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Protein

Genome polyprotein

Gene
N/A
Organism
Human hepatitis A virus genotype IB (isolate HM175) (HHAV) (Human hepatitis A virus (isolate Human/Australia/HM175/1976))
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

Capsid protein VP1: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome (PubMed:25327248, PubMed:28074040). All these proteins contain a beta-sheet structure called beta-barrel jelly roll (PubMed:25327248). Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms (PubMed:25327248). VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (PubMed:25327248). The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell (PubMed:9658108, PubMed:11134285, PubMed:29437974).5 Publications
Capsid protein VP2: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome (PubMed:25327248, PubMed:28074040). All these proteins contain a beta-sheet structure called beta-barrel jelly roll (PubMed:25327248). Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms (PubMed:25327248). VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (PubMed:25327248). The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell (PubMed:9658108, PubMed:11134285, PubMed:29437974).5 Publications
Capsid protein VP3: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome (PubMed:25327248, PubMed:28074040). All these proteins contain a beta-sheet structure called beta-barrel jelly roll (PubMed:25327248). Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms (PubMed:25327248). VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (PubMed:25327248). The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell (PubMed:9658108, PubMed:11134285, PubMed:29437974).5 Publications
Protein VP0: VP0 precursor is a component of the immature procapsids.1 Publication
Protein VP4: Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size.1 Publication
Protein VP1-2A: Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1 (PubMed:9988685, PubMed:12097562). After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein (PubMed:9988685).2 Publications
Protein 2B: Function as a viroporin (PubMed:26515753). Affects membrane integrity and causes an increase in membrane permeability (PubMed:9875331). Involved in host intracellular membrane rearrangements probably to give rise to the viral factories (PubMed:9344908). Does not disrupt calcium homeostasis or glycoprotein trafficking (PubMed:18216106). Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the DDX58/IFIH1 (RIG-I/MDA5) pathway (PubMed:18559929).5 Publications
Protein 2BC: Affects membrane integrity and causes an increase in membrane permeability.2 Publications
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes (PubMed:9344908). Displays RNA-binding activity (PubMed:9645199).2 Publications
Protein 3ABC: The precursor 3ABC is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway (PubMed:17438296). In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein (PubMed:10559299).2 Publications
Protein 3AB: Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome (PubMed:10562502). Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs (PubMed:9705870).2 Publications
Protein 3A: May serve as membrane anchor to the 3AB and 3ABC precursors via its hydrophobic domain (PubMed:9705870). May interact with RNA (PubMed:10562502).2 Publications
Viral protein genome-linked: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome.1 PublicationBy similarity
Protease 3C: Cysteine protease that generates mature viral proteins from the precursor polyprotein (PubMed:1850033). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication (PubMed:15361063). RNA and substrate bind cooperatively to the protease (PubMed:9032381). Cleaves IKBKG/NEMO to impair innate immune signaling (PubMed:24920812). Cleaves host PABPC1 which may participate to the switch of viral translation to RNA synthesis (PubMed:17726047).5 Publications
Protein 3CD: Interacts with the 3AB precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome (PubMed:10562502). Disrupts TLR3 signaling by degrading the host adapter protein TICAM1/TRIF (PubMed:21931545).2 Publications
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.Curated

Miscellaneous

The need for an intact eIF4G factor for the initiation of translation of HAV results in an inability to shut off host protein synthesis by a mechanism similar to that of other picornaviruses.Curated
During infection, enveloped virions (eHAV) are released from cells (PubMed:23542590). These eHAV are cloaked in host-derived membranes and resemble exosomes (PubMed:28490497). The membrane of eHAV is devoid of viral proteins and thus prevents their neutralization by antibodies (PubMed:23542590). eHAV budding is dependent on ESCRT-associated proteins VPS4B and PDCD6IP/ALIX (PubMed:23542590). eHAV are produced and released in the serum and plasma, but not in bile and feces which only contain the naked, nonenveloped virions (Probable). It is likely that eHAV also use HAVCR1 as a functional receptor to infect cells, an evolutionary trait that may enhance HAV infectivity (PubMed:29437974).1 PublicationCurated3 Publications
Wild-type HM175 (HM175/wt) comes from a sample isolated from a patient in Australia in 1976 and subsequently passaged three times in marmosets. HM175/7 is an attenuated strain derived from HM175 by 32 passages in African green monkey kidney cells. HM175/18f, HM175/24a, and HM175/43c are cytopathic isolates derived from HM175 by serial passages in FRhK-4 cells.Curated
Mutations in proteins 2B and 2C seem to be essential for strain HM175 adaptation to growth in cell culture.

