NSP5_ROTPC
ID NSP5_ROTPC Reviewed; 210 AA.
AC P36358;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 (strain RVC/Pig/United States/Cowden/1980) (RV-C).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX NCBI_TaxID=10916;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8389118; DOI=10.1007/bf01318998;
RA Bremont M., Chabanne-Vautherot D., Cohen J.;
RT "Sequence analysis of three non structural proteins of a porcine group C
RT (Cowden strain) rotavirus.";
RL Arch. Virol. 130:85-92(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 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 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; X65938; CAA46741.1; -; mRNA.
DR PIR; B48357; B48357.
DR Proteomes; UP000008175; 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; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; RNA-binding.
FT CHAIN 1..210
FT /note="Non-structural protein 5"
FT /id="PRO_0000149644"
FT REGION 119..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04092"
SQ SEQUENCE 210 AA; 23393 MW; 4A3CD910803B0943 CRC64;
MSDFGINLDA ICDNVKYKSS NSRTGSQVSN RSSRRMDFVD EEELSTYFNS KASVTQSDSC
SNDLAVKTSI ITEAVICDES EHVSADAIQE KEESIMQVDD NVMKWMMDSH DGISMNGGIN
FSRSKSKTGR SDFTESKSET SVSAHVSAGI SSQLGMFNPI QNTVKKEAIS EMFEDEDGDG
CTCRNCPYRE KYLKLRNKMK SVLVDMINEM
