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Entry version 143 (29 Sep 2021)
Sequence version 4 (24 Jul 2013)
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Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 3 (HRV-3)
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>
-Experimental evidence at protein leveli <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_section">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_section">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_section">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 sitei875For protease 2A activityBy similarity1
Active sitei893For protease 2A activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi910Zinc; structuralBy similarity1
Metal bindingi912Zinc; structuralBy similarity1
Active sitei964For protease 2A activityBy similarity1
Metal bindingi970Zinc; structuralBy similarity1
Metal bindingi972Zinc; 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>Sitei1124Involved in the interaction with host RTN3By similarity1
Metal bindingi1368ZincBy similarity1
Metal bindingi1371ZincBy similarity1
Metal bindingi1380ZincBy similarity1
Metal bindingi1385ZincBy similarity1
Active sitei1576For protease 3C activityPROSITE-ProRule annotation1
Active sitei1607For protease 3C activityPROSITE-ProRule annotation1
Active sitei1682For protease 3C activityPROSITE-ProRule annotation1
Metal bindingi1951Magnesium 1; catalytic; for RdRp activityBy similarity1
Metal bindingi1951Magnesium 2; catalytic; for RdRp activityBy similarity1
Metal bindingi2045Magnesium 1; catalytic; for RdRp activityBy similarity1
Metal bindingi2045Magnesium 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_section">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 fingeri1368 – 1385C4-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

GO - Biological processi

<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
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_and_taxonomy_section">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:
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Virion protein 4
Alternative name(s):
P1B
Virion protein 2
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
P1D
Virion protein 1
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
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_and_taxonomy_section">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>OrganismiHuman rhinovirus 3 (HRV-3)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri44130 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiVirusesRiboviriaOrthornaviraePisuviricotaPisoniviricetesPicornaviralesPicornaviridaeEnterovirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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
  • UP000165566 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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
  • UP000013737 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_location_section">'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 – 1490CytoplasmicSequence analysisAdd BLAST1489
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Intramembranei1491 – 1506Sequence analysisAdd BLAST16
Topological domaini1507 – 2178CytoplasmicSequence analysisAdd BLAST672

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_processing_section">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_00004265212 – 2178Genome polyproteinAdd BLAST2177
ChainiPRO_00004265222 – 855P1Add BLAST854
ChainiPRO_00004265232 – 331Capsid protein VP0Add BLAST330
ChainiPRO_00004265242 – 69Capsid protein VP4Add BLAST68
ChainiPRO_000042652570 – 331Capsid protein VP2Add BLAST262
ChainiPRO_0000426526332 – 561Capsid protein VP3Add BLAST230
ChainiPRO_0000426527562 – 855Capsid protein VP1Add BLAST294
ChainiPRO_0000426528856 – 1428P2Add BLAST573
ChainiPRO_0000423099856 – 1001Protease 2AAdd BLAST146
ChainiPRO_00004231001002 – 1098Protein 2BAdd BLAST97
ChainiPRO_00004265291099 – 1428Protein 2CAdd BLAST330
ChainiPRO_00004265301429 – 2178P3Add BLAST750
ChainiPRO_00004265311429 – 1536Protein 3ABAdd BLAST108
ChainiPRO_00004231021429 – 1513Protein 3AAdd BLAST85
ChainiPRO_00004265321514 – 1536Viral protein genome-linkedAdd BLAST23
ChainiPRO_00004265331537 – 2178Protein 3CDAdd BLAST642
ChainiPRO_00004265341537 – 1718Protease 3CAdd BLAST182
ChainiPRO_00004265351719 – 2178RNA-directed RNA polymeraseAdd BLAST460

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 residuei1516O-(5'-phospho-RNA)-tyrosineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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
Sitei331 – 332Cleavage; by protease 3CBy similarity2
Sitei855 – 856Cleavage; by autolysisBy similarity2
Sitei1001 – 1002Cleavage; by protease 3CBy similarity2
Sitei1098 – 1099Cleavage; by protease 3CBy similarity2
Sitei1428 – 1429Cleavage; by protease 3CBy similarity2
Sitei1513 – 1514Cleavage; by protease 3CBy similarity2
Sitei1536 – 1537Cleavage; by protease 3CBy similarity2
Sitei1718 – 1719Cleavage; by protease 3CBy similarity2

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q82081

<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_section">'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_section">'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

