mutations in the hepatitis C virus polymerase that increase RNA binding can confer resistance to cyclosporine A, an inhibitor that is used as therpeutic against HCV-induced acute and chronic liver disease
malfunction
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RRF-3 mutation is involved in compromised spermatogenesis, that accounts for reduced brood size and X-chromosome loss from rrf-3 mutant hermaphrodites
malfunction
in deletion strains of the RNA-dependent RNA polymerase RrpC, full-length and shorter retrotransposable element DIRS-1 (Dictyostelium intermediate repeat sequence 1) messenger RNAs are strongly enriched, shorter versions of long non-coding RNA in DIRS-1 antisense orientation are also enriched in rrpC- strains. DIRS-1 misregulation in the absence of RrpC leads to retrotransposon mobilization
malfunction
silencing SlRDR1 using virus-induced gene silencing system significantly reduces SlRDR1 expression and tomato defense against tobacco mosaic virus but has no evident effect on alternative oxidase SlAOX1a transcription
malfunction
StRDR1 transcript accumulation decreases in transgenic potato plants constitutively expressing a hairpin construct. These plants when challenged with three viruses, potato virus Y, potato virus X, and tobacco mosaic virus show no increase in the susceptibility of potato to these viruses. Suppression of StRDR1 gene expression does not increase in the susceptibility to the viruses
malfunction
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suppression of Nicotiana benthamiana canonical 9-zinc finger transcription factor TFIIIA-7ZF reduces PSTVd replication, and overexpression of TFIIIA-7ZF enhances PSTVd replication in planta
malfunction
inhibition of RDR1c1/c2 expression leads to increased virus accumulation
malfunction
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in deletion strains of the RNA-dependent RNA polymerase RrpC, full-length and shorter retrotransposable element DIRS-1 (Dictyostelium intermediate repeat sequence 1) messenger RNAs are strongly enriched, shorter versions of long non-coding RNA in DIRS-1 antisense orientation are also enriched in rrpC- strains. DIRS-1 misregulation in the absence of RrpC leads to retrotransposon mobilization
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malfunction
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RRF-3 mutation is involved in compromised spermatogenesis, that accounts for reduced brood size and X-chromosome loss from rrf-3 mutant hermaphrodites
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metabolism
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key enzyme involved in vrial replication
metabolism
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Pol IV functions independently of the small RNA accumulation facilitated by RMR1 and RDR2. RMR1, RNA-directed DNA methylation factor, acts upstream of the RNA-dependent RNA polymerase, RDR2. While transposon-like sequences may be a common target of the maize RdDM pathway, the RMR1 and RDR2 proteins act differently with respect to their roles in mediating the type of trans-regulation induced by inverted repeats
metabolism
the salicylic acid-induced viral defense in plants is distinct from the pathways mediating bacterial and fungal defense, which is pathogenesis-related protein-independent but involves an RNA-dependent RNA polymerase 1 (RDR1)-mediated RNA silencing mechanism and/or an alternative oxidase (AOX)-associated defense pathway. As the RDR1-mediated RNA silencing pathway and the AOX-regulated pathway are both involved in the salicylic acid-induced defense against viruses but are independent of pathogenesis-related protein genes, crosstalk between these two antiviral pathways may exist
metabolism
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key enzyme involved in vrial replication
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physiological function
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D-elp1 is required for RNA interference, interacts with Dcr-2 protein, and has a role in transposon suppression, overview. It might be interacting with components of the RISC
physiological function
Q9LKP0
RDR6 functions in trans-acting short interfering RNA, ta-siRNA, production. Positive regulators or effectors of SI and pistil development are regulated by ta-siRNAs, regulation, overview
physiological function
Cystovirus phi6
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RdRps are unique in that they create dsRNA by initiating polymerization at the 3' end of the substrate
physiological function
RDRs play a key role in RNA silencing, heterochromatin formation and natural gene regulation. It may play an important role in response to biotic and abiotic stresses
physiological function
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RRF-3 is required for spermatocyte cell division, overview
physiological function
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small RNA deep sequencing reveals a functional role for RDR in promoting viral siRNA biogenesis through distinct mechanisms, overview. RDR1and RDR6 are also implicated in antiviral defense
physiological function
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the enzyme is required for replication of the genomes of positive-strand RNA viruses occuring in highly oligomeric complexes on the cytosolic surfaces of the intracellular membranes of infected host cells
physiological function
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the enzyme is required for the RNA-directed DNA methylation, dedicated to the methylation of target sequences, which include transposable elements, regulatory regions of several protein-coding genes, and 5S rRNA-encoding DNA arrays. Pol IV, RDR2, DRM2, and Pol V, actors of the RdDM, are required to maintain a transcriptional silencing of 5S RNA genes at chromosomes 4 and 5, regulation, overview
physiological function
the enzyme is responsible for replication and transcription of the eight separate segments of the viral RNA genome in the nuclei of infected cells
physiological function
