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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

Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. 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
Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. 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
Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. 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. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).By similarity
Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).By similarity
Protein 2B: 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).By similarity
Protein 2C: 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).By similarity
Protein 3AB: 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).By similarity
Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).By similarity
Viral protein genome-linked: 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. 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. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).By similarity
Protein 3CD: Is 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. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).By similarity
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).By similarity
RNA-directed RNA polymerase: 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).PROSITE-ProRule annotation

<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

  • Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. EC:3.4.22.29
  • Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly. EC:3.4.22.28

<p>This subsection of the ‘Function’ 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

RNA-directed RNA polymerase: replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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
Active sitei987For Protease 2A activityBy similarity1
Active sitei1602For Protease 3C activitySequence analysis1
Active sitei1633For Protease 3C activitySequence analysis1
Active sitei1709For Protease 3C activitySequence analysis1
Active sitei2073For RdRp activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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>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, 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 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, Nucleotide-binding

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C03.001

<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:3.4.22.29)
Short name:
P2A
Alternative name(s):
Picornain 2A
Protein 2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3A
Short name:
P3A
Alternative name(s):
Protein 3B
Short name:
P3B
Protease 3C (EC:3.4.22.28)
Short name:
P3C
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>OrganismiPoliovirus type 3 (strain 23127)
<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 identifieri12087 [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 lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus C
<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
  • UP000008474 <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

<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

Capsid protein VP0 :
Capsid protein VP2 :
Capsid protein VP3 :
Capsid protein VP1 :
Protein 2B :
Protein 2C :
Protein 3A :
Protein 3AB :
Protein 3CD :
RNA-directed RNA polymerase :

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 – 1517CytoplasmicSequence analysisAdd BLAST1516
<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>Intramembranei1518 – 1533Sequence analysisAdd BLAST16
Topological domaini1534 – 2206CytoplasmicSequence analysisAdd BLAST673

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004266412 – 2206Genome polyproteinBy similarityAdd BLAST2205
ChainiPRO_00004266422 – 878P1By similarityAdd BLAST877
ChainiPRO_00004266432 – 340Capsid protein VP0Sequence analysisAdd BLAST339
ChainiPRO_00004266442 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000042664570 – 340Capsid protein VP2Sequence analysisAdd BLAST271
ChainiPRO_0000426646341 – 578Capsid protein VP3Sequence analysisAdd BLAST238
ChainiPRO_0000426647579 – 878Capsid protein VP1Sequence analysisAdd BLAST300
ChainiPRO_0000426648879 – 1453P2By similarityAdd BLAST575
ChainiPRO_0000426649879 – 1027Protease 2ASequence analysisAdd BLAST149
ChainiPRO_00000401291028 – 1124Protein 2BSequence analysisAdd BLAST97
ChainiPRO_00000401301125 – 1453Protein 2CSequence analysisAdd BLAST329
ChainiPRO_00004266501454 – 2206P3By similarityAdd BLAST753
ChainiPRO_00004266511454 – 1562Protein 3ABSequence analysisAdd BLAST109
ChainiPRO_00000401311454 – 1540Protein 3ASequence analysisAdd BLAST87
ChainiPRO_00004266521541 – 1562Viral protein genome-linkedSequence analysisAdd BLAST22
ChainiPRO_00004266531563 – 2206Protein 3CDSequence analysisAdd BLAST644
ChainiPRO_00004266541563 – 1744Protease 3CSequence analysisAdd BLAST182
ChainiPRO_00004266551745 – 2206RNA-directed RNA polymeraseBy similarityAdd BLAST462

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 residuei1543O-(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 a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (By similarity).By similarity
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity
Capsid protein VP0: 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).By similarity
Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.By similarity
Capsid protein VP0: 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).By similarity
Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei69 – 70Cleavage; by autolysisSequence analysis2
Sitei340 – 341Cleavage; by Protease 3CSequence analysis2
Sitei878 – 879Cleavage; by Protease 2ASequence analysis2
Sitei1027 – 1028Cleavage; by Protease 3CSequence analysis2
Sitei1124 – 1125Cleavage; by Protease 3CSequence analysis2
Sitei1453 – 1454Cleavage; by Protease 3CSequence analysis2
Sitei1540 – 1541Cleavage; by Protease 3CSequence analysis2
Sitei1562 – 1563Cleavage; by Protease 3CSequence analysis2
Sitei1745 – 1746Cleavage; by Protease 3CSequence analysis2

Keywords - PTMi

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_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

Capsid protein VP1: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid (By similarity). Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 (By similarity). Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity). Protein 3AB: interacts with protein 3CD (By similarity). Viral protein genome-linked: interacts with RNA-directed RNA polymerase (By similarity). Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked and with protein 3CD (By similarity).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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P06209

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

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SMRi
P06209

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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_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>Domaini1229 – 1385SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1563 – 1728Peptidase C3Add BLAST166
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 – 603Amphipatic alpha-helixSequence analysisAdd BLAST25
Regioni1454 – 1476DisorderedBy similarityAdd BLAST23

<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

Keywords - Domaini

Repeat

Phylogenomic databases

Database of Orthologous Groups

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OrthoDBi
VOG0900006M

Family and domain databases

Conserved Domains Database

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CDDi
cd00205 rhv_like, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.870, 1 hit
2.60.120.20, 3 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000605 Helicase_SF3_ssDNA/RNA_vir
IPR014759 Helicase_SF3_ssRNA_vir
IPR027417 P-loop_NTPase
IPR014838 P3A
IPR036203 P3A_soluble_dom
IPR000081 Peptidase_C3
IPR000199 Peptidase_C3A/C3B_picornavir
IPR009003 Peptidase_S1_PA
IPR003138 Pico_P1A
IPR002527 Pico_P2B
IPR001676 Picornavirus_capsid
IPR033703 Rhv-like
IPR001205 RNA-dir_pol_C
IPR007094 RNA-dir_pol_PSvirus
IPR029053 Viral_coat

Pfam protein domain database

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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

ProDom; a protein domain database

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ProDomi
View protein in ProDom or Entries sharing at least one domain
PD001306 Peptidase_C3, 1 hit
PD649346 Pico_P2B, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50494 SSF50494, 2 hits
SSF52540 SSF52540, 1 hit
SSF89043 SSF89043, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
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>.<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.

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

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X04468 Genomic RNA Translation: CAA28155.1

Protein sequence database of the Protein Information Resource

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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

ProteinModelPortaliP06209
SMRiP06209
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC03.001

Proteomic databases

PRIDEiP06209

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG0900006M

Family and domain databases

CDDicd00205 rhv_like, 3 hits
Gene3Di1.10.10.870, 1 hit
2.60.120.20, 3 hits
InterProiView protein in InterPro
IPR000605 Helicase_SF3_ssDNA/RNA_vir
IPR014759 Helicase_SF3_ssRNA_vir
IPR027417 P-loop_NTPase
IPR014838 P3A
IPR036203 P3A_soluble_dom
IPR000081 Peptidase_C3
IPR000199 Peptidase_C3A/C3B_picornavir
IPR009003 Peptidase_S1_PA
IPR003138 Pico_P1A
IPR002527 Pico_P2B
IPR001676 Picornavirus_capsid
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
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001306 Peptidase_C3, 1 hit
PD649346 Pico_P2B, 1 hit
SUPFAMiSSF50494 SSF50494, 2 hits
SSF52540 SSF52540, 1 hit
SSF89043 SSF89043, 1 hit
PROSITEiView protein in PROSITE
PS50507 RDRP_SSRNA_POS, 1 hit
PS51218 SF3_HELICASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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_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: January 1, 1988
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 158 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

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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