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UniProtKB - A5LGW7 (POLG_HAVJ8)

Entry version 83 (07 Oct 2020)
Sequence version 1 (10 Jul 2007)
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Protein

Genome polyprotein

Gene
N/A
Organism
Human hepatitis A virus genotype IIIB (isolate HAJ85-1) (HHAV) (Human hepatitis A virus (isolate Human/Japan/HAJ85-1/1985))
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

Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. 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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.By similarity
Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. 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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.By similarity
Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. 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. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.By similarity
VP0 precursor is a component of the immature procapsids.By similarity
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.By similarity
Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein.By similarity
Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. 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.By similarity
Affects membrane integrity and causes an increase in membrane permeability.By similarity
Associates with and induces structural rearrangements of intracellular membranes. Displays RNA-binding activity.By similarity
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. 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. Possible viroporin.By similarity
Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. 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.By similarity
May serve as membrane anchor to the 3AB and 3ABC precursors via its hydrophobic domain. May interact with RNA.By similarity
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.By similarity
Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis.By similarity
Interacts with the 3AB precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Disrupts TLR3 signaling by degrading the host adapter protein TICAM1/TRIF.By similarity
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.By similarity

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.By similarity
During infection, enveloped virions (eHAV) are released from cells. These eHAV are cloaked in host-derived membranes and resemble exosomes. The membrane of eHAV is devoid of viral proteins and thus prevents their neutralization by antibodies. eHAV budding is dependent on ESCRT-associated proteins VPS4B and PDCD6IP/ALIX. eHAV are produced and released in the serum and plasma, but not in bile and feces which only contain the naked, nonenveloped virions. It is likely that eHAV also use HAVCR1 as a functional receptor to infect cells, an evolutionary trait that may enhance HAV infectivity.By similarity

Caution

It is uncertain whether Met-1 or Met-3 is the initiator.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 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 assemblyBy similarity1
<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 sitei1563For protease 3C activityPROSITE-ProRule annotation1
Active sitei1603For protease 3C activityPROSITE-ProRule annotation1
Active sitei1691For protease 3C activityPROSITE-ProRule annotation1

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 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

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 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%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 18 chains:
Protein VP0
Alternative name(s):
VP4-VP2
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
Protein VP1-2A
Alternative name(s):
VPX
Capsid protein VP1
Alternative name(s):
P1D
Virion protein 1
Assembly signal 2A
Alternative name(s):
pXBy similarity
Protein 2BC
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3ABCD
Short name:
P3
Protein 3ABC
Protein 3AB
Protein 3A
Short name:
P3A
Viral protein genome-linked
Short name:
VPg
Alternative name(s):
Protein 3B
Short name:
P3B
Protein 3CD
Protease 3C (EC:3.4.22.28By similarity)
Short name:
P3C
Alternative name(s):
Picornain 3C
RNA-directed RNA polymerase 3D-POL (EC:2.7.7.48By similarity)
Short name:
P3D-POL
<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>OrganismiHuman hepatitis A virus genotype IIIB (isolate HAJ85-1) (HHAV) (Human hepatitis A virus (isolate Human/Japan/HAJ85-1/1985))
<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 identifieri474341 [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 › Hepatovirus ›
<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 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%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
  • UP000007902 <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

  • Virion By similarity
    • Note: Present in the full mature virion. The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies.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>Transmembranei1011 – 1031HelicalSequence analysisAdd BLAST21
Transmembranei1462 – 1482HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host endosome, Host membrane, Host mitochondrion, Host mitochondrion outer membrane, 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_00003106361 – 2228Genome polyproteinAdd BLAST2228
ChainiPRO_00003106371 – 245Protein VP0Add BLAST245
ChainiPRO_00003106381 – 23Protein VP4Add BLAST23
ChainiPRO_000031063924 – 245Capsid protein VP2Add BLAST222
ChainiPRO_0000310640246 – 491Capsid protein VP3Add BLAST246
ChainiPRO_0000310641492 – 836Protein VP1-2AAdd BLAST345
ChainiPRO_0000310642492 – 765Capsid protein VP1Add BLAST274
ChainiPRO_0000310643766 – 836Assembly signal 2AAdd BLAST71
ChainiPRO_0000310644837 – 1422Protein 2BCAdd BLAST586
ChainiPRO_0000310645837 – 1087Protein 2BAdd BLAST251
ChainiPRO_00003106461088 – 1422Protein 2CAdd BLAST335
ChainiPRO_00003106471423 – 2228Protein 3ABCDAdd BLAST806
ChainiPRO_00003106481423 – 1739Protein 3ABCAdd BLAST317
ChainiPRO_00003106491423 – 1519Protein 3ABAdd BLAST97
ChainiPRO_00003106501423 – 1496Protein 3AAdd BLAST74
ChainiPRO_00003106511497 – 1519Viral protein genome-linkedAdd BLAST23
ChainiPRO_00003106521520 – 2228Protein 3CDAdd BLAST709
ChainiPRO_00003106531520 – 1739Protease 3CAdd BLAST220
ChainiPRO_00003106541740 – 2228RNA-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 bondi1543InterchainBy similarity

