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UniProtKB - P08545 (POLG_TMEVG)

Entry version 162 (23 Feb 2022)
Sequence version 2 (01 Jan 1990)
Previous versions | rss
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Protein

Genome polyprotein

Gene
N/A
Organism
Theiler's murine encephalomyelitis virus (strain GDVII) (TMEV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Forms 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 (By similarity).

Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore (efflux) (By similarity).

The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).

The leader protein also inhibits host interferon regulatory factor 3 (IRF3) dimerization, thereby blocking the transcriptional activation of IFN genes (By similarity).

Binds to host RNase L thereby preventing its activation by 2'-5' oligoadenylates in order to counteract the antiviral interferon-inducible OAS/RNase L pathway (By similarity).

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

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 (By similarity).

Nuclear localization is required for this function (By similarity).

The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).

Inhibits the phosphorylation of the leader protein (By similarity).

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

By similarity

Affects membrane integrity and causes an increase in membrane permeability.

By similarity

Associates with and induces structural rearrangements of intracellular membranes (Probable). It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).

By similarity1 Publication

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).

By similarity

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

Performs VPg uridylylation (By similarity).

By similarity

Miscellaneous

Persistent strains of Theiler's virus (e.g. DA, TO, BeAn) cause persistent demyelinating disease whereas neurovirulent strains (such as GDVII) cause acute encephalitis.

<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 sitei1680For protease 3C activityPROSITE-ProRule annotation1
Active sitei1714For protease 3C activityPROSITE-ProRule annotation1
Active sitei1793For protease 3C activityPROSITE-ProRule annotation1
Active sitei2077For RdRp activityBy similarity1
Active sitei2175For 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 fingeri3 – 14By similarityAdd BLAST12
<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 bindingi1312 – 1319ATPPROSITE-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		C03.010

<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
Virion protein 4
Capsid protein VP2
Alternative name(s):
P1B
Virion protein 2
Capsid protein VP3
Alternative name(s):
P1C
Virion protein 3
Capsid protein VP1
Alternative name(s):
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.4.13)
Short name:
P2C
Protein 3A
Short name:
P3A
VPg
Short name:
P3B
Alternative name(s):
Protein 3B
Protease 3C (EC:3.4.22.28By similarity)
Short name:
P3C
Alternative name(s):
Picornain 3C
RNA-directed RNA polymerase (EC:2.7.7.48PROSITE-ProRule annotation)
Short name:
RdRp
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiTheiler's murine encephalomyelitis virus (strain GDVII) (TMEV)
<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 identifieri12127 [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 hostiMus musculus (Mouse) [TaxID: 10090]
<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
  • UP000008247 <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 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_00004460991 – 2303Genome polyproteinAdd BLAST2303
ChainiPRO_00000401921 – 76Leader proteinAdd BLAST76
ChainiPRO_000031097277 – 414Capsid protein VP0Add BLAST338
ChainiPRO_000004019377 – 147Capsid protein VP4Add BLAST71
ChainiPRO_0000040194148 – 414Capsid protein VP2Add BLAST267
ChainiPRO_0000040195415 – 646Capsid protein VP3Add BLAST232
ChainiPRO_0000040196647 – 922Capsid protein VP1Add BLAST276
ChainiPRO_0000040197923 – 1055Protein 2AAdd BLAST133
ChainiPRO_00000401981056 – 1191Protein 2BAdd BLAST136
ChainiPRO_00000401991192 – 1517Protein 2CAdd BLAST326
ChainiPRO_00000402001518 – 1605Protein 3AAdd BLAST88
ChainiPRO_00000402011606 – 1625VPgAdd BLAST20
ChainiPRO_00000402021626 – 1842Protease 3CAdd BLAST217
ChainiPRO_00000402031843 – 2303RNA-directed RNA polymeraseAdd BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi77N-myristoyl glycine; by hostBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi501 ↔ 503By similarity
<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 residuei1608O-(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.By similarity
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>Sitei147 – 148CleavageSequence analysis2
Sitei414 – 415Cleavage; by protease 3CBy similarity2
Sitei646 – 647Cleavage; by protease 3CBy similarity2
Sitei922 – 923Cleavage; by protease 3CBy similarity2
Sitei1055 – 1056Cleavage; by ribosomal skipBy similarity2
Sitei1191 – 1192Cleavage; by protease 3CBy similarity2
Sitei1517 – 1518Cleavage; by protease 3CBy similarity2
Sitei1605 – 1606Cleavage; by protease 3CBy similarity2
Sitei1625 – 1626Cleavage; by protease 3CBy similarity2
Sitei1842 – 1843Cleavage; by protease 3CBy similarity2

Keywords - PTMi

Covalent protein-RNA linkage, Disulfide bond, Lipoprotein, Myristate, Phosphoprotein

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

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

Interacts with host EIF4E (By similarity).

Interacts with the leader protein (By similarity).

By similarity

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

Interacts with the protein 2A (By similarity).

