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7  structures 1014  species 0  interactions 5206  sequences 136  architectures

Family: RdRP (PF05183)

Summary: RNA dependent RNA polymerase

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This is the Wikipedia entry entitled "RNA-dependent RNA polymerase". More...

RNA-dependent RNA polymerase Edit Wikipedia article

RNA-dependent RNA polymerase
HCV NS5B RdRP stalled 4WTG.png
Stalled HCV RNA replicase (NS5B), in complex with sofosbuvir (PDB 4WTG).
EC no.
CAS no.9026-28-2
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

RNA-dependent RNA polymerase (RdRp) or RNA replicase is an enzyme that catalyzes the replication of RNA from an RNA template. Specifically, it catalyzes synthesis of the RNA strand complementary to a given RNA template. This is in contrast to typical DNA-dependent RNA polymerases, which all organisms use to catalyze the transcription of RNA from a DNA template.

RdRp is an essential protein encoded in the genomes of most RNA-containing viruses with no DNA stage[1][2] including SARS-CoV-2. Some eukaryotes also contain RdRps, which are involved in RNA interference and differ structurally from viral RdRps.


Viral RdRps were discovered in the early 1960s from studies on mengovirus and polio virus when it was observed that these viruses were not sensitive to actinomycin D, a drug that inhibits cellular DNA-directed RNA synthesis. This lack of sensitivity suggested that there is a virus-specific enzyme that could copy RNA from an RNA template and not from a DNA template.


Structure and replication elongation mechanism of a RdRp

RdRps are highly conserved throughout viruses and are even related to telomerase, though the reason for this is an ongoing question as of 2009.[3] The similarity has led to speculation that viral RdRps are ancestral to human telomerase.

The most famous example of RdRp is that of the polio virus. The viral genome is composed of RNA, which enters the cell through receptor-mediated endocytosis. From there, the RNA is able to act as a template for complementary RNA synthesis, immediately. The complementary strand is then, itself, able to act as a template for the production of new viral genomes that are further packaged and released from the cell ready to infect more host cells. The advantage of this method of replication is that there is no DNA stage; replication is quick and easy. The disadvantage is that there is no 'back-up' DNA copy.

Many RdRps are associated tightly with membranes and are, therefore, difficult to study. The best-known RdRps are polioviral 3Dpol, vesicular stomatitis virus L,[4] and hepatitis C virus NS5B protein.

Many eukaryotes also have RdRps and these are involved in RNA interference: these amplify microRNAs and small temporal RNAs and produce double-stranded RNA using small interfering RNAs as primers.[5] In fact these same RdRps that are used in the defense mechanisms can be usurped by RNA viruses for their benefit.[6] Their evolutionary history has been reviewed.[7]

Replication process

RdRp differs from RNA polymerase as it works to catalyze the synthesis of an RNA strand complementary to a given RNA template, rather than using a DNA template. The RNA replication process is a four-step mechanism, as described.

  1. Nucleoside triphosphate (NTP) binding – initially, the RdRp presents with a vacant active site in which an NTP binds, complementary to the corresponding nucleotide on the template strand. Correct NTP binding causes the RdRp to undergo a conformational change.[8]
  2. Active site closure – the conformational change, initiated by the correct NTP binding, results in the restriction of active site access and produces a catalytically competent state.[8]
  3. Phosphodiester bond formation – two Mg2+ ions are present in the catalytically active state and arrange themselves in such a way around the newly synthesized RNA chain that the substrate NTP is able to undergo a phosphatidyl transfer and form a phosphodiester bond with the newly synthesized chain.[9] With the use of these Mg2+ ions, the active site is no longer catalytically stable and the RdRp complex changes to an open conformation.[9]
  4. Translocation – once the active site is open, the RNA template strand is able to move by one position through the RdRp protein complex and continue chain elongation by binding a new NTP, unless otherwise specified by the template.[8]

RNA synthesis can be performed by means of a primer-independent (de novo) or a primer-dependent mechanism that utilizes a viral protein genome-linked (VPg) primer.[10] The de novo initiation consists in the addition of a nucleoside triphosphate (NTP) to the 3'-OH of the first initiating NTP.[10] During the following so-called elongation phase, this nucleotidyl transfer reaction is repeated with subsequent NTPs to generate the complementary RNA product. Termination of the nascent RNA chain produced by RdRp is not completely known, however, it has been shown that RdRp termination is sequence-independent.[11]

One major drawback of RNA-dependent RNA polymerase replication is the immense error rate during transcription.[10] RdRps are known to have a lack of fidelity on the order of 104 nucleotides, which is thought to be a direct result of its insufficient proofreading abilities.[10] This high rate of variation is favored in viral genomes as it allows for the pathogen to overcome defenses developed by hosts trying to avoid infection allowing for evolutionary growth.