<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 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. The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini.By similarity
Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle.By similarity
The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L in nacked virions. This cleavage does not occur in enveloped virions. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini.By similarity
VPg is uridylylated prior to priming replication into VPg-pUpU.By similarity
Unlike other picornaviruses, does not seem to be myristoylated.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei23 – 24CleavageSequence analysis2
Sitei245 – 246Cleavage; by protease 3CBy similarity2
Sitei491 – 492Cleavage; by protease 3CBy similarity2
Sitei765 – 766Cleavage; partial; by hostBy similarity2
Sitei836 – 837Cleavage; by protease 3CBy similarity2
Sitei1087 – 1088Cleavage; by protease 3CBy similarity2
Sitei1422 – 1423Cleavage; by protease 3CBy similarity2
Sitei1496 – 1497Cleavage; by protease 3CBy similarity2
Sitei1519 – 1520Cleavage; by protease 3CBy similarity2
Sitei1739 – 1740Cleavage; by protease 3CBy similarity2

Keywords - PTMi

Covalent protein-RNA linkage, Disulfide bond, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		A5LGW7

<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

Homodimer. Homomultimer; probably interacts with membranes in a multimeric form. Seems to assemble into amyloid-like fibers.

By similarity

Homodimer. Monomer.

Interacts with protein 3CD.

By similarity

Interacts with host ACBD3 (By similarity).

By similarity

Interacts with protein 3AB.

By similarity

Interacts with human MAVS.

By similarity

Homodimer; disulfide-linked.

By similarity

Homopentamer. Homooligomer.

By similarity

Interacts with capsid protein VP2.

Interacts with capsid protein VP3.

By similarity

Interacts with capsid protein VP1.

Interacts with capsid protein VP3.

By similarity

Interacts with capsid protein VP1.

Interacts with capsid protein VP2.

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

Biological Magnetic Resonance Data Bank

More...BMRBi		A5LGW7

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

<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>Domaini1204 – 1366SF3 helicasePROSITE-ProRule annotationAdd BLAST163
Domaini1514 – 1728Peptidase C3PROSITE-ProRule annotationAdd BLAST215
Domaini1977 – 2098RdRp 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 pentamerizationBy similarityAdd BLAST71
Regioni1043 – 1070Membrane-penetrating abilityBy similarityAdd BLAST28

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili1127 – 1152Sequence analysisAdd BLAST26

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 motifBy similarity5
Motifi200 – 205(L)YPX(n)L motifBy similarity6

<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 assembly signal 2A region mediates pentamerization of P1-2A.By similarity
Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. 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.By similarity
Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. Capsid protein VP2 contains two L domains: a tandem of (L)YPX(n)L domain which is known to bind the Alix adaptater protein.By similarity
The C-terminus displays a membrane-penetrating ability.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 picornaviridae polyprotein family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...CDDi		cd00205, rhv_like, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.10.10, 2 hits
2.60.120.20, 3 hits
3.30.70.270, 1 hit

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
IPR024354, Hepatitis_A_VP1-2A
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
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
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>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.

