Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - Q66849 (POLG_EC09H)

Entry version 166 (23 Feb 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Genome polyprotein

Gene
N/A
Organism
Echovirus 9 (strain Hill)
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 to provide virion attachment to target host cells (By similarity).

This attachment induces virion internalization (By similarity).

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

Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (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

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

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

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 sitei880For protease 2A activityBy similarity1
Active sitei898For 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 bindingi915Zinc; structuralBy similarity1
Metal bindingi917Zinc; structuralBy similarity1
Active sitei969For protease 2A activityBy similarity1
Metal bindingi975Zinc; structuralBy similarity1
Metal bindingi977Zinc; 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>Sitei1133Involved in the interaction with host RTN3By similarity1
Metal bindingi1377ZincBy similarity1
Metal bindingi1389ZincBy similarity1
Metal bindingi1394ZincBy similarity1
Active sitei1588For protease 3C activityPROSITE-ProRule annotation1
Active sitei1619For protease 3C activityPROSITE-ProRule annotation1
Active sitei1695For protease 3C activityPROSITE-ProRule annotation1
Metal bindingi1964Magnesium 1; catalytic; for RdRp activityBy similarity1
Metal bindingi1964Magnesium 2; catalytic; for RdRp activityBy similarity1
Metal bindingi2060Magnesium 1; catalytic; for RdRp activityBy similarity1
Metal bindingi2060Magnesium 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 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 fingeri1377 – 1394C4-type; degenerateBy 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, DNA replication, Eukaryotic host gene expression 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 host innate immune response 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		C03.011

<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:
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
P3
Protein 3AB
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>OrganismiEchovirus 9 (strain Hill)
<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 identifieri103915 [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 B ›
<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
  • UP000008272 <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 – 1503CytoplasmicSequence analysisAdd BLAST1502
<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>Intramembranei1504 – 1519Sequence analysisAdd BLAST16
Topological domaini1520 – 2193CytoplasmicSequence analysisAdd BLAST674

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_00004264162 – 2193Genome polyproteinAdd BLAST2192
ChainiPRO_00004264172 – 855P1Add BLAST854
ChainiPRO_00004264182 – 330Capsid protein VP0Add BLAST329
ChainiPRO_00004264192 – 69Capsid protein VP4Add BLAST68
ChainiPRO_000042642070 – 330Capsid protein VP2Add BLAST261
ChainiPRO_0000426421331 – 569Capsid protein VP3Add BLAST239
ChainiPRO_0000426422570 – 855Capsid protein VP1Add BLAST286
ChainiPRO_0000426423856 – 1437P2Add BLAST582
ChainiPRO_0000426424856 – 1009Protease 2AAdd BLAST154
ChainiPRO_00000396971010 – 1108Protein 2BAdd BLAST99
ChainiPRO_00000396981109 – 1437Protein 2CAdd BLAST329
ChainiPRO_00004264251438 – 2193P3Add BLAST756
ChainiPRO_00004264261438 – 1548Protein 3ABAdd BLAST111
ChainiPRO_00000396991438 – 1526Protein 3AAdd BLAST89
ChainiPRO_00004264271527 – 1548Viral protein genome-linkedAdd BLAST22
ChainiPRO_00004264281549 – 2193Protein 3CDAdd BLAST645
ChainiPRO_00004264291549 – 1731Protease 3CAdd BLAST183
ChainiPRO_00004264301732 – 2193RNA-directed RNA polymeraseAdd BLAST462

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 residuei1529O-(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
Sitei330 – 331Cleavage; by protease 3CBy similarity2
Sitei855 – 856Cleavage; by autolysisBy similarity2
Sitei1009 – 1010Cleavage; by protease 3CBy similarity2
Sitei1108 – 1109Cleavage; by protease 3CBy similarity2
Sitei1437 – 1438Cleavage; by protease 3CBy similarity2
Sitei1526 – 1527Cleavage; by protease 3CBy similarity2
Sitei1548 – 1549Cleavage; by protease 3CBy similarity2
Sitei1731 – 1732Cleavage; by protease 3CBy similarity2

Keywords - PTMi

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

<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). 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

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

More...SMRi		Q66849

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>Domaini1213 – 1369SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1549 – 1727Peptidase C3PROSITE-ProRule annotationAdd BLAST179
Domaini1958 – 2074RdRp catalyticPROSITE-ProRule annotationAdd BLAST117