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the FHV RNA-dependent RNA polymerase, protein A, is the only viral protein necessary for genome replication in the budding yeast Saccharomyces cerevisiae
physiological function
expression in Drosophila melanogaster enhances transitive dsRNA-dependent silencing
physiological function
expression in Drosophila melanogaster triggers transcriptional silencing of unpaired DNA during embryonic mitosis. Isoform ego-1 triggers dsRNA-independent silencing, specifically of transgenes. The strain w, da-Gal4, UAST-ego-1, constitutively expressing ego-1, is capable of silencing transgene including dsRNA hairpin upon a single cross
physiological function
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isoform RDR6 acts in the biogenesis of various types and sizes of small RNAs. An rdr6-1 mutant, which is temperature sensitive and shows spikelet defects, displays reduced accumulation of trans-acting siR-auxin response factors, the conserved trans-acting siRNAs derived from the TAS3 locus, and ectopic expression of trans-acting siR-auxin response factors target genes. 21-Nucleotide phased small RNAs are also largely dependent on isoform RDR6. Isoform RDR6 has a strong impact on the accumulation of 24-nt phased small RNAs, but not on unphased ones
physiological function
isoform RDR6 is required for efficient hpRNA-induced RNA silencing in plants. Generation of wild-type and rdr6-11 Arabidopsis thaliana lines expressing green fluorescent protein and transformation with a green fluorescent protein-RNA interference construct leads to almost complete silencing of green fluorescent protein expression in the T1 generation of most green fluorescent protein-RNAi-transformed wild-type lines, whereas various levels of green fluorescent protein expression remain among the green fluorescent protein-RNAi-transformed rdr6-11 lines. Homozygous expression of green fluorescent protein-RNAi in the T3 generation is not sufficient to induce complete green fluorescent protein silencing in several rdr6-11 lines
physiological function
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Nicotiana benthamiana transformed with isoform RDR1 from Nicotiana tabacum exhibits hypersusceptibility to plum pox potyvirus and other viruses, resembling RDR6-silenced Nicotiana benthamiana. Nicotiana tabacum-RDR1 possesses silencing suppression activity and does not interfere with isoform RDR6-dependent siRNA accumulation but turns out to suppress RDR6-dependent sense-transgenes Isoform RDR1 might have a dual role, contributing, on one hand, to salicylic acid-mediated antiviral defense, and suppressing, on the other hand, the RDR6-mediated antiviral RNA silencing
physiological function
systematic analysis of susceptibility and small RNA formation in Arabidopsis mutants lacking combinations of RNA-dependent RNA polymerase isoforms and dicer-like proteins. The vast majority of turnip mosaic virus-derived small interfering RNAs are dependent on dicer-like protein isoform DCL4 and RNA polymerase isoform RDR1, although full antiviral defense also requires isoforms DCL2 and RDR6. DCL4 is sufficient for antiviral silencing in inoculated leaves, but isoforms DCL2 and DCL4 are both involved in silencing in systemic tissues. Basal levels of antiviral RNA silencing and siRNA biogenesis are detected in mutants lacking isoforms RDR1, RDR2, and RDR6, indicating an alternate route to form double-stranded RNA that does not depend on the three previously characterized RNA-dependent RNA polymerase proteins
physiological function
cellular RNA-dependent RNA polymerases catalyze synthesis of double-stranded RNAs that can serve to initiate or amplify RNA silencing. Enzyme RDR1 contributes to basal virus resistance in several plants
physiological function
enzyme RDR1 is involved in the AOXmediated defense pathway against tobacco mosaic virus infection and plays a crucial role in enhancing RNA silencing to limit virus systemic spread
physiological function
mechanism of viruses attacking hosts whereby picornaviral 3D polymerase (3Dpol) enters the nucleus and targets the central pre-mRNA processing factor 8 (Prp8) to block premRNA splicing and mRNA synthesis. The 3Dpol inhibits the second catalytic step of the splicing process, resulting in the accumulation of the lariat-form and the reduction of the mRNA. 3Dpol inhibits intracellular pre-mRNA splicing by interacting with Prp8, modelling, overview
physiological function
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negative-sense RNA viruses, such as influenza, encode large, multidomain RNA-dependent RNA polymerases that can both transcribe and replicate the viral RNA genome. Replication occurs through de novo initiation and involves a complementary RNA intermediate
physiological function
P2, an RNA-directed polymerase (RdRp), is the critical component of a four-protein polymerase complex (PX) that includes in addition to P2, the major capsid protein, P1, a packaging NTPase, P4, and an accessory protein, P71. P2 performs the dual tasks of transcription and replication de novo without the use of a primer (i. e. P2 is a self-priming RdRp), and plays a critical role in the cystoviral life cycle
physiological function
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probing of the entire Dengue genome for interactions via Y3H with viral RNA-dependent RNA polymerase reveals a dominant interaction as a loop-forming ACAG motif in the 3' positive-stranded terminus, RdRp recognizes the top loop of 3'-SL in both genomic forms, interactions sites coincides with known flaviviral recombination sites inside the viral protein-coding region. Specific recognition of the RNA element occurs via an arginine patch in the C-terminal thumb domain of enzyme RdRp. Disruption of the interaction results in loss of viral replication ability in cells. This unique RdRp-RNA interface is found throughout flaviviruses
physiological function
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RNA polymerase II acts as an RNA-dependent RNA polymerase to extend and destabilize a non-coding RNA. Mammalian Pol II acts as an RdRP to control the stability of a cellular RNA by extending its 3'-end. Extended B2 RNA can repress transcription, but with decreased potency
