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UniProtKB - P06209 (POLG_POL32)

Entry version 177 (23 Feb 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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Protein

Genome polyprotein

Gene
N/A
Organism
Poliovirus type 3 (strain 23127)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity).

The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).

Capsid protein VP1 mainly forms the vertices of the capsid (By similarity).

Capsid protein VP1 interacts with host cell receptor PVR to provide virion attachment to target host cells (By similarity).

This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells (By similarity).

Tyrosine kinases are probably involved in the entry process (By similarity).

Virus binding to PVR induces increased junctional permeability and rearrangement of junctional proteins (By similarity).

Modulation of endothelial tight junctions, as well as cytolytic infection of endothelial cells themselves, may result in loss of endothelial integrity which may help the virus to reach the CNS (By similarity).

After binding to its receptor, the capsid undergoes conformational changes (By similarity).

Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity).

Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity).

By similarity

Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity).

The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).

By similarity

Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity).

The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).

By similarity

Lies on the inner surface of the capsid shell (By similarity).

After binding to the host receptor, the capsid undergoes conformational changes (By similarity).

Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity).

By similarity

Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity).

Allows the capsid to remain inactive before the maturation step (By similarity).

By similarity

Cysteine protease that cleaves viral polyprotein and specific host proteins (By similarity).

It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein (By similarity).

Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation (By similarity).

Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores including NUP98, NUP62 and NUP153 (By similarity).

Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity).

Cleaves and inhibits host IFIH1/MDA5, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (By similarity).

Cleaves and inhibits host MAVS, thereby inhibiting the type-I IFN production and the establishment of the antiviral state (By similarity).

By similarity

Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.

By similarity

Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.

By similarity

Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity.

By similarity

Localizes the viral replication complex to the surface of membranous vesicles (By similarity).

It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (By similarity).

This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).

Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (By similarity).

By similarity

Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity).

The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity).

Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity).

During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (By similarity).

By similarity

Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome.

By similarity

Major viral protease that mediates proteolytic processing of the polyprotein (By similarity).

Cleaves host EIF5B, contributing to host translation shutoff (By similarity).

Cleaves also host PABPC1, contributing to host translation shutoff (By similarity).

Cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production (By similarity).

Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment (By similarity).

By similarity

Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated.

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

RNA-directed RNA polymerase:
Mg2+By similarityNote: Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence of 3CDpro or 3CPro (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei898For protease 2A activityBy similarity1
Active sitei916For protease 2A activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi933Zinc; structuralBy similarity1
Metal bindingi935Zinc; structuralBy similarity1
Active sitei987For protease 2A activityBy similarity1
Metal bindingi993Zinc; structuralBy similarity1
Metal bindingi995Zinc; via pros nitrogen; structuralBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1149Involved in the interaction with host RTN3By similarity1
Metal bindingi1393ZincBy similarity1
Metal bindingi1396ZincBy similarity1
Metal bindingi1405ZincBy similarity1
Metal bindingi1410ZincBy similarity1
Active sitei1602For protease 3C activityPROSITE-ProRule annotation1
Active sitei1633For protease 3C activityPROSITE-ProRule annotation1
Active sitei1709For protease 3C activityPROSITE-ProRule annotation1
Metal bindingi1978Magnesium 1; catalytic; for RdRp activityBy similarity1
Metal bindingi1978Magnesium 2; catalytic; for RdRp activityBy similarity1
Metal bindingi2073Magnesium 1; catalytic; for RdRp activityBy similarity1
Metal bindingi2073Magnesium 2; catalytic; for RdRp activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1253 – 1260ATPPROSITE-ProRule annotation8
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1393 – 1410C4-typeBy similarityAdd BLAST18

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHelicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel
Biological processActivation of host autophagy by virus, Clathrin- and caveolin-independent endocytosis of virus by host, DNA replication, Eukaryotic host gene expression shutoff by virus, Eukaryotic host transcription shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of eukaryotic host transcription initiation by virus, Inhibition of host innate immune response by virus, Inhibition of host MAVS by virus, Inhibition of host MDA5 by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cell, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Protein family/group databases