Caution

It is uncertain whether Met-1 or Met-3 is the initiator. In vitro, both are used, with a preference for Met-3.1 Publication

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

  • Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.1 Publication EC:3.4.22.28

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>Sitei769Important for VP1 folding and capsid assembly2 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1563For protease 3C activityBy similarity1
Active sitei1603For protease 3C activityBy similarity1
Active sitei1691For protease 3C activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1230 – 1237ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

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

Molecular functionHelicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel
Biological processHost-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host MAVS by virus, Inhibition of host RLR pathway by virus, Interferon antiviral system evasion, Ion transport, Transport, Viral attachment to host cell, Viral immunoevasion, 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_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 18 chains:
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Virion protein 4
Alternative name(s):
P1B
Virion protein 2
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
VP1-pX
Alternative name(s):
P1D
Virion protein 1
Alternative name(s):
pX1 Publication
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3ABCD
Short name:
P3
Protein 3A
Short name:
P3A
Alternative name(s):
Protein 3B
Short name:
P3B
Protease 3C (EC:3.4.22.281 Publication)
Short name:
P3C
Alternative name(s):
Picornain 3C
RNA-directed RNA polymerase 3D-POL (EC:2.7.7.481 Publication)
Short name:
P3D-POL
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHuman hepatitis A virus genotype IB (isolate HM175) (HHAV) (Human hepatitis A virus (isolate Human/Australia/HM175/1976))
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri12098 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeHepatovirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiCercopithecus hamlyni (Owl-faced monkey) (Hamlyn's monkey) [TaxID: 9536]
Homo sapiens (Human) [TaxID: 9606]
Macaca (macaques) [TaxID: 9539]
Pan troglodytes (Chimpanzee) [TaxID: 9598]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000155985 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
  • UP000096966 Componenti: Genome
  • UP000157977 Componenti: Genome
  • UP000139151 Componenti: Genome
  • UP000006724 Componenti: Genome

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

Capsid protein VP2 :
Capsid protein VP3 :
Capsid protein VP1 :
Protein VP4 :
  • Virion 1 Publication
  • Note: Present in the full mature virion (PubMed:25327248). The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies (Probable).1 Publication1 Publication
Protein 2B :
Protein 2C :
Protein 3ABC :
Protein 3AB :
Protein 3A :
RNA-directed RNA polymerase 3D-POL :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the 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>Transmembranei1011 – 1031HelicalSequence analysisAdd BLAST21
Transmembranei1462 – 1482HelicalSequence analysis1 PublicationAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host endosome, Host membrane, Host mitochondrion, Host mitochondrion outer membrane, Membrane, 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_and_biotech_section">'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>Mutagenesisi167Y → A: Severely decreases virus release but does not impair viral RNA replication. 1 Publication1
Mutagenesisi200Y → A: Severely decreases virus release but does not impair viral RNA replication. 1 Publication1
Mutagenesisi769R → M: Complete loss of viral particles assembly. Interferes with oligomerization of protein VP1-2A and maturation of procapsids. 2 Publications1
Mutagenesisi836Q → N: Partial loss of VP1-2A-2B cleavage. 1 Publication1
Mutagenesisi836Q → R: Complete loss of VP1-2A-2B cleavage. 1 Publication1
Mutagenesisi1052A → I, L or V: 10-20 fold increase in virus yield. 1 Publication1
Mutagenesisi1543C → S: Complete loss of protease 3C dimerization. 1 Publication1
Mutagenesisi1691C → A: Complete loss of enzymatic activity. Complete loss of cleavage of host TICAM1. 1 Publication1
Mutagenesisi1691C → A: Complete loss of proteolytic activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04634 N-BENZYLOXYCARBONYL-L-SERINE-BETALACTONE
DB04029 Phenylalanine Amide