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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segment 2 (S2)-encoded RNA-dependent RNA polymerase (RdRp) helps the virus to propagate its genome in the host cell of the silkworm, Antheraea mylitta
physiological function
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the DNA-dependent RNA polymerase (DdRP) from Potato spindle tuber viroid (PSTVd) RNA genome in Solanum lycopersicum possesses RNA-dependent RNA polymerase activity. A land plant-specific transcription factor directly enhances transcription of a pathogenic noncoding RNA template by DNA-dependent RNA polymerase II
physiological function
the RNA-dependent RNA polymerase activity resides in the C-terminal two-thirds of non-structural protein (NS) 5 responsible for the de novo synthesis of the viral RNA genome. RdRp specifically binds to the viral UTR
physiological function
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the RNA-dependent RNA polymerase of rice stripe virus is critical for both the transcription and replication of the viral genome
physiological function
the RNA-dependent RNA polymerase RrpC silences the centromeric retrotransposon DIRS-1 post-transcriptionally and is required for the spreading of RNA silencing signals. RrpC is a key player in the silencing of centromeric retrotransposon DIRS-1. RrpC acts at the post-transcriptional level and is involved in spreading of RNA silencing signals, both in the 5' and 3' directions
physiological function
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viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription
physiological function
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viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription
physiological function
essential enzyme for viral RNA replication
physiological function
essential enzyme of the coronaviral replication/transcription machinery. It catalyzes the synthesis of coronavirus RNA
physiological function
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expression of rabbit calicivirus RNA-dependent RNA polymerase induces a redistribution of both cis/medial and medial/trans Golgi membrane markers, but not that of an endoplasmic reticulum membrane marker
physiological function
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Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
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Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
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Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
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Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
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Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
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Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
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Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
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Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to ex0ecient genomic RNA replication
physiological function
key enzyme responsible for the SARS-CoV-2 replication process, catalyzes the synthesis of complementary minus strand RNA and genomic plus strand RNA
physiological function
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potyviral RNA-dependent RNA polymerase NIb plays key roles in diverse virus-host interactions. It recruits several host proteins into the viral replication complexes (VRCs), which are essential for the formation of functional VRCs for virus multiplication, and interacts with the sumoylation pathway proteins to suppress NPR1-mediated immunity response. NIb serves as a target of selective autophagy as well as an elicitor of effector-triggered immunity, resulting in attenuated virus infection
physiological function
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potyviral RNA-dependent RNA polymerase NIb plays key roles in diverse virus-host interactions. It recruits several host proteins into the viral replication complexes (VRCs), which are essential for the formation of functional VRCs for virus multiplication, and interacts with the sumoylation pathway proteins to suppress NPR1-mediated immunity response. NIb serves as a target of selective autophagy as well as an elicitor of effector-triggered immunity, resulting in attenuated virus infection
physiological function
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potyviral RNA-dependent RNA polymerase NIb plays key roles in diverse virus-host interactions. It recruits several host proteins into the viral replication complexes (VRCs), which are essential for the formation of functional VRCs for virus multiplication, and interacts with the sumoylation pathway proteins to suppress NPR1-mediated immunity response. NIb serves as a target of selective autophagy as well as an elicitor of effector-triggered immunity, resulting in attenuated virus infection
physiological function
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potyviral RNA-dependent RNA polymerase NIb plays key roles in diverse virus-host interactions. It recruits several host proteins into the viral replication complexes (VRCs), which are essential for the formation of functional VRCs for virus multiplication, and interacts with the sumoylation pathway proteins to suppress NPR1-mediated immunity response. NIb serves as a target of selective autophagy as well as an elicitor of effector-triggered immunity, resulting in attenuated virus infection
physiological function
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RNA-dependent RNA polymerase 6 is a core component of the small RNA biogenesis pathway. Based on its core role in small RNA processing, it plays an important role in plant development and immunity. The enzyme plays an important role in DNA methylation. It contributes to double-strand break formation in meiosis
