NSP5_ROTGI
ID NSP5_ROTGI Reviewed; 174 AA.
AC P30890;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 23-FEB-2022, entry version 49.
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 B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B)
OS (Rotavirus B (isolate infectious diarrhea of infant rats)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX NCBI_TaxID=28877;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1658208; DOI=10.1099/0022-1317-72-11-2801;
RA Petric M., Mayur K., Vonderfecht S., Eiden J.J.;
RT "Comparison of group B rotavirus genes 9 and 11.";
RL J. Gen. Virol. 72:2801-2804(1991).
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 -!- 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; D00912; BAA00758.1; -; Genomic_RNA.
DR PIR; JQ1310; JQ1310.
DR PRIDE; P30890; -.
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.
PE 3: Inferred from homology;
KW Glycoprotein; Host cytoplasm; Nucleotide-binding; RNA-binding.
FT CHAIN 1..174
FT /note="Non-structural protein 5"
FT /id="PRO_0000149630"
FT REGION 18..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 174 AA; 20057 MW; 76AE32FD271140DE CRC64;
MAEASEFNFN LRRKSRAVTA SRRVKEEVKE KQKMDDSKSQ VVDVDSVSVY SHESSRSNYS
DAYEKLKREP VVEESNDARY RTFEFSEDEE TFKPANKMSD KSQRNSKSKH TEGLECSDTV
LEKISELTLE IEKVKQMNQP ITVDAAFNMT LRNVDNLTTR QKQALVNSII NSMN