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Q03243 (NSP2_ROTSR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 (strain SA11-Ramig G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Ramig))
Taxonomic identifier36435 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostMacaca mulatta (Rhesus macaque) [TaxID: 9544]

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.

Cofactor

Magnesium for NTPase activity By similarity.

Subunit structure

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

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.

Ontologies

Keywords
   Cellular componentHost cytoplasm
   LigandMagnesium
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionHydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processviral genome replication

Inferred from electronic annotation. Source: InterPro

   Cellular_componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

hydrolase activity, acting on acid anhydrides

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Non-structural protein 2
PRO_0000149552

Regions

Region205 – 24137RNA-binding Potential

Sites

Active site2251For NTPase/RTPase activity Probable
Metal binding1531Magnesium Potential
Metal binding1711Magnesium Potential

Secondary structure

............................................................ 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03243 [UniParc].

Last modified June 1, 1994. 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]"Nucleotide and amino acid sequence analysis of the rotavirus nonstructural RNA-binding protein NS35."
Patton J.T., Salter-Cid L., Kalbach A.N., Mansell E.A., Kattoura M.D.
Virology 192:438-446(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold."
Jayaram H., Taraporewala Z.F., Patton J.T., Prasad B.V.V.
Nature 417:311-315(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[3]"Crystallographic and biochemical analysis of rotavirus NSP2 with nucleotides reveals a nucleoside diphosphate kinase-like activity."
Kumar M., Jayaram H., Vasquez-Del Carpio R., Jiang X., Taraporewala Z.F., Jacobson R.H., Patton J.T., Prasad B.V.V.
J. Virol. 81:12272-12284(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04532 Genomic RNA. Translation: AAA47299.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L9VX-ray2.60A1-317[»]
2R7CX-ray2.70A1-317[»]
2R7JX-ray2.60A1-317[»]
2R7PX-ray2.80A1-317[»]
2R8FX-ray2.80A1-317[»]
4G0AX-ray2.10A/B/C/D1-317[»]
4G0JX-ray3.40A/B/C/D/E/F/G/H/I/J1-294[»]
ProteinModelPortalQ03243.
SMRQ03243. Positions 1-313.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceQ03243.

Entry information

Entry nameNSP2_ROTSR
AccessionPrimary (citable) accession number: Q03243
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 70 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references