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Q03242

- NSP2_ROTSP

UniProt

Q03242 - NSP2_ROTSP

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Protein

Non-structural protein 2

Gene
N/A
Organism
Rotavirus A (strain SA11-Patton G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Patton))
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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), ATP-independent helix-unwinding and nucleoside diphosphate kinase-like 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.2 Publications

Cofactori

Magnesium for NTPase activity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi153 – 1531MagnesiumSequence Analysis
Metal bindingi171 – 1711MagnesiumSequence Analysis
Active sitei225 – 2251For NTPase/RTPase activityBy similarity

GO - Molecular functioni

  1. hydrolase activity, acting on acid anhydrides Source: InterPro
  2. metal ion binding Source: UniProtKB-KW
  3. nucleotide binding Source: UniProtKB-KW
  4. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. viral genome replication Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-structural protein 2 (EC:3.6.4.-)
Short name:
NSP2
Alternative name(s):
NCVP3
Non-structural RNA-binding protein 35
Short name:
NS35
OrganismiRotavirus A (strain SA11-Patton G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Patton))
Taxonomic identifieri36434 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiMacaca mulatta (Rhesus macaque) [TaxID: 9544]

Subcellular locationi

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

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Non-structural protein 2PRO_0000149551Add
BLAST

Interactioni

Subunit structurei

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ03242.
SMRiQ03242. Positions 1-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni205 – 24137RNA-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the rotavirus NSP2 family.Curated

Family and domain databases

Gene3Di3.30.428.20. 1 hit.
3.90.1400.10. 1 hit.
InterProiIPR003668. Rotavirus_NSP2.
IPR024076. Rotavirus_NSP2_C-term.
IPR024068. Rotavirus_NSP2_N.
[Graphical view]
PfamiPF02509. Rota_NS35. 1 hit.
[Graphical view]
SUPFAMiSSF75347. SSF75347. 1 hit.
SSF75574. SSF75574. 1 hit.

Sequencei

Sequence statusi: Complete.

Q03242-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAELACFCYP HLENDSYKFI PFNNLAIKAM LTAKVDKKDM DKFYDSIIYG
60 70 80 90 100
IAPPPQFKKR YNTNDNSRGM NFETIMFTKV AMLICEALNS LKVTQANVSN
110 120 130 140 150
VLSRVVSIRH LENLVIRKEN PQDILFHSKD LLLKSTLIAI GQSKEIETTI
160 170 180 190 200
TAEGGEIVFQ NAAFTMWKLT YLEHQLMPIL DQNFIEYKVT LNEDKPISDV
210 220 230 240 250
HVKELVAELR WQYNKFAVIT HGKGHYRIVK YSSVANHADR VYATFKSNVK
260 270 280 290 300
TGVNNDFNLL DQRIIWQNWY AFTSTMKQGN TLDVCKRLLF QKMKPEKNPF
310
KGLSTDRKMD EVSQVGV
Length:317
Mass (Da):36,583
Last modified:June 1, 1994 - v1
Checksum:i3D7BEC23CFF84E62
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04531 Genomic RNA. Translation: AAA47298.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04531 Genomic RNA. Translation: AAA47298.1 .

3D structure databases

ProteinModelPortali Q03242.
SMRi Q03242. Positions 1-313.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.30.428.20. 1 hit.
3.90.1400.10. 1 hit.
InterProi IPR003668. Rotavirus_NSP2.
IPR024076. Rotavirus_NSP2_C-term.
IPR024068. Rotavirus_NSP2_N.
[Graphical view ]
Pfami PF02509. Rota_NS35. 1 hit.
[Graphical view ]
SUPFAMi SSF75347. SSF75347. 1 hit.
SSF75574. SSF75574. 1 hit.
ProtoNeti Search...

Publicationsi

  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. "The rotavirus nonstructural protein, NS35, possesses RNA-binding activity in vitro and in vivo."
    Kattoura M.D., Clapp L.L., Patton J.T.
    Virology 191:698-708(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
  3. "The rotavirus RNA-binding protein NS35 (NSP2) forms 10S multimers and interacts with the viral RNA polymerase."
    Kattoura M.D., Chen X., Patton J.T.
    Virology 202:803-813(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VP1.
  4. "Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity."
    Taraporewala Z.F., Chen D., Patton J.T.
    J. Virol. 73:9934-9943(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, RNA-BINDING.
  5. "Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes."
    Schuck P., Taraporewala Z.F., McPhie P., Patton J.T.
    J. Biol. Chem. 276:9679-9687(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, FUNCTION.
  6. "Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2."
    Taraporewala Z.F., Patton J.T.
    J. Virol. 75:4519-4527(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiNSP2_ROTSP
AccessioniPrimary (citable) accession number: Q03242
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3