ID   NSP5_ROTHW              Reviewed;         197 AA.
AC   P04516; Q80IQ6; Q993T2;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   24-JAN-2024, entry version 90.
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/Human/United States/Wa/1974/G1P1A[8]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10962;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6300836; DOI=10.1073/pnas.80.2.373;
RA   Imai M., Richardson M.A., Ikegami N., Shatkin A.J., Furuichi Y.;
RT   "Molecular cloning of double-stranded RNA virus genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:373-377(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11778700; DOI=10.1023/a:1012577407824;
RA   Mohan K.V.K., Atreya C.D.;
RT   "Nucleotide sequence analysis of rotavirus gene 11 from two tissue culture-
RT   adapted ATCC strains, RRV and Wa.";
RL   Virus Genes 23:321-329(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2-197.
RX   PubMed=16121367; DOI=10.1002/jmv.20451;
RA   Ahmed K., Nakagomi T., Nakagomi O.;
RT   "Isolation and molecular characterization of a naturally occurring non-
RT   structural protein 5 (NSP5) gene reassortant of group A rotavirus of
RT   serotype G2P[4] with a long RNA pattern.";
RL   J. Med. Virol. 77:323-330(2005).
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   -!- SIMILARITY: Belongs to the rotavirus NSP5 family. {ECO:0000255|HAMAP-
CC       Rule:MF_04092}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA24511.1; Type=Frameshift;
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DR   EMBL; V01191; CAA24511.1; ALT_FRAME; Genomic_RNA.
DR   EMBL; AF306494; AAK15269.1; -; Genomic_RNA.
DR   EMBL; AB091726; BAC65999.1; -; Genomic_RNA.
DR   PIR; A04147; VHXREH.
DR   Proteomes; UP000006581; 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   RNA-binding.
FT   CHAIN           1..197
FT                   /note="Non-structural protein 5"
FT                   /id="PRO_0000149637"
FT   REGION          17..36
FT                   /note="Disordered"
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   CONFLICT        82
FT                   /note="K -> E (in Ref. 1; CAA24511)"
SQ   SEQUENCE   197 AA;  21670 MW;  5B0C1F736614E864 CRC64;
     MSLSIDVTSL PSISSSIFKN ESSSTTSTLS GKSIGRNEQY VSSDIEAFNK YMLSKSPEDI
     GPSDSASNNP LTSFSIRSNA VKTNADAGVS MDSSTQSRPS SNVGCDQMDF SLTKGINVSA
     SLDSCVSIST NHKKEKSKKD KSRKHYPRIE ADSDYEDYVL DDSDSDDGKC KNCKYKKKYF
     ALRMRMKQVA MQLIEDL
//