Summary: Birnavirus RNA dependent RNA polymerase (VP1), C-terminal
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This is the Wikipedia entry entitled "Birnaviridae". More...
Birnaviridae Edit Wikipedia article
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Template:Taxobox begin placement virus
Template:Taxobox group iii entry
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Aquabirnavirus
Avibirnavirus
Entomobirnavirus
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The viridae are a family of viruses, including the following genera:
- Genus Aquabirnavirus; type species: Infectious pancreatic necrosis virus
- Genus Avibirnavirus; type species: Infectious bursal disease virus
- Genus Entomobirnavirus; type species: Drosophila X virus
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Birnavirus RNA dependent RNA polymerase (VP1), C-terminal Provide feedback
Birnaviruses are dsRNA viruses. This entry corresponds to the C-terminal domain of RNA dependent RNA polymerase also known as VP1. All of the birnavirus VP1 proteins contain conserved RdRp motifs that reside in the catalytic "palm" domain of all classes of polymerases. However, the birnavirus RdRps lack the highly conserved Gly-Asp-Asp (GDD) sequence, a component of the proposed catalytic site of this enzyme family that exists in the conserved motif VI of the palm domain of other RdRps [1]. This RdRp has the five essential RNA polymerase motifs in a permuted order of C-A-B-D-E to form a conserved catalytic active site [2,3]. This domain is mostly alpha-helical that runs across the canyon in the front of the palm, and wraps around the fingers subdomain [2] which may function to prevent back-primed RNA synthesis during protein priming.
Literature references
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Shwed PS, Dobos P, Cameron LA, Vakharia VN, Duncan R; , Virology 2002;296:241-250.: Birnavirus VP1 Proteins Form a Distinct Subgroup of RNA-Dependent RNA Polymerases Lacking a GDD Motif. PUBMED:12069523 EPMC:12069523
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Pan J, Vakharia VN, Tao YJ;, Proc Natl Acad Sci U S A. 2007;104:7385-7390.: The structure of a birnavirus polymerase reveals a distinct active site topology. PUBMED:17456597 EPMC:17456597
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Gorbalenya AE, Pringle FM, Zeddam JL, Luke BT, Cameron CE, Kalmakoff J, Hanzlik TN, Gordon KH, Ward VK;, J Mol Biol. 2002;324:47-62.: The palm subdomain-based active site is internally permuted in viral RNA-dependent RNA polymerases of an ancient lineage. PUBMED:12421558 EPMC:12421558
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Domain organisation
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Seed (3) |
Full (8) |
Representative proteomes | UniProt (276) |
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RP15 (8) |
RP35 (8) |
RP55 (8) |
RP75 (8) |
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PP/heatmap | 1 |
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Seed (3) |
Full (8) |
Representative proteomes | UniProt (276) |
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RP15 (8) |
RP35 (8) |
RP55 (8) |
RP75 (8) |
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Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Curation
This family is new in this Pfam release.
Seed source: | Pfam-B_2204 (release 7.3) |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 3 |
Number in full: | 8 |
Average length of the domain: | 105.4 aa |
Average identity of full alignment: | 43 % |
Average coverage of the sequence by the domain: | 12.29 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 106 | ||||||||||||
Family (HMM) version: | 1 | ||||||||||||
Download: | download the raw HMM for this family |
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Structures
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 Birna_RdRp_C domain has been found. There are 29 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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