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Protein

Non-structural protein 5

Gene
N/A
Organism
Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (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)DescriptionActionsGraphical viewLength
Metal bindingi92MagnesiumSequence analysis1

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 RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (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]
Proteomesi
  • UP000001119 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67S → A: Loss of hyperphosphorylation. 1 Publication1
Mutagenesisi67S → D: Constitutively hyperphosphorylated even in the absence of infection. 1 Publication1
Mutagenesisi154 – 166SDSDD…DDSDS → ADADDYVLDDADA: Loss of phosphorylation. 1 PublicationAdd BLAST13

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003678251 – 198Non-structural protein 5Add BLAST198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei67Phosphoserine; by host CK11 Publication1
Modified residuei154Phosphoserine; by host1 Publication1
Modified residuei156Phosphoserine; by host1 Publication1
Modified residuei164Phosphoserine; by host1 Publication1
Modified residuei166Phosphoserine; by host1 Publication1

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

PTM databases

iPTMnetiA2T3Q9.

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)DescriptionActionsGraphical viewLength
Regioni1 – 48Interaction with VP11 PublicationAdd BLAST48
Regioni189 – 198Homodimerization and interaction with NSP6By similarity10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 101Ser-richAdd BLAST100

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...

PTM databases

iPTMnetiA2T3Q9.

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...

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: November 30, 2016
This is version 29 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

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 one 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.