Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - O91464 (POLG_AIVA8)

Entry version 144 (02 Dec 2020)
Sequence version 2 (16 Oct 2019)
Previous versions | rss
Add a publicationFeedback
Protein

Genome polyprotein

Gene
N/A
Organism
Aichi virus (strain Human/A846/88/1989) (AiV) (Aichi virus (strain A846/88))
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

Required for viral RNA replication and viral RNA encapsidation (PubMed:14512530). Does not have any proteolytic activity (PubMed:14512530).1 Publication
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (PubMed:27681122, PubMed:27595320). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (PubMed:27681122, PubMed:27595320). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (PubMed:27595320).2 Publications
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3 (PubMed:27681122, PubMed:27595320). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (PubMed:27681122, PubMed:27595320). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (PubMed:27595320).2 Publications
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP1 (PubMed:27681122, PubMed:27595320). Together they form an icosahedral capsid composed of 60 copies of each VP0, VP1, and VP3 (PubMed:27681122, PubMed:27595320). All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll (PubMed:27595320).2 Publications
Required for viral RNA replication (PubMed:18653460). Does not have any proteolytic activity (PubMed:18653460).1 Publication
Affects membrane integrity and causes an increase in membrane permeability.By similarity
Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.By similarity
Serves as membrane anchor via its hydrophobic domain. Plays an essential role in viral RNA replication by recruiting PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (PubMed:22124328, PubMed:24672044, PubMed:27989622, PubMed:30755512, PubMed:22258260). Stimulates the enzymatic activity of PI4KB, this activation is sensitized by ACBD3 (PubMed:24672044, PubMed:27989622).5 Publications
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 (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 sitei1816For protease 3C activityPROSITE-ProRule annotationBy similarity1
Active sitei1844For protease 3C activityBy similarity1
Active sitei1917For protease 3C activityPROSITE-ProRule annotationBy similarity1
Active sitei2199For RdRp activityBy similarity1
Active sitei2294For 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 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 bindingi1448 – 1455ATPPROSITE-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 mRNA nuclear export by virus, Ion transport, Transport, Viral attachment to host cell, Viral RNA replication, Virus entry into host cell
LigandATP-binding, Nucleotide-binding

<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 12 chains:
Leader protein
Short name:
L
Capsid protein VP0
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:3.6.4.13By similarity)
Short name:
P2C
Protein 3A
Short name:
P3A
VPg
Short name:
P3B
Alternative name(s):
Protein 3B
Protein 3CD (EC:3.4.22.28)
Protease 3CPROSITE-ProRule annotation (EC:3.4.22.28PROSITE-ProRule annotation)
Alternative name(s):
Picornain 3CPROSITE-ProRule annotation
Short name:
P3CPROSITE-ProRule annotation
RNA-directed RNA 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>OrganismiAichi virus (strain Human/A846/88/1989) (AiV) (Aichi virus (strain A846/88))
<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 identifieri650132 [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 › Kobuvirus ›
<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]
<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
  • UP000119554 <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
  • UP000137558 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

  • Virion 2 Publications
  • Host cytoplasm By similarity
  • Virion 2 Publications
  • Host cytoplasm By similarity
  • Virion 2 Publications
  • Host cytoplasm By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1712 – 1732HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host Golgi apparatus, 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

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>Mutagenesisi168Q → P: Complete loss of proteolytic cleavage between the leader protein and VP1 protein. 1 Publication1
Mutagenesisi1043 – 1046HWAI → AWAA: Complete loss of interaction between the 3C-3D precursor and protein 2A. 1 Publication4
Mutagenesisi1105 – 1106NC → AA: No effect on the interaction between the 3C-3D precursor and protein 2A. 1 Publication2
Mutagenesisi1653G → A: Complete loss of myristoylation. 1 Publication1
Mutagenesisi1654N → A: Complete loss of myristoylation. 1 Publication1
Mutagenesisi1655R → A: Complete loss of myristoylation; loss of interaction with host ACBD3. Loss of activation of host PI4KB in vitro. 2 Publications1
Mutagenesisi1657I → A: Loss of interaction with host ACBD3 and PI4KB. 1 Publication1
Mutagenesisi1663E → A: Loss of activation of host PI4KB in vitro. 1 Publication1
Mutagenesisi1963 – 1964QQ → AA: Complete loss of cleavage at the 3C-3D junction. 1 Publication2

