UniProt functional annotation for P04517



	UniProt functional annotation for P04517

UniProt code: P04517.

Organism: Tobacco etch virus (TEV).

Taxonomy: Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes; Patatavirales; Potyviridae; Potyvirus.

Function: [Capsid protein]: involved in aphid transmission, cell-to- cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.

Function: [Nuclear inclusion protein B]: an RNA-dependent RNA polymerase that plays an essential role in the virus replication.

Function: [Helper component proteinase]: required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.

Function: [Cytoplasmic inclusion protein]: has helicase activity. It may be involved in replication.

Function: Both 6K peptides are indispensable for virus replication. {ECO:0000250, ECO:0000269|PubMed:11414807, ECO:0000269|PubMed:9880030}.

Function: [Nuclear inclusion protein A]: has RNA-binding and proteolytic activities.

Catalytic activity: Reaction=Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.; EC=3.4.22.44;

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};

Catalytic activity: Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.; EC=3.4.22.45;

Subunit: Nuclear inclusion protein A protease is a dimer; disulfide- linked. {ECO:0000269|PubMed:12377789, ECO:0000269|PubMed:15919091}.

Subcellular location: [Capsid protein]: Virion {ECO:0000305}.

Domain: The N-terminus of helper component proteinase is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus.

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

Ptm: Potyviral RNA is expressed as two polyproteins which undergo post- translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity). {ECO:0000250}.

Miscellaneous: [Isoform Genome polyprotein]: Produced by conventional translation.

Similarity: Belongs to the potyviridae genome polyprotein family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Tobacco etch virus (TEV).
Taxonomy:		Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes; Patatavirales; Potyviridae; Potyvirus.



Function:		[Capsid protein]: involved in aphid transmission, cell-to- cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.



Function:		[Nuclear inclusion protein B]: an RNA-dependent RNA polymerase that plays an essential role in the virus replication.



Function:		[Helper component proteinase]: required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.



Function:		[Cytoplasmic inclusion protein]: has helicase activity. It may be involved in replication.



Function:		Both 6K peptides are indispensable for virus replication. {ECO:0000250, ECO:0000269\|PubMed:11414807, ECO:0000269\|PubMed:9880030}.



Function:		[Nuclear inclusion protein A]: has RNA-binding and proteolytic activities.


Catalytic activity:		Reaction=Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-\|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.; EC=3.4.22.44;
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};
Catalytic activity:		Reaction=Hydrolyzes a Gly-\|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-\|-Gly, in the processing of the potyviral polyprotein.; EC=3.4.22.45;
Subunit:		Nuclear inclusion protein A protease is a dimer; disulfide- linked. {ECO:0000269\|PubMed:12377789, ECO:0000269\|PubMed:15919091}.
Subcellular location:		[Capsid protein]: Virion {ECO:0000305}.
Domain:		The N-terminus of helper component proteinase is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus.
Ptm:		VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250}.
Ptm:		Potyviral RNA is expressed as two polyproteins which undergo post- translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity). {ECO:0000250}.
Miscellaneous:		[Isoform Genome polyprotein]: Produced by conventional translation.
Similarity:		Belongs to the potyviridae genome polyprotein family. {ECO:0000305}.