ID   NSP5_ROTRF              Reviewed;         198 AA.
AC   Q9E8F2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 52.
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/France/RF/1975/G6P6[1]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10933;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Duarte M., Castagne N., Poncet D.;
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=8985320; DOI=10.1128/jvi.71.1.34-41.1997;
RA   Poncet D., Lindenbaum P., L'Haridon R., Cohen J.;
RT   "In vivo and in vitro phosphorylation of rotavirus NSP5 correlates with its
RT   localization in viroplasms.";
RL   J. Virol. 71:34-41(1997).
RN   [3]
RP   INTERACTION WITH VP2.
RX   PubMed=12525609; DOI=10.1128/jvi.77.3.1757-1763.2003;
RA   Berois M., Sapin C., Erk I., Poncet D., Cohen J.;
RT   "Rotavirus nonstructural protein NSP5 interacts with major core protein
RT   VP2.";
RL   J. Virol. 77:1757-1763(2003).
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       Note=Magnesium is required for ATPase activity.;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-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. {ECO:0000255|HAMAP-Rule:MF_04092, ECO:0000269|PubMed:12525609,
CC       ECO:0000269|PubMed:8985320}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04092,
CC       ECO:0000269|PubMed:8985320}. Note=Found in spherical cytoplasmic
CC       structures, called virus factories, that appear early after infection
CC       and are the site of viral replication and packaging.
CC       {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; AF188126; AAG15311.1; -; mRNA.
DR   Proteomes; UP000007179; 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   1: Evidence at protein level;
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_0000367824"
FT   REGION          16..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..166
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   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;  21644 MW;  F8CE19C16E0EA4B6 CRC64;
     MSLSIDVTSL PSISSSIYKN ESSSTTSTLS GKSIGRSEQY ISPDAEAFSK YMLSKSPEDI
     GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSTQSRPS SNVGCDQVDF SFNKGISMNA
     NLDSSISIST SSKKEKSKSD HKSRKHYPKI EAESDSDDYI LDDSDSDDGK CKNCKYKRKY
     FALRMRMKQV AMQLIEDL