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Entry version 181 (18 Sep 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Genome polyprotein

Gene
N/A
Organism
Bovine enterovirus (strain VG-5-27) (BEV)
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

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. 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.PROSITE-ProRule annotation EC:3.4.22.28

<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

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 <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 sitei861For Protease 2A activityBy similarity1
Active sitei879For Protease 2A activityBy similarity1
Active sitei950For Protease 2A activityBy similarity1
Active sitei1571For protease 3C activityPROSITE-ProRule annotation1
Active sitei1602For protease 3C activityPROSITE-ProRule annotation1
Active sitei1678For protease 3C activityPROSITE-ProRule annotation1
Active sitei2042For RdRp activityBy similarity1

<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, Nucleotide-binding

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C03.014

<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
Protein 3CD (EC:3.4.22.28)
Protease 3C (EC:3.4.22.28)
Short name:
P3C
RNA-directed RNA polymerase (EC:2.7.7.48)
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>OrganismiBovine enterovirus (strain VG-5-27) (BEV)
<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 identifieri12065 [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 lineageiVirusesRiboviriaPicornaviralesPicornaviridaeEnterovirus
<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 hostiBos taurus (Bovine) [TaxID: 9913]
<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
  • UP000006566 <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 – 1485CytoplasmicSequence analysisAdd BLAST1484
<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>Intramembranei1486 – 1501Sequence analysisAdd BLAST16
Topological domaini1502 – 2175CytoplasmicSequence analysisAdd BLAST674

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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB08231 Myristic acid

<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_00004261072 – 2175Genome polyproteinBy similarityAdd BLAST2174
ChainiPRO_00004261082 – 840P1By similarityAdd BLAST839
ChainiPRO_00004261092 – 317Capsid protein VP0Sequence analysisAdd BLAST316
ChainiPRO_00004261102 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000042611170 – 317Capsid protein VP2Sequence analysisAdd BLAST248
ChainiPRO_0000426112318 – 557Capsid protein VP3Sequence analysisAdd BLAST240
ChainiPRO_0000426113557 – 840Capsid protein VP1Sequence analysisAdd BLAST284
ChainiPRO_0000426114841 – 1419P2By similarityAdd BLAST579
ChainiPRO_0000039463841 – 990Protease 2ASequence analysisAdd BLAST150
ChainiPRO_0000039464991 – 1089Protein 2BSequence analysisAdd BLAST99
ChainiPRO_00000394651090 – 1419Protein 2CSequence analysisAdd BLAST330
ChainiPRO_00004261151420 – 2175P3By similarityAdd BLAST756
ChainiPRO_00004261161420 – 1531Protein 3ABSequence analysisAdd BLAST112
ChainiPRO_00000394661420 – 1508Protein 3ASequence analysisAdd BLAST89
ChainiPRO_00004261171509 – 1531Viral protein genome-linkedSequence analysisAdd BLAST23
ChainiPRO_00004261181532 – 2175Protein 3CDSequence analysisAdd BLAST644
ChainiPRO_00004261191532 – 1713Protease 3CSequence analysisAdd BLAST182
ChainiPRO_00004261201714 – 2175RNA-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 residuei1511O-(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 uridylated 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 is followed by a conformational change of the particle.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>Sitei317 – 318Cleavage; by Protease 3CSequence analysis2
Sitei840 – 841Cleavage; by Protease 2ASequence analysis2
Sitei990 – 991Cleavage; by Protease 3CSequence analysis2
Sitei1419 – 1420Cleavage; by Protease 3CSequence analysis2
Sitei1508 – 1509Cleavage; by Protease 3CSequence analysis2
Sitei1531 – 1532Cleavage; by Protease 3CSequence analysis2
Sitei1714 – 1715Cleavage; by Protease 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P12915

<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

Secondary structure

12175
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

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SMRi
P12915

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P12915

<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>Domaini1194 – 1352SF3 helicasePROSITE-ProRule annotationAdd BLAST159
Domaini1532 – 1710Peptidase C3PROSITE-ProRule annotationAdd BLAST179
Domaini1941 – 2056RdRp 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>Regioni557 – 574Amphipatic alpha-helixSequence analysisAdd BLAST18
Regioni1420 – 1443DisorderedBy similarityAdd BLAST24

<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

Family and domain databases

Conserved Domains Database

More...
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
IPR004004 Helic/Pol/Pept_Calicivir-typ
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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00918 CALICVIRUSNS

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
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.

