NSP2_ROT41
ID NSP2_ROT41 Reviewed; 317 AA.
AC Q3ZK62;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 54.
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/Human/Belgium/B4106/2000/G3P11[14]) (RV-A)
OS (Rotavirus A (isolate B4106)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=578843;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16571797; DOI=10.1128/jvi.80.8.3801-3810.2006;
RA Matthijnssens J., Rahman M., Martella V., Xuelei Y., De Vos S.,
RA De Leener K., Ciarlet M., Buonavoglia C., Van Ranst M.;
RT "Full genomic analysis of human rotavirus strain B4106 and lapine rotavirus
RT strain 30/96 provides evidence for interspecies transmission.";
RL J. Virol. 80:3801-3810(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; AY740734; AAU43792.1; -; Genomic_RNA.
DR SMR; Q3ZK62; -.
DR PRIDE; Q3ZK62; -.
DR Proteomes; UP000008655; 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 3: Inferred from homology;
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_0000369529"
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; 36573 MW; 3CCFA3F4EA05A19C CRC64;
MAELACFCYP HLENDSYKFI PFNSLAIKCM LTAKVDKKDQ DKFYNSIIYG IAPPPQFKKR
YNTNDNSRGM NYETSMFNKV AVLICEALNS IKVTQSDVAN VLSKVVSVRH LENLVLRREN
HQDVLFHSRD LLLKSVLIAI GHSKEIETTA TAEGGEIVFQ NAAFTMWKLT YLEHELMPIL
DQNFVEYKIT VNEDKPLSES HIKELIAELR WQYNKFAVIT HGKGHYRVVK YSSVANHADR
VYATFKSNSK NGGMIEFNLL DQRIIWQNWY AFTSSMKQGN TLETCKKLLF QKMKRESNPF
KGLSTDRKMD EVSQIGI