MEROPS protease database

More...MEROPSi		N08.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 17 chains:
P3
Protein 3AB
P1
Capsid protein VP0
Alternative name(s):
VP4-VP2
Capsid protein VP4
Alternative name(s):
P1A
Virion protein 4
Capsid protein VP2
Alternative name(s):
P1B
Virion protein 2
Capsid protein VP3
Alternative name(s):
P1C
Virion protein 3
Capsid protein VP1
Alternative name(s):
P1D
Virion protein 1
P2
Protease 2A (EC:3.4.22.29By similarity)
Short name:
P2A
Alternative name(s):
Picornain 2A
Protein 2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15By similarity)
Short name:
P2C
Protein 3A
Short name:
P3A
Viral protein genome-linked
Short name:
VPg
Alternative name(s):
Protein 3B
Short name:
P3B
Protein 3CD (EC:3.4.22.28)
Protease 3CPROSITE-ProRule annotation (EC:3.4.22.28PROSITE-ProRule annotation)
Alternative name(s):
Picornain 3CPROSITE-ProRule annotation
Short name:
P3CPROSITE-ProRule annotation
RNA-directed RNA polymerasePROSITE-ProRule annotation (EC:2.7.7.48PROSITE-ProRule annotation)
Short name:
RdRp
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPoliovirus type 3 (strain 23127)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri12087 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiViruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Picornavirales › Picornaviridae › Enterovirus › Enterovirus C ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008474 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 1517CytoplasmicSequence analysisAdd BLAST1516
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1518 – 1533Sequence analysisAdd BLAST16
Topological domaini1534 – 2206CytoplasmicSequence analysisAdd BLAST673

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, T=pseudo3 icosahedral capsid protein, Virion

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; by hostBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004266412 – 2206Genome polyproteinAdd BLAST2205
ChainiPRO_00004266422 – 878P1Add BLAST877
ChainiPRO_00004266432 – 340Capsid protein VP0Add BLAST339
ChainiPRO_00004266442 – 69Capsid protein VP4Add BLAST68
ChainiPRO_000042664570 – 340Capsid protein VP2Add BLAST271
ChainiPRO_0000426646341 – 578Capsid protein VP3Add BLAST238
ChainiPRO_0000426647579 – 878Capsid protein VP1Add BLAST300
ChainiPRO_0000426648879 – 1453P2Add BLAST575
ChainiPRO_0000426649879 – 1027Protease 2AAdd BLAST149
ChainiPRO_00000401291028 – 1124Protein 2BAdd BLAST97
ChainiPRO_00000401301125 – 1453Protein 2CAdd BLAST329
ChainiPRO_00004266501454 – 2206P3Add BLAST753
ChainiPRO_00004266511454 – 1562Protein 3ABAdd BLAST109
ChainiPRO_00000401311454 – 1540Protein 3AAdd BLAST87
ChainiPRO_00004266521541 – 1562Viral protein genome-linkedAdd BLAST22
ChainiPRO_00004266531563 – 2206Protein 3CDAdd BLAST644
ChainiPRO_00004266541563 – 1745Protease 3CAdd BLAST183
ChainiPRO_00004266551746 – 2206RNA-directed RNA polymeraseAdd BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine; by hostBy similarity1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1543O-(5'-phospho-RNA)-tyrosineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.By similarity
Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion.By similarity
During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion.By similarity
Myristoylation is required during RNA encapsidation and formation of the mature virus particle.By similarity
VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei69 – 70Cleavage; by autolysisBy similarity2
Sitei340 – 341Cleavage; by protease 3CBy similarity2
Sitei878 – 879Cleavage; by autolysisBy similarity2
Sitei1027 – 1028Cleavage; by protease 3CBy similarity2
Sitei1124 – 1125Cleavage; by protease 3CBy similarity2
Sitei1453 – 1454Cleavage; by protease 3CBy similarity2
Sitei1540 – 1541Cleavage; by protease 3CBy similarity2
Sitei1562 – 1563Cleavage; by protease 3CBy similarity2
Sitei1745 – 1746Cleavage; by protease 3CBy similarity2

Keywords - PTMi

Autocatalytic cleavage, Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P06209

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers.

By similarity

Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers (By similarity).

