NSP2_ROTSR
ID NSP2_ROTSR Reviewed; 317 AA.
AC Q03243;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 94.
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-Ramig/G3P[X]) (RV-A) (Simian Agent 11 (strain
OS Ramig)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=36435;
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 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=12015608; DOI=10.1038/417311a;
RA Jayaram H., Taraporewala Z.F., Patton J.T., Prasad B.V.V.;
RT "Rotavirus protein involved in genome replication and packaging exhibits a
RT HIT-like fold.";
RL Nature 417:311-315(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ATP ANALOG, AND
RP ACTIVE SITE.
RX PubMed=17804496; DOI=10.1128/jvi.00984-07;
RA Kumar M., Jayaram H., Vasquez-Del Carpio R., Jiang X., Taraporewala Z.F.,
RA Jacobson R.H., Patton J.T., Prasad B.V.V.;
RT "Crystallographic and biochemical analysis of rotavirus NSP2 with
RT nucleotides reveals a nucleoside diphosphate kinase-like activity.";
RL J. Virol. 81:12272-12284(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND RNA-BINDING.
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}.
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; L04532; AAA47299.1; -; Genomic_RNA.
DR PDB; 1L9V; X-ray; 2.60 A; A=1-317.
DR PDB; 2R7C; X-ray; 2.70 A; A=1-317.
DR PDB; 2R7J; X-ray; 2.60 A; A=1-317.
DR PDB; 2R7P; X-ray; 2.80 A; A=1-317.
DR PDB; 2R8F; X-ray; 2.80 A; A=1-317.
DR PDB; 4G0A; X-ray; 2.10 A; A/B/C/D=1-317.
DR PDB; 4G0J; X-ray; 3.40 A; A/B/C/D/E/F/G/H/I/J=1-294.
DR PDBsum; 1L9V; -.
DR PDBsum; 2R7C; -.
DR PDBsum; 2R7J; -.
DR PDBsum; 2R7P; -.
DR PDBsum; 2R8F; -.
DR PDBsum; 4G0A; -.
DR PDBsum; 4G0J; -.
DR SMR; Q03243; -.
DR EvolutionaryTrace; Q03243; -.
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; RNA-binding.
FT CHAIN 1..317
FT /note="Non-structural protein 2"
FT /id="PRO_0000149552"
FT REGION 205..241
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089,
FT ECO:0000269|PubMed:22811529"
FT ACT_SITE 225
FT /note="For NTPase and RTPase activities"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089,
FT ECO:0000305|PubMed:17804496"
FT BINDING 107..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089,
FT ECO:0007744|PDB:2R7P"
FT BINDING 188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089,
FT ECO:0007744|PDB:2R7P"
FT BINDING 221..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089,
FT ECO:0007744|PDB:2R7P"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089,
FT ECO:0007744|PDB:2R7P"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:4G0A"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:4G0A"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4G0A"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:4G0A"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:4G0A"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4G0A"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2R7J"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:4G0A"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4G0A"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:4G0A"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:4G0A"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2R7J"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:4G0A"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 234..251
FT /evidence="ECO:0007829|PDB:4G0A"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:4G0A"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1L9V"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:4G0A"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:4G0A"
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