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003089691 – 2227Genome polyproteinAdd BLAST2227
ChainiPRO_00003089701 – 245Protein VP0Add BLAST245
ChainiPRO_00000399461 – 23Protein VP4Add BLAST23
ChainiPRO_000003994724 – 245Capsid protein VP2Add BLAST222
ChainiPRO_0000039948246 – 491Capsid protein VP3Add BLAST246
ChainiPRO_0000308971492 – 836Protein VP1-2AAdd BLAST345
ChainiPRO_0000039949492 – 765Capsid protein VP1Add BLAST274
ChainiPRO_0000039950766 – 836Assembly signal 2AAdd BLAST71
ChainiPRO_0000308972837 – 1422Protein 2BCAdd BLAST586
ChainiPRO_0000039951837 – 1087Protein 2BAdd BLAST251
ChainiPRO_00000399521088 – 1422Protein 2CAdd BLAST335
ChainiPRO_00003089731423 – 2227Protein 3ABCDAdd BLAST805
ChainiPRO_00003089741423 – 1738Protein 3ABCAdd BLAST316
ChainiPRO_00003089751423 – 1519Protein 3ABAdd BLAST97
ChainiPRO_00000399531423 – 1496Protein 3AAdd BLAST74
ChainiPRO_00000399541497 – 1519Viral protein genome-linkedAdd BLAST23
ChainiPRO_00003089761520 – 2227Protein 3CDAdd BLAST708
ChainiPRO_00000399551520 – 1738Protease 3CAdd BLAST219
ChainiPRO_00000399561739 – 2227RNA-directed RNA polymerase 3D-POLAdd BLAST489

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 residuei1499O-(5'-phospho-RNA)-tyrosineBy 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 bondi1543Interchain1 Publication

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

Genome polyprotein: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a stable and catalytically active precursor of 3A, 3B and 3C proteins, 3AB and 3CD precursors (PubMed:7483265, PubMed:1850033, PubMed:8382411, PubMed:8291234, PubMed:9060697, PubMed:9733840, PubMed:8259663, PubMed:7853510, PubMed:10559299). The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L (PubMed:18823593). This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini (PubMed:10364353). During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (PubMed:12782637, PubMed:8291234, PubMed:9060697, PubMed:9733840).12 Publications
Protein VP1-2A: The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L in nacked virions (PubMed:18823593). This cleavage does not occur in enveloped virions (PubMed:28490497). This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini (PubMed:10364353).3 Publications
Viral protein genome-linked: VPg is uridylylated prior to priming replication into VPg-pUpU.By similarity
Protein VP4: Unlike other picornaviruses, does not seem to be myristoylated.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei245 – 246Cleavage; by protease 3C1 Publication2
Sitei491 – 492Cleavage; by protease 3C1 Publication2
Sitei765 – 766Cleavage; partial; by host2 Publications2
Sitei836 – 837Cleavage; by protease 3C2 Publications2
Sitei1087 – 1088Cleavage; by protease 3C1 Publication2
Sitei1422 – 1423Cleavage; by protease 3C1 Publication2
Sitei1496 – 1497Cleavage; by protease 3C1 Publication2
Sitei1519 – 1520Cleavage; by protease 3C1 Publication2
Sitei1738 – 1739Cleavage; by protease 3C1 Publication2

Keywords - PTMi

Covalent protein-RNA linkage, Disulfide bond, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P08617