Interacts with human PVR (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity).

Interacts with capsid protein VP2, capsid protein VP3 and capsid protein VP4 following cleavage of capsid protein VP0 (By similarity).

By similarity

Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid.

By similarity

Interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity).

Interacts with capsid protein VP4 in the mature capsid (By similarity).

Interacts with protein 2C; this interaction may be important for virion morphogenesis (By similarity).

By similarity

Interacts with capsid protein VP1 and capsid protein VP3.

By similarity

Homodimer.

By similarity

Homohexamer; forms a hexameric ring structure with 6-fold symmetry characteristic of AAA+ ATPases (By similarity).

Interacts (via N-terminus) with host RTN3 (via reticulon domain); this interaction is important for viral replication (By similarity).

Interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity).

By similarity

Interacts with protein 3CD.

By similarity

Homodimer (By similarity).

Interacts with host GBF1 (By similarity).

Interacts (via GOLD domain) with host ACBD3 (via GOLD domain); this interaction allows the formation of a viral protein 3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will stimulate the recruitment of host PI4KB in order to synthesize PI4P at the viral RNA replication sites (By similarity).

By similarity

Interacts with RNA-directed RNA polymerase.

By similarity

Interacts with protein 3AB and with RNA-directed RNA polymerase.

By similarity

Interacts with Viral protein genome-linked and with protein 3CD.

By similarity

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P06209

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P06209

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1229 – 1385SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1563 – 1741Peptidase C3PROSITE-ProRule annotationAdd BLAST179
Domaini1972 – 2087RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni579 – 603Amphipathic alpha-helixSequence analysisAdd BLAST25
Regioni579 – 599Amphipathic alpha-helixSequence analysisAdd BLAST21
Regioni1125 – 1263OligomerizationBy similarityAdd BLAST139
Regioni1125 – 1197Membrane-bindingBy similarityAdd BLAST73
Regioni1146 – 1150RNA-bindingBy similarity5
Regioni1437 – 1444RNA-bindingBy similarity8
Regioni1448 – 1453OligomerizationBy similarity6

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminus has membrane-binding (By similarity). The N-terminus also displays RNA-binding properties (By similarity). The N-terminus is involved in oligomerization (By similarity). The central part contains an ATPase domain and a C4-type zinc-finger (By similarity). The C-terminus is involved in RNA-binding (By similarity). The extreme C-terminus contains a region involved in oligomerization (By similarity).By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1393 – 1410C4-typeBy similarityAdd BLAST18

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Conserved Domains Database

More...CDDi		cd00205, rhv_like, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.10.10, 4 hits
2.60.120.20, 3 hits
3.30.70.270, 1 hit
6.10.20.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR043502, DNA/RNA_pol_sf
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
IPR014838, P3A
IPR036203, P3A_soluble_dom
IPR044067, PCV_3C_PRO
IPR000081, Peptidase_C3
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR003138, Pico_P1A
IPR002527, Pico_P2B
IPR001676, Picornavirus_capsid
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR033703, Rhv-like
IPR001205, RNA-dir_pol_C
IPR007094, RNA-dir_pol_PSvirus
IPR029053, Viral_coat

