ID   NSP5_ROTBU              Reviewed;         198 AA.
AC   P04515;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=Non-structural protein 5 {ECO:0000255|HAMAP-Rule:MF_04092};
DE            Short=NSP5 {ECO:0000255|HAMAP-Rule:MF_04092};
DE   AltName: Full=NS26 {ECO:0000255|HAMAP-Rule:MF_04092};
OS   Rotavirus A (strain RVA/Cow/United Kingdom/UK/1975/G6P7[5]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10934;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2998051; DOI=10.1016/0042-6822(85)90275-2;
RA   Ward C.W., Azad A.A., Dyall-Smith M.L.;
RT   "Structural homologies between RNA gene segments 10 and 11 from UK bovine,
RT   simian SA11, and human Wa rotaviruses.";
RL   Virology 144:328-336(1985).
CC   -!- FUNCTION: Plays an essential role in the viral genome replication.
CC       Participates, together with NSP2, in the formation of viral factories
CC       (viroplasms), which are large inclusions in the host cytoplasm where
CC       replication intermediates are assembled and viral RNA replication takes
CC       place. Orchestrates the recruitment of viroplasmic proteins such as
CC       capsid proteins to these factories. Participates in the selective
CC       exclusion of host proteins from stress granules (SG) and P bodies (PB).
CC       Participates also in the sequestration of these remodeled organelles in
CC       viral factories. {ECO:0000255|HAMAP-Rule:MF_04092}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_04092};
CC   -!- SUBUNIT: Homodimer. Interacts with VP1. Interacts with VP2. Interacts
CC       with NSP2; this interaction leads to up-regulation of NSP5
CC       hyperphosphorylation and formation of virus factories. Interacts with
CC       NSP6. Participates in the selective exclusion of host proteins from
CC       stress granules (SG) and P bodies (PB). Participates also in the
CC       sequestration of these remodeled organelles in viral factories.
CC       {ECO:0000255|HAMAP-Rule:MF_04092}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04092}.
CC       Note=Found in spherical cytoplasmic structures, called virus factories,
CC       that appear early after infection and are the site of viral replication
CC       and packaging. {ECO:0000255|HAMAP-Rule:MF_04092}.
CC   -!- PTM: O-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04092}.
CC   -!- PTM: Hyperphosphorylated on serine residues, when in dimeric form.
CC       Phosphorylation by host CK1 is required for the hyperphosphorylation of
CC       NSP5 dimer. {ECO:0000255|HAMAP-Rule:MF_04092}.
CC   -!- SIMILARITY: Belongs to the rotavirus NSP5 family. {ECO:0000255|HAMAP-
CC       Rule:MF_04092}.
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DR   EMBL; K03385; AAA47289.1; -; Genomic_RNA.
DR   Proteomes; UP000008657; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide 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   HAMAP; MF_04092; ROTA_NSP5; 1.
DR   InterPro; IPR002512; Rotavirus_A/C_NSP5.
DR   Pfam; PF01525; Rota_NS26; 1.
DR   PIRSF; PIRSF004006; Rota_NS26; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Host cytoplasm; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; RNA-binding.
FT   CHAIN           1..198
FT                   /note="Non-structural protein 5"
FT                   /id="PRO_0000149631"
FT   REGION          17..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT   MOD_RES         67
FT                   /note="Phosphoserine; by host CK1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT   MOD_RES         154
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT   MOD_RES         156
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT   MOD_RES         164
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT   MOD_RES         166
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
SQ   SEQUENCE   198 AA;  21705 MW;  2DCD6924E5669B28 CRC64;
     MYLSIDVTSL PSISSSIYKN ESSSTASTLS GKSIGRSEQY VSPDAEASSK YMLSKSPEDI
     GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSVQSRPS SNVGCDQVDF SFNKGIKVNA
     NLDSSISVST NSRKEKSKND HKSRKHYPRI EAESDSDDYV LDDSDSDDGK CKNCKYKRKY
     FALRMRMKQV AMQLIEDL
//