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

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

Protein 2B: Homodimer. Homomultimer; probably interacts with membranes in a multimeric form (PubMed:26515753). Seems to assemble into amyloid-like fibers (PubMed:25589659). Protein 3AB: Homodimer. Monomer (PubMed:9705870). Protein 3AB: Interacts with protein 3CD (PubMed:10562502). Protein 3CD: Interacts with protein 3AB (PubMed:10562502). Protein 3ABC: Interacts with human MAVS (PubMed:17438296). Protease 3C: Homodimer; disulfide-linked (PubMed:15361063). Protein VP1-2A: Homopentamer (PubMed:12782637). Protein VP1-2A: Homooligomer (PubMed:18823593, PubMed:12782637). Capsid protein VP1: Interacts with capsid protein VP2 (PubMed:25327248, PubMed:28074040). Capsid protein VP1: Interacts with capsid protein VP3 (PubMed:25327248, PubMed:28074040). Capsid protein VP2: Interacts with capsid protein VP1 (PubMed:25327248, PubMed:28074040). Capsid protein VP2: Interacts with capsid protein VP3 (PubMed:25327248, PubMed:28074040). Capsid protein VP3: Interacts with capsid protein VP1 (PubMed:25327248, PubMed:28074040). Capsid protein VP3: Interacts with capsid protein VP2 (PubMed:25327248, PubMed:28074040).10 Publications

<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

12227
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P08617

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

More...
SMRi
P08617

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P08617

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1204 – 1366SF3 helicasePROSITE-ProRule annotationAdd BLAST163
Domaini1520 – 1716Peptidase C3Sequence analysisAdd BLAST197
Domaini1976 – 2097RdRp catalyticPROSITE-ProRule annotationAdd BLAST122

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>Regioni766 – 836Involved in P1-2A pentamerization2 PublicationsAdd BLAST71
Regioni1043 – 1070Membrane-penetrating ability1 PublicationAdd BLAST28

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>Motifi167 – 171(L)YPX(n)L motif1 Publication5
Motifi200 – 205(L)YPX(n)L motif1 Publication6

<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

Protein VP1-2A: The assembly signal 2A region mediates pentamerization of P1-2A.2 Publications
Genome polyprotein: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding (Probable). They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins (Probable). The genome polyprotein contains two L domains: a tandem of (L)YPX(n)L domain which is known to bind the PDCD6IP/ALIX adaptater protein (PubMed:23542590).Curated1 Publication
Capsid protein VP2: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding (Probable). They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins (Probable). Capsid protein VP2 contains two L domains: a tandem of (L)YPX(n)L domain which is known to bind the Alix adaptater protein (PubMed:23542590).Curated1 Publication
Protein 2B: The C-terminus displays a membrane-penetrating ability.1 Publication

<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 picornaviridae polyprotein family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
VOG090000BA

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00205 rhv_like, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.20, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004004 Helic/Pol/Pept_Calicivir-typ
IPR000605 Helicase_SF3_ssDNA/RNA_vir
IPR014759 Helicase_SF3_ssRNA_vir
IPR024354 Hepatitis_A_VP1-2A
IPR000199 Peptidase_C3A/C3B_picornavir
IPR009003 Peptidase_S1_PA
IPR001676 Picornavirus_capsid
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
PF12944 HAV_VP, 1 hit
PF00548 Peptidase_C3, 1 hit
PF00680 RdRP_1, 1 hit
PF00073 Rhv, 2 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

PROSITE; a protein domain and family database

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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