A5LGW7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNMSRQGIFQ TVGSGLDHIL SLADVEEEQM IQSVDRTAVT GASYFTSVDQ 
        60         70         80         90        100
SSVHTAEVGA HQSEPLKTSV DKPGSKRTQG 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 WKSDASQGGG IKITHFTTWT 
       310        320        330        340        350
SIPTLAAQFP FNASDSVGQQ IKVIPVDPYF FQMTNTNPEQ KCITALASIC 
       360        370        380        390        400
QMFCFWRGDL VFDFQVFPTK YHSGRLLFCF VPGNELIDVS HITLKQATTA 
       410        420        430        440        450
PCAVMDITGV QSTLRFRVPW ISDTPYRVNR YTKSSHQKGE YTAIGKLIVY 
       460        470        480        490        500
CYNRLTSPSN VASHVRVNVY LSAINLECFA PLYHAMDVTT QVGDDSGGFS 
       510        520        530        540        550
TTVSTKQNVP DPQVGITTVR DLKGKANQGK 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
PRAPLNTNAM MSSETMLDRI ALGDLESSVD DPRSEEDRKF ESHIEKRKPY 
       810        820        830        840        850
KELRLEVGKQ RLKYAQEELS NEVLPPPRKI KGVFSQAKIS LFYTEDHEIM 
       860        870        880        890        900
KFSWKGITAD TRALRRFGFS LAAGRSVWTL EMDAGVLTGR LVRVNDEKWT 
       910        920        930        940        950
EMKDDKIVSL VEKFTSNKHW SKINFPHGML DLEEIAANSK EFPNMSETDL 
       960        970        980        990       1000
CFLLHWLNPK KINLADRMLG MSGIQEIKEK GVGLIGECRA FLDSITTTLK 
      1010       1020       1030       1040       1050
SMMFGFHHSV TVEIINTVLC FVKSGILLYV IQQLNQEEHS HIIGLLRVMN 
      1060       1070       1080       1090       1100
YADIGCSVIS CGKVFSKMLE TVFNWQMDSR MMELRTQSIS NWLRDICSGI 
      1110       1120       1130       1140       1150
TIFKSFKDAI YWLYTRIREY YDVNYGNKKD VLNILKDNQQ KIERAIEEAD 
      1160       1170       1180       1190       1200
NFCVLQIQDV EKFEQYQKGV DLIQKLRTVH SMAQVDPGLT VHLAPLRDCI 
      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 MSCVDLVMDS HNISLSELLS 
      1410       1420       1430       1440       1450
SLVMTVEIRK QNMSEFMELW SQGMSDDDND SAVAEFFQSF PSGEPSGSKL 
      1460       1470       1480       1490       1500
SRFFQSVTNH KWVAVGAAVG VLGVLVGGWY VYKHFTKKKE EPIPSEGVYH 
      1510       1520       1530       1540       1550
GVTKPKQVIK LDADPVESQS TLEIAGLVRK NLVQFGVGEK NGCVRWVMNA 
      1560       1570       1580       1590       1600
LGIKDDWLLV PSHAYKFEKD YEMMEFYFNR GGTYYSISAG NVVIQSLDVG 
      1610       1620       1630       1640       1650
FQDVVLMKVP TIPKFRDITE HFIKKSDVPR ALNRLATLVT TVNGTPMLIS 
      1660       1670       1680       1690       1700
EGPLKMEEKA TYVHKKNDGT TIDLTVDQAW RGKGEGLPGM CGGALISSNQ 
      1710       1720       1730       1740       1750
SIQNAILGIH VAGGNSILVA KLVTQEMFQN IDKKIVESQR IMKVEFTQCS 
      1760       1770       1780       1790       1800
MNVVSKTLFK KSPIHHHIDK NMINFPAVMP FSRAEIDPMA VMLSKYSLPI 
      1810       1820       1830       1840       1850
VDEPEDYKDV SVFFQNKILG KSPLVDDFLD IEMAITGAPG IDAINMDSSP 
      1860       1870       1880       1890       1900
GYPYVQEKLT KRDLIWLDDN GMFLGVHPRL AQRILFNTTM MENCSDLDVV 
      1910       1920       1930       1940       1950
FTTCPKDELR PLDKVLESKT RAIDSCPLDY TILCRMYWGP AISYFHLNPG 
      1960       1970       1980       1990       2000
FHTGVAIGID PDRQWDQLFK TMIRFGDVGL DLDFSAFDAS LSPFMIREAG 
      2010       2020       2030       2040       2050
RILTEMSGAP NHFGEALINT IIYSKHLLYN CCYHVYGSMP SGSPCTALLN 
      2060       2070       2080       2090       2100
SIINNVNLYY VFSKIFKKSP VFFCDAIRIL CYGDDVLIVF SRQVQFDNLD 
      2110       2120       2130       2140       2150
SIGQRIVDEF RKLGMTATSA DKSVPQLKPV SELTFLKRSF NLVDDRIRPA 
      2160       2170       2180       2190       2200
IAEKTIWSLV AWQRSNAEFE QNLENAQWFA FMHGYEFYQD FYHFVQSCLE 
      2210       2220 
KEMIEYRLKS YDWWRMKFND QCFVCDLS
Length:2,228
Mass (Da):251,802
Last modified:July 10, 2007 - 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:iC4F840E5C277FEB5
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AB279735 Genomic RNA Translation: BAF63623.1

<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
AB279735 Genomic RNA Translation: BAF63623.1

3D structure databases

BMRBiA5LGW7
ModBaseiSearch...
SWISS-MODEL-WorkspaceiSubmit a new modelling project...

Proteomic databases

PRIDEiA5LGW7

Family and domain databases

CDDicd00205, rhv_like, 2 hits
Gene3Di2.40.10.10, 2 hits
2.60.120.20, 3 hits
3.30.70.270, 1 hit
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
IPR024354, Hepatitis_A_VP1-2A
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
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
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

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_HAVJ8
<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: A5LGW7
<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: November 13, 2007
Last sequence update: July 10, 2007
Last modified: October 7, 2020
This is version 83 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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