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Protein

Non-structural protein 5

Gene
N/A
Organism
Rotavirus A (strain Cow/France/RF/1975 G6-P6[1]-I2-R2-C2-M2-A3-N2-T6-E2-H3) (RV-A)
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.

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 (strain Cow/France/RF/1975 G6-P6[1]-I2-R2-C2-M2-A3-N2-T6-E2-H3) (RV-A)
Taxonomic identifieri10933 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiBos taurus (Bovine) [TaxID: 9913]
ProteomesiUP000007179 Componenti: Genome

Subcellular locationi

  • Host cytoplasm 1 Publication

  • Note: Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 198198Non-structural protein 5PRO_0000367824Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671Phosphoserine; by host CK1By similarity
Modified residuei154 – 1541Phosphoserine; by hostBy similarity
Modified residuei156 – 1561Phosphoserine; by hostBy similarity
Modified residuei164 – 1641Phosphoserine; by hostBy similarity
Modified residuei166 – 1661Phosphoserine; by hostBy similarity

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.

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 VP1By similarityAdd
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.

Q9E8F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSIDVTSL PSISSSIYKN ESSSTTSTLS GKSIGRSEQY ISPDAEAFSK
60 70 80 90 100
YMLSKSPEDI GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSTQSRPS
110 120 130 140 150
SNVGCDQVDF SFNKGISMNA NLDSSISIST SSKKEKSKSD HKSRKHYPKI
160 170 180 190
EAESDSDDYI LDDSDSDDGK CKNCKYKRKY FALRMRMKQV AMQLIEDL
Length:198
Mass (Da):21,644
Last modified:March 1, 2001 - v1
Checksum:iF8CE19C16E0EA4B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188126 mRNA. Translation: AAG15311.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188126 mRNA. Translation: AAG15311.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. 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.

Entry informationi

Entry nameiNSP5_ROTRF
AccessioniPrimary (citable) accession number: Q9E8F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 1, 2001
Last modified: April 1, 2015
This is version 34 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

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.