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UniProtKB - Q66765 (POLG_EMCVR)

Entry version 129 (23 Feb 2022)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
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Protein

Genome polyprotein

Gene
N/A
Organism
Encephalomyocarditis virus (strain Rueckert) (EMCV)
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 a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (PubMed:19073724, PubMed:20881039, PubMed:16888036, PubMed:26492198, PubMed:26115166).

Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore (efflux) (PubMed:19073724, PubMed:20881039, PubMed:16888036).

The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (PubMed:19073724, PubMed:20881039, PubMed:16888036).

5 Publications

Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.

By similarity

Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.

By similarity

Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.

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).

After genome has been released, the channel shrinks (By similarity).

By similarity

VP0 precursor is a component of immature procapsids.

By similarity

Involved in host translation shutoff by inhibiting cap-dependent mRNA translation (PubMed:12921995, PubMed:21145089).

Nuclear localization is required for this function (PubMed:12921995, PubMed:21145089).

The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (Probable). Inhibits the phosphorylation of the leader protein (PubMed:25210192).

Binds to the RNA stem-loop essential for the ribosomal frameshift event and trans-activates the production of protein 2B* (By similarity).

By similarityCurated3 Publications

Affects membrane integrity and causes an increase in membrane permeability.

By similarity

Associates with and induces structural rearrangements of intracellular membranes (By similarity).

It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).

Interacts with IFIH1/MDA5 to inhibit the induction of the IFN-beta signal pathway (By similarity).

By similarity

Serves as membrane anchor via its hydrophobic domain.

By similarity

Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains.

By similarity

Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity).

In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease. Cleaves host PABP1, this cleavage is important for viral replication (By similarity).

Cleaves host TANK and disrupts the TANK-TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the IFN-beta signal pathway (By similarity).

By similarity

Replicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity).

Performs VPg uridylylation (By similarity).

By similarity

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

  • 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1673For protease 3C activityPROSITE-ProRule annotation1
Active sitei1707For protease 3C activityPROSITE-ProRule annotation1
Active sitei1786For protease 3C activityPROSITE-ProRule annotation1
Active sitei2067For RdRp activityBy similarity1
Active sitei2165For RdRp activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri10 – 22By similarityAdd BLAST13
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1313 – 1320ATPPROSITE-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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionHelicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel
Biological processEukaryotic 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, Transport, Viral attachment to host cell, Viral immunoevasion, Viral RNA replication, Virus entry into host cell
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Protein family/group databases

MEROPS protease database

More...MEROPSi		C03.009

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Leader protein
Short name:
L
Capsid protein VP0
Alternative name(s):
VP4-VP2
Capsid protein VP4
Alternative name(s):
P1A
Rho
Virion protein 4
Capsid protein VP2
Alternative name(s):
Beta
P1B
Virion protein 2
Capsid protein VP3
Alternative name(s):
Gamma
P1C
Virion protein 3
Capsid protein VP1
Alternative name(s):
Alpha
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Alternative name(s):
G
Protein 2B
Short name:
I
Short name:
P2B
Protein 2C (EC:3.6.4.13)
Short name:
C
Short name:
P2C
Protein 3A
Short name:
P3A
VPg
Short name:
P3B
Alternative name(s):
H
Protein 3B
Protease 3C (EC:3.4.22.28By similarity)
Short name:
P3C
Alternative name(s):
Picornain 3C
p22
RNA-directed RNA polymerase (EC:2.7.7.48PROSITE-ProRule annotation)
Short name:
RdRp
Alternative name(s):
3D polymerase
Short name:
3Dpol
E
Protein 3D
Short name:
3D
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEncephalomyocarditis virus (strain Rueckert) (EMCV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri650129 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiViruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Picornavirales › Picornaviridae › Cardiovirus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mus musculus (Mouse) [TaxID: 10090]
Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
Sus scrofa (Pig) [TaxID: 9823]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002319 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

