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P19715 (NSP5_ROTP5) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 46. Feed History...

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

Protein namesRecommended name:
Non-structural protein 5

Short name=NSP5
Alternative name(s):
NS26
OrganismRotavirus A (strain Pig/United States/OSU/1977 G5-P9[7]-I5-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) (Rotavirus A (strain Ohio State University))
Taxonomic identifier10915 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostSus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length197 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 By similarity.

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.4

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

Post-translational modification

O-glycosylated. Ref.2

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.3 Ref.5

Sequence similarities

Belongs to the rotavirus A NSP5 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197Non-structural protein 5
PRO_0000149638

Regions

Region1 – 4848Interaction with VP1 By similarity
Region188 – 19710Homodimerization 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 residue1531Phosphoserine; by host By similarity
Modified residue1551Phosphoserine; by host By similarity
Modified residue1631Phosphoserine; by host By similarity
Modified residue1651Phosphoserine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P19715 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 28536725F281CDDA

FASTA19721,459
        10         20         30         40         50         60 
MSLSIDVTSL PSISSSIFKN ESSSTTSTLS GKSIGRSEQY ISPDAEAFNK YMLSKSPEDI 

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

       130        140        150        160        170        180 
NLDSCVSIST DNKKEKSKKD KSRKHYPRIE ADSDSEDYVL DDSDSDDGKC KNCKYKKRCF 

       190 
ALRVRMKQVA MQLIEDL 

« Hide

References

[1]"Porcine OSU rotavirus segment II sequence shows common features with the viral gene of human origin."
Gonzalez S.A., Burrone O.R.
Nucleic Acids Res. 17:6402-6402(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Rotavirus NS26 is modified by addition of single O-linked residues of N-acetylglucosamine."
Gonzalez S.A., Burrone O.R.
Virology 182:8-16(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[3]"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.
[4]"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.
[5]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15519 Genomic RNA. Translation: CAA33540.1.
PIRVHXRPU. A34009.

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_ROTP5
AccessionPrimary (citable) accession number: P19715
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 3, 2013
This is version 46 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