Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q03245 (NSP2_ROTHW) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. 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 (strain Human/United States/Wa/1974 G1-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) [Complete proteome]
Taxonomic identifier10962 [NCBI]
Taxonomic lineageVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 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 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 By similarity.

Sequence similarities

Belongs to the rotavirus NSP2 family.

Ontologies

Keywords
   Cellular componentHost cytoplasm
   LigandMagnesium
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionHydrolase
   Technical termComplete proteome
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_0000149548

Regions

Region205 – 24137RNA-binding Potential

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q03245 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 343C247E52EAD4F5

FASTA31736,541
        10         20         30         40         50         60 
MAELACFCYP HLENDSYKFI PFNNLAIKCM LTAKVEKKDQ DKFYNSIVYG IAPPPQFKKR 

        70         80         90        100        110        120 
YNTSDNSRGM NYETIMFNKV AVLICEALNS IKITQSDVAN VLSRVVSVRH LENLVLRKEN 

       130        140        150        160        170        180 
HQDVLFHSKE LLLKSVLIAI GQSKEIETTA TAEGGEIVFQ NAAFTMWKLT YLDHKLMPIL 

       190        200        210        220        230        240 
DQNFIEYKIT LNEDKPISDV CIKELVAELR WQYNRFAVIT HGKGHYRVVK YSSVANHADR 

       250        260        270        280        290        300 
VFATYKNSAK SGNVIDFNLL DQRIIWQNWY AFTSSMKQGN TLDVCKKLLF QKMKQEKNPF 

       310 
KGLSTDRKMD EVSHVGI 

« 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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04534 Genomic RNA. Translation: AAA47301.1.

3D structure databases

ProteinModelPortalQ03245.
SMRQ03245. 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...

Entry information

Entry nameNSP2_ROTHW
AccessionPrimary (citable) accession number: Q03245
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 59 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