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

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi19C → A: Complete loss of inhibitory activity of nucleocytoplasmic transport. 2 Publications1
Mutagenesisi35K → Q: 25% loss of 2A-Leader interaction. 1 Publication1
Mutagenesisi37D → A: 30% loss of 2A-Leader interaction. 1 Publication1
Mutagenesisi40W → A: 20% loss of 2A-Leader interaction. 1 Publication1
Mutagenesisi41Y → F: No effect on the inhibitory activity of nucleocytoplasmic transport. 1 Publication1
Mutagenesisi47T → A: No effect on the inhibitory activity of nucleocytoplasmic transport. 1 Publication1
Mutagenesisi993 – 994YY → AA: 5-10 fold decreased viral growth. 1 Publication2
Mutagenesisi996R → A: No effect on viral growth. 1 Publication1
Mutagenesisi998R → E: 5-10 fold decreased viral growth. 1 Publication1
Mutagenesisi1006Q → A: No effect on viral growth. 1 Publication1
Mutagenesisi1035L → A: Complete loss of interaction with host EIF4E. 1 Publication1

<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 '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_00004461001 – 2292Genome polyproteinAdd BLAST2292
ChainiPRO_00004231461 – 67Leader proteinAdd BLAST67
ChainiPRO_000042314768 – 393Capsid protein VP0Add BLAST326
ChainiPRO_500014356968 – 137Capsid protein VP4Add BLAST70
ChainiPRO_5000143570138 – 393Capsid protein VP2Add BLAST256
ChainiPRO_5000143571394 – 624Capsid protein VP3Add BLAST231
ChainiPRO_5000143572625 – 901Capsid protein VP1Add BLAST277
ChainiPRO_5000143573902 – 1044Protein 2AAdd BLAST143
ChainiPRO_50001435741045 – 1194Protein 2BAdd BLAST150
ChainiPRO_50001435751195 – 1519Protein 2CAdd BLAST325
ChainiPRO_50001435761520 – 1607Protein 3AAdd BLAST88
ChainiPRO_00004231481608 – 1627VPgAdd BLAST20
ChainiPRO_50001435771628 – 1832Protease 3CAdd BLAST205
ChainiPRO_50001435781833 – 2292RNA-directed RNA polymeraseAdd BLAST460

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei41Phosphotyrosine; by host SYK1 Publication1
Modified residuei47Phosphothreonine; by host CK21 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi68N-myristoyl glycine; by hostBy similarity1
Modified residuei1610O-(5'-phospho-RNA)-tyrosineBy similarity1

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

Phosphorylated.2 Publications
Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond (By similarity). This process would release the P1-2A peptide from the translational complex (By similarity).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 is followed by a conformational change of the particle.By similarity
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
Myristoylation is required during RNA encapsidation and formation of the mature virus particle.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>Sitei137 – 138CleavageSequence analysis2
Sitei393 – 394Cleavage; by protease 3CBy similarity2
Sitei624 – 625Cleavage; by protease 3CBy similarity2
Sitei901 – 902Cleavage; by protease 3CBy similarity2
Sitei1044 – 1045Cleavage; by ribosomal skipBy similarity2
Sitei1194 – 1195Cleavage; by protease 3CBy similarity2
Sitei1519 – 1520Cleavage; by protease 3CBy similarity2
Sitei1607 – 1608Cleavage; by protease 3CBy similarity2
Sitei1627 – 1628Cleavage; by protease 3CBy similarity2
Sitei1832 – 1833Cleavage; by protease 3CBy similarity2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q66765

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

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

Interacts with host TRIM22; this interaction leads to the ubiquitination of protease 3C and may restrict the virus replication (By similarity).

By similarity

Interacts with host EIF4E (PubMed:21145089).

Interacts with the leader protein (PubMed:25210192).

2 Publications

Interacts with host RAN; the complex L-RAN recruits cellular kinases responsible for the L-induced nucleocytoplasmic trafficking inhibition (PubMed:16888036). The complex L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS (PubMed:26492198).

