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A2T3Q9 (NSP5_ROTSH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in genome replication. Plays a crucial role, together with NSP2, 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. May regulate NSP2-RNA interactions during genome replication, since NSP5 competes with RNA for the same binding site on the NSP2 octamer. Binds to either ssRNA or dsRNA with similar affinities. Displays ATPase and autokinase activities. Ref.4 Ref.8

Cofactor

Magnesium for ATPase activity.

Subunit structure

Homodimer. Interacts with VP1. Interacts with VP2. Interacts with NSP2; this interaction leads to up-regulation of NSP5 hyperphosphorylation and formation of virus factories. Interacts with NSP6 By similarity. Ref.6 Ref.9

Subcellular location

Host cytoplasm. Note: Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. Ref.4 Ref.6 Ref.9

Post-translational modification

O-glycosylated By similarity.

Hyperphosphorylated on serine residues, when in dimeric form. Ser-67 phosphorylation by CK1 is required for the hyperphosphorylation of NSP5 dimer. Impaired phosphorylation is associated with a profound morphological change in virus factories and a moderate decrease in virus replication. Ref.2 Ref.4 Ref.5 Ref.7

Sequence similarities

Belongs to the rotavirus A NSP5 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198Non-structural protein 5
PRO_0000367825

Regions

Region1 – 4848Interaction with VP1
Region189 – 19810Homodimerization and interaction with NSP6 By similarity
Compositional bias2 – 101100Ser-rich

Sites

Metal binding921Magnesium Potential

Amino acid modifications

Modified residue671Phosphoserine; by host CK1 Ref.5
Modified residue1541Phosphoserine; by host Probable
Modified residue1561Phosphoserine; by host Probable
Modified residue1641Phosphoserine; by host Probable
Modified residue1661Phosphoserine; by host Probable

Experimental info

Mutagenesis671S → A: Loss of hyperphosphorylation. Ref.5
Mutagenesis671S → D: Constitutively hyperphosphorylated even in the absence of infection. Ref.5
Mutagenesis154 – 16613SDSDD…DDSDS → ADADDYVLDDADA: Loss of phosphorylation. Ref.4

Sequences

Sequence LengthMass (Da)Tools
A2T3Q9 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 1DE1EC4A803E1D57

FASTA19821,722
        10         20         30         40         50         60 
MSLSIDVTSL PSIPSTIYKN ESSSTTSTLS GKSIGRSEQY ISPDAEAFNK YMLSKSPEDI 

        70         80         90        100        110        120 
GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSAQSRPS SNVGCDQVDF SLNKGLKVKA 

       130        140        150        160        170        180 
NLDSSISIST DTKKEKSKQN HKSRKHYPRI EAESDSDDYV LDDSDSDDGK CKNCKYKKKY 

       190 
FALRMRMKQV AMQLIEDL 

« Hide

References

[1]"Genome heterogeneity of SA11 rotavirus due to reassortment with 'O' agent."
Small C., Barro M., Brown T.L., Patton J.T.
Virology 359:415-424(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Phosphorylation generates different forms of rotavirus NSP5."
Afrikanova I., Miozzo M.C., Giambiagi S., Burrone O.R.
J. Gen. Virol. 77:2059-2065(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[3]"RNA-binding activity of the rotavirus phosphoprotein NSP5 includes affinity for double-stranded RNA."
Vende P., Taraporewala Z.F., Patton J.T.
J. Virol. 76:5291-5299(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING.
[4]"Rotavirus NSP5: mapping phosphorylation sites and kinase activation and viroplasm localization domains."
Eichwald C., Vascotto F., Fabbretti E., Burrone O.R.
J. Virol. 76:3461-3470(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-154; SER-156; SER-164 AND SER-166, MUTAGENESIS OF 154-SER--SER-166.
[5]"Uncoupling substrate and activation functions of rotavirus NSP5: phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation."
Eichwald C., Jacob G., Muszynski B., Allende J.E., Burrone O.R.
Proc. Natl. Acad. Sci. U.S.A. 101:16304-16309(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-67 BY CK1, MUTAGENESIS OF SER-67.
[6]"Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of viroplasm formation."
Eichwald C., Rodriguez J.F., Burrone O.R.
J. Gen. Virol. 85:625-634(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NSP2.
[7]"Impaired hyperphosphorylation of rotavirus NSP5 in cells depleted of casein kinase 1alpha is associated with the formation of viroplasms with altered morphology and a moderate decrease in virus replication."
Campagna M., Budini M., Arnoldi F., Desselberger U., Allende J.E., Burrone O.R.
J. Gen. Virol. 88:2800-2810(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE OF PHOSPHORYLATION BY CK1.
[8]"An ATPase activity associated with the rotavirus phosphoprotein NSP5."
Bar-Magen T., Spencer E., Patton J.T.
Virology 369:389-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2."
Arnoldi F., Campagna M., Eichwald C., Desselberger U., Burrone O.R.
J. Virol. 81:2128-2137(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VP1, SUBCELLULAR LOCATION.
[10]"Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication."
Jiang X., Jayaram H., Kumar M., Ludtke S.J., Estes M.K., Prasad B.V.V.
J. Virol. 80:10829-10835(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) IN COMPLEX WITH NSP2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ838630 Genomic RNA. Translation: ABG75808.1.
RefSeqYP_002302224.1. NC_011505.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7011364.

Family and domain databases

InterProIPR002512. Rotavirus_A/C_NSP5.
[Graphical view]
PfamPF01525. Rota_NS26. 1 hit.
[Graphical view]
PIRSFPIRSF004006. Rota_NS26. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNSP5_ROTSH
AccessionPrimary (citable) accession number: A2T3Q9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: December 14, 2011
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families