Secondary structure

12178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q82081

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q82081

<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_and_domains_section">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>Domaini1204 – 1360SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1537 – 1714Peptidase C3PROSITE-ProRule annotationAdd BLAST178
Domaini1946 – 2059RdRp catalyticPROSITE-ProRule annotationAdd BLAST114

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>Regioni1 – 20DisorderedSequence analysisAdd BLAST20
Regioni564 – 584Amphipathic alpha-helixSequence analysisAdd BLAST21
Regioni1100 – 1238OligomerizationBy similarityAdd BLAST139
Regioni1100 – 1172Membrane-bindingBy similarityAdd BLAST73
Regioni1121 – 1125RNA-bindingBy similarity5
Regioni1412 – 1419RNA-bindingBy similarity8
Regioni1423 – 1428OligomerizationBy 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 fingeri1368 – 1385C4-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
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
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

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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q82081-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASSS SAGQSFSMDP
60 70 80 90 100
SKFTEPVKDL MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA
110 120 130 140 150
IVCYAEWPEY LSDNDASDVN KTSKPDISVC RFYTLDSKTW KATSKGWCWK
160 170 180 190 200
LPDALKDMGV FGQNMFYHSL GRTGYTIHVQ CNATKFHSGC LLVVVIPEHQ
210 220 230 240 250
LASHEGGTVS VKYKYTHPGD RGIDLDTVEV AGGPTSDAIY NMDGTLLGNL
260 270 280 290 300
LIFPHQFINL RTNNTATIVV PYINSVPIDS MTRHNNVSLM VVPIAPLNAP
310 320 330 340 350
TGSSPTLPVT VTIAPMCTEF TGIRSRSIVP QGLPTTTLPG SGQFLTTDDR
360 370 380 390 400
QSPSALPSYE PTPRIHIPGK VRNLLEIIQV GTLIPMNNTG TNDNVTNYLI
410 420 430 440 450
PLHADRQNEQ IFGTKLYIGD GVFKTTLLGE IAQYYTHWSG SLRISLMYTG
460 470 480 490 500
PALSSAKIIL AYTPPGTRGP EDRKEAMLGT HVVWDIGLQS TIVMTIPWTS
510 520 530 540 550
GVQFRYTDPD TYTSAGYLSC WYQTSLILPP QTSGQVYLLS FISACPDFKL
560 570 580 590 600
RLMKDTQTIS QTDALTEGLS DELEEVIVEK TKQTLASVSS GPKHTQSVPA
610 620 630 640 650
LTANETGATL PTRPSDNVET RTTYMHFNGS ETDVESFLGR AACVHVTEIK
660 670 680 690 700
NKNAAGLDNH RKEGLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT
710 720 730 740 750
ASQPEASSYS SNLTVQAMYV PPGAPNPKEW DDYTWQSASN PSVFFKVGET
760 770 780 790 800
SRFSVPFVGI ASAYNCFYDG YSHDDPDTPY GITVLNHMGS MAFRVVNEHD
810 820 830 840 850
VHTTIVKIRV YHRAKHVEAW IPRAPRALPY VSIGRTNYPR DSKTIIKKRT
860 870 880 890 900
NIKTYGLGPR FGGVFTSNVK IINYHLMTPD DHLNLVAPYP NRDLAVVATG
910 920 930 940 950
AHGAETIPHC NCTSGVYYSR YYRKFYPIIC ERPTNIWIEG SSYYPSRYQA
960 970 980 990 1000
GVMKGVGPAE PGDCGGILRC IHGPIGLLTA GGGGYVCFAD IRQLDFIADE
1010 1020 1030 1040 1050
QGLGDYITSL GRAFGTGFTD QISAKVCELQ DVAKDFLTTK VLSKVVKMIS
1060 1070 1080 1090 1100
ALVIICRNHD DLVTVTATLA LLGCDGSPWR FLKMYISKHF QVPYIERQAN
1110 1120 1130 1140 1150
DGWFRKFNDA CNAAKGLEWI ANKISKLIEW IKNKVLPQAR EKLEFCSKLK
1160 1170 1180 1190 1200
QLDILERQIA SIHDSNPTQE KREQLFNNVL WLEQMSQKFS PLYASEAKRI
1210 1220 1230 1240 1250
RDLKNKITNY MQFKSKQRTE PVCVLIHGTP GSGKSLTTSI VGRALAEHFN