physiological function
RNA-dependent RNA polymerase is a critical enzyme for coronavirus replication
physiological function
RNA-dependent RNA polymerase is a key enzyme which regulates the viral replication of SARS-CoV-2
physiological function
the enzyme (RdRP) is essential for both transcription and replication of the viral RNA genome
physiological function
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the enzyme catalyzes the replication of the hepatitis C virus genome
physiological function
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the enzyme induces a rearrangement of the Golgi network. Inactivating mutations in the conserved GDD motif do not abolish the ability of Rabbit haemorrhagic disease virus RNA-dependent RNA polymerase to rearrange the Golgi network, suggesting that polymerase activity and metal co-factors are not required for this function
physiological function
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the enzyme is central for viral genome replication
physiological function
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the enzyme is central for viral genome replication
physiological function
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the enzyme is essential for replicating the genome of the virus
physiological function
the enzyme plays a crucial role in plant defence against viruses
physiological function
the enzyme plays a crucial role in plant defence against viruses. A constitutive high level of RDR1b gene expression independent of salicylic acid is associated with broad virus resistance
physiological function
the enzyme plays a crucial role in SARS-CoV-2 replication
physiological function
the enzyme plays a key role in the replication of SARS-CoV-2
physiological function
the nsp12 (RdRp) is a central component of SARS-CoV-2 replication/transcription machinery. It catalyzes the synthesis of a complementary RNA strand using the virus RNA template with the assistance of nsp7 and nsp8 as cofactors
physiological function
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virally-encoded RNA-dependent RNA polymerases of RNA viruses synthesizes new genomes in the infected host
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
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physiological function
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the RNA-dependent RNA polymerase RrpC silences the centromeric retrotransposon DIRS-1 post-transcriptionally and is required for the spreading of RNA silencing signals. RrpC is a key player in the silencing of centromeric retrotransposon DIRS-1. RrpC acts at the post-transcriptional level and is involved in spreading of RNA silencing signals, both in the 5' and 3' directions
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physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
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physiological function
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the enzyme is responsible for replication and transcription of the eight separate segments of the viral RNA genome in the nuclei of infected cells
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physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
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physiological function
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RRF-3 is required for spermatocyte cell division, overview
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physiological function
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mechanism of viruses attacking hosts whereby picornaviral 3D polymerase (3Dpol) enters the nucleus and targets the central pre-mRNA processing factor 8 (Prp8) to block premRNA splicing and mRNA synthesis. The 3Dpol inhibits the second catalytic step of the splicing process, resulting in the accumulation of the lariat-form and the reduction of the mRNA. 3Dpol inhibits intracellular pre-mRNA splicing by interacting with Prp8, modelling, overview
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additional information
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efficient polymerase assembly is a limiting factor in the viability of reassortant viruses, mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview
additional information
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the RNA polymerase of influenza virus is a heterotrimeric complex of PB1, PB2 and PA subunits, which cooperate in the transcription and replication of the viral genome
additional information
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overall enzyme structure analysis from crystal structure, PDB ID 1WNE. Structure solution of RdRP-RNA-rNTP complexes, overview
additional information
overall enzyme structure analysis from crystal structure, PDB ID 3ZED. Structure solution of RdRP-RNA-rNTP complexes, open and closed conformations of the B-loop in IBDV VP, overview
additional information
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overall enzyme structure analysis from crystal structure, PDB IDs 2PUS and 2R70. Structure solution of RdRP-RNA-rNTP complexes, conformational changes in the B-loop of RdRP, overview
additional information
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overall enzyme structure analysis from crystal structure, PDB IDs 2XXD and 4E76. Structure solution of RdRP-RNA-rNTP complexes, overview
additional information
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overall enzyme structure analysis from crystal structure, PDB IDs 3N6L, 3N6N, and 3N6M, conformational changes in the B-loop of RdRP. Structure solution of RdRP-RNA-rNTP complexes, overview
additional information
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overall enzyme structure analysis from crystal structures, PDB IDs 1SH0, 3BSO, and 1SH3. Structure solution of RdRP-RNA-rNTP complexes, conformational changes in the B-loop of RdRP, overview
additional information
