AC   MF_04089;
DC   Protein; auto
TR   HAMAP; MF_04089; -; 1; level=0
XX
Names: ROTA_NSP2
XX
ID   NSP2
DE   RecName: Full=Non-structural protein 2;
DE            Short=NSP2;
DE            EC=3.6.4.-;
DE   AltName: Full=NCVP3;
DE   AltName: Full=Non-structural RNA-binding protein 35;
DE            Short=NS35;
XX
CC   -!- FUNCTION: Participates in replication and packaging of the viral
CC       genome. Plays a crucial role, together with NSP5, in the formation of
CC       virus factories (viroplasms) which are large inclusions in the host
CC       cytoplasm where replication intermediates are assembled and viral RNA
CC       replication takes place. Displays ssRNA binding, NTPase, RNA
CC       triphosphatase (RTPase) and ATP-independent helix-unwinding activities.
CC       The unwinding activity may prepare and organize plus-strand RNAs for
CC       packaging and replication by removing interfering secondary structures.
CC       The RTPase activity plays a role in the removal of the gamma-phosphate
CC       from the rotavirus RNA minus strands of dsRNA genome segments.
CC       Participates in the selective exclusion of host proteins from stress
CC       granules (SG) and P bodies (PB). Participates also in the sequestration
CC       of these remodeled organelles in viral factories.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBUNIT: Homooctamer. Interacts with VP1; this interaction is weak.
CC       Interacts with NSP5; this interaction leads to up-regulation of NSP5
CC       phosphorylation and formation of viral factories. Interacts with host
CC       DCP1A, DCP1B, DDX6, EDC4 and EIF2S1/eIF2-alpha; these interactions are
CC       probably part of the sequestration of some host SGs and PBs proteins in
CC       viral factories.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm. Note=Found in spherical
CC       cytoplasmic structures, called viral factories, that appear early after
CC       infection and are the site of viral replication and packaging.
CC   -!- SIMILARITY: Belongs to the rotavirus NSP2 family.
XX
DR   Pfam; PF02509; Rota_NS35; 1; trigger=no
XX
KW   ATP-binding
KW   Host cytoplasm
KW   Hydrolase
KW   Magnesium
KW   Metal-binding
KW   Nucleotide-binding
KW   RNA-binding
XX
GO   GO:0030430; C:host cell cytoplasm
GO   GO:0016817; F:hydrolase activity, acting on acid anhydrides
GO   GO:0046872; F:metal ion binding
GO   GO:0000166; F:nucleotide binding
GO   GO:0003723; F:RNA binding
GO   GO:0019079; P:viral genome replication
XX
FT   From: NSP2_ROTS1 (P03537)
FT   REGION          205..241
FT                   /note="RNA-binding"
FT   ACT_SITE        225
FT                   /note="For NTPase and RTPase activities"
FT   Condition: H
FT   From: NSP2_ROTSR (Q03243)
FT   BINDING         107..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [SDQ]-[VI]-[RLF]
FT   BINDING         221..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: H-G-[KH]
FT   BINDING         188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
FT   BINDING         227
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
XX
Size: 279-317;
Related: None;
Template: P03537; Q03243;
Scope:
 Viruses; Rotavirus
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.7 2023/08/29
//