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Protein

Non-structural protein 5

Gene
N/A
Organism
Rotavirus A (isolate Monkey/South Africa/SA11-H96/1958 G3-P5B[2]-I2-R2-C5-M5-A5-N5-T5-E2-H5) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Cofactori

Mg2+Note: Magnesium is required for ATPase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921MagnesiumSequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-structural protein 5
Short name:
NSP5
Alternative name(s):
NS26
OrganismiRotavirus A (isolate Monkey/South Africa/SA11-H96/1958 G3-P5B[2]-I2-R2-C5-M5-A5-N5-T5-E2-H5) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Taxonomic identifieri450149 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiChlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus) [TaxID: 60710]
ProteomesiUP000001119 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671S → A: Loss of hyperphosphorylation. 1 Publication
Mutagenesisi67 – 671S → D: Constitutively hyperphosphorylated even in the absence of infection. 1 Publication
Mutagenesisi154 – 16613SDSDD…DDSDS → ADADDYVLDDADA: Loss of phosphorylation. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 198198Non-structural protein 5PRO_0000367825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671Phosphoserine; by host CK11 Publication
Modified residuei154 – 1541Phosphoserine; by host1 Publication
Modified residuei156 – 1561Phosphoserine; by host1 Publication
Modified residuei164 – 1641Phosphoserine; by host1 Publication
Modified residuei166 – 1661Phosphoserine; by host1 Publication

Post-translational modificationi

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.3 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Interactioni

Subunit structurei

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).By similarity

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4848Interaction with VP1Add
BLAST
Regioni189 – 19810Homodimerization and interaction with NSP6By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 101100Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the rotavirus A NSP5 family.Curated

Family and domain databases

InterProiIPR002512. Rotavirus_A/C_NSP5.
[Graphical view]
PfamiPF01525. Rota_NS26. 1 hit.
[Graphical view]
PIRSFiPIRSF004006. Rota_NS26. 1 hit.

Sequencei

Sequence statusi: Complete.

A2T3Q9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSIDVTSL PSIPSTIYKN ESSSTTSTLS GKSIGRSEQY ISPDAEAFNK
60 70 80 90 100
YMLSKSPEDI GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSAQSRPS
110 120 130 140 150
SNVGCDQVDF SLNKGLKVKA NLDSSISIST DTKKEKSKQN HKSRKHYPRI
160 170 180 190
EAESDSDDYV LDDSDSDDGK CKNCKYKKKY FALRMRMKQV AMQLIEDL
Length:198
Mass (Da):21,722
Last modified:January 15, 2008 - v1
Checksum:i1DE1EC4A803E1D57
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ838630 Genomic RNA. Translation: ABG75808.1.
RefSeqiYP_002302224.1. NC_011505.2.

Genome annotation databases

GeneIDi7011364.
KEGGivg:7011364.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ838630 Genomic RNA. Translation: ABG75808.1.
RefSeqiYP_002302224.1. NC_011505.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi7011364.
KEGGivg:7011364.

Family and domain databases

InterProiIPR002512. Rotavirus_A/C_NSP5.
[Graphical view]
PfamiPF01525. Rota_NS26. 1 hit.
[Graphical view]
PIRSFiPIRSF004006. Rota_NS26. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiNSP5_ROTSH
AccessioniPrimary (citable) accession number: A2T3Q9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: June 24, 2015
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.