1260 1270 1280 1290 1300
SSVYSLPPDP KHFDGYQQQE VVIMDDLNQN PDGQDISMFC QMVSSVDFLP
1310 1320 1330 1340 1350
PMASLDNKGM LFTSNFVLAS TNSNTLSPPT ILNPEALIRR FGFDLDICMH
1360 1370 1380 1390 1400
STYTKNGKLN AAMATSLCKD CHQPSNFKKC CPLVCGKAIS LVDRVSNVRF
1410 1420 1430 1440 1450
SIDQLVTAII NDYKNKVKIT DSLEVLFQGP VYKDLEIDIC NTPPPECISD
1460 1470 1480 1490 1500
LLKSVDSEEV REYCKKKKWI IPQISTNIER AVNQASMIIN TILMFVSTLG
1510 1520 1530 1540 1550
IVYVIYKLFA QTQGPYSGNP VHNKLKPPTL KPVVVQGPNT EFALSLLRKN
1560 1570 1580 1590 1600
ILTITTEKGE FTSLGIHDRI CVLPTHAQPG DNVLVNGQKI QIKDKYKLVD
1610 1620 1630 1640 1650
PDNTNLELTI IELDRNEKFR DIRGFISEDL EGLDATLVVH SNGFTNTILD
1660 1670 1680 1690 1700
VGPITMAGLI NLSNTPTTRM IRYDYPTKTG QCGGVLCTTG KIFGIHVGGN
1710 1720 1730 1740 1750
GRRGFSAQLK KQYFVEKQGL IVSKQKVRDI GLNPINTPTK TKLHPSVFYN
1760 1770 1780 1790 1800
VFPGSKQPAV LNDNDPRLEV KLAESLFSKY KGNVQMEPTE NMLIAVDHYA
1810 1820 1830 1840 1850
GQLMSLDIST KELTLKEALY GVDGLEPIDV TTSAGYPYVS LGIKKRDILN
1860 1870 1880 1890 1900
KETQDVEKMK FYLDKYGIDL PLVTYIKDEL RSVDKVRLGK SRLIEASSLN
1910 1920 1930 1940 1950
DSVNMRMKLG NLYKAFHQNP GIITESAVGC DPDVFWSVIP CLMDGHLMAF
1960 1970 1980 1990 2000
DYSNFDASLS PVWFECLEKV LNKLGFKQPS LIQSICNTHH IFRDEIYRVE
2010 2020 2030 2040 2050
GGMPSGCSGT SIFNSMINNI IIRTLILDAY KGIDLDSLRI LAYGDDLIVS
2060 2070 2080 2090 2100
YPFELDSNIL AAIGKNYGLT ITPPDKSDAF TKITWENITF LKRYFRPDPQ
2110 2120 2130 2140 2150
FPFLIHPVMP MQDIYESIRW TRDPRNTQDH VRSLCMLAWH SGEKDYNDFI
2160 2170
TKIRTTDIGK CLNLPEYSVL RRRWLDLF
Length:2,178
Mass (Da):242,794
Last modified:July 24, 2013 - v4
<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:i0DFED5280AF25CCF
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti87L → M. 1
Natural varianti98A → R. 1
Natural varianti260L → M. 1
Natural varianti475E → K. 1
Natural varianti523Q → L. 1
Natural varianti846I → V. 1
Natural varianti1349M → L. 1
Natural varianti1389I → V. 1
Natural varianti1703R → Q. 1
Natural varianti1925E → G. 1
Natural varianti1978Q → H. 1

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
DQ473485 Genomic RNA Translation: ABF51179.1
EF173422 Genomic RNA Translation: ABO69378.1
U60874 Genomic RNA Translation: AAB05616.1

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ473485 Genomic RNA Translation: ABF51179.1
EF173422 Genomic RNA Translation: ABO69378.1
U60874 Genomic RNA Translation: AAB05616.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RHIX-ray3.001568-855[»]
270-331[»]
3332-567[»]
42-69[»]
SMRiQ82081
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiN08.001

Proteomic databases

PRIDEiQ82081

Miscellaneous databases

EvolutionaryTraceiQ82081

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
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
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_HRV3
<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: Q82081
Secondary accession number(s): A5GZD4, A7KC14
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 24, 2013
Last modified: September 29, 2021
This is version 143 of the entry and version 4 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

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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