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Entry version 158 (18 Sep 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Genome polyprotein

Gene
N/A
Organism
Hepatitis GB virus B (GBV-B) (GB virus B)
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

Core protein packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Probably also regulates many host cellular functions such as antiviral state inhibition, cell transformation and apoptosis (By similarity).By similarity
Envelope glycoproteins E1 and E2 are involved in virus attachment to the host cell as well as in virus endocytosis and fusion with host membrane.By similarity
P13 may function as a multimeric ion channel protein (viroporin).1 Publication
Protease NS2-3 is a cysteine protease responsible for the autocatalytic cleavage of NS2-NS3.By similarity
NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B (By similarity). NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction and likely RNA stable secondary structure in the template strand. Cleaves and inhibits the human antiviral protein MAVS.By similarity1 Publication
NS5A is a component of the replication complex involved in RNA-binding.By similarity
NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication.By similarity

Miscellaneous

Of all animal viruses, GBV-B is the most closely related to HCV.

Caution

The core gene probably also codes for alternative reading frame proteins (ARFPs). Many functions depicted for the core protein might belong to the ARFPs.Curated

<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

  • Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'. EC:3.4.21.98

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.64 mM for ATP for NS3 NTPase
  2. KM=1.41 mM for CTP for NS3 NTPase
  3. KM=1.12 mM for UTP for NS3 NTPase
  4. KM=1.87 mM for dATP for NS3 NTPase
  5. KM=1.22 mM for dCTP for NS3 NTPase
  6. KM=0.65 mM for dTTP for NS3 NTPase

    pH dependencei

    Stable from 6 to 8.5.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei997Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
    Active sitei1021Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1037ZincPROSITE-ProRule annotation1
    Metal bindingi1039ZincPROSITE-ProRule annotation1
    Active sitei1079Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
    Metal bindingi1085ZincPROSITE-ProRule annotation1
    Metal bindingi1089ZincPROSITE-ProRule annotation1
    Metal bindingi1905ZincBy similarity1
    Metal bindingi1923ZincBy similarity1
    Metal bindingi1925ZincBy similarity1
    Metal bindingi1947ZincBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi1144 – 1151ATPCurated8

    <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, Multifunctional enzyme, Nucleotidyltransferase, Protease, Ribonucleoprotein, RNA-binding, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase, Viral ion channel, Viral nucleoprotein
    Biological processActivation of host autophagy by virus, Apoptosis, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host MAVS by virus, Inhibition of host RLR pathway by virus, Interferon antiviral system evasion, Ion transport, Transcription, Transcription regulation, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus entry into host cell
    LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    C18.002

    <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 12 chains:
    Alternative name(s):
    NS1
    Protease NS2-3 (EC:3.4.22.-)
    Serine protease NS3 (EC:3.4.21.98, EC:3.6.1.15, EC:3.6.4.13)
    Alternative name(s):
    Hepacivirin
    NS3P
    RNA-directed RNA polymerase (EC:2.7.7.48)
    Alternative name(s):
    NS5B
    <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>OrganismiHepatitis GB virus B (GBV-B) (GB virus B)
    <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 identifieri39113 [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 lineageiVirusesRiboviriaFlaviviridaeHepacivirus
    <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 hostiCallithrix jacchus (White-tufted-ear marmoset) [TaxID: 9483]
    Saguinus [TaxID: 9486]
    <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
    • UP000172018 <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
    • UP000165726 Componenti: Genome
    • UP000114117 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

    Envelope glycoprotein E1 :
    • Virion membrane Curated; Single-pass type I membrane protein Curated
    • Host endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity
    • Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein (By similarity).By similarity
    Envelope glycoprotein E2 :
    • Virion membrane Curated; Single-pass type I membrane protein Curated
    • Host endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity
    • Note: The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor. A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain. These events explain the final topology of the protein (By similarity).By similarity
    Serine protease NS3 :
    Non-structural protein 5A :
    RNA-directed RNA polymerase :