P12915-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGAQLSRNTA GSHTTGTYAT GGSTINYNNI NYYSHAASAA QNKQDFTQDP
60 70 80 90 100
SKFTQPIADV IKETAVPLKS PSAEACGYSD RVAQLTLGNS TITTQEAANI
110 120 130 140 150
CVAYGCWPAK LSDTDATSVD KPTEPGVSAD AFYTLRSKPW QADSKGWYWK
160 170 180 190 200
LPDALNNTGM FGQNAQFHYI YRGGWAVHVQ CNATKFHQGT LLVLAIPEHQ
210 220 230 240 250
IATQEQPAFD RTMPGSEGGT FQEPFWLEDG TSLGNSLIYP HQWINLRTNN
260 270 280 290 300
SATLILPYVN AIPMDSAIRH SNWTLAIIPV APLKYAAETT PLVPITVTIA
310 320 330 340 350
PMETEYNGLR RAIASNQGLP TKPGPGSYQF MTTDEDCSPC ILPDFQPTLE
360 370 380 390 400
IFIPGKVNNL LEIAQVESIL EANNREGVEG VERYVIPVSV QDALDAQIYA
410 420 430 440 450
LRLELGGSGP LSSSLLGTLA KHYTQWSGSV EITCMFTGTF MTTGKVLLAY
460 470 480 490 500
TPPGGDMPRN REEAMLGTHV VWDFGLQSSI TLVIPWISAS HFRGVSNDDV
510 520 530 540 550
LNYQYYAAGH VTIWYQTNMV IPPGFPNTAG IIMMIAAQPN FSFRIQKDRE
560 570 580 590 600
DMTQTAILQN DPGKMLKDAI DKQVAGALVA GTTTSTHSVA TDSTPALQAA
610 620 630 640 650
ETGATSTARD ESMIETRTIV PTHGIHETSV ESFFGRSSLV GMPLLATGTS
660 670 680 690 700
ITNWRIDFRE FVQLRAKMSW FTYMRFDVEF TIIATSSTGQ NVTTEQHTTY
710 720 730 740 750
QVMYVPPGAP VPSNQDSFQW QSGCNPSVFA DTDGPPAQFS VPFMSSANAY
760 770 780 790 800
STVYDGYARF MDTDPDRYGI LPSNFLGFMY FRTLEDAAHQ VRFRICAKIK
810 820 830 840 850
HTSCWIPRAP RQAPYKKRYN LVFSGDSDRI CSNRASLTSY GPFGQQQGAA
860 870 880 890 900
YVGSYKILNR HLATYADWEN EVWQSYQRDL LVTRVDAHGC DTIARCNCRS
910 920 930 940 950
GIYYCKSTAK HYPIVVTPPS IYKIEANDYY PERMQTHILL GIGFAEPGDC
960 970 980 990 1000
GGLLRCEHGV MGILTVGGGD HVGFADVRDL LWIEDDAMEQ GITDYVQQLG
1010 1020 1030 1040 1050
NAFGAGFTAE IANYTNQLRD MLMGSDSVVE KIIRSLVRLV SALVIVVRNH
1060 1070 1080 1090 1100
QDLITVGATL ALLGCEGSPW KWLKRKVCQI LGINMAERQS DNWMKKFTEM
1110 1120 1130 1140 1150
CNAFRGLDWI AAKISKFIDW LKQKILPELK ERAEFVKKLK QLPLLEAQVN
1160 1170 1180 1190 1200
TLEHSSASQE RQEQLFGNVQ YLAHHCRKNA PLYAAEAKRV YHLEKRVLGA
1210 1220 1230 1240 1250
MQFKTKNRIE PVCALIHGSP GTGQSLATMI VGRKLAEYEG SDVYSLPPDP
1260 1270 1280 1290 1300
DHFDGYQQQA VVVMDDLLQN PDGKDMTLFC QMVSTAPFTV PMAALEDKGK
1310 1320 1330 1340 1350
LFTSKFVLAS TNAGQVTPPT VADYKALQRR FFFDCDIEVQ KEYKRDGVTL
1360 1370 1380 1390 1400
DVAKATETCE DCSPANFKKC MPLICGKALQ LKSRKGDGMR YSLDTLISEL
1410 1420 1430 1440 1450
RRESNRRYNI GNVLEALFQG PVCYKPLRIE VHEEEPAPSA ISDLLQAVDS
1460 1470 1480 1490 1500
EEVREYCRSK GWIVEERVTE LKLERNVNRA LAVIQSVSLI AAVAGTIYIV
1510 1520 1530 1540 1550
YRLFSGMQGP YSGIGTNYAT KKPVVRQVQT QGPLFDFGVS LLKKNIRTVK
1560 1570 1580 1590 1600
TGAGEFTALG VYDTVVVLPR HAMPGKTIEM NGKDIEVLDA YDLNDKTDTS
1610 1620 1630 1640 1650
LELTIVKLKM NEKFRDIRAM VPDQITDYNE AVVVVNTSYY PQLFTCVGRV
1660 1670 1680 1690 1700
KDYGFLNLAG RPTHRVLMYE FPTKAGQCGG VVISMGKIVG VHVGGNGAQG
1710 1720 1730 1740 1750
