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0  structures 3  species 0  interactions 3  sequences 1  architecture

Family: GBR_NSP5 (PF17580)

Summary: Group B Rotavirus Non-structural protein 5

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This is the Wikipedia entry entitled "NSP5 (rotavirus)". More...

NSP5 (rotavirus) Edit Wikipedia article

NSP5 (rotavirus)

NSP5 (nonstructural protein 5) encoded by genome segment 11 of group A rotaviruses. In virus-infected cells NSP5 accumulates in the viroplasms. NSP5 has been shown to be autophosphorylated.[1] Interaction of NSP5 with NSP2 was also demonstrated.[2] In rotavirus-infected cells, the non-structural proteins NSP5 and NSP2 localize in complexes called viroplasms, where replication and assembly occur and they can drive the formation of viroplasm-like structures in the absence of other rotaviral proteins and rotavirus replication.[3]

There is no atomic-resolution structure of NSP5 determined as of June 2019. However, the low resolution three-dimensional structure of the NSP2-NSP5 assembly has been observed by cryo-EM. NSP5 occupies the same site as RNA when binding to NSP2. The EM data from this 2006 study has not been published.[4]


  1. ^ Afrikanova I, Miozzo MC, Giambiagi S, Burrone O (September 1996). "Phosphorylation generates different forms of rotavirus NSP5". The Journal of General Virology. 77 ( Pt 9) (9): 2059–65. doi:10.1099/0022-1317-77-9-2059. PMID 8811003.
  2. ^ Afrikanova I, Fabbretti E, Miozzo MC, Burrone OR (November 1998). "Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2". The Journal of General Virology. 79 (11): 2679–86. doi:10.1099/0022-1317-79-11-2679. PMID 9820143.
  3. ^ Fabbretti E, Afrikanova I, Vascotto F, Burrone OR (February 1999). "Two non-structural rotavirus proteins, NSP2 and NSP5, form viroplasm-like structures in vivo". The Journal of General Virology. 80 ( Pt 2) (2): 333–9. doi:10.1099/0022-1317-80-2-333. PMID 10073692.
  4. ^ Jiang X, Jayaram H, Kumar M, Ludtke SJ, Estes MK, Prasad BV (November 2006). "Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication". Journal of Virology. 80 (21): 10829–35. doi:10.1128/JVI.01347-06. PMC 1641785. PMID 16928740.

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.

Group B Rotavirus Non-structural protein 5 Provide feedback

Family members such as non-structural protein 5 (NSP5), are found in Group B rotaviruses (GBR). Group B rotavirus (GBR) is genetically and antigenically distinct from Group A rotavirus (GAR). Hence phylogneetic studies have been carried out and show that the C-terminal region of NSP5, which is conserved among GAR and critical for its function for viroplasm-like structure formation in cells, was also conserved in GBR NSP5 [1].

Literature references

  1. Yamamoto D, Ghosh S, Ganesh B, Krishnan T, Chawla-Sarkar M, Alam MM, Aung TS, Kobayashi N;, J Gen Virol. 2010;91:1772-1781.: Analysis of genetic diversity and molecular evolution of human group B rotaviruses based on whole genome segments. PUBMED:20200192 EPMC:20200192

This tab holds annotation information from the InterPro database.

InterPro entry IPR020244

This entry represents non-structural protein 5 from rotaviruses. It is involved in genome replication, playing a crucial role in the formation of virus factories (viroplasms) which are large inclusions in the cytoplasm where core-like replication intermediates are assembled and RNA replication takes place. It forms a homodimer that interacts with VP1, VP2 and NSP2; these interaction lead to the formation of the virus factories.

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Seed source: PRODOM:PD035122
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: El-Gebali S
Number in seed: 1
Number in full: 3
Average length of the domain: 177.30 aa
Average identity of full alignment: 73 %
Average coverage of the sequence by the domain: 100.00 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 41.9 41.9
Trusted cut-off 46.0 215.0
Noise cut-off 38.4 38.1
Model length: 176
Family (HMM) version: 4
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