Overview of the flavivirus RdRp structure based on West Nile Virus (WNV) NS5Pol

Viral/prokaryotic RNA-directed RNA polymerases, along with many single-subunit DNA-directed polymerases, employ a fold whose organization has been linked to the shape of a right hand with three subdomains termed fingers, palm, and thumb.[12] Only the palm subdomain, composed of a four-stranded antiparallel beta sheet with two alpha helices, is well conserved among all of these enzymes. In RdRp, the palm subdomain comprises three well-conserved motifs (A, B, and C). Motif A (D-x(4,5)-D) and motif C (GDD) are spatially juxtaposed; the aspartic acid residues of these motifs are implied in the binding of Mg2+ and/or Mn2+. The asparagine residue of motif B is involved in selection of ribonucleoside triphosphates over dNTPs and, thus, determines whether RNA rather than DNA is synthesized.[13] The domain organization[14] and the 3D structure of the catalytic centre of a wide range of RdRps, even those with a low overall sequence homology, are conserved. The catalytic center is formed by several motifs containing a number of conserved amino acid residues.

Eukaryotic RNA interference requires a cellular RNA-dependent RNA polymerase (c RdRp). Unlike the "hand" polymerases, they resemble simplified multi-subunit DNA-dependent RNA polymerases (DdRPs), specifically in the catalytic β/β' subunits, in that they use two sets of double-psi β-barrels in the active site. QDE1 (Q9Y7G6) in Neurospora crassa, which has both barrels in the same chain,[15] is an example of such an c RdRp enzyme.[16] Bacteriophage homologs of c RdRp, including the similarly single-chain DdRp yonO (O31945), appear to be closer to c RdRps than DdRPs are.[5][17]

RNA dependent RNA polymerase[a]
Pfam clanCL0027
RNA-dependent RNA polymerase, eukaryotic-type
Bunyavirus RNA replicase[b]

In viruses

Structure and evolution of RdRp in RNA viruses and their superfamilies

There are 4 superfamilies of viruses that cover all RNA-containing viruses with no DNA stage:

Flaviviruses produce a polyprotein from the ssRNA genome. The polyprotein is cleaved to a number of products, one of which is NS5, an RNA-dependent RNA polymerase. This RNA-directed RNA polymerase possesses a number of short regions and motifs homologous to other RNA-directed RNA polymerases.[18]

RNA replicase found in positive-strand ssRNA viruses are related to each other, forming three large superfamilies.[19] Birnaviral RNA replicase is unique in that it lacks motif C (GDD) in the palm.[20] Mononegaviral RdRp (PDB 5A22) has been automatically classified as similar to (+)−ssRNA RdRps, specifically one from Pestivirus and one from Leviviridae.[21] Bunyaviral RdRp monomer (PDB 5AMQ) resembles the heterotrimeric complex of Orthomyxoviral (Influenza; PDB 4WSB) RdRp.[22]

Since it is a protein universal to RNA-containing viruses, RdRp is a useful marker for understanding their evolution.[23] The overall structural evolution of viral RdRps has been reviewed.[24]


When replicating its (+)ssRNA genome, the poliovirus RdRp is able to carry out recombination. Recombination appears to occur by a copy choice mechanism in which the RdRp switches (+)ssRNA templates during negative strand synthesis.[25] Recombination frequency is determined in part by the fidelity of RdRp replication.[26] RdRp variants with high replication fidelity show reduced recombination, and low fidelity RdRps exhibit increased recombination.[26] Recombination by RdRp strand switching also occurs frequently during replication in the (+)ssRNA plant carmoviruses and tombusviruses.[27]

Intragenic complementation

Sendai virus (family Paramyxoviridae) has a linear, single stranded, negative-sense, nonsegmented RNA genome. The viral RdRp consists of two virus-encoded subunits, a smaller one P and a larger one L. When different inactive RdRp mutants with defects throughout the length of the L subunit where tested in pairwise combinations, restoration of viral RNA synthesis was observed in some combinations.[28] This positive L–L interaction is referred to as intragenic complementation and indicates that the L protein is an oligomer in the viral RNA polymerase complex.

