ID   NSP5_ROTHK              Reviewed;         197 AA.
AC   Q9QNA5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 55.
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/Japan/KU/1995/G1P1A[8]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10952;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Taniguchi K.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9598939;
RX   DOI=10.1002/(sici)1096-9071(199806)55:2<168::aid-jmv14>3.0.co;2-e;
RA   Wu H., Taniguchi K., Urasawa T., Urasawa S.;
RT   "Serological and genomic characterization of human rotaviruses detected in
RT   China.";
RL   J. Med. Virol. 55:168-176(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=30258011; DOI=10.1128/jvi.01363-18;
RA   Dhillon P., Rao C.D.;
RT   "Rotavirus Induces Formation of Remodeled Stress Granules and P Bodies and
RT   Their Sequestration in Viroplasms To Promote Progeny Virus Production.";
RL   J. Virol. 92:0-0(2018).
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 (By similarity). Participates in the
CC       selective exclusion of host proteins from stress granules (SG) and P
CC       bodies (PB) (PubMed:30258011). Participates also in the sequestration
CC       of these remodeled organelles in viral factories (PubMed:30258011).
CC       {ECO:0000255|HAMAP-Rule:MF_04092, ECO:0000269|PubMed:30258011}.
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. Interacts with host DCP1A, DCP1B, DDX6, EDC4, EIF2S1/eIF2-alpha,
CC       AGO2 and CAPRIN1; these interactions are probably part of the
CC       sequestration of some host SGs and PBs proteins in viral factories.
CC       {ECO:0000255|HAMAP-Rule:MF_04092, ECO:0000269|PubMed:30258011}.
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; AB022773; BAA84970.1; -; mRNA.
DR   EMBL; AB008661; BAB83818.1; -; mRNA.
DR   SMR; Q9QNA5; -.
DR   Proteomes; UP000001458; 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   2: Evidence at transcript level;
KW   Glycoprotein; Host cytoplasm; Host-virus interaction; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; RNA-binding.
FT   CHAIN           1..197
FT                   /note="Non-structural protein 5"
FT                   /id="PRO_0000369501"
FT   REGION          16..36
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          129..167
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         153
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT   MOD_RES         155
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT   MOD_RES         163
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
FT   MOD_RES         165
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
SQ   SEQUENCE   197 AA;  21595 MW;  5EB50A87DC9A4FE5 CRC64;
     MSLSIDVTSL PSISSSIFKN ESSSTTSTLS GKSIGRNEQY VSPDIDAFNK YMLSKSPEDI
     GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSTQSRPS SNVGCDQMDF SLNKGINVSA
     SLDSCVSIST NQKKEKSKKD KSRKHYPRIE ADSDSEDYVL DDSDSDDGKC KNCKYKKKYF
     ALRMRMKQVA MQLIEDL
//