ID   NSP5_ROTGA              Reviewed;         170 AA.
AC   P18571;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   24-JAN-2024, entry version 57.
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/Human/China/ADRV/1982) (RV-B) (Rotavirus B
OS   (isolate adult diarrhea rotavirus)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus B.
OX   NCBI_TaxID=10942;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2158190; DOI=10.1016/0042-6822(90)90450-6;
RA   Chen G.-M., Hung T., Mackow E.R.;
RT   "cDNA cloning of each genomic segment of the group B rotavirus ADRV:
RT   molecular characterization of the 11th RNA segment.";
RL   Virology 175:605-609(1990).
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; M34380; AAA42674.1; -; Genomic_RNA.
DR   SMR; P18571; -.
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   InterPro; IPR020244; Rotavirus_B_NSP5.
DR   Pfam; PF17580; GBR_NSP5; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Host cytoplasm; Nucleotide-binding; RNA-binding.
FT   CHAIN           1..170
FT                   /note="Non-structural protein 5"
FT                   /id="PRO_0000149629"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   170 AA;  19938 MW;  34DFC9F882F9FE91 CRC64;
     MAEASEFNFT IKRKQRTMSD RRTREDTKQK KIEEKSDIDL VDSASVYSQE SSRSNYSDAY
     DKLKREPMVE ESNDAKYRNF EFSEDEEVHR PSSKASDKSY REMKRKHDDI NTSDSILEKL
     SELNLEIEKI KQMNQPITID AAFNMILRNV DNLTIRQKQA LINAIVNSMN
//