<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_00004480061 – 2432Genome polyproteinAdd BLAST2432
ChainiPRO_00004480071 – 170Leader proteinAdd BLAST170
ChainiPRO_0000448008171 – 540Capsid protein VP0Add BLAST370
ChainiPRO_0000448009541 – 763Capsid protein VP3Add BLAST223
ChainiPRO_0000448010764 – 1016Capsid protein VP1Add BLAST253
ChainiPRO_00004480111017 – 1152Protein 2AAdd BLAST136
ChainiPRO_00004480121153 – 1317Protein 2BAdd BLAST165
ChainiPRO_00004480131175 – 2431Protein 3CDAdd BLAST1257
ChainiPRO_00004480141318 – 1652Protein 2CAdd BLAST335
ChainiPRO_00004480151653 – 1747Protein 3AAdd BLAST95
ChainiPRO_00004480161748 – 1774VPgAdd BLAST27
ChainiPRO_00004480171775 – 1964Protease 3CAdd BLAST190
ChainiPRO_00004480181965 – 2431RNA-directed RNA polymeraseAdd BLAST467

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 residuei109Phosphotyrosine; by host SYKBy similarity1
Modified residuei115Phosphoserine; by host CK2By similarity1
<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>Lipidationi171N-myristoyl glycine; by hostBy similarity1
Lipidationi1653N-myristoyl glycine; by host1 Publication1
Modified residuei1750O-(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

Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (PubMed:22226945). The leader protein-VP0 junction is cleaved by 3C proteinase (PubMed:14512530). The VP1/2A junction is cleaved by the protein 3CD in association with protein 2A (PubMed:22226945).2 Publications
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

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>Sitei170 – 171Cleavage; by protease 3C1 Publication2
Sitei540 – 541Cleavage; by protease 3CBy similarity2
Sitei763 – 764Cleavage; by protease 3CBy similarity2
Sitei1016 – 1017Cleavage; by protein 3CD1 Publication2
Sitei1152 – 1153Cleavage; by protease 3CBy similarity2
Sitei1317 – 1318Cleavage; by protease 3CBy similarity2
Sitei1652 – 1653Cleavage; by protease 3CBy similarity2
Sitei1747 – 1748Cleavage; by protease 3CBy similarity2
Sitei1774 – 1775Cleavage; by protease 3CBy similarity2
Sitei1964 – 1965Cleavage; by protease 3C1 Publication2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O91464

<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 capsid protein VP1 (PubMed:27681122, PubMed:27595320).

Interacts with capsid protein VP3 (PubMed:27681122, PubMed:27595320).

2 Publications

Interacts with capsid protein VP0 (PubMed:27681122, PubMed:27595320).

Interacts with capsid protein VP3 (PubMed:27681122, PubMed:27595320).

2 Publications

Interacts with capsid protein VP0 (PubMed:27681122, PubMed:27595320).

Interacts with capsid protein VP1 (PubMed:27681122, PubMed:27595320).

2 Publications

Homodimer (PubMed:19879907).

Interacts with protein 2B (PubMed:19879907).

Interacts with protein 2C (PubMed:19879907).

1 Publication

Homodimer (PubMed:19879907).

Interacts with host ABCD3 (PubMed:22124328).

Interacts with protein 2A (PubMed:19879907).

Interacts with host ACBD3 (PubMed:22124328).

2 Publications

Homodimer (PubMed:19879907).

Interacts with host ABCD3 (PubMed:22124328).

Interacts with protein 2A (PubMed:19879907).

Interacts with protein 3A (PubMed:22124328).

