ID   NSP5_ROTHC              Reviewed;         212 AA.
AC   Q00682;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   08-NOV-2023, entry version 70.
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 C (isolate RVC/Human/United Kingdom/Bristol/1989) (RV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus C.
OX   NCBI_TaxID=31567;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1371174; DOI=10.1128/jvi.66.3.1817-1822.1992;
RA   Lambden P.R., Cooke S.J., Caul E.O., Clarke I.N.;
RT   "Cloning of noncultivatable human rotavirus by single primer
RT   amplification.";
RL   J. Virol. 66:1817-1822(1992).
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. {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 and NSP6. {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}.
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DR   EMBL; M81488; AAA47354.1; -; Genomic_RNA.
DR   PIR; A42188; MNXRB1.
DR   RefSeq; YP_392511.1; NC_007569.1.
DR   IntAct; Q00682; 1.
DR   GeneID; 3773138; -.
DR   KEGG; vg:3773138; -.
DR   Proteomes; UP000007664; 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   Reference proteome; RNA-binding.
FT   CHAIN           1..212
FT                   /note="Non-structural protein 5"
FT                   /id="PRO_0000149643"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
SQ   SEQUENCE   212 AA;  23793 MW;  3C6FA60E17E46C5D CRC64;
     MSDFGINLDA ICDNVKKGQT ESRTGSQLSN RSSRRMDFVD DEELSTYFNS KASVTQSDSC
     SNDLEIKHSI ITEAVVCDES AHVSADAIQE KDETVPQMDH RIMKWMLDSH DGVSLNGGIN
     FTKAKSKLKE TENEITEMKS KTNLLVNASV GINSNVGAFN PINQTIKTEA VSDMFEDEDI
     EGCICKNCPY REKYRKLRSK MKNVLIDMIN EM
//