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

P08617-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNMSRQGIFQ TVGSGLDHIL SLADIEEEQM IQSVDRTAVT GASYFTSVDQ
60 70 80 90 100
SSVHTAEVGS HQVEPLRTSV DKPGSKKTQG EKFFLIHSAD WLTTHALFHE
110 120 130 140 150
VAKLDVVKLL YNEQFAVQGL LRYHTYARFG IEIQVQINPT PFQQGGLICA
160 170 180 190 200
MVPGDQSYGS IASLTVYPHG LLNCNINNVV RIKVPFIYTR GAYHFKDPQY
210 220 230 240 250
PVWELTIRVW SELNIGTGTS AYTSLNVLAR FTDLELHGLT PLSTQMMRNE
260 270 280 290 300
FRVSTTENVV NLSNYEDARA KMSFALDQED WKSDPSQGGG IKITHFTTWT
310 320 330 340 350
SIPTLAAQFP FNASDSVGQQ IKVIPVDPYF FQMTNTNPDQ KCITALASIC
360 370 380 390 400
QMFCFWRGDL VFDFQVFPTK YHSGRLLFCF VPGNELIDVS GITLKQATTA
410 420 430 440 450
PCAVMDITGV QSTLRFRVPW ISDTPYRVNR YTKSAHQKGE YTAIGKLIVY
460 470 480 490 500
CYNRLTSPSN VASHVRVNVY LSAINLECFA PLYHAMDVTT QVGDDSGGFS
510 520 530 540 550
TTVSTEQNVP DPQVGITTMK DLKGKANRGK MDVSGVQAPV GAITTIEDPV
560 570 580 590 600
LAKKVPETFP ELKPGESRHT SDHMSIYKFM GRSHFLCTFT FNSNNKEYTF
610 620 630 640 650
PITLSSTSNP PHGLPSTLRW FFNLFQLYRG PLDLTIIITG ATDVDGMAWF
660 670 680 690 700
TPVGLAVDTP WVEKESALSI DYKTALGAVR FNTRRTGNIQ IRLPWYSYLY
710 720 730 740 750
AVSGALDGLG DKTDSTFGLV SIQIANYNHS DEYLSFSCYL SVTEQSEFYF
760 770 780 790 800
PRAPLNSNAM LSTESMMSRI AAGDLESSVD DPRSEEDKRF ESHIECRKPY
810 820 830 840 850
KELRLEVGKQ RLKYAQEELS NEVLPPPRKM KGLFSQAKIS LFYTEEHEIM
860 870 880 890 900
KFSWRGVTAD TRALRRFGFS LAAGRSVWTL EMDAGVLTGR LIRLNDEKWT
910 920 930 940 950
EMKDDKIVSL IEKFTSNKYW SKVNFPHGML DLEEIAANSK DFPNMSETDL
960 970 980 990 1000
CFLLHWLNPK KINLADRMLG LSGVQEIKEQ GVGLIAECRT FLDSIAGTLK
1010 1020 1030 1040 1050
SMMFGFHHSV TVEIINTVLC FVKSGILLYV IQQLNQDEHS HIIGLLRVMN
1060 1070 1080 1090 1100
YADIGCSVIS CGKVFSKMLE TVFNWQMDSR MMELRTQSFS NWLRDICSGI
1110 1120 1130 1140 1150
TIFKNFKDAI YWLYTKLKDF YEVNYGKKKD ILNILKDNQQ KIEKAIEEAD
1160 1170 1180 1190 1200
EFCILQIQDV EKFEQYQKGV DLIQKLRTVH SMAQVDPNLM VHLSPLRDCI
1210 1220 1230 1240 1250
ARVHQKLKNL GSINQAMVTR CEPVVCYLYG KRGGGKSLTS IALATKICKH
1260 1270 1280 1290 1300
YGVEPEKNIY TKPVASDYWD GYSGQLVCII DDIGQNTTDE DWSDFCQLVS
1310 1320 1330 1340 1350
GCPMRLNMAS LEEKGRHFSS PFIIATSNWS NPSPKTVYVK EAIDRRLHFK
1360 1370 1380 1390 1400
VEVKPASFFK NPHNDMLNVN LAKTNDAIKD MSCVDLIMDG HNVSLMDLLS
1410 1420 1430 1440 1450
SLVMTVEIRK QNMTEFMELW SQGISDDDND SAVAEFFQSF PSGEPSNSKL
1460 1470 1480 1490 1500
SGFFQSVTNH KWVAVGAAVG ILGVLVGGWF VYKHFSRKEE EPIPAEGVYH
1510 1520 1530 1540 1550
GVTKPKQVIK LDADPVESQS TLEIAGLVRK NLVQFGVGEK NGCVRWVMNA
1560 1570 1580 1590 1600
LGVKDDWLLV PSHAYKFEKD YEMMEFYFNR GGTYYSISAG NVVIQSLDVG
1610 1620 1630 1640 1650
FQDVVLMKVP TIPKFRDITQ HFIKKGDVPR ALNRLATLVT TVNGTPMLIS
1660 1670 1680 1690 1700
EGPLKMEEKA TYVHKKNDGT TVDLTVDQAW RGKGEGLPGM CGGALVSSNQ
1710 1720 1730 1740 1750
SIQNAILGIH VAGGNSILVA KLVTQEMFQN IDKKIESQRI MKVEFTQCSM
1760 1770 1780 1790 1800
NVVSKTLFRK SPIYHHIDKT MINFPAAMPF SKAEIDPMAV MLSKYSLPIV
1810 1820 1830 1840 1850
EEPEDYKEAS IFYQNKIVGK TQLVDDFLDL DMAITGAPGI DAINMDSSPG
1860 1870 1880 1890 1900
FPYVQEKLTK RDLIWLDENG LLLGVHPRLA QRILFNTVMM ENCSDLDVVF
1910 1920 1930 1940 1950
TTCPKDELRP LEKVLESKTR AIDACPLDYS ILCRMYWGPA ISYFHLNPGF
1960 1970 1980 1990 2000
HTGVAIGIDP DRQWDELFKT MIRFGDVGLD LDFSAFDASL SPFMIREAGR
2010 2020 2030 2040 2050
