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Q9PY93 (NSP2_ROTHC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. 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 C (isolate Human/United Kingdom/Bristol/1989) (RV-C) [Reference proteome]
Taxonomic identifier31567 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length312 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.

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.

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 – 312312Non-structural protein 2
PRO_0000367815

Regions

Region202 – 23837RNA-binding Potential

Sites

Active site2221For NTPase activity By similarity
Metal binding1531Magnesium Potential
Metal binding1711Magnesium Potential

Experimental info

Mutagenesis1851K → A: Loss of NTPase activity and dsRNA synthesis. No effect on octamerization. Ref.2
Mutagenesis2221H → A: Loss of NTPase activity and dsRNA synthesis. No effect on octamerization. Ref.2

Secondary structure

....................................................... 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9PY93 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D2E6C11B6582637F

FASTA31235,915
        10         20         30         40         50         60 
MAELACFVSF SLTEDKVVWY PINKKAVQTM LCAKVEKDQR SNYYDTILYG VAPPPEFRNR 

        70         80         90        100        110        120 
FKTNERYGLD YESDQYTELV NLLADTLNMV SMPTEKFQFD IVKTVVQVRH LENLLCRIKD 

       130        140        150        160        170        180 
VNDILNANVK LRVKAVMIAC NLVNETETTP LTESNDIVYQ DSYFTITKLD YSNHKLLPLM 

       190        200        210        220        230        240 
ADEYKITINT KTDIPDRNQT AFAAYIRYNF NKFAAISHGK RHWRLVLHSQ LMSHAERLDR 

       250        260        270        280        290        300 
KIKSDKKHGR QFSYDDGDMA FVHPGWKTCI GQLCGGTTFE VAKTSLYSIK PSKTVRTATN 

       310 
KIESDLISMV GN 

« Hide

References

[1]"Molecular characterization of human group C rotavirus genes 6, 7 and 9."
James V.L., Lambden P.R., Deng Y., Caul E.O., Clarke I.N.
J. Gen. Virol. 80:3181-3187(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Structure-function analysis of rotavirus NSP2 octamer by using a novel complementation system."
Taraporewala Z.F., Jiang X., Vasquez-Del Carpio R., Jayaram H., Prasad B.V.V., Patton J.T.
J. Virol. 80:7984-7994(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), MUTAGENESIS OF LYS-185 AND HIS-222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ132205 Genomic RNA. Translation: CAB52753.1.
RefSeqYP_392488.1. NC_007545.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GU0X-ray2.80A/B1-312[»]
ProteinModelPortalQ9PY93.
SMRQ9PY93. Positions 2-309.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3773135.

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

EvolutionaryTraceQ9PY93.

Entry information

Entry nameNSP2_ROTHC
AccessionPrimary (citable) accession number: Q9PY93
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 56 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