Drug therapies

  • RdRps can be used as drug targets for viral pathogens as their function is not necessary for eukaryotic survival. By inhibiting RNA-dependent RNA polymerase function, new RNAs cannot be replicated from an RNA template strand, however, DNA-dependent RNA polymerase will remain functional.
  • There are currently antiviral drugs against Hepatitis C and COVID-19 that specifically target RdRp. These include Sofosbuvir and Ribavirin against Hepatitis C[29] and Remdesivir, the only FDA approved drug against COVID-19.
  • GS-441524 triphosphate, is a substrate for RdRp, but not mammalian polymerases. It results in premature chain termination and inhibition of viral replication. GS-441524 triphosphate is the biologically active form of the phosphate pro-drug, Remdesivir. Remdesivir is classified as a nucleotide analog in which it works to inhibit the function of RdRp by covalently binding to and interrupting termination of the nascent RNA through early or delayed termination or preventing further elongation of the RNA polynucleotide.[30][31] This early termination leads to nonfunctional RNA that will be degraded through normal cellular processes.

RNA interference

The use of RNA-dependent RNA polymerase plays a major role in RNA interference in eukaryotes, a process used to silence gene expression via small interfering RNAs (siRNAs) binding to mRNA rendering them inactive.[32] Eukaryotic RdRp becomes active in the presence of dsRNA, however, RdRp is only present in a select subset of eukaryotes, including C. elegans and P. tetraurelia.[33] This presence of dsRNA triggers the activation of RdRp and RNAi processes by priming the initiation of RNA transcription through the introduction of siRNAs into the system.[33] In C. elegans, siRNAs are integrated into the RNA-induced silencing complex, RISC, which works alongside mRNAs targeted for interference to recruit more RdRps to synthesize more secondary siRNAs and repress gene expression.[34]

See also


  1. ^ See Pfam clan for other (+)ssRNA/dsRNA families.
  2. ^ A (−)ssRNA polymerase.


