NSP2_ROTS1
ID NSP2_ROTS1 Reviewed; 317 AA.
AC P03537;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Non-structural protein 2 {ECO:0000255|HAMAP-Rule:MF_04089};
DE Short=NSP2 {ECO:0000255|HAMAP-Rule:MF_04089};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04089};
DE AltName: Full=NCVP3 {ECO:0000255|HAMAP-Rule:MF_04089};
DE AltName: Full=Non-structural RNA-binding protein 35 {ECO:0000255|HAMAP-Rule:MF_04089};
DE Short=NS35 {ECO:0000255|HAMAP-Rule:MF_04089};
OS Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain
OS Both)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=37137;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6296764; DOI=10.1093/nar/10.22.7075;
RA Both G.W., Bellamy A.R., Street J.E., Siegman L.J.;
RT "A general strategy for cloning double-stranded RNA: nucleotide sequence of
RT the Simian-11 rotavirus gene 8.";
RL Nucleic Acids Res. 10:7075-7088(1982).
RN [2]
RP COFACTOR, AND FUNCTION.
RX PubMed=10559306; DOI=10.1128/jvi.73.12.9934-9943.1999;
RA Taraporewala Z.F., Chen D., Patton J.T.;
RT "Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA
RT and have nucleoside triphosphatase activity.";
RL J. Virol. 73:9934-9943(1999).
RN [3]
RP FUNCTION, INTERACTION WITH NSP5, AND SUBCELLULAR LOCATION.
RX PubMed=14993647; DOI=10.1099/vir.0.19611-0;
RA Eichwald C., Rodriguez J.F., Burrone O.R.;
RT "Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of
RT viroplasm formation.";
RL J. Gen. Virol. 85:625-634(2004).
RN [4]
RP FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=22811529; DOI=10.1128/jvi.01201-12;
RA Hu L., Chow D.C., Patton J.T., Palzkill T., Estes M.K., Prasad B.V.;
RT "Crystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific
RT Recognition of 5' GG Sequence for RTPase Activity.";
RL J. Virol. 86:10547-10557(2012).
CC -!- FUNCTION: Participates in replication and packaging of the viral
CC genome. Plays a crucial role, together with NSP5, in the formation of
CC virus factories (viroplasms) which are large inclusions in the host
CC cytoplasm where replication intermediates are assembled and viral RNA
CC replication takes place. Displays ssRNA binding, NTPase, RNA
CC triphosphatase (RTPase) and ATP-independent helix-unwinding activities.
CC The unwinding activity may prepare and organize plus-strand RNAs for
CC packaging and replication by removing interfering secondary structures.
CC The RTPase activity plays a role in the removal of the gamma-phosphate
CC from the rotavirus RNA minus strands of dsRNA genome segments.
CC {ECO:0000255|HAMAP-Rule:MF_04089, ECO:0000269|PubMed:14993647,
CC ECO:0000269|PubMed:22811529}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04089};
CC -!- SUBUNIT: Homooctamer (PubMed:22811529). Interacts with VP1; this
CC interaction is weak. Interacts with NSP5; this interaction leads to up-
CC regulation of NSP5 phosphorylation and formation of viral factories.
CC {ECO:0000255|HAMAP-Rule:MF_04089, ECO:0000269|PubMed:14993647,
CC ECO:0000269|PubMed:22811529}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04089}.
CC Note=Found in spherical cytoplasmic structures, called viral factories,
CC that appear early after infection and are the site of viral replication
CC and packaging. {ECO:0000255|HAMAP-Rule:MF_04089}.
CC -!- SIMILARITY: Belongs to the rotavirus NSP2 family. {ECO:0000255|HAMAP-
CC Rule:MF_04089}.
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DR EMBL; J02353; AAA47293.1; -; Genomic_RNA.
DR PIR; A04144; WMXR3S.
DR SMR; P03537; -.
DR Proteomes; UP000007180; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019079; P:viral genome replication; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.428.20; -; 1.
DR Gene3D; 3.90.1400.10; -; 1.
DR HAMAP; MF_04089; ROTA_NSP2; 1.
DR InterPro; IPR003668; Rotavirus_NSP2.
DR InterPro; IPR024076; Rotavirus_NSP2_C.
DR InterPro; IPR024068; Rotavirus_NSP2_N.
DR Pfam; PF02509; Rota_NS35; 1.
DR SUPFAM; SSF75347; SSF75347; 1.
DR SUPFAM; SSF75574; SSF75574; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; RNA-binding.
FT CHAIN 1..317
FT /note="Non-structural protein 2"
FT /id="PRO_0000149550"
FT REGION 205..241
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT ACT_SITE 225
FT /note="For NTPase and RTPase activities"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089,
FT ECO:0000269|PubMed:22811529"
FT BINDING 107..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT BINDING 221..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
SQ SEQUENCE 317 AA; 36628 MW; 25670C29E6607474 CRC64;
MAELACFCYP HLENDSYRFI PFNSLAIKCM LTAKVDKKDQ DKFYNSIIYG IAPPPQFKKR
YNTSDNSRGM NYETSMFNKV AALICEALNS IKVTQSDVAS VLSKIVSVRH LENLVLRREN
HQDVLFHSKE LLLKSVLIAI GHSKEIETTA TAEGGEIVFQ NAAFTMWKLT YLEHKLMPIL
DQNFIEYKIT LNEDKPISES HVKELIAELR WQYNKFAVIT HGKGHYRVVK YSSVANHADR
VYATFKSNNK NGNMIEFNLL DQRIIWQNWY AFTSSMKQGN TLEICKKLLF QKMKRESNPF
KGLSTDRKMD EVSQIGI