Interacts with host RNASEL; this interaction prevents RNASEL activation by its substrate 2'-5' oligoadenylates (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		P08545

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>Domaini1283 – 1448SF3 helicasePROSITE-ProRule annotationAdd BLAST166
Domaini1636 – 1829Peptidase C3PROSITE-ProRule annotationAdd BLAST194
Domaini2071 – 2189RdRp 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>Regioni30 – 46AcidicCuratedAdd BLAST17
Regioni60 – 73TheiloBy similarityAdd BLAST14
Regioni73 – 93DisorderedSequence analysisAdd BLAST21
Regioni1041 – 1047Host EIF4E bindingBy similarity7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi74 – 93Polar residuesSequence analysisAdd BLAST20

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The Theilo and zinc-finger regions may both play a role in the inhibition of host nucleocytoplasmic trafficking and IRF-3 dimerization antagonism by the L protein.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri3 – 14By similarityAdd BLAST12

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
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

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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00918, CALICVIRUSNS

Superfamily database of structural and functional annotation

More...SUPFAMi		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: P08545-1) [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.

« Hide
        10         20         30         40         50
MACKHGYPDV CPICTAVDAT PDFEYLLMAD GEWFPTDLLC VDLDDDVFWP 
        60         70         80         90        100
SDTSTQPQTM EWTDVPLVCD TVMEPQGNAS SSDKSNSQSS GNEGVIINNF 
       110        120        130        140        150
YSNQYQNSID LSASGGNAGD APQNNGQLSS ILGGAANAFA TMAPLLMDQN 
       160        170        180        190        200
TEEMENLSDR VASDKAGNSA TNTQSTVGRL CGYGKSHHGE HPTSCADAAT 
       210        220        230        240        250
DKVLAAERYY TIDLASWTTS QEAFSHIRIP LPHVLAGEDG GVFGATLRRH 
       260        270        280        290        300
YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKSG TMEPSDPFTM 
       310        320        330        340        350
DTTWRSPQSA PTGYRYDRQA GFFAMNHQNQ WQWTVYPHQI LNLRTNTTVD 
       360        370        380        390        400
LEVPYVNVAP SSSWTQHANW TLVVAVLSPL QYATGSSPDV QITASLQPVN 
       410        420        430        440        450
PVFNGLRHET VLAQSPIPVT VREHQGCFYS TNPDTTVPIY GKTISTPSDY 
       460        470        480        490        500
MCGEFSDLLE LCKLPTFLGN PSTDNKRYPY FSATNSVPAT SLVDYQVALS 
       510        520        530        540        550
CSCTANSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFR IAYTPPGAGK 
       560        570        580        590        600
PTTRDQAMQA TYAIWDLGLN SSFNFTAPFI SPTHYRQTSY TSPTITSVDG 
       610        620        630        640        650
WVTVWQLTPL TYPSGTPTHS DILTLVSAGD DFTLRMPISP TKWVPQGIDN 
       660        670        680        690        700
AEKGKVSNDD ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNMET 
       710        720        730        740        750
TFSYQENDFR LNCLLLTPLP SYCPDSSSGP VRTKAPVQWR WVRSGGANGA 
       760        770        780        790        800
NFPLMTKQDY AFLCFSPFTY YKCDLEVTVS AMGAGTVSSV LRWAPTGAPA 
       810        820        830        840        850
DVTDQLIGYT PSLGETRNPH MWIVGSGNSQ ISFVVPYNSP LSVLPAAWFN 
       860        870        880        890        900
GWSDFGNTKD FGVAPTSDFG RIWIQGNSSA SVRIRYKKMK VFCPRPTLFF 
       910        920        930        940        950
PWPTPTTTKI NADNPVPILE LENPASLYRI DLFITFTDEL ITFDYKVHGR 
       960        970        980        990       1000
PVLTFRIPGF GLTPAGRMLV CMGAKPAHSP FTSSKSLYHV IFTSTCNSFS 
      1010       1020       1030       1040       1050
FTIYKGRYRS WKKPIHDELV DRGYTTFREF FKAVRGYHAD YYKQRLIHDV 
      1060       1070       1080       1090       1100
EMNPGPVQSV FQPQGAVLTK SLAPQAGIQN ILLRLLGIEG DCSEVSKAIT 
      1110       1120       1130       1140       1150
VVTDLVAAWE KAKTTLVSPE FWSELILKTT KFIAASVLYL HNPDFTTTVC 
      1160       1170       1180       1190       1200
LSLMTGVDLL TNDSVFDWLK SKLSSFFRTP PPACPNVMQP QGPLREANEG 
      1210       1220       1230       1240       1250
FTFAKNIEWA TKTIQSIVNW LTSWFKQEED HPQSKLDKLL MEFPDHCRNI 
      1260       1270       1280       1290       1300
MDMRNGRKAY CECTASFKYF DDLYNLAVTC KRIPLASLCE KFKNRHDHSV 
      1310       1320       1330       1340       1350
TRPEPVVAVL RGAAGQGKSV TSQIIAQSVS KMAFGRQSVY SMPPDSEYFD 
      1360       1370       1380       1390       1400
GYENQFSVIM DDLGQNPDGE DFTVFCQMVS STNFLPNMAH LERKGTPFTS 
      1410       1420       1430       1440       1450
SFIVATTNLP KFRPVTVAHY PAVDRRITFD FTVTAGPHCK TPAGMLDIEK 
      1460       1470       1480       1490       1500
AFDEIPGSKP QLACFSADCP LLHKRGVMFT CNRTKTVYNL QQVVKMVNDT 
      1510       1520       1530       1540       1550
ITRKTENVKK MNSLVAQSPP DWQHFENILT CLRQNNAALQ DQVDELQEAF 
      1560       1570       1580       1590       1600
TQARERSDFL SDWLKVSAII FAGIVSLSAV IKLASKFKES IWPTPVRVEL 
      1610       1620       1630       1640       1650
SEGEQAAYAG RARAQKQALQ VLDIQGGGKV LAQAGNPVMD FELFCAKNMV 
      1660       1670       1680       1690       1700
SPITFYYPDK AEVTQSCLLL RAHLFVVNRH VAETEWTAFK LRDVRHERDT 
      1710       1720       1730       1740       1750
VVMRSVNRSG AETDLTFVKV TKGPLFKDNV NKFCSNKDDF PARNDTVTGI 
      1760       1770       1780       1790       1800
MNTGLAFVYS GNFLIGNQPV NTTTGACFNH CLHYRAQTRR GWCGSAIICN 
      1810       1820       1830       1840       1850
VNGKKAVYGM HSAGGGGLAA ATIITRELIE AAEKSMLALE PQGAIVDIST 
      1860       1870       1880       1890       1900
GSVVHVPRKT KLRRTVAHDV FQPKFEPAVL SRYDPRTDKD VDVVAFSKHT 
      1910       1920       1930       1940       1950
TNMESLPPIF DIVCGEYANR VFTILGKDNG LLTVEQAVLG LSGMDPMEKD 
      1960       1970       1980       1990       2000
TSPGLPYTQQ GLRRTDLLDF NTAKMTPQLD YAHSKLVLGV YDDVVYQSFL 
      2010       2020       2030       2040       2050
KDEIRPLEKI HEAKTRIVDV PPFAHCIWGR QLLGRFASKF QTKPGFELGS 
      2060       2070       2080       2090       2100
AIGTDPDVDW TRYAAELSGF NYVYDVDYSN FDASHSTAMF ECLINNFFTE 
      2110       2120       2130       2140       2150
QNGFDRRIAE YLRSLAVSRH AYEDRRVLIR GGLPSGCAAT SMLNTIMNNV 
      2160       2170       2180       2190       2200
IIRAALYLTY SNFEFDDIKV LSYGDDLLIG TNYQIDFNLV KERLAPFGYK 
      2210       2220       2230       2240       2250
ITPANKTTTF PLTSHLQDVT FLKRRFVRFN SYLFRPQMDA VNLKAMVSYC 
      2260       2270       2280       2290       2300
KPGTLKEKLM SIALLAVHSG PDIYDEIFLP FRNVGIVVPT YDSMLYRWLS 