  1. ^ Koonin EV, Gorbalenya AE, Chumakov KM (July 1989). "Tentative identification of RNA-dependent RNA polymerases of dsRNA viruses and their relationship to positive strand RNA viral polymerases". FEBS Letters. 252 (1–2): 42–6. doi:10.1016/0014-5793(89)80886-5. PMID 2759231. S2CID 36482110.
  2. ^ Zanotto PM, Gibbs MJ, Gould EA, Holmes EC (September 1996). "A reevaluation of the higher taxonomy of viruses based on RNA polymerases". Journal of Virology. 70 (9): 6083–96. doi:10.1128/JVI.70.9.6083-6096.1996. PMC 190630. PMID 8709232.
  3. ^ Suttle CA (September 2005). "Viruses in the sea". Nature. 437 (7057): 356–61. Bibcode:2005Natur.437..356S. doi:10.1038/nature04160. PMID 16163346. S2CID 4370363.
  4. ^ Timm C, Gupta A, Yin J (August 2015). "Robust kinetics of an RNA virus: Transcription rates are set by genome levels". Biotechnology and Bioengineering. 112 (8): 1655–62. doi:10.1002/bit.25578. PMC 5653219. PMID 25726926.
  5. ^ a b Iyer LM, Koonin EV, Aravind L (January 2003). "Evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases and the origin of RNA polymerases". BMC Structural Biology. 3: 1. doi:10.1186/1472-6807-3-1. PMC 151600. PMID 12553882.
  6. ^ Tan FL, Yin JQ (December 2004). "RNAi, a new therapeutic strategy against viral infection". Cell Research. 14 (6): 460–6. doi:10.1038/ PMC 7092015. PMID 15625012.
  7. ^ Zong J, Yao X, Yin J, Zhang D, Ma H (November 2009). "Evolution of the RNA-dependent RNA polymerase (RdRP) genes: duplications and possible losses before and after the divergence of major eukaryotic groups". Gene. 447 (1): 29–39. doi:10.1016/j.gene.2009.07.004. PMID 19616606.
  8. ^ a b c Wu J, Gong P (January 2018). "Visualizing the Nucleotide Addition Cycle of Viral RNA-Dependent RNA Polymerase". Viruses. 10 (1): 24. doi:10.3390/v10010024. PMC 5795437. PMID 29300357.
  9. ^ a b Shu B, Gong P (July 2016). "Structural basis of viral RNA-dependent RNA polymerase catalysis and translocation". Proceedings of the National Academy of Sciences of the United States of America. 113 (28): E4005–14. doi:10.1073/pnas.1602591113. PMC 4948327. PMID 27339134.
  10. ^ a b c d Venkataraman S, Prasad BV, Selvarajan R (February 2018). "RNA Dependent RNA Polymerases: Insights from Structure, Function and Evolution". Viruses. 10 (2): 76. doi:10.3390/v10020076. PMC 5850383. PMID 29439438.
  11. ^ Adkins S, Stawicki SS, Faurote G, Siegel RW, Kao CC (April 1998). "Mechanistic analysis of RNA synthesis by RNA-dependent RNA polymerase from two promoters reveals similarities to DNA-dependent RNA polymerase". RNA. 4 (4): 455–70. PMC 1369631. PMID 9630251.
  12. ^ Hansen JL, Long AM, Schultz SC (August 1997). "Structure of the RNA-dependent RNA polymerase of poliovirus". Structure. 5 (8): 1109–22. doi:10.1016/S0969-2126(97)00261-X. PMID 9309225.
  13. ^ Gohara DW, Crotty S, Arnold JJ, Yoder JD, Andino R, Cameron CE (August 2000). "Poliovirus RNA-dependent RNA polymerase (3Dpol): structural, biochemical, and biological analysis of conserved structural motifs A and B". The Journal of Biological Chemistry. 275 (33): 25523–32. doi:10.1074/jbc.M002671200. PMID 10827187.
  14. ^ O'Reilly EK, Kao CC (December 1998). "Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure". Virology. 252 (2): 287–303. doi:10.1006/viro.1998.9463. PMID 9878607.
  15. ^ Sauguet L (September 2019). "The Extended "Two-Barrel" Polymerases Superfamily: Structure, Function and Evolution". Journal of Molecular Biology. 431 (20): 4167–4183. doi:10.1016/j.jmb.2019.05.017. PMID 31103775.
  16. ^ Werner F, Grohmann D (February 2011). "Evolution of multisubunit RNA polymerases in the three domains of life". Nature Reviews. Microbiology. 9 (2): 85–98. doi:10.1038/nrmicro2507. PMID 21233849. S2CID 30004345.
  17. ^ Forrest D, James K, Yuzenkova Y, Zenkin N (June 2017). "Single-peptide DNA-dependent RNA polymerase homologous to multi-subunit RNA polymerase". Nature Communications. 8: 15774. Bibcode:2017NatCo...815774F. doi:10.1038/ncomms15774. PMC 5467207. PMID 28585540.