IMSELSGTPS HFGTALINTI IYSKHLLYNC CYHVCGSMPS GSPCTALLNS
2060 2070 2080 2090 2100
IINNVNLYYV FSKIFGKSPV FFCQALKILC YGDDVLIVFS RDVQIDNLDL
2110 2120 2130 2140 2150
IGQKIVDEFK KLGMTATSAD KNVPQLKPVS ELTFLKRSFN LVEDRIRPAI
2160 2170 2180 2190 2200
SEKTIWSLIA WQRSNAEFEQ NLENAQWFAF MHGYEFYQKF YYFVQSCLEK
2210 2220
EMIEYRLKSY DWWRMRFYDQ CFICDLS
Length:2,227
Mass (Da):251,508
Last modified:August 1, 1988 - 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:i01E225E7AEB740A6
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 AAA45466 differs from that shown. Reason: Erroneous initiation.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 conflicti67R → K in AAL66215 (PubMed:12409389).Curated1
Sequence conflicti1825D → V in AAA45476 (PubMed:2984684).Curated1
Sequence conflicti1850G → R in AAA45476 (PubMed:2984684).Curated1
Sequence conflicti1856E → G in AAA45476 (PubMed:2984684).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti77K → R in strain: HM175/7, HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti315D → A in strain: HM175/24a and HM175/43c. 1
Natural varianti336T → K in strain: HM175/18f. 1
Natural varianti638I → V in strain: HM175/24a. 1
Natural varianti688N → S in strain: HM175/24a and HM175/43c. 1
Natural varianti762S → P in strain: HM175/18f. 1
Natural varianti764E → V in strain: HM175/7. 1
Natural varianti767M → V in strain: HM175/24a and HM175/43c. 1
Natural varianti821N → S in strain: HM175/7. 1
Natural varianti838K → N in strain: HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti849I → M in strain: HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti941D → E in 24. 1
Natural varianti993D → H in strain: HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1052A → V in strain: HM175/7, HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1062G → A in strain: HM175/7. 1
Natural varianti1109 – 1111AIY → GIC in strain: HM175/18f, HM175/24a and HM175/43c. 3
Natural varianti1118K → M in strain: HM175/7. 1
Natural varianti1151E → K in strain: HM175/7, HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1163F → S in strain: HM175/7, HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1180H → Y in strain: HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1212S → F in strain: HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1229Y → H in strain: HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1277V → I in strain: HM175/7. 1
Natural varianti1407E → D in strain: HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1428Missing in strain: HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1480F → V in strain: HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1487R → H in strain: HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1500H → Y in strain: HM175/7. 1
Natural varianti1507Q → H in strain: HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1524I → V in strain: HM175/43c. 1
Natural varianti1620Q → E in strain: HM175/18f and HM175/24a. 1
Natural varianti1675T → A in strain: HM175/43c. 1
Natural varianti1805D → G in strain: HM175/7, HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1930S → T in strain: HM175/7, HM175/18f, HM175/24a and HM175/43c. 1
Natural varianti1962R → K in strain: HM175/18f, HM175/24a and HM175/43c. 1