LFR
Note: Produced by conventional translation.1 Publication
Length:2,303
Mass (Da):256,344
Last modified:January 1, 1990 - v2
<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:i5D0FBE6E47F72A04
GO
Isoform 2B* (identifier: P0DOK5-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0DOK5.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:14
Mass (Da):1,437
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti1747 – 1750VTGI → CYRD in AAA47933 (PubMed:3023668).Curated4
Sequence conflicti1992 – 2000DDVVYQSFL → GRRCLPIIF in AAA47933 (PubMed:3023668).Curated9
Sequence conflicti2003E → Q (PubMed:3023668).Curated1
Sequence conflicti2008E → H in AAA47933 (PubMed:3023668).Curated1
Sequence conflicti2046F → L in AAA47933 (PubMed:3023668).Curated1
Sequence conflicti2128 – 2134LIRGGLP → YSWGPA in AAA47933 (PubMed:3023668).Curated7

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
M20562 Genomic RNA Translation: AAA47929.1
M14703 Genomic RNA Translation: AAA47933.1

Protein sequence database of the Protein Information Resource

More...PIRi		A26100
A29193, GNNYTP

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
M20562 Genomic RNA Translation: AAA47929.1
M14703 Genomic RNA Translation: AAA47933.1
PIRiA26100
A29193, GNNYTP

3D structure databases

SMRiP08545
ModBaseiSearch...

Protein family/group databases

MEROPSiC03.010

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
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
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
PRINTSiPR00918, CALICVIRUSNS
SUPFAMiSSF50494, 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_TMEVG
<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: P08545
Secondary accession number(s): Q88593, Q88594
<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: August 1, 1988
Last sequence update: January 1, 1990
Last modified: February 23, 2022
This is version 162 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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