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>Regioni567 – 583Amphipathic alpha-helixSequence analysisAdd BLAST17
Regioni1109 – 1247OligomerizationBy similarityAdd BLAST139
Regioni1109 – 1181Membrane-bindingBy similarityAdd BLAST73
Regioni1130 – 1134RNA-bindingBy similarity5
Regioni1421 – 1428RNA-bindingBy similarity8
Regioni1432 – 1437OligomerizationBy 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 degenerate C4-type zinc-finger with only 3 cysteines (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 fingeri1377 – 1394C4-type; degenerateBy 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
4.10.80.10, 1 hit
6.10.20.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003593, AAA+_ATPase
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
IPR036988, Pico_P1A_sf
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

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00382, AAA, 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.

Q66849-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGAQVSTQKT GAHEASLSAT GSSIIHYTNI NYYKDSASNS ANRQDFTQDP 
        60         70         80         90        100
SKFTEPVKDV MIKSLPALNS PSAEECGFSD RVRSITIGNS TITTQECANV 
       110        120        130        140        150
VVAYGRWPTY LRDDEATAED QPTQPDVATC RFYTLESVQW QENSAGWWWK 
       160        170        180        190        200
FPDALSNMGL FGQNMLYHYL GRAGYTIHVQ CNASKFHQGC LLVVCVPEAE 
       210        220        230        240        250
MGCSKVDGVV NAQGLSKGEI PIEFERTSTT AEVGVVQKAV YNAGMGIGVG 
       260        270        280        290        300
NLTIFPHQWI NLRTNNSATI VIPYINCVPM DNMFRHNNFT LMVIPFAPLK 
       310        320        330        340        350
SSGGTNYVPV TITVAPMDAE YNGLRLAGHQ GLPTMNTPGS TQFLTSDDFQ 
       360        370        380        390        400
SPCAMPEFDV TPCMDIPGKV HNLMEIAEVD IGVPVNNTST HMEGTDAFQI 
       410        420        430        440        450
KVTAGNVQDK NAIFSFQLNP GNSTVLRRTL LGEILNYYAH WSGSIKLTFL 
       460        470        480        490        500
FCGSAMATGK LLLAYSPPGA SVPKARRDAM LGTHVIWDVG LQSSCVLCVP 
       510        520        530        540        550
WISQTHYRLV AQDEYTSAGY ITCWYQTNIV VPPETPSDCV VLCFVSACND 
       560        570        580        590        600
FSVRMLKDTP FIEQTTELQS DVREAVEGAI GRVADTIRSG PSNSEAVPAL 
       610        620        630        640        650
TAAETGHTSQ VVPSDTMQTR HVKNYHSRSE STIENFLCRS ACVRMAKYEA 
       660        670        680        690        700
RGNLKALTLD AWEISVRDMV QLRRKCEMFT YLRFDVEVTF VITSYQRQGT 
       710        720        730        740        750
SSIQICPYDA HQIMYIPPGG PIPKKVDGYE WQTSTNPSIF WTEGNAPPRM 
       760        770        780        790        800
SIPFISIGNA YSSFYDGWSH FDSKGAYGFN TLNKMGHIYC RHVNKETPTK 
       810        820        830        840        850
VTSYIRIYFK PKHVRAWVPR PPRLCQYMNK ANVNFEATAV TDTRDTINTV 
       860        870        880        890        900
PLSTHGVSRG AYGHQSGARY VGNYRIVNRH LATHTDWQKC VWEDYNRDLL 
       910        920        930        940        950
VSTTTAHGCD TIARCQCTTG VYFCASKNKH YPVSFEGPGL VEVQASEYYP 
       960        970        980        990       1000
KRYQSHVLLA AGFSEPGDCG GILRCEHGVI GIVTMGGEGV VGFADVRDLL 
      1010       1020       1030       1040       1050
WLEDDAMEQG VKDYVEQLGN AFGSGFTNQI CEQVNLLKES LVGQDSILEK 
      1060       1070       1080       1090       1100
SLKALVKIIS ALVIVVRNHD DLITVTAVLA LIGCTTSPWR WLKQKVSQYY 