FAASLLRRYF TAEQGQIEYI EKSKDAGYPV INAPTQTKLE PSVFFDVFPG
1760 1770 1780 1790 1800
VKEPAVLHKK DKRLETNFEE ALFSKYIGNV QRDMPEELLI AIDHYSEQLK
1810 1820 1830 1840 1850
MLNIDPRPIS MEDAIYGTEG LEALDLGTSA SYPYVAMGIK KRDILNKETR
1860 1870 1880 1890 1900
DVTKMQECID KYGLNLPMVT YVKDELRAPD KIRKGKSRLI EASSLNDSVA
1910 1920 1930 1940 1950
MRCYFGNLYK VFHTNPGTIS GCAVGCDPET FWSKIPVMMD GELFGFDYTA
1960 1970 1980 1990 2000
YDASLSPMWF HALAEVLRRI GFVECKHFID QLCCSHHLYM DKHYYVVGGM
2010 2020 2030 2040 2050
PSGCSGTSIF NSMINNLIIR TLVLTVYKNI DLDDLKIIAY GDDVLASYPY
2060 2070 2080 2090 2100
EIDASLLAEA GKSFGLIMTP PDKSAEFVKL TWDNVTFLKR KFVRDARYPF
2110 2120 2130 2140 2150
LVHPVMDMSN IHESIRWTKD PRHTEDHVRS LCLLAWHCGE EEYNEFVTKI
2160 2170
RSVPVGRALH LPSFKALERK WYDSF
Length:2,175
Mass (Da):242,504
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:i44FCADE8704E48FD
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
D00214 Genomic RNA Translation: BAA24003.1 Sequence problems.

Protein sequence database of the Protein Information Resource

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PIRi
A29824 GNNYBE

NCBI Reference Sequences

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RefSeqi
NP_045756.1, NC_001859.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
1493914

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
vg:1493914

<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
D00214 Genomic RNA Translation: BAA24003.1 Sequence problems.
PIRiA29824 GNNYBE
RefSeqiNP_045756.1, NC_001859.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BEVX-ray3.001560-840[»]
270-317[»]
3318-559[»]
42-69[»]
SMRiP12915
ModBaseiSearch...

Chemistry databases

DrugBankiDB08231 Myristic acid

Protein family/group databases

MEROPSiC03.014

Proteomic databases

PRIDEiP12915

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1493914
KEGGivg:1493914

Miscellaneous databases

EvolutionaryTraceiP12915

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
IPR004004 Helic/Pol/Pept_Calicivir-typ
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
PRINTSiPR00918 CALICVIRUSNS
SUPFAMiSSF50494 SSF50494, 2 hits
SSF52540 SSF52540, 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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_BOVEV
<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: P12915
<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: October 1, 1989
Last sequence update: January 23, 2007
Last modified: September 18, 2019
This is version 181 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

3D-structure, Complete proteome

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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