NSP5_ROTBS
ID NSP5_ROTBS Reviewed; 209 AA.
AC P34718;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 58.
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/Cow/Japan/Shintoku/1991/G2P[3]) (RV-C).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX NCBI_TaxID=33723;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8389040; DOI=10.1093/nar/21.9.2250;
RA Jiang B., Tsunemitsu H., Gentsch J.R., Saif L.J., Glass R.I.;
RT "Nucleotide sequences of genes 6 and 10 of a bovine group C rotavirus.";
RL Nucleic Acids Res. 21:2250-2250(1993).
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 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; L12391; -; NOT_ANNOTATED_CDS; Genomic_RNA.
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 RNA-binding.
FT CHAIN 1..209
FT /note="Non-structural protein 5"
FT /id="PRO_0000149642"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
SQ SEQUENCE 209 AA; 23438 MW; 820AC9B3C9DA1956 CRC64;
MSDFGINLDA ICDNVRRNSS NSSIKSQVSN RSSRKMDFVD EDELSTYFNS KTSVTQSDSC
SNDLNVKHSI IAEAVVCDES AHVSADAVQE KDVVVPKMDE SVMKWMMDSH DGICVNGGLN
FSKLKNKSNE HETKVTSETN VSAHVSAGIN SQLGMFNPIQ HKIKKEAIPE MFEDEDTDEC
TCRNCPYKEK YLKLRKKLKN VLVDIITEM