NSP5_ROTHD
ID NSP5_ROTHD Reviewed; 198 AA.
AC P23048; B3SRT3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 69.
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/DS-1/1976/G2P1B[4]) (RV-A)
OS (Rotavirus A (strain DS1)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10950;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2152809; DOI=10.1128/jvi.64.1.120-124.1990;
RA Matsui S.M., Mackow E.R., Matsuno S., Paul P.S., Greenberg H.B.;
RT "Sequence analysis of gene 11 equivalents from 'short' and 'super short'
RT strains of rotavirus.";
RL J. Virol. 64:120-124(1990).
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; M33608; AAA47327.1; -; Genomic_RNA.
DR EMBL; EF672583; ABV53258.1; -; Genomic_RNA.
DR Proteomes; UP000001457; 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..198
FT /note="Non-structural protein 5"
FT /id="PRO_0000149636"
FT REGION 13..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..106
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"
FT CONFLICT 9
FT /note="G -> S (in Ref. 2; ABV53258)"
FT CONFLICT 49
FT /note="R -> N (in Ref. 2; ABV53258)"
FT CONFLICT 138
FT /note="K -> KQE (in Ref. 2; ABV53258)"
SQ SEQUENCE 198 AA; 21741 MW; 0E4D75A0EE588A14 CRC64;
MSLSIDVTGL PSISSSVYKN ESSSTTSTIS GKSIGRSEQY ISPDAEAFRK YMLSKSPEDI
GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSAQSRPS SDIGYDQMDF SLNKGIKFDA
TVDSSISIST TSKKEKSKNK NKYKKCYPKI EAESDSDDYI LDDSDSDDGK CKNCKYKKKY
FALRLRMKQV AMQLIKDL
