ID   NSP2_ROTPC              Reviewed;         312 AA.
AC   Q86484;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, 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 C (strain RVC/Pig/United States/Cowden/1980) (RV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=10916;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cohen J.;
RT   "Sequence of the gene encoding the outer glycoprotein of the bovine
RT   rotavirus (RF strain) and comparison with homologous genes from four
RT   bovine, simian and human rotaviruses.";
RL   Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
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; X65939; CAA46742.1; -; mRNA.
DR   PIR; S25545; S25545.
DR   SMR; Q86484; -.
DR   Proteomes; UP000008175; 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   2: Evidence at transcript level;
KW   ATP-binding; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; RNA-binding.
FT   CHAIN           1..312
FT                   /note="Non-structural protein 2"
FT                   /id="PRO_0000369882"
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"
SQ   SEQUENCE   312 AA;  35833 MW;  127A5CBE9637C782 CRC64;
     MAELACFVSF SLTEDKVKWF PINKKAVKTM LCAKVEKDQR SNYYDTILYG VAPPPEFRNR
     FKTTERYGLD YESDQYSEVA NLLADVLNMV SMPTEKFQFD IVKTVVQVRH LENLLLRIKD
     TDDILSENVK LRVKAVMIAC NLVNETETTP LTESNEIVYQ DSYFTITKLD YSSHKLLPLM
     ADEYKITINT KTDIPDRDQT AFAAYIRYNF NKFAAISHGK RHWRLVLHSQ LMSHAERLDR
     KIKSDKKHGR QFAYDDGDMA FVHPGWKACI GQLCGGTTFE VAKTSLYSVK TSKTVRTATN
     KIESDLISMV GN