NSP2_ROTHC
ID NSP2_ROTHC Reviewed; 312 AA.
AC Q9PY93;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 C (isolate RVC/Human/United Kingdom/Bristol/1989) (RV-C).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX NCBI_TaxID=31567;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10567650; DOI=10.1099/0022-1317-80-12-3181;
RA James V.L., Lambden P.R., Deng Y., Caul E.O., Clarke I.N.;
RT "Molecular characterization of human group C rotavirus genes 6, 7 and 9.";
RL J. Gen. Virol. 80:3181-3187(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND MUTAGENESIS OF LYS-185 AND
RP HIS-222.
RX PubMed=16873255; DOI=10.1128/jvi.00172-06;
RA Taraporewala Z.F., Jiang X., Vasquez-Del Carpio R., Jayaram H.,
RA Prasad B.V.V., Patton J.T.;
RT "Structure-function analysis of rotavirus NSP2 octamer by using a novel
RT complementation system.";
RL J. Virol. 80:7984-7994(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}.
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; AJ132205; CAB52753.1; -; Genomic_RNA.
DR RefSeq; YP_392488.1; NC_007545.1.
DR PDB; 2GU0; X-ray; 2.80 A; A/B=1-312.
DR PDBsum; 2GU0; -.
DR SMR; Q9PY93; -.
DR GeneID; 3773135; -.
DR KEGG; vg:3773135; -.
DR EvolutionaryTrace; Q9PY93; -.
DR Proteomes; UP000007664; 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..312
FT /note="Non-structural protein 2"
FT /id="PRO_0000367815"
FT REGION 202..238
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT ACT_SITE 222
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 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT BINDING 218..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT MUTAGEN 185
FT /note="K->A: Loss of NTPase activity and dsRNA synthesis.
FT No effect on octamerization."
FT /evidence="ECO:0000269|PubMed:16873255"
FT MUTAGEN 222
FT /note="H->A: Loss of NTPase activity and dsRNA synthesis.
FT No effect on octamerization."
FT /evidence="ECO:0000269|PubMed:16873255"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2GU0"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:2GU0"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:2GU0"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2GU0"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 74..90
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2GU0"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:2GU0"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:2GU0"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2GU0"
FT STRAND 182..192
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:2GU0"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2GU0"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:2GU0"
FT HELIX 293..307
FT /evidence="ECO:0007829|PDB:2GU0"
SQ SEQUENCE 312 AA; 35915 MW; D2E6C11B6582637F CRC64;
MAELACFVSF SLTEDKVVWY PINKKAVQTM LCAKVEKDQR SNYYDTILYG VAPPPEFRNR
FKTNERYGLD YESDQYTELV NLLADTLNMV SMPTEKFQFD IVKTVVQVRH LENLLCRIKD
VNDILNANVK LRVKAVMIAC NLVNETETTP LTESNDIVYQ DSYFTITKLD YSNHKLLPLM
ADEYKITINT KTDIPDRNQT AFAAYIRYNF NKFAAISHGK RHWRLVLHSQ LMSHAERLDR
KIKSDKKHGR QFSYDDGDMA FVHPGWKTCI GQLCGGTTFE VAKTSLYSIK PSKTVRTATN
KIESDLISMV GN
