AC   MF_04092;
DC   Protein; auto
TR   HAMAP; MF_04092; -; 1; level=0
XX
Names: ROTA_NSP5
XX
ID   NSP5
DE   RecName: Full=Non-structural protein 5;
DE            Short=NSP5;
DE   AltName: Full=NS26;
XX
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. Participates in the selective
CC       exclusion of host proteins from stress granules (SG) and P bodies (PB).
CC       Participates also in the sequestration of these remodeled organelles in
CC       viral factories.
case <FTTag:Metal>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
end case
case <FTGroup:1>
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. Interacts with host DCP1A, DCP1B, DDX6, EDC4, EIF2S1/eIF2-alpha,
CC       AGO2 and CAPRIN1; these interactions are probably part of the
CC       sequestration of some host SGs and PBs proteins in viral factories.
else
CC   -!- SUBUNIT: Homodimer. Interacts with VP1. Interacts with VP2. Interacts
CC       with NSP2 and NSP6.
end case
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm. Note=Found in spherical
CC       cytoplasmic structures, called virus factories, that appear early after
CC       infection and are the site of viral replication and packaging.
CC   -!- PTM: O-glycosylated.
case <FTGroup:1>
CC   -!- PTM: Hyperphosphorylated on serine residues, when in dimeric form.
CC       Phosphorylation by host CK1 is required for the hyperphosphorylation of
CC       NSP5 dimer.
end case
CC   -!- SIMILARITY: Belongs to the rotavirus NSP5 family.
XX
DR   Pfam; PF01525; Rota_NS26; 1; trigger=no
DR   Pfam; PF17580; GBR_NSP5; 1; trigger=no
DR   PIRSF; PIRSF004006; Rota_NS26; 1; trigger=no
XX
KW   Glycoprotein
KW   Host cytoplasm
case <FTTag:Metal>
KW   Magnesium
KW   Metal-binding
end case
KW   Nucleotide-binding
KW   RNA-binding
case <FTGroup:1>
KW   Phosphoprotein
end case
XX
GO   GO:0030430; C:host cell cytoplasm
GO   GO:0016887; F:ATP hydrolysis activity
GO   GO:0000287; F:magnesium ion binding
GO   GO:0000166; F:nucleotide binding
GO   GO:0003723; F:RNA binding
GO   GO:0019079; P:viral genome replication
XX
FT   From: NSP5_ROTSH (A2T3Q9)
FT   BINDING         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Tag: Metal; Condition: D
FT   MOD_RES         67
FT                   /note="Phosphoserine; by host CK1"
FT   Group: 1; Condition: S
FT   MOD_RES         154
FT                   /note="Phosphoserine; by host"
FT   Group: 1; Condition: S
FT   MOD_RES         156
FT                   /note="Phosphoserine; by host"
FT   Group: 1; Condition: S
FT   MOD_RES         164
FT                   /note="Phosphoserine; by host"
FT   Group: 1; Condition: S
FT   MOD_RES         166
FT                   /note="Phosphoserine; by host"
FT   Group: 1; Condition: S
XX
Size: 170-212;
Related: None;
Template: A2T3Q9;
Scope:
 Viruses; Rotavirus
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.8 2023/08/29
//