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08727, P3A, 1 hit
PF00548, Peptidase_C3, 1 hit
PF02226, Pico_P1A, 1 hit
PF00947, Pico_P2A, 1 hit
PF01552, Pico_P2B, 1 hit
PF00680, RdRP_1, 1 hit
PF00073, Rhv, 3 hits
PF00910, RNA_helicase, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494, SSF50494, 2 hits
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit
SSF89043, SSF89043, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51874, PCV_3C_PRO, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51218, SF3_HELICASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P06209-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYKDSASNA ASKQDYSQDP 
        60         70         80         90        100
SKFTEPLKDV LIKTAPALNS PNVEACGYSD RVLQLTLGNS TITTQEAANS 
       110        120        130        140        150
VVAYGRWPEF IRDDEANPVD QPTEPDVATS RFYTLDTVMW GKESRGWWWK 
       160        170        180        190        200
LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ CNASKFHQGS LGVFAIPEFC 
       210        220        230        240        250
LAGDSDTQRY TSYANANPGE KGGKFYAQFN KDTAVTSPKR EFCPVDYLLG 
       260        270        280        290        300
CGVLIGNAFV FPHQIINLRT NNSATLVLPY VNALSIDSMV KHNNWGIAIL 
       310        320        330        340        350
PLSPLDFAQD SSVEIPITVT IAPMCSEFNG LRNVTAPKLQ GLPVLNTPGS 
       360        370        380        390        400
NQYLTSDNHQ SPCAIPEFDV TPPIDIPGEV KNVMELAEID TMIPLNLENT 
       410        420        430        440        450
KRNTMDMYRV RLSDSANLSG PILCLSLSPA ADPRLSHTML GEVLNYYTHW 
       460        470        480        490        500
AGSLKFTFLF CGSMMATGKL LVAYAPPGAQ PPTSRKEAML GTHVIWDLGL 
       510        520        530        540        550
QSSCTMVVPW ISNVTYRQTT QDSFTEGGYI SMFYQTRIVV PLSTPKAMDM 
       560        570        580        590        600
LGFVSACNDF SVRLLRDTTH ISQAAMPQGV DDLITEVAQN ALALSLPKPQ 
       610        620        630        640        650
SNLPDTKASG PAHSKEVPTL TAVETGATNP LVPSDTVQTR HVIQQRSRSE 
       660        670        680        690        700
STIESFFARG ACVAIIEVDN EQPATNVQKL FATWRITYKD TVQLRRKLEF 
       710        720        730        740        750
FTYSRFDMEF TFVVTANFTN SNNGHALNQV YQIMYIPPGA PTPKSWDDYT 
       760        770        780        790        800
WQTSSNPSIF YTYGAAPARI SVPYVGLANA YSHFYDGFAK VPLKSDANDQ 
       810        820        830        840        850
VGDSLYSAMA VDDFGVLAIR VVNDHNPTKV TSKVRVYMKP KHVRVWCPRP 
       860        870        880        890        900
PRAVPYYGPG VDYKDGLAPL SEKGLTTYGF GHQNKAVYTA GYKICNYHLA 
       910        920        930        940        950
TQEDLQNAVS VMWNRDLLVT ESKAQGIDSI ARCNCSTGVY YCESRSRYYP 
       960        970        980        990       1000
VSFVGPTFQY MEANDYYPAR YQSHMLIGHG FASPGDCGGI LRCQHGVIGI 
      1010       1020       1030       1040       1050
ITAGGEGLVA FSDIRDLYAY EEEAMEQGIS SYVESLGAAF GSGFTQQIGD 
      1060       1070       1080       1090       1100
KIIELTGMVT STITEKLLKN LIKIVSSLVI ITRNYDDTTT VLATLALLGC 
      1110       1120       1130       1140       1150
DVSPWQWLKK KACDILEIPY VMRQGDSWLK KFTEACNAAK GLEWVSNKIS 
      1160       1170       1180       1190       1200
KFIDWLREKI IPQARDKLEF VTKLKQLEML ENQIATIHQS CPSQEHQEIL 
      1210       1220       1230       1240       1250
FNNVRWLSIQ SKRFAPLYAL EAKRIQKLEH TINNYIQFKS KHRIEPVCLL 
      1260       1270       1280       1290       1300
VHGSPGTGKS VATNLIARAI AEKENTSTYS LPPDPSHFDG YKQQGVVIMD 
      1310       1320       1330       1340       1350
DLNQNPDGAD MKLFCQMVST VEFIPPMASL EEKGILFTSN YVLASTNSSR 
      1360       1370       1380       1390       1400
ITPPTVAHSD ALARRFAFDM DIQVMSEYSR DGKLNMTMAT EMCKNCHQPA 
      1410       1420       1430       1440       1450
NFKRCCPLVC GKAIQLMDKS SRVRYSIDQI TTMIVNEKNR RSNIGNCMEA 
      1460       1470       1480       1490       1500
LFQGPLQYKD LKIDIKTTPP PECINDLLQA VDSQEVRDYC EKKGWIVNIT 
      1510       1520       1530       1540       1550
SQVQTERNIN RAMTILQAVT TFAAVAGVVY VMYKLFAGHQ GAYTGLPNKR 
      1560       1570       1580       1590       1600
PNVPTIRTAK VQGPGFDYAV AMAKRNILTA TTSKGEFTML GVHDNVAILP 
      1610       1620       1630       1640       1650
THASPGETIV IDGKEIEVLD AKALEDQAGT NLEITIVTLK RNEKFRDIRP 
      1660       1670       1680       1690       1700
HIPAQITETN DGVLIVNTSK YPNMYVPVGA VTEQGYLNLG GRQTARTLMY 
      1710       1720       1730       1740       1750
NFPTRAGQCG GVITCTGKVI GMHVGGNGSH GFAAALKRSY FTQSQGEIQW 
      1760       1770       1780       1790       1800
MRPSKEVGYP IINAPSKTKL EPSAFHYVFE GVKEPAVLTK NDPRFKTGFE 
      1810       1820       1830       1840       1850
EAIFSKYVGN KITEVDEYMK EAVDHYAGQL MSLDINTEQM CLEDAMYGTD 
      1860       1870       1880       1890       1900
GLEALDLSTS AGYPYVTMGK KKRDILNKQT RDTKEMQRLL DTYGINLPLV 
      1910       1920       1930       1940       1950
TYVKDELRSK TKVEQGKSRL IEASSLNDSV AMRMAFGNLY AAFHKNPGVV 
      1960       1970       1980       1990       2000
TGSAVGCDPD LFWSKIPVLM EEKLFAFDYT GYDASLSPAW FEALKMVLEK 
      2010       2020       2030       2040       2050
IGFGDRVDYI DYLNHSHHLY KNKTYCVKGG MPSGCSGTSI FNSMINNLII 
      2060       2070       2080       2090       2100
RTLLLKTYKG IDLDHLKMIA YGDDVIASYP HEVDASLLAQ SGKDYGLTMT 
      2110       2120       2130       2140       2150
PADKSATFET VTWENVTFLK RFFRADERYP FLIHPVMPMK EIHESIRWTK 
      2160       2170       2180       2190       2200
DPRNTQDHVR SLCLLAWHNG EDEYNKFLAM IRSVPIGRAL LLPEYSTLYR 

