NSP2_ROTSH
ID NSP2_ROTSH Reviewed; 317 AA.
AC A2T3P0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
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 (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A)
OS (Simian Agent 11 (isolate SI/South Africa/H96/58)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=450149;
OH NCBI_TaxID=60710; Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17059839; DOI=10.1016/j.virol.2006.09.024;
RA Small C., Barro M., Brown T.L., Patton J.T.;
RT "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O'
RT agent.";
RL Virology 359:415-424(2007).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF HIS-110; GLU-153; TYR-171; LYS-188; HIS-221;
RP LYS-223; HIS-225 AND ARG-227.
RX PubMed=14699117; DOI=10.1074/jbc.m311563200;
RA Carpio R.V., Gonzalez-Nilo F.D., Jayaram H., Spencer E., Prasad B.V.V.,
RA Patton J.T., Taraporewala Z.F.;
RT "Role of the histidine triad-like motif in nucleotide hydrolysis by the
RT rotavirus RNA-packaging protein NSP2.";
RL J. Biol. Chem. 279:10624-10633(2004).
RN [3]
RP INTERACTION WITH NSP5.
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 INTERACTION WITH VP1.
RX PubMed=17182692; DOI=10.1128/jvi.01494-06;
RA Arnoldi F., Campagna M., Eichwald C., Desselberger U., Burrone O.R.;
RT "Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is
RT stronger than that with NSP2.";
RL J. Virol. 81:2128-2137(2007).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) IN COMPLEX WITH NSP5 OR
RP RNA.
RX PubMed=16928740; DOI=10.1128/jvi.01347-06;
RA Jiang X., Jayaram H., Kumar M., Ludtke S.J., Estes M.K., Prasad B.V.V.;
RT "Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA
RT complexes: implications for genome replication.";
RL J. Virol. 80:10829-10835(2006).
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:14699117}.
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, ECO:0000269|PubMed:14993647,
CC ECO:0000269|PubMed:17182692}.
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; DQ838615; ABG75789.1; -; Genomic_RNA.
DR RefSeq; YP_002302221.1; NC_011502.2.
DR PDB; 6AUK; X-ray; 2.60 A; A=1-317.
DR PDB; 6CY9; X-ray; 2.62 A; A=1-317.
DR PDB; 6CYA; X-ray; 2.60 A; A=1-317.
DR PDBsum; 6AUK; -.
DR PDBsum; 6CY9; -.
DR PDBsum; 6CYA; -.
DR SMR; A2T3P0; -.
DR GeneID; 7011357; -.
DR KEGG; vg:7011357; -.
DR Proteomes; UP000001119; 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 3D-structure; ATP-binding; Host cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; RNA-binding.
FT CHAIN 1..317
FT /note="Non-structural protein 2"
FT /id="PRO_0000367818"
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"
FT MUTAGEN 110
FT /note="H->A: 35% loss of NTPase activity."
FT /evidence="ECO:0000269|PubMed:14699117"
FT MUTAGEN 153
FT /note="E->A: Almost complete loss of NTPase activity.
FT Unable to induce NSP5 phosphorylation."
FT /evidence="ECO:0000269|PubMed:14699117"
FT MUTAGEN 171
FT /note="Y->A: Almost complete loss of NTPase activity."
FT /evidence="ECO:0000269|PubMed:14699117"
FT MUTAGEN 188
FT /note="K->A: Almost complete loss of NTPase activity.
FT Unable to induce NSP5 phosphorylation."
FT /evidence="ECO:0000269|PubMed:14699117"
FT MUTAGEN 221
FT /note="H->A: Almost complete loss of NTPase activity."
FT /evidence="ECO:0000269|PubMed:14699117"
FT MUTAGEN 223
FT /note="K->A: 75% loss of NTPase activity."
FT /evidence="ECO:0000269|PubMed:14699117"
FT MUTAGEN 225
FT /note="H->A: Almost complete loss of NTPase activity.
FT Unable to induce NSP5 phosphorylation."
FT /evidence="ECO:0000269|PubMed:14699117"
FT MUTAGEN 227
FT /note="R->A: Almost complete loss of NTPase activity."
FT /evidence="ECO:0000269|PubMed:14699117"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:6CYA"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:6CYA"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6CYA"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:6CYA"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:6CYA"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:6CYA"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 75..90
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:6CYA"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:6CYA"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6CYA"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6CYA"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:6CYA"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6AUK"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6CYA"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 234..251
FT /evidence="ECO:0007829|PDB:6CYA"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:6CYA"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:6CYA"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:6CY9"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:6CYA"
SQ SEQUENCE 317 AA; 36569 MW; 3D7BEA9514934E62 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 AFTSSMKQGN TLDVCKRLLF QKMKPEKNPF
KGLSTDRKMD EVSQVGV