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
M14707 Genomic RNA Translation: AAA45465.1
M14707 Genomic RNA Translation: AAA45466.1 Different initiation.
M16632 Genomic RNA Translation: AAA45471.1
M59808 Genomic RNA Translation: AAA45467.1
M59809 Genomic RNA Translation: AAA45469.1
M59810 Genomic RNA Translation: AAA45468.1
M14114 Genomic RNA Translation: AAA45475.1
M14115 Genomic RNA Translation: AAA45476.1
K00386 Genomic RNA No translation available.
AF396398 Genomic RNA Translation: AAL66215.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A03905
A25981 GNNYHM
A94149 GNNYMK
JH0135
PQ0427
PQ0428
PQ0431

NCBI Reference Sequences

More...
RefSeqi
NP_041007.1, NC_001489.1
NP_041008.1, NC_001489.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1493918
1493919

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:1493918
vg:1493919

<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
M14707 Genomic RNA Translation: AAA45465.1
M14707 Genomic RNA Translation: AAA45466.1 Different initiation.
M16632 Genomic RNA Translation: AAA45471.1
M59808 Genomic RNA Translation: AAA45467.1
M59809 Genomic RNA Translation: AAA45469.1
M59810 Genomic RNA Translation: AAA45468.1
M14114 Genomic RNA Translation: AAA45475.1
M14115 Genomic RNA Translation: AAA45476.1
K00386 Genomic RNA No translation available.
AF396398 Genomic RNA Translation: AAL66215.1
PIRiA03905
A25981 GNNYHM
A94149 GNNYMK
JH0135
PQ0427
PQ0428
PQ0431
RefSeqiNP_041007.1, NC_001489.1
NP_041008.1, NC_001489.1

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
1HAVX-ray2.00A/B1520-1736[»]
1QA7X-ray1.90A/B/C/D1520-1736[»]
2H6MX-ray1.40A1520-1731[»]
2H9HX-ray1.39A1520-1731[»]
2HALX-ray1.35A1520-1731[»]
4QPGX-ray3.50B41-244[»]
C246-491[»]
4QPIX-ray3.01B24-245[»]
C246-491[»]
4WZNX-ray2.70A/B765-981[»]
5WTEelectron microscopy3.40A492-769[»]
B24-245[»]
C246-491[»]
5WTFelectron microscopy3.90A540-763[»]
B42-244[»]
C246-491[»]
5WTHelectron microscopy4.20A492-769[»]
B24-245[»]
C246-491[»]
ProteinModelPortaliP08617
SMRiP08617
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB04634 N-BENZYLOXYCARBONYL-L-SERINE-BETALACTONE
DB04029 Phenylalanine Amide

Proteomic databases

PRIDEiP08617

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1493918
1493919
KEGGivg:1493918
vg:1493919

Phylogenomic databases

OrthoDBiVOG090000BA

Miscellaneous databases

EvolutionaryTraceiP08617

Family and domain databases

CDDicd00205 rhv_like, 2 hits
Gene3Di2.60.120.20, 3 hits
InterProiView protein in InterPro
IPR004004 Helic/Pol/Pept_Calicivir-typ
IPR000605 Helicase_SF3_ssDNA/RNA_vir
IPR014759 Helicase_SF3_ssRNA_vir
IPR024354 Hepatitis_A_VP1-2A
IPR000199 Peptidase_C3A/C3B_picornavir
IPR009003 Peptidase_S1_PA
IPR001676 Picornavirus_capsid
IPR033703 Rhv-like
IPR001205 RNA-dir_pol_C
IPR007094 RNA-dir_pol_PSvirus
IPR029053 Viral_coat
PfamiView protein in Pfam
PF12944 HAV_VP, 1 hit
PF00548 Peptidase_C3, 1 hit
PF00680 RdRP_1, 1 hit
PF00073 Rhv, 2 hits
PF00910 RNA_helicase, 1 hit
PRINTSiPR00918 CALICVIRUSNS
SUPFAMiSSF50494 SSF50494, 1 hit
PROSITEiView protein in PROSITE
PS50507 RDRP_SSRNA_POS, 1 hit
PS51218 SF3_HELICASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_HAVHM
<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: P08617
Secondary accession number(s): P06443
, P26580, P26581, P26582, Q81082, Q81094, Q8V405
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: December 5, 2018
This is version 159 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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