      1110       1120       1130       1140       1150
GIPMAERQNN RWLKKFTEMT NACKGMEWIA IKIQKFIEWL KIKILPEVKE 
      1160       1170       1180       1190       1200
KHEFLNRLKQ LPLLESQIAT IEQSAPSQGD QEQLFSNIQY FAHYCRKYAP 
      1210       1220       1230       1240       1250
LYAAEAKRVF SLEKKMSNYI QFKSKCRIEP VCLLLHGSPG AGKSVATNLI 
      1260       1270       1280       1290       1300
GRSLAEKLNS SVYSLPPDPD HFDGYKQQAV VIMDDLCQNP DGKDVSLFCQ 
      1310       1320       1330       1340       1350
MVSSVDFVPP MAALEEKGIL FTSPFVLAST NAGSINAPTV SDSRALARRF 
      1360       1370       1380       1390       1400
HFDMNIEVIS MYSQNGKINM PMSVKTCDEE CCPVNFKKCC PLVCGKAIQF 
      1410       1420       1430       1440       1450
IDRRTQVRYS LDMLVTEMFR EYNHRHSVGT TLEALFQGPP IYREIKISVA 
      1460       1470       1480       1490       1500
PETPPPPAIA DLLKSVDSEA VREYCKEKGW LVPEVNSTLQ IEKHVSRAFI 
      1510       1520       1530       1540       1550
CLQALTTFVS VAGIIYIIYK LFAGFQGAYT GMPNQKPRVP TLRQAKVQGP 
      1560       1570       1580       1590       1600
AFEFAVAMMK RNSSTVKTEY GEFTMLGIYD RWAVLPRHAK PGPTILMNDQ 
      1610       1620       1630       1640       1650
EVGVLDAKEL VDKDGTNLEL TLLKLNRNEK FRDIRGFLAK EEVEVNEAVL 
      1660       1670       1680       1690       1700
AINTSKFPNM YIPVGQVTDY GFLNLGGTPT KRMLMYNFPT RAGQCGGVLM 
      1710       1720       1730       1740       1750
STGKVLGIHV GGNGHQGFSA ALLKHYFNDE QGEIEFIESS KEAGFPVINT 
      1760       1770       1780       1790       1800
PSKTKLEPSV FHQVFEGNKE PAVLRNGDPR LKANFEEALF SKYIGNVNTH 
      1810       1820       1830       1840       1850
VDEYMLEAVD HYAGQLATLD ISTEPMRLED AVYGTEGLEA LDLTTSAGYP 
      1860       1870       1880       1890       1900
YVALGIKKRD ILSKKTRDLT KLKECMDKYG LNLPMVTYVK DELRSAEKVA 
      1910       1920       1930       1940       1950
KGKSRLIEAS SLNDSVAMRQ TFGNLYKTFH LNPGIVTGSA SGCDPDLFWS 
      1960       1970       1980       1990       2000
KIPVMLDGHL IAFDYSGYDA SLSPVWFACL KLLLEKLGYS HKETNYIDYL 
      2010       2020       2030       2040       2050
CNSHHLYRDK HYFVRGGMPS GCSGTSIFNS MINNIIIRTL MLKVYKGIDL 
      2060       2070       2080       2090       2100
DQFRMIAYGD DVIASYPWPI DASLLAEAGK DYGLIMTPAD KGECFNEVTW 
      2110       2120       2130       2140       2150
TNVTFLKRYF RADEQYPFLV HPVMPMKDIH ESIRWTKDPK NTQDHVRSLC 
      2160       2170       2180       2190 
LLAWHNGERE YEEFIRKIRS VPVGRCLTLP AFSTLRRKWL DSF
Length:2,193
Mass (Da):245,058
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:iE6ADD3091293C64A
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
X84981 Genomic RNA Translation: CAA59341.1

<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
X84981 Genomic RNA Translation: CAA59341.1

3D structure databases

SMRiQ66849
ModBaseiSearch...

Protein family/group databases

MEROPSiC03.011

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
4.10.80.10, 1 hit
6.10.20.20, 1 hit
InterProiView protein in InterPro
IPR003593, AAA+_ATPase
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
IPR036988, Pico_P1A_sf
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
SMARTiView protein in SMART
SM00382, AAA, 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_EC09H
<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: Q66849
<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: July 15, 1999
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 166 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again