NSP5_ROTHL
ID NSP5_ROTHL Reviewed; 197 AA.
AC A3DSL0; B3SRU9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 38.
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/Philippines/L26/1987/G12P1B[4]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10953;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17166908; DOI=10.1128/jvi.01622-06;
RA Rahman M., Matthijnssens J., Yang X., Delbeke T., Arijs I., Taniguchi K.,
RA Iturriza-Gomara M., Iftekharuddin N., Azim T., Van Ranst M.;
RT "Evolutionary history and global spread of the emerging G12 human
RT rotaviruses.";
RL J. Virol. 81:2382-2390(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=18786998; DOI=10.1128/jvi.01402-08;
RA Heiman E.M., McDonald S.M., Barro M., Taraporewala Z.F., Bar-Magen T.,
RA Patton J.T.;
RT "Group A human rotavirus genomics: evidence that gene constellations are
RT influenced by viral protein interactions.";
RL J. Virol. 82:11106-11116(2008).
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;
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}.
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; DQ146698; ABA34252.1; -; Genomic_RNA.
DR EMBL; EF672597; ABV53274.1; -; Genomic_RNA.
DR Proteomes; UP000001459; 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..197
FT /note="Non-structural protein 5"
FT /id="PRO_0000369503"
FT REGION 17..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 130..157
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; 21647 MW; 7B6473BC858FA36E CRC64;
MSLSIDVTSL PSISSSIFKN ESSSTTSTLS GKSIGRSEQY ISPDAEAFNK YMLSKSPEDI
GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSTQSRSS SNVGCDQLDF SLTKGINVNA
NLESCISIST DHKKEKSKKD KSRKHYPRIE ADSDSEDYIL DDSDSDDGKC KNCKYKKKYF
ALRMRMKRVA MQLIEDL