  18. ^ Tan BH, Fu J, Sugrue RJ, Yap EH, Chan YC, Tan YH (February 1996). "Recombinant dengue type 1 virus NS5 protein expressed in Escherichia coli exhibits RNA-dependent RNA polymerase activity". Virology. 216 (2): 317–25. doi:10.1006/viro.1996.0067. PMID 8607261.
  19. ^ Koonin EV (September 1991). "The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses". The Journal of General Virology. 72 ( Pt 9) (9): 2197–206. doi:10.1099/0022-1317-72-9-2197. PMID 1895057.
  20. ^ Shwed PS, Dobos P, Cameron LA, Vakharia VN, Duncan R (May 2002). "Birnavirus VP1 proteins form a distinct subgroup of RNA-dependent RNA polymerases lacking a GDD motif". Virology. 296 (2): 241–50. doi:10.1006/viro.2001.1334. PMID 12069523.
  21. ^ Structural Similarities for the Entities in PDB 5A22.
  22. ^ Gerlach P, Malet H, Cusack S, Reguera J (June 2015). "Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter". Cell. 161 (6): 1267–79. doi:10.1016/j.cell.2015.05.006. PMC 4459711. PMID 26004069.
  23. ^ Wolf YI, Kazlauskas D, Iranzo J, Lucía-Sanz A, Kuhn JH, Krupovic M, et al. (November 2018). "Origins and Evolution of the Global RNA Virome". mBio. 9 (6). doi:10.1128/mBio.02329-18. PMC 6282212. PMID 30482837.
  24. ^ Černý J, Černá Bolfíková B, Valdés JJ, Grubhoffer L, Růžek D (2014). "Evolution of tertiary structure of viral RNA dependent polymerases". PLOS ONE. 9 (5): e96070. Bibcode:2014PLoSO...996070C. doi:10.1371/journal.pone.0096070. PMC 4015915. PMID 24816789.
  25. ^ Kirkegaard K, Baltimore D (November 1986). "The mechanism of RNA recombination in poliovirus". Cell. 47 (3): 433–43. doi:10.1016/0092-8674(86)90600-8. PMC 7133339. PMID 3021340.
  26. ^ a b Woodman A, Arnold JJ, Cameron CE, Evans DJ (August 2016). "Biochemical and genetic analysis of the role of the viral polymerase in enterovirus recombination". Nucleic Acids Research. 44 (14): 6883–95. doi:10.1093/nar/gkw567. PMC 5001610. PMID 27317698.
  27. ^ Cheng CP, Nagy PD (November 2003). "Mechanism of RNA recombination in carmo- and tombusviruses: evidence for template switching by the RNA-dependent RNA polymerase in vitro". Journal of Virology. 77 (22): 12033–47. doi:10.1128/jvi.77.22.12033-12047.2003. PMC 254248. PMID 14581540.
  28. ^ Smallwood S, Cevik B, Moyer SA (December 2002). "Intragenic complementation and oligomerization of the L subunit of the sendai virus RNA polymerase". Virology. 304 (2): 235–45. doi:10.1006/viro.2002.1720. PMID 12504565.
  29. ^ Waheed Y, Bhatti A, Ashraf M (March 2013). "RNA dependent RNA polymerase of HCV: a potential target for the development of antiviral drugs". Infection, Genetics and Evolution. 14: 247–57. doi:10.1016/j.meegid.2012.12.004. PMID 23291407.
  30. ^ Yin W, Mao C, Luan X, Shen DD, Shen Q, Su H, et al. (June 2020). "Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir". Science. 368 (6498): 1499–1504. Bibcode:2020Sci...368.1499Y. doi:10.1126/science.abc1560. PMC 7199908. PMID 32358203.
  31. ^ Malin JJ, Suárez I, Priesner V, Fätkenheuer G, Rybniker J (December 2020). "Remdesivir against COVID-19 and Other Viral Diseases". Clinical Microbiology Reviews. 34 (1). doi:10.1128/CMR.00162-20. PMC 7566896. PMID 33055231.
  32. ^ Simaan JA, Aviado DM (November 1975). "Hemodynamic effects of aerosol propellants. II. Pulmonary circulation in the dog". Toxicology. 5 (2): 139–46. doi:10.1016/0300-483x(75)90110-9. PMID 1873.
  33. ^ a b Marker S, Le Mouël A, Meyer E, Simon M (July 2010). "Distinct RNA-dependent RNA polymerases are required for RNAi triggered by double-stranded RNA versus truncated transgenes in Paramecium tetraurelia". Nucleic Acids Research. 38 (12): 4092–107. doi:10.1093/nar/gkq131. PMC 2896523. PMID 20200046.
  34. ^ Zhang C, Ruvkun G (August 2012). "New insights into siRNA amplification and RNAi". RNA Biology. 9 (8): 1045–9. doi:10.4161/rna.21246. PMC 3551858. PMID 22858672.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR000208

