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A2T3P0

- NSP2_ROTSH

UniProt

A2T3P0 - NSP2_ROTSH

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Protein

Non-structural protein 2

Gene
N/A
Organism
Rotavirus A (isolate Monkey/South Africa/SA11-H96/1958 G3-P5B[2]-I2-R2-C5-M5-A5-N5-T5-E2-H5) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Status
Reviewed - Annotation score: 4 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) 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).By similarity

Cofactori

Mg2+Note: Magnesium is required for NTPase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi153 – 1531MagnesiumSequence Analysis
Metal bindingi171 – 1711MagnesiumSequence Analysis
Active sitei225 – 2251For NTPase 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 (isolate Monkey/South Africa/SA11-H96/1958 G3-P5B[2]-I2-R2-C5-M5-A5-N5-T5-E2-H5) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Taxonomic identifieri450149 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiCercopithecus pygerythrus (Vervet monkey) [TaxID: 60710]
ProteomesiUP000001119: Genome

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi110 – 1101H → A: 35% loss of NTPase activity. 1 Publication
Mutagenesisi153 – 1531E → A: Almost complete loss of NTPase activity. Unable to induce NSP5 phosphorylation. 1 Publication
Mutagenesisi171 – 1711Y → A: Almost complete loss of NTPase activity. 1 Publication
Mutagenesisi188 – 1881K → A: Almost complete loss of NTPase activity. Unable to induce NSP5 phosphorylation. 1 Publication
Mutagenesisi221 – 2211H → A: Almost complete loss of NTPase activity. 1 Publication
Mutagenesisi223 – 2231K → A: 75% loss of NTPase activity. 1 Publication
Mutagenesisi225 – 2251H → A: Almost complete loss of NTPase activity. Unable to induce NSP5 phosphorylation. 1 Publication
Mutagenesisi227 – 2271R → A: Almost complete loss of NTPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317Non-structural protein 2PRO_0000367818Add
BLAST

Interactioni

Subunit structurei

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 similarity2 Publications

Structurei

3D structure databases

ProteinModelPortaliA2T3P0.
SMRiA2T3P0. 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.

A2T3P0-1 [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 AFTSSMKQGN TLDVCKRLLF QKMKPEKNPF
310
KGLSTDRKMD EVSQVGV
Length:317
Mass (Da):36,569
Last modified:January 15, 2008 - v1
Checksum:i3D7BEA9514934E62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ838615 Genomic RNA. Translation: ABG75789.1.
RefSeqiYP_002302221.1. NC_011502.2.

Genome annotation databases

GeneIDi7011357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ838615 Genomic RNA. Translation: ABG75789.1 .
RefSeqi YP_002302221.1. NC_011502.2.

3D structure databases

ProteinModelPortali A2T3P0.
SMRi A2T3P0. Positions 1-313.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 7011357.

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. "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O' agent."
    Small C., Barro M., Brown T.L., Patton J.T.
    Virology 359:415-424(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Role of the histidine triad-like motif in nucleotide hydrolysis by the rotavirus RNA-packaging protein NSP2."
    Carpio R.V., Gonzalez-Nilo F.D., Jayaram H., Spencer E., Prasad B.V.V., Patton J.T., Taraporewala Z.F.
    J. Biol. Chem. 279:10624-10633(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF HIS-110; GLU-153; TYR-171; LYS-188; HIS-221; LYS-223; HIS-225 AND ARG-227.
  3. "Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of viroplasm formation."
    Eichwald C., Rodriguez J.F., Burrone O.R.
    J. Gen. Virol. 85:625-634(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NSP5.
  4. "Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2."
    Arnoldi F., Campagna M., Eichwald C., Desselberger U., Burrone O.R.
    J. Virol. 81:2128-2137(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VP1.
  5. "Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication."
    Jiang X., Jayaram H., Kumar M., Ludtke S.J., Estes M.K., Prasad B.V.V.
    J. Virol. 80:10829-10835(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) IN COMPLEX WITH NSP5 OR RNA.

Entry informationi

Entry nameiNSP2_ROTSH
AccessioniPrimary (citable) accession number: A2T3P0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: November 26, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3