UniProt functional annotation for Q83883



	UniProt functional annotation for Q83883

UniProt code: Q83883.

Organism: Norwalk virus (strain GI/Human/United States/Norwalk/1968) (Hu/NV/NV/1968/US).

Taxonomy: Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; Picornavirales; Caliciviridae; Norovirus.

Function: Protein p48 may play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes.

Function: NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.

Function: Protein P22 may play a role in targeting replication complex to intracellular membranes.

Function: Viral genome-linked protein is covalently linked to the 5'- end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation.

Function: 3C-like protease processes the polyprotein: 3CLpro-RdRp is first released by autocleavage, then all other proteins are cleaved. May cleave host polyadenylate-binding protein thereby inhibiting cellular translation (By similarity). {ECO:0000250}.

Function: RNA-directed RNA polymerase replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA codes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.

Catalytic activity: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;

Catalytic activity: Reaction=Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE- ProRule:PRU00870};

Catalytic activity: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};

Subunit: [Protein p48]: Interacts with human VAPA. {ECO:0000269|PubMed:14557663}.

Subcellular location: [Protein p48]: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.

Subcellular location: [NTPase]: Host membrane {ECO:0000305}; Single- pass membrane protein {ECO:0000305}.

Subcellular location: [Protein p22]: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.

Ptm: Specific enzymatic cleavages in vivo yield mature proteins. 3CLpro is first autocatalytically cleaved, then processes the whole polyprotein. {ECO:0000255|PROSITE-ProRule:PRU00870, ECO:0000269|PubMed:17554035}.

Ptm: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250}.

Annotations taken from UniProtKB at the EBI.


Organism:		Norwalk virus (strain GI/Human/United States/Norwalk/1968) (Hu/NV/NV/1968/US).
Taxonomy:		Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; Picornavirales; Caliciviridae; Norovirus.



Function:		Protein p48 may play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes.



Function:		NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.



Function:		Protein P22 may play a role in targeting replication complex to intracellular membranes.



Function:		Viral genome-linked protein is covalently linked to the 5'- end of the positive-strand, negative-strand genomic RNAs and subgenomic RNA. Acts as a genome-linked replication primer. May recruit ribosome to viral RNA thereby promoting viral proteins translation.



Function:		3C-like protease processes the polyprotein: 3CLpro-RdRp is first released by autocleavage, then all other proteins are cleaved. May cleave host polyadenylate-binding protein thereby inhibiting cellular translation (By similarity). {ECO:0000250}.



Function:		RNA-directed RNA polymerase replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This sgRNA codes for structural proteins. Catalyzes the covalent attachment VPg with viral RNAs (By similarity). {ECO:0000255\|PROSITE-ProRule:PRU00539}.


Catalytic activity:		Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
Catalytic activity:		Reaction=Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-\|-Xaa and the P1' position is occupied by Gly-\|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255\|PROSITE- ProRule:PRU00870};
Catalytic activity:		Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255\|PROSITE-ProRule:PRU00539};
Subunit:		[Protein p48]: Interacts with human VAPA. {ECO:0000269\|PubMed:14557663}.
Subcellular location:		[Protein p48]: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Subcellular location:		[NTPase]: Host membrane {ECO:0000305}; Single- pass membrane protein {ECO:0000305}.
Subcellular location:		[Protein p22]: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Ptm:		Specific enzymatic cleavages in vivo yield mature proteins. 3CLpro is first autocatalytically cleaved, then processes the whole polyprotein. {ECO:0000255\|PROSITE-ProRule:PRU00870, ECO:0000269\|PubMed:17554035}.
Ptm:		VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250}.