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A2T3P0 (NSP2_ROTSH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Non-structural protein 2

Short name=NSP2
EC=3.6.4.-
Alternative name(s):
NCVP3
Non-structural RNA-binding protein 35
Short name=NS35
OrganismRotavirus 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)) [Reference proteome]
Taxonomic identifier450149 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostCercopithecus pygerythrus (Vervet monkey) [TaxID: 60710]

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in genome replication and packaging. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the cytoplasm where replication intermediates are assembled and RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activity activities. The unwiding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. Unlike typical helicases, NSP2 requires neither a divalent cation nor a nucleotide energy source for helix destabilization. The RTPase activity may account for the absence of the 5'-terminal gamma-phosphate on the minus-strands of dsRNA genome segments By similarity. Ref.2

Cofactor

Magnesium for NTPase activity.

Subunit structure

Homooctamer By similarity. Interacts with VP1; this interaction is weak. Interacts with NSP5; this interaction leads to up-regulation of NSP5 hyperphosphorylation and formation of virus factories. Ref.3 Ref.4

Subcellular location

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

Sequence similarities

Belongs to the rotavirus NSP2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Non-structural protein 2
PRO_0000367818

Regions

Region205 – 24137RNA-binding Potential

Sites

Active site2251For NTPase activity By similarity
Metal binding1531Magnesium Potential
Metal binding1711Magnesium Potential

Experimental info

Mutagenesis1101H → A: 35% loss of NTPase activity. Ref.2
Mutagenesis1531E → A: Almost complete loss of NTPase activity. Unable to induce NSP5 phosphorylation. Ref.2
Mutagenesis1711Y → A: Almost complete loss of NTPase activity. Ref.2
Mutagenesis1881K → A: Almost complete loss of NTPase activity. Unable to induce NSP5 phosphorylation. Ref.2
Mutagenesis2211H → A: Almost complete loss of NTPase activity. Ref.2
Mutagenesis2231K → A: 75% loss of NTPase activity. Ref.2
Mutagenesis2251H → A: Almost complete loss of NTPase activity. Unable to induce NSP5 phosphorylation. Ref.2
Mutagenesis2271R → A: Almost complete loss of NTPase activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A2T3P0 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 3D7BEA9514934E62

FASTA31736,569
        10         20         30         40         50         60 
MAELACFCYP HLENDSYKFI PFNNLAIKAM LTAKVDKKDM DKFYDSIIYG IAPPPQFKKR 

        70         80         90        100        110        120 
YNTNDNSRGM NFETIMFTKV AMLICEALNS LKVTQANVSN VLSRVVSIRH LENLVIRKEN 

       130        140        150        160        170        180 
PQDILFHSKD LLLKSTLIAI GQSKEIETTI TAEGGEIVFQ NAAFTMWKLT YLEHQLMPIL 

       190        200        210        220        230        240 
DQNFIEYKVT LNEDKPISDV HVKELVAELR WQYNKFAVIT HGKGHYRIVK YSSVANHADR 

       250        260        270        280        290        300 
VYATFKSNVK TGVNNDFNLL DQRIIWQNWY AFTSSMKQGN TLDVCKRLLF QKMKPEKNPF 

       310 
KGLSTDRKMD EVSQVGV 

« Hide

References

[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]"Role of the histidine triad-like motif in nucleotide hydrolysis by the rotavirus RNA-packaging protein NSP2."
Carpio R.V., Gonzalez-Nilo F.D., Jayaram H., Spencer E., Prasad B.V.V., Patton J.T., Taraporewala Z.F.
J. Biol. Chem. 279:10624-10633(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF HIS-110; GLU-153; TYR-171; LYS-188; HIS-221; LYS-223; HIS-225 AND ARG-227.
[3]"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: INTERACTION WITH NSP5.
[4]"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.
[5]"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 NSP5 OR RNA.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ838615 Genomic RNA. Translation: ABG75789.1.
RefSeqYP_002302221.1. NC_011502.2.

3D structure databases

ProteinModelPortalA2T3P0.
SMRA2T3P0. Positions 1-313.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7011357.

Family and domain databases

Gene3D3.30.428.20. 1 hit.
3.90.1400.10. 1 hit.
InterProIPR003668. Rotavirus_NSP2.
IPR024076. Rotavirus_NSP2_C-term.
IPR024068. Rotavirus_NSP2_N.
[Graphical view]
PfamPF02509. Rota_NS35. 1 hit.
[Graphical view]
SUPFAMSSF75347. SSF75347. 1 hit.
SSF75574. SSF75574. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNSP2_ROTSH
AccessionPrimary (citable) accession number: A2T3P0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: April 16, 2014
This is version 28 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