Interacts with protein 3C (PubMed:19879907).

Interacts with host ACBD3 (PubMed:22124328).

2 Publications

Homodimer (PubMed:19879907).

Interacts with host ABCD3 (via GOLD domain) and PI4KB; these interactions allow the formation of a viral protein/ACBD3/PI4KB complex in order to synthesize PI4P at the viral RNA replication sites (PubMed:22124328, PubMed:22258260, PubMed:24672044, PubMed:27989622, PubMed:30755512, PubMed:28065508) (Probable).

Interacts with protein 2C (PubMed:19879907).

Interacts with protein 3C (PubMed:19879907). Protein 3C:

Interacts with protein 2A (PubMed:19879907). Protein 3C:

Interacts with protein 2C (PubMed:19879907).

2 Publications3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		O91464, 1 interactor

Molecular INTeraction database

More...MINTi		O91464

<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

12432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		O91464

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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>Domaini1033 – 1121LRATPROSITE-ProRule annotationAdd BLAST89
Domaini1422 – 1586SF3 helicasePROSITE-ProRule annotationAdd BLAST165
Domaini1773 – 1954Peptidase C3PROSITE-ProRule annotationAdd BLAST182
Domaini2193 – 2308RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

Keywords - Domaini

Transmembrane, Transmembrane helix

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, 2 hits
2.60.120.20, 3 hits
3.30.70.270, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR043502, DNA/RNA_pol_sf
IPR004004, Helic/Pol/Pept_Calicivir-typ
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
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, 3 hits
PF00910, RNA_helicase, 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
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51934, LRAT, 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>Sequencei

<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.

