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A3DSK8 (NSP2_ROTHL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 27. 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/Philippines/L26/1987 G12-P1B[4]-I2-R2-C2-M1/M2-A2-N1-T2-E2-H1) (RV-A) [Complete proteome]
Taxonomic identifier10953 [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_0000369537

Regions

Region205 – 24137RNA-binding Potential

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A3DSK8 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 90CA5180EE18D54C

FASTA31736,556
        10         20         30         40         50         60 
MAELACFCYP HLENDSYKFI PFNSLAIKCM LTAKVDKKDQ DKFYNSIIYG IAPPPQFKKR 

        70         80         90        100        110        120 
YNTNDNSRGM NYETSMFNKV AILICEALNS IRVTQSDVAN VLSRVVSVRH LENLVLRKEN 

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

       190        200        210        220        230        240 
DQNFIEYKIT LNEDKPISDI CVKELVAELR WQYNRFAVIT HGKGHYRVIK YSSVANHADR 

       250        260        270        280        290        300 
VFATYKNNAK SGNVTDFNLL DQRIIWQNWY AFTSSMKQGN TLDVCKKLLF QKMKQEKNPF 

       310 
KGLSTDRKMD EVSHVGI 

« Hide

References

[1]"Evolutionary history and global spread of the emerging G12 human rotaviruses."
Rahman M., Matthijnssens J., Yang X., Delbeke T., Arijs I., Taniguchi K., Iturriza-Gomara M., Iftekharuddin N., Azim T., Van Ranst M.
J. Virol. 81:2382-2390(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Group A human rotavirus genomics: evidence that gene constellations are influenced by viral protein interactions."
Heiman E.M., McDonald S.M., Barro M., Taraporewala Z.F., Bar-Magen T., Patton J.T.
J. Virol. 82:11106-11116(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ146696 Genomic RNA. Translation: ABA34232.1.
EF672594 Genomic RNA. Translation: ABV53271.1.

3D structure databases

ProteinModelPortalA3DSK8.
SMRA3DSK8. 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_ROTHL
AccessionPrimary (citable) accession number: A3DSK8
Secondary accession number(s): B3SRU6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 20, 2007
Last modified: April 16, 2014
This is version 27 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