Interacts with the protein 2A (PubMed:25210192).

3 Publications

Interacts with host IFIH1/MDA5; this interaction inhibits the induction of the IFN-beta signal pathway (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

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

More...SMRi		Q66765

Database of comparative protein structure models

More...ModBasei		Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1281 – 1447SF3 helicasePROSITE-ProRule annotationAdd BLAST167
Domaini1630 – 1822Peptidase C3PROSITE-ProRule annotationAdd BLAST193
Domaini2061 – 2179RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

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>Regioni37 – 61AcidicCuratedAdd BLAST25
Regioni1030 – 1036Host EIF4E binding1 Publication7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi995 – 1003Nuclear localization signal1 Publication9

<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 fingeri10 – 22By similarityAdd BLAST13

Keywords - Domaini

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, 1 hit
2.60.120.20, 3 hits
3.30.70.270, 2 hits
4.10.90.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR015031, Capsid_VP4_Picornavir
IPR037080, Capsid_VP4_sf_Picornavirus
IPR043502, DNA/RNA_pol_sf
IPR004004, Helic/Pol/Pept_Calicivir-typ
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR021573, Leader_pept_picornaV
IPR044067, PCV_3C_PRO
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001676, Picornavirus_capsid
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR033703, Rhv-like
IPR001205, RNA-dir_pol_C
IPR007094, RNA-dir_pol_PSvirus
IPR029053, Viral_coat
IPR037243, Viral_lead_polypep_zc_finger

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00548, Peptidase_C3, 1 hit
PF00680, RdRP_1, 1 hit
PF00073, Rhv, 2 hits
PF00910, RNA_helicase, 1 hit
PF08935, VP4_2, 1 hit
PF11475, VP_N-CPKC, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00918, CALICVIRUSNS

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF144251, SSF144251, 1 hit
SSF50494, SSF50494, 1 hit
SSF56672, SSF56672, 1 hit

PROSITE; a protein domain and family database

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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