O91464-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAATRVSRSV LAAVAHSAAH RTYHTVLDCY DRLYLNTNPH LSYPLPKNSS 
        60         70         80         90        100
FPCPFCQYDE QNEVLSPESL RGEGAEPCWK CSQDKPRRKY NTTPPEDWLY 
       110        120        130        140        150
DSDVQSWFYP ETYYSDLQQK FFDKLALLSL PGAYQAKTPE ERALAGALTQ 
       160        170        180        190        200
LLNFPSTPPL TLPTTNLQRQ GNSVTNIYGN GNNVTTDVGA NGWAPTVSTG 
       210        220        230        240        250
LGDGPVSASA DSLPGRSGGA SSEKTHTVSG SSNKVGSRFS KWWEPAAARA 
       260        270        280        290        300
SESATDSAIE GIDAAGKAAS KAITRKLDRP AAPSSTANPQ PSLIALNPSA 
       310        320        330        340        350
TQSGNASILT GSTAPSLLAY PTATPVPLPN PDEPSQPGPS GDRTWLLDTV 
       360        370        380        390        400
TWSQEFTRGW NIAGSNGMQW TGLESLIFPV STDTNWTSTS SPTAYPLPFS 
       410        420        430        440        450
FVRAYPDSSW AAMYNTHSMW NCGWRVQVTV NGSQFHAGAL ILYMVPEATT 
       460        470        480        490        500
HAIQTARDNA GFVFPYVILN LYESNTATIE VPYISPTPNT SSGLHAPWTF 
       510        520        530        540        550
YLQVLSPLNP PPSLPTSLSC SIYVTPVDSS FHGLRYLAPQ HWKTRAVPGA 
       560        570        580        590        600
GTFGSAVAGQ ELPLCGVRAY YPPNAYIPAQ VRDWLEFAHR PGLMATVPWT 
       610        620        630        640        650
MADEPAERLG IFPVSPSAIA GTGAPISYVI SLFSQWRGEL AAHLLFTGSA 
       660        670        680        690        700
QHYGRLVVCY TPAAPQPPST MQEAMRGTYT VWDVNAASTL EFTIPFISNS 
       710        720        730        740        750
YWKTVDVNNP DALLSTTGYV SIWVQNPLVG PHTAPASALV QAFISAGESF 
       760        770        780        790        800
NVRLMQNPAL TSQTLTEDLD APQDTGNIEN GAADNSPQPR TTFDYTGNPL 
       810        820        830        840        850
PPDTKLENFF SFYRLLPMGG SGAPSLSFPA DEGTIIPLNP INWLKGADVS 
       860        870        880        890        900
GIAAMLSCFT YIAADLRITL RFSNPNDNPA TMLVAFAPPG ATIPLKPTRQ 
       910        920        930        940        950
MLSNFYMAEV PVSAATSTMV SFSIPYTSPL SAIPTSYFGW EDWSGTNFGQ 
       960        970        980        990       1000
LSSGSWGNLM LIPSLSVDSA IPFDFQLSCW VAFGNFKAWV PRPPPPLPPL 
      1010       1020       1030       1040       1050
PTPAANAERT VAVIKQGAAS ATPDVDPDDR VYIVRAQRPT YVHWAIRKVA 
      1060       1070       1080       1090       1100
PDGSAKQISL SRSGIQALVA LEPPEGEPYL EILPSHWTLA ELQLGNKWEY 
      1110       1120       1130       1140       1150
SATNNCTHFV SSITGESLPN TGFSLALGIG ALTAIAASAA VAVKALPGIR 
      1160       1170       1180       1190       1200
RQGLLTLSAD TETNQTLNKI TESVNQAAQV VSQFDLSGPA NSVSLAASDI 
      1210       1220       1230       1240       1250
REAAHKVASS LNGFTDVIAD IKDSLFTRVS DAVESGVATF LTWLVKLFGY 
      1260       1270       1280       1290       1300
LLVLFGSPTP MSISGLLVII CADLAPHARE FFTASGNVLS SLYYWIASKL 
      1310       1320       1330       1340       1350
GLSVTPQECE RATLEPQGLK DFNDGALAMR NVEWIGETAW KWAHRLLDWI 
      1360       1370       1380       1390       1400
RGKAKTDPQA KLADVHDEIM LHYSDSILAL GSEKLPIDHI TKSISRCREL 
      1410       1420       1430       1440       1450
VSIAQEAKSG PHSSFLNQAI KNYTLAISQH RKCQTGPRPE PVVVYLYGPP 
      1460       1470       1480       1490       1500
GTGKSLLASL LAQTLSQRLA GTPDDVYSPS SASCEYFDGY TGQTVHFIDD 
      1510       1520       1530       1540       1550
IGQDPEGRDW ANFPNLVSSA PFIVPMASLE EKGTHYTSKV IVVTSNFHEP 
      1560       1570       1580       1590       1600
NERAARSMGA LRRRVHLRIN VTSNGVPFDP TNALNPIPGT QSKYFTAQTP 
      1610       1620       1630       1640       1650
LTLFQSNTVR LDRDSIWTPT FTNMDELVDA IVTRLDRSTG VSNSLASLIR 
      1660       1670       1680       1690       1700
RQGNRVIDAE PREIPLEYAD DLLEAMAHHR PVPCSLGLSQ AIANNTPIQQ 
      1710       1720       1730       1740       1750
ISETFWKYRK PIFTCTTFLA VLGFLCSVIP LARSLWKSKQ DTPQEPQAAY 
      1760       1770       1780       1790       1800
SAISHQKPKP KSQKPVPTRH IQRQGISPAV PGISNNVVHV ESGNGLNKNV 
      1810       1820       1830       1840       1850
MSGFYIFSRF LLVPTHLREP HHTTLTVGAD TYDWATLQTQ EFGEITIVHT 
      1860       1870       1880       1890       1900
PTSRQYKDMR RFIGAHPHPT GLLVSQFKAA PLYVRISDNR ILDLDFPGVV 
      1910       1920       1930       1940       1950
VCKQAYGYRA ATFEGLCGSP LVTDDPSGVK ILGLHVAGVA GTSGFSAPIH 
      1960       1970       1980       1990       2000
PILGQITQFA TTQQSLIVPT AEVRPGVNVN RMSRLHPSPA YGAFPVKKQP 
      2010       2020       2030       2040       2050
APLKRNDKRL QEGVDLDTQL FLKHGKGDVT EPWPGLEAAA DLYFSTFPTS 
      2060       2070       2080       2090       2100
LPVLTQEQAI HGTPNMEGLD MGQAAGYPWN TLGRSRRSLF DEVEPGVFVP 
      2110       2120       2130       2140       2150
KPELQAEINQ TLEDPDYVYS TFLKDELRPT AKVEQGLTRI VEAAPIHAIV 
      2160       2170       2180       2190       2200
AGRMLLGGLI DYMQGRPGEH GSAVGCNPDV HWTSFFYAFS EFSQVYDLDY 
      2210       2220       2230       2240       2250
KCFDATLPSA VFTLVADHLT RITGDPRVGR YIHSIRHSHH IYGNRMYDMI 
      2260       2270       2280       2290       2300
GGNPSGCVAT SILNTIINNI CVLSALIQHP DFSPSRFHIL AYGDDVIYAT 
      2310       2320       2330       2340       2350
EPPIHPSFLR EFYQKHTPLV VTPANKGQDF PPTSTIYEVT FLKRWFVPDD 
      2360       2370       2380       2390       2400
VRPIYIHPVM DPDTYEQSVM WLRDGDFQDV VTSLCHLAFH SGPKTYAAWC 
      2410       2420       2430 
MKVREQCLKS GFAPNFLPYS YLQLRWLNLL AA
Length:2,432
Mass (Da):265,458
Last modified:October 16, 2019 - 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:iE451BABAD3CD1460
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA31356 differs from that shown. Reason: Frameshift.Curated