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phase-distributed sRNAs are identified within the dsRNA-seq read-covered regions. sRNA sequences from Col-0 (GSM121455, GSM154336, and GSM154375) are mapped onto the sequence regions with two or more phase-distributed, RDRdependent sRNA loci
additional information
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polymerase FluPol is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase active site, whereas PB2 and PA/P3 contain, respectively, cap-binding and endonuclease domains required for transcription initiation by cap-snatching. Comparison of apo-FluPolC with promoter-bound FluPolA, overview
additional information
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seven RdRP elongation complex structures derived from a crystal lattice that allows three RdRP nucleotide addition cycle (NAC) events. NTP recognition and translocation mechanisms in viral RdRPs and uniqueness of the viral RdRPs compared with other processive polymerases, modelling, overview. Determination of initial NTP binding, active site closure, and, in particular the RNA motion during translocation that shows an asymmetric movement of the two strands in the template-product duplex
additional information
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several structural states of the poliovirus RdRP nucleotide addition cycle (NAC) reveal a unique palm domain-based active site closure mechanism and propose a six-state NAC model including a hypothetical state representing translocation intermediates. NTP recognition and translocation mechanisms in viral RdRPs and uniqueness of the viral RdRPs compared with other processive polymerases, modelling, overview
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structure of P2, the self-priming RdRp from cystovirus phi12, crystal structure analysis, overview. The tunnel through which template ssRNA accesses the active site is partially occluded by a flexible loop; this feature, along with sub-optimal positioning of other structural elements that prevent the formation of a stable initiation complex, indicate an inactive conformation in crystallo
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the in vitro polymerase activity of a non-pathogenic calicivirus RdRp is at least two times higher than that of the RdRp of the highly virulent RHDV
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the in vitro polymerase activity of a non-pathogenic calicivirus RdRp is at least two times higher than that of the RdRp of the highly virulent RHDV
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the RNA-dependent RNA polymerase (RdRp) in equine arteritis virus is expressed as the C-terminal domain of nonstructural protein 9 (nsp9)
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treatment of cells with a-amanitin or actinomycin D revealed that extension of B2 RNA by Pol II destabilizes the RNA
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viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements
additional information
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viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements, birnaviral RdRP contains a K+-binding site within its palm subdomain. In most known polymerases, the conservative elements are arranged in alphabetical order, but variants with non-canonical sequence in the primarystructure also exist. In this way the polymerases of birnaviruses and some insect viruses possess elements of the active site in the order: C-A-B-D-E-F. Motif F carries conservative basic lysine and arginine residues that may be involved in the binding of RNA polymerase of birnaviruses. In birnavirus polymerases a serine residue located in the fingers subdomain can be subjected to guanidylation that birnavirus RdRP requires for self-priming. The thumb subdomain of birnaviral RdRP is close in size to the latter and also consists of four alpha-helices and small beta-sheet, which interacts with two beta-strands of the palm subdomain. The C-terminal subdomains of birnaviral polymerase represents an extra, expanded region with several alpha-helices not assembled into compact structure, and interact with the thumb subdomain and fingertips
additional information
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viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements. Molecular dynamics of hepatitis C virus RdRP, when interacting with the molecule of a specific inhibitor that binds to the thumb subdomain, show that the ligand binding significantly reduces the ability of the polymerase to change its conformation
additional information
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viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. The Gly64 in the polymerase molecule binds through hydrogen with N-terminal Gly1, which, in turn, interacts with the amino acid residues from the fingers subdomain (Ala239 and Leu241). Formation of the active site by palm conservative elements
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overall enzyme structure analysis from crystal structure, PDB ID 1WNE. Structure solution of RdRP-RNA-rNTP complexes, overview
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overall enzyme structure analysis from crystal structure, PDB IDs 2PUS and 2R70. Structure solution of RdRP-RNA-rNTP complexes, conformational changes in the B-loop of RdRP, overview
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phase-distributed sRNAs are identified within the dsRNA-seq read-covered regions. sRNA sequences from Col-0 (GSM121455, GSM154336, and GSM154375) are mapped onto the sequence regions with two or more phase-distributed, RDRdependent sRNA loci
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overall enzyme structure analysis from crystal structure, PDB IDs 2XXD and 4E76. Structure solution of RdRP-RNA-rNTP complexes, overview
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additional information
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the in vitro polymerase activity of a non-pathogenic calicivirus RdRp is at least two times higher than that of the RdRp of the highly virulent RHDV
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