RWLDSF
Length:2,206
Mass (Da):245,733
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF226AD85403C37BA
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X04468 Genomic RNA Translation: CAA28155.1

Protein sequence database of the Protein Information Resource

More...PIRi		A27245, GNNY27

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04468 Genomic RNA Translation: CAA28155.1
PIRiA27245, GNNY27

3D structure databases

BMRBiP06209
SMRiP06209
ModBaseiSearch...

Protein family/group databases

MEROPSiN08.001

Proteomic databases

PRIDEiP06209

Family and domain databases

CDDicd00205, rhv_like, 3 hits
Gene3Di2.40.10.10, 4 hits
2.60.120.20, 3 hits
3.30.70.270, 1 hit
6.10.20.20, 1 hit
InterProiView protein in InterPro
IPR043502, DNA/RNA_pol_sf
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
IPR014838, P3A
IPR036203, P3A_soluble_dom
IPR044067, PCV_3C_PRO
IPR000081, Peptidase_C3
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR003138, Pico_P1A
IPR002527, Pico_P2B
IPR001676, Picornavirus_capsid
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR033703, Rhv-like
IPR001205, RNA-dir_pol_C
IPR007094, RNA-dir_pol_PSvirus
IPR029053, Viral_coat
PfamiView protein in Pfam
PF08727, P3A, 1 hit
PF00548, Peptidase_C3, 1 hit
PF02226, Pico_P1A, 1 hit
PF00947, Pico_P2A, 1 hit
PF01552, Pico_P2B, 1 hit
PF00680, RdRP_1, 1 hit
PF00073, Rhv, 3 hits
PF00910, RNA_helicase, 1 hit
SUPFAMiSSF50494, SSF50494, 2 hits
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit
SSF89043, SSF89043, 1 hit
PROSITEiView protein in PROSITE
PS51874, PCV_3C_PRO, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51218, SF3_HELICASE_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_POL32
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06209
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 177 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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