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

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

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by ribosomal frameshifting. AlignAdd to basket
Isoform Genome polyprotein (identifier: Q66765-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MATTMEQETC AHSLTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE 
        60         70         80         90        100
DDVFDPELDM EVVFELQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI 
       110        120        130        140        150
DLSANAAGSD PPRTYGQFSN LFSGAVNAFS NMLPLLADQN TEEMENLSDR 
       160        170        180        190        200
VSQDTAGNTV TNTQSTVGRL VGYGTVHDGE HPASCADTAS EKILAVERYY 
       210        220        230        240        250
TFKVNDWTST QKPFEYIRIP LPHVLSGEDG GVFGAALRRH YLVKTGWRVQ 
       260        270        280        290        300
VQCNASQFHA GGLLVFMAPE YPTLDAFAMD NRWSKDNLPN GTRTQTNKKG 
       310        320        330        340        350
PFAMDHQNFW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT 
       360        370        380        390        400
LVIAVVAPLT YSTGASTSLD ITASIQPVRP VFNGLRHETL SRQSPIPVTI 
       410        420        430        440        450
REHAGTWYST LPDSTVPIYG KTPVAPSNYM VGEYKDFLEI AQIPTFIGNK 
       460        470        480        490        500
IPNAVPYIEA SNTAVKTQPL ATYQVTLSCS CLANTFLAAL SRNFAQYRGS 
       510        520        530        540        550
LVYTFVFTGT AMMKGKFLIA YTPPGAGKPT SRDQAMQATY AIWDLGLNSS 
       560        570        580        590        600
YSFTVPFISP THFRMVGTDQ VNITNADGWV TVWQLTPLTY PPGCPTSAKI 
       610        620        630        640        650
LTMVSAGKDF SLKMPISPAP WSPQGVENAE KGVTENTNAT ADFVAQPVYL 
       660        670        680        690        700
PENQTKVAFF YNRSSPIGAF TVKSGSLESG FAPFSNGTCP NSVILTPGPQ 
       710        720        730        740        750
FDPAYDQLRP QRLTEIWGNG NEETSKVFPL KSKQDYSFCL FSPFVYYKCD 
       760        770        780        790        800
LEVTLSPHTS GNHGLLVRWC PTGTPTKPTT QVLHEVSSLS EGRTPQVYSA 
       810        820        830        840        850
GPGISNQISF VVPYNSPLSV LSAVWYNGHK RFDNTGSLGI APNSDFGTLF 
       860        870        880        890        900
FAGTKPDIKF TVYLRYKNKR VFCPRPTVFF PWPTSGDKID MTPRAGVLML 
       910        920        930        940        950
ESPNALDISR TYPTLHVLIQ FNHRGLEVRL FRHGHFWAET RADVILRSKT 
       960        970        980        990       1000
KQVSFLSNGN YPSMDSRAPW NPWKNTYQAV LRAEPCRVTM DIYYKRVRPF 
      1010       1020       1030       1040       1050
RLPLVQKEWP VREENVFGLY RIFNAHYAGY FADLLIHDIE TNPGPFMFRP 
      1060       1070       1080       1090       1100
RKQVFQTQGA AVSSMAQTLL PNDLASKAMG SAFTALLDAN EDAQKAMKII 
      1110       1120       1130       1140       1150
KTLSSLSDAW ENVKETLNNP EFWKQLLSRC VQLIAGMTIA VMHPDPLTLL 
      1160       1170       1180       1190       1200
CLGTLTAAEI TSQTSLCEEI AAKFKTIFIT PPPRFPTISL FQQQSPLKQV 
      1210       1220       1230       1240       1250
NDIFSLAKNL DWAVKTVEKV VDWFGTWIVQ EEKEQTLDQL LQRFPEHAKR 
      1260       1270       1280       1290       1300
ISDLRNGMAA YVECKESFDF FEKLYNQAVK EKRTGIAAVC EKFRQKHDHA 
      1310       1320       1330       1340       1350
TARCEPVVIV LRGDAGQGKS LSSQVIAQAV SKTIFGRQSV YSLPPDSDFF 
      1360       1370       1380       1390       1400
DGYENQFAAI MDDLGQNPDG SDFTTFCQMV STTNFLPNMA SLERKGTPFT 
      1410       1420       1430       1440       1450
SQLVVATTNL PEFRPVTIAH YPAVERRITF DYSVSAGPVC SKTEAGYKVL 
      1460       1470       1480       1490       1500
DVERAFRPTG EAPLPCFQNN CLFLEKAGLQ FRDNRTKEII SLVDVIERAV 
      1510       1520       1530       1540       1550
ARIERKKKVL TTVQTLVAQG PVDEVSFHSV VQQLKARQQA TDEQLEELQE 
      1560       1570       1580       1590       1600
AFAKVQERNS VFSDWLKISA MLCAATLALS QVVKMAKAVK QMVKPDLVRV 
      1610       1620       1630       1640       1650
QLDEQEQGPY NETARVKPKT LQLLDIQGPN PVMDFEKYVA KHVTAPIGFV 
      1660       1670       1680       1690       1700
YPTGVSTQTC LLVRGRTLVV NRHMAESDWT SIVVRGVTHA RSTVKILAIA 
      1710       1720       1730       1740       1750
KAGKETDVSF IRLSSGPLFR DNTSKFVKAG DVLPTGAAPV TGIMNTDIPM 
      1760       1770       1780       1790       1800
MYTGTFLKAG VSVPVETGQT FNHCIHYKAN TRKGWCGSAL LADLGGSKKI 
      1810       1820       1830       1840       1850
LGIHSAGSMG IAAASIVSQE MIRAVVNAFE PQGALERLPD GPRIHVPRKT 
      1860       1870       1880       1890       1900
ALRPTVARQV FQPAYAPAVL SKFDPRTEAD VDEVAFSKHT SNQESLPPVF 
      1910       1920       1930       1940       1950
RMVAKEYANR VFTLLGKDNG RLTVKQALEG LEGMDPMDRN TSPGLPYTAL 
      1960       1970       1980       1990       2000
GMRRTDVVDW ESATLIPFAA ERLRKMNEGD FSEVVYQTFL KDELRPIEKV 
      2010       2020       2030       2040       2050
QAAKTRIVDV PPFEHCILGR QLLGKFASKF QTQPGLELGS AIGCDPDVHW 
      2060       2070       2080       2090       2100
TAFGVAMQGF ERVYDVDYSN FDSTHSVAMF RLLAEEFFTP ENGFDPLTRE 
      2110       2120       2130       2140       2150
YLESLAISTH AFEEKRFLIT GGLPSGCAAT SMLNTIMNNI IIRAGLYLTY 
      2160       2170       2180       2190       2200
KNFEFDDVKV LSYGDDLLVA TNYQLDFDKV RASLAKTGYK ITPANTTSTF 
      2210       2220       2230       2240       2250
PLNSTLEDVV FLKRKFKKEG PLYRPVMNRE ALEAMLSYYR PGTLSEKLTS 
      2260       2270       2280       2290 
ITMLAVHSGK QEYDRLFAPF REVGVVVPSF ESVEYRWRSL FW
Note: Produced by conventional translation.By similarity
Length:2,292
Mass (Da):255,459
Last modified:November 1, 1996 - v1
<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:i01C0537888CEFC94
GO
Isoform 2B* (identifier: P0DJX6-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0DJX6.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:128
Mass (Da):14,449
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M81861 Genomic RNA Translation: AAA43037.1