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 conflicti71R → C in BAA31356 (PubMed:9733894).Curated1
Sequence conflicti185T → N in BAA31356 (PubMed:9733894).Curated1
Sequence conflicti839N → D in BAA31356 (PubMed:9733894).Curated1
Sequence conflicti1172E → G in BAA31356 (PubMed:9733894).Curated1
Sequence conflicti1351R → P in BAA31356 (PubMed:9733894).Curated1
Sequence conflicti1420I → V in BAA31356 (PubMed:9733894).Curated1
Sequence conflicti2031E → G in BAA31356 (PubMed:9733894).Curated1

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
AB010145 Genomic RNA Translation: BAA31356.1 Frameshift.
AB040749 Genomic RNA Translation: BAB62889.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010145 Genomic RNA Translation: BAA31356.1 Frameshift.
AB040749 Genomic RNA Translation: BAB62889.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AOOX-ray2.10A764-1016[»]
B171-540[»]
C541-763[»]
5GKAelectron microscopy3.70A764-1016[»]
B174-540[»]
C541-762[»]
5LVCelectron microscopy4.20a764-1016[»]
b171-540[»]
c541-763[»]
5LZ3X-ray3.00B1653-1710[»]
SMRiO91464
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiO91464, 1 interactor
MINTiO91464

PTM databases

iPTMnetiO91464

Family and domain databases

CDDicd00205, rhv_like, 3 hits
Gene3Di2.40.10.10, 2 hits
2.60.120.20, 3 hits
3.30.70.270, 2 hits
InterProiView protein in InterPro
IPR043502, DNA/RNA_pol_sf
IPR004004, Helic/Pol/Pept_Calicivir-typ
IPR000605, Helicase_SF3_ssDNA/RNA_vir
IPR014759, Helicase_SF3_ssRNA_vir
IPR027417, P-loop_NTPase
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, 3 hits
PF00910, RNA_helicase, 1 hit
PRINTSiPR00918, CALICVIRUSNS
SUPFAMiSSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS51934, LRAT, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51218, SF3_HELICASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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_AIVA8
<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: O91464
Secondary accession number(s): Q91QP4
<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: October 16, 2019
Last sequence update: October 16, 2019
Last modified: December 2, 2020
This is version 144 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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again