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Q9E8F2 (NSP5_ROTRF) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Non-structural protein 5

Short name=NSP5
Alternative name(s):
NS26
OrganismRotavirus A (strain Cow/France/RF/1975 G6-P6[1]-I2-R2-C2-M2-A3-N2-T6-E2-H3) (RV-A) [Complete proteome]
Taxonomic identifier10933 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostBos taurus (Bovine) [TaxID: 9913]

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.

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.2 Ref.3

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.2

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.

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_0000367824

Regions

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

Sites

Metal binding921Magnesium Potential

Amino acid modifications

Modified residue671Phosphoserine; by host CK1 By similarity
Modified residue1541Phosphoserine; by host By similarity
Modified residue1561Phosphoserine; by host By similarity
Modified residue1641Phosphoserine; by host By similarity
Modified residue1661Phosphoserine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9E8F2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F8CE19C16E0EA4B6

FASTA19821,644
        10         20         30         40         50         60 
MSLSIDVTSL PSISSSIYKN ESSSTTSTLS GKSIGRSEQY ISPDAEAFSK YMLSKSPEDI 

        70         80         90        100        110        120 
GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSTQSRPS SNVGCDQVDF SFNKGISMNA 

       130        140        150        160        170        180 
NLDSSISIST SSKKEKSKSD HKSRKHYPKI EAESDSDDYI LDDSDSDDGK CKNCKYKRKY 

       190 
FALRMRMKQV AMQLIEDL 

« Hide

References

[1]Duarte M., Castagne N., Poncet D.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"In vivo and in vitro phosphorylation of rotavirus NSP5 correlates with its localization in viroplasms."
Poncet D., Lindenbaum P., L'Haridon R., Cohen J.
J. Virol. 71:34-41(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[3]"Rotavirus nonstructural protein NSP5 interacts with major core protein VP2."
Berois M., Sapin C., Erk I., Poncet D., Cohen J.
J. Virol. 77:1757-1763(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VP2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF188126 mRNA. Translation: AAG15311.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_ROTRF
AccessionPrimary (citable) accession number: Q9E8F2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 1, 2001
Last modified: April 3, 2013
This is version 28 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