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Q9E8F2

- NSP5_ROTRF

UniProt

Q9E8F2 - NSP5_ROTRF

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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: 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

Magnesium for ATPase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Magnesium Reviewed prediction

GO - Molecular functioni

  1. ATPase activity Source: InterPro
  2. RNA binding Source: UniProtKB-KW
  3. magnesium ion binding Source: InterPro
  4. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. viral genome replication Source: InterPro
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: Genome

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671Phosphoserine; by host CK1 By similarity
Modified residuei154 – 1541Phosphoserine; by host By similarity
Modified residuei156 – 1561Phosphoserine; by host By similarity
Modified residuei164 – 1641Phosphoserine; by host By similarity
Modified residuei166 – 1661Phosphoserine; by host By 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.2 Publications

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4848Interaction with VP1 By similarity
Add
BLAST
Regioni189 – 19810Homodimerization and interaction with NSP6 By similarity

Compositional bias

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

Sequence similaritiesi

Belongs to the rotavirus A NSP5 family.

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

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MSLSIDVTSL PSISSSIYKN ESSSTTSTLS GKSIGRSEQY ISPDAEAFSK    50
YMLSKSPEDI GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSTQSRPS 100
SNVGCDQVDF SFNKGISMNA NLDSSISIST SSKKEKSKSD HKSRKHYPKI 150
EAESDSDDYI LDDSDSDDGK CKNCKYKRKY FALRMRMKQV AMQLIEDL 198
Length:198
Mass (Da):21,644
Last modified:March 1, 2001 - v1
Checksum:iF8CE19C16E0EA4B6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF188126 mRNA. Translation: AAG15311.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF188126 mRNA. Translation: AAG15311.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR002512. Rotavirus_A/C_NSP5.
[Graphical view ]
Pfami PF01525. Rota_NS26. 1 hit.
[Graphical view ]
PIRSFi PIRSF004006. Rota_NS26. 1 hit.
ProtoNeti Search...

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 3, 2013
This is version 28 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

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