NCBI Reference Sequences

More...RefSeqi		NP_056777.1, NC_001479.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1493923

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		vg:1493923

Keywords - Coding sequence diversityi

Ribosomal frameshifting

<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
M81861 Genomic RNA Translation: AAA43037.1
RefSeqiNP_056777.1, NC_001479.1

3D structure databases

SMRiQ66765
ModBaseiSearch...

Protein family/group databases

MEROPSiC03.009

PTM databases

iPTMnetiQ66765

Genome annotation databases

GeneIDi1493923
KEGGivg:1493923

Family and domain databases

CDDicd00205, rhv_like, 3 hits
Gene3Di2.40.10.10, 1 hit
2.60.120.20, 3 hits
3.30.70.270, 2 hits
4.10.90.10, 1 hit
InterProiView protein in InterPro
IPR015031, Capsid_VP4_Picornavir
IPR037080, Capsid_VP4_sf_Picornavirus
IPR043502, DNA/RNA_pol_sf
IPR004004, Helic/Pol/Pept_Calicivir-typ
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR021573, Leader_pept_picornaV
IPR044067, PCV_3C_PRO
IPR000199, Peptidase_C3A/C3B_picornavir
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001676, Picornavirus_capsid
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR033703, Rhv-like
IPR001205, RNA-dir_pol_C
IPR007094, RNA-dir_pol_PSvirus
IPR029053, Viral_coat
IPR037243, Viral_lead_polypep_zc_finger
PfamiView protein in Pfam
PF00548, Peptidase_C3, 1 hit
PF00680, RdRP_1, 1 hit
PF00073, Rhv, 2 hits
PF00910, RNA_helicase, 1 hit
PF08935, VP4_2, 1 hit
PF11475, VP_N-CPKC, 1 hit
PRINTSiPR00918, CALICVIRUSNS
SUPFAMiSSF144251, SSF144251, 1 hit
SSF50494, SSF50494, 1 hit
SSF56672, SSF56672, 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_EMCVR
<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: Q66765
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 24, 2013
Last sequence update: November 1, 1996
Last modified: February 23, 2022
This is version 129 of the entry and version 1 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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