NSP2_ROTSP
ID NSP2_ROTSP Reviewed; 317 AA.
AC Q03242;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 77.
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-Patton/G3P[X]) (RV-A) (Simian Agent 11 (strain
OS Patton)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=36434;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8380660; DOI=10.1006/viro.1993.1059;
RA Patton J.T., Salter-Cid L., Kalbach A.N., Mansell E.A., Kattoura M.D.;
RT "Nucleotide and amino acid sequence analysis of the rotavirus nonstructural
RT RNA-binding protein NS35.";
RL Virology 192:438-446(1993).
RN [2]
RP RNA-BINDING.
RX PubMed=1333119; DOI=10.1016/0042-6822(92)90245-k;
RA Kattoura M.D., Clapp L.L., Patton J.T.;
RT "The rotavirus nonstructural protein, NS35, possesses RNA-binding activity
RT in vitro and in vivo.";
RL Virology 191:698-708(1992).
RN [3]
RP INTERACTION WITH VP1.
RX PubMed=8030243; DOI=10.1006/viro.1994.1402;
RA Kattoura M.D., Chen X., Patton J.T.;
RT "The rotavirus RNA-binding protein NS35 (NSP2) forms 10S multimers and
RT interacts with the viral RNA polymerase.";
RL Virology 202:803-813(1994).
RN [4]
RP SUBUNIT, AND RNA-BINDING.
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 [5]
RP SUBUNIT, AND FUNCTION.
RX PubMed=11121414; DOI=10.1074/jbc.m009398200;
RA Schuck P., Taraporewala Z.F., McPhie P., Patton J.T.;
RT "Rotavirus nonstructural protein NSP2 self-assembles into octamers that
RT undergo ligand-induced conformational changes.";
RL J. Biol. Chem. 276:9679-9687(2001).
RN [6]
RP FUNCTION.
RX PubMed=11312322; DOI=10.1128/jvi.75.10.4519-4527.2001;
RA Taraporewala Z.F., Patton J.T.;
RT "Identification and characterization of the helix-destabilizing activity of
RT rotavirus nonstructural protein NSP2.";
RL J. Virol. 75:4519-4527(2001).
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:11121414,
CC ECO:0000269|PubMed:11312322}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04089};
CC -!- SUBUNIT: Homooctamer. Interacts with VP1; this interaction is weak.
CC Interacts with NSP5; this interaction leads to up-regulation of NSP5
CC phosphorylation and formation of viral factories. {ECO:0000255|HAMAP-
CC Rule:MF_04089}.
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; L04531; AAA47298.1; -; Genomic_RNA.
DR SMR; Q03242; -.
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; RNA-binding.
FT CHAIN 1..317
FT /note="Non-structural protein 2"
FT /id="PRO_0000149551"
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 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; 36583 MW; 3D7BEC23CFF84E62 CRC64;
MAELACFCYP HLENDSYKFI PFNNLAIKAM LTAKVDKKDM DKFYDSIIYG IAPPPQFKKR
YNTNDNSRGM NFETIMFTKV AMLICEALNS LKVTQANVSN VLSRVVSIRH LENLVIRKEN
PQDILFHSKD LLLKSTLIAI GQSKEIETTI TAEGGEIVFQ NAAFTMWKLT YLEHQLMPIL
DQNFIEYKVT LNEDKPISDV HVKELVAELR WQYNKFAVIT HGKGHYRIVK YSSVANHADR
VYATFKSNVK TGVNNDFNLL DQRIIWQNWY AFTSTMKQGN TLDVCKRLLF QKMKPEKNPF
KGLSTDRKMD EVSQVGV