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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RNA dependent RNA polymerase Provide feedback

This family of proteins are eukaryotic RNA dependent RNA polymerases. These proteins are involved in post transcriptional gene silencing where they are thought to amplify dsRNA templates.

Literature references

  1. Sijen T, Fleenor J, Simmer F, Thijssen KL, Parrish S, Timmons L, Plasterk RH, Fire A; , Cell 2001;107:465-476.: On the role of RNA amplification in dsRNA-triggered gene silencing. PUBMED:11719187 EPMC:11719187

  2. Dalmay T, Hamilton A, Rudd S, Angell S, Baulcombe DC; , Cell 2000;101:543-553.: An RNA-dependent RNA polymerase gene in Arabidopsis is required for posttranscriptional gene silencing mediated by a transgene but not by a virus. PUBMED:10850496 EPMC:10850496

  3. Iyer LM, Koonin EV, Aravind L;, BMC Struct Biol. 2003;3:1.: Evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases and the origin of RNA polymerases. PUBMED:12553882 EPMC:12553882

This tab holds annotation information from the InterPro database.

InterPro entry IPR007855

This entry represents various eukaryotic RNA-dependent RNA polymerases (RDRP; EC ), such as RCRP-1, RDRP-2 and RDRP-6. These enzymes are involved in the amplification of regulatory microRNAs during post-transcriptional gene silencing [ PUBMED:12553882 ]; they are also required for transcriptional gene silencing. Double-stranded RNA has been shown to induce gene silencing in diverse eukaryotes and by a variety of pathways [ PUBMED:16691418 ]. These enzymes also play a role in the RNA interference (RNAi) pathway, which is important for heterochromatin formation, accurate chromosome segregation, centromere cohesion and telomere function during mitosis and meiosis. RDRP enzymes are highly conserved in most eukaryotes, but are missing in archaea and bacteria. The core catalytic domain of RDRP enzymes is structurally similar to the beta' subunit of DNA-dependent RNA polymerases (DDRP), however the other domains of DDRP show no similarity to those of RDRP.

This entry also includes QDE-1 from the filamentous fungus Neurospora. QDE-1 is both an RdRP and a DNA-dependent RNA polymerase (DdRP). It is able to synthesize RNA from both ssRNA and single-stranded DNA (ssDNA) [ PUBMED:20957187 ].

Gene Ontology

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Domain organisation

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_2226 (release 7.7)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Wood V , Bateman A
Number in seed: 256
Number in full: 5206
Average length of the domain: 481.30 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 48.09 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.8 23.8
Trusted cut-off 24.4 23.8
Noise cut-off 23.7 23.7
Model length: 586
Family (HMM) version: 15
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Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the RdRP domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0R0JN45 View 3D Structure Click here
A0A0R0JXX8 View 3D Structure Click here
A0A1D6E8W9 View 3D Structure Click here
A0A1D6EFA2 View 3D Structure Click here
A0A1D6EFA3 View 3D Structure Click here
A0A1D6EFB2 View 3D Structure Click here
A0A1D6HJL8 View 3D Structure Click here
A0A1D6MTP6 View 3D Structure Click here
A0A1D6MTP7 View 3D Structure Click here
A0A1D6P5B6 View 3D Structure Click here
A0A1D6P5I1 View 3D Structure Click here
G5EBQ3 View 3D Structure Click here
G5ECM1 View 3D Structure Click here
G5EE53 View 3D Structure Click here
G5EFA8 View 3D Structure Click here
I1KKW7 View 3D Structure Click here
I1MTJ2 View 3D Structure Click here
K7K152 View 3D Structure Click here
K7K760 View 3D Structure Click here
K7KIJ3 View 3D Structure Click here
K7VBP9 View 3D Structure Click here
O14227 View 3D Structure Click here
O82188 View 3D Structure Click here
O82189 View 3D Structure Click here
O82190 View 3D Structure Click here
O82504 View 3D Structure Click here
Q0DXS3 View 3D Structure Click here
Q0JPV9 View 3D Structure Click here
Q54EH7 View 3D Structure Click here
Q54H25 View 3D Structure Click here
Q54UI6 View 3D Structure Click here
Q5QMN4 View 3D Structure Click here
Q5QMN5 View 3D Structure Click here
Q7XM31 View 3D Structure Click here
Q8LHH9 View 3D Structure Click here
Q9LQV2 View 3D Structure Click here
Q9SG02 View 3D Structure Click here