    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>Transmembranei133 – 153HelicalSequence analysisAdd BLAST21
    Transmembranei324 – 344HelicalSequence analysisAdd BLAST21
    Transmembranei582 – 602HelicalSequence analysisAdd BLAST21
    Transmembranei628 – 648HelicalSequence analysisAdd BLAST21
    Transmembranei660 – 680HelicalSequence analysisAdd BLAST21
    Transmembranei706 – 726HelicalSequence analysisAdd BLAST21
    Transmembranei737 – 757HelicalSequence analysisAdd BLAST21
    Transmembranei790 – 810HelicalSequence analysisAdd BLAST21
    Transmembranei847 – 867HelicalSequence analysisAdd BLAST21
    Transmembranei1565 – 1585HelicalSequence analysisAdd BLAST21
    Transmembranei1653 – 1673HelicalSequence analysisAdd BLAST21
    Transmembranei1678 – 1698HelicalSequence analysisAdd BLAST21
    Transmembranei1722 – 1742HelicalSequence analysisAdd BLAST21
    Transmembranei1783 – 1803HelicalSequence analysisAdd BLAST21
    Transmembranei1864 – 1884HelicalSequence analysisAdd BLAST21
    Transmembranei2844 – 2864HelicalSequence analysisAdd BLAST21

    GO - Cellular componenti

    Keywords - Cellular componenti

    Capsid protein, Host endoplasmic reticulum, Host membrane, Membrane, Viral envelope 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_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>Mutagenesisi613G → A: Reduces cleavage between E2 and p13. 1 Publication1
    Mutagenesisi669G → N: Reduces cleavage between E2 and p13. 1 Publication1
    Mutagenesisi730 – 732ASA → NSN: Reduces cleavage between p13 and NS2-3. 1 Publication3
    Mutagenesisi1150K → A: Complete loss of ATPase and dsRNA unwinding activities. 1 Publication1

    Keywords - Diseasei

    Oncogene

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5981

    <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_00000376781 – 156Core proteinSequence analysisAdd BLAST156
    ChainiPRO_0000037679157 – 349Envelope glycoprotein E1Add BLAST193
    ChainiPRO_0000037680350 – 613Envelope glycoprotein E2Add BLAST264
    ChainiPRO_0000037681614 – 732p13CuratedAdd BLAST119
    ChainiPRO_0000284104614 – 669p6Sequence analysisAdd BLAST56
    ChainiPRO_0000284105670 – 732p7Sequence analysisAdd BLAST63
    ChainiPRO_0000037682733 – 940Protease NS2-3PROSITE-ProRule annotationAdd BLAST208
    ChainiPRO_0000037683941 – 1564Serine protease NS3Sequence analysisAdd BLAST624
    ChainiPRO_00000376841565 – 1615Non-structural protein 4ASequence analysisAdd BLAST51
    ChainiPRO_00000376851616 – 1863Non-structural protein 4BSequence analysisAdd BLAST248
    ChainiPRO_00000376861864 – 2274Non-structural protein 5ASequence analysisAdd BLAST411
    ChainiPRO_00000376872275 – 2864RNA-directed RNA polymeraseSequence analysisAdd BLAST590

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi165N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi212N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi264N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi380N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi400N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi422N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi446N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi467N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi512N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi782N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi1057N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi1273N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi1559N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Lipidationi1863S-palmitoyl cysteine; by hostBy similarity1
    Glycosylationi2640N-linked (GlcNAc...) asparagine; by hostSequence analysis1
    Glycosylationi2722N-linked (GlcNAc...) asparagine; by hostSequence analysis1

    <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

    Specific enzymatic cleavages in vivo yield mature proteins. P13 may be further cleaved into p6 and p7 if the internal cleavage site is used.2 Publications
    Envelope E1 and E2 glycoproteins are highly N-glycosylated.
    NS5A is phosphorylated in a basal form termed p56. p58 is a hyperphosphorylated form of p56. p56 and p58 coexist in the cell in roughly equivalent amounts. Hyperphosphorylation is dependent on the presence of NS4A. Human AKT1, RPS6KB1/p70S6K, MAP2K1/MEK1, MAP2K6/MKK6 and CSNK1A1/CKI-alpha kinases may be responsible for NS5A phosphorylation (By similarity).By similarity
    NS4B is palmitoylated. This modification may play a role in its polymerization or in protein-protein interactions (By similarity).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>Sitei156 – 157Cleavage; by host signal peptidaseSequence analysis2
    Sitei349 – 350Cleavage; by host signal peptidaseCurated2
    Sitei613 – 614Cleavage; by host signal peptidaseCurated2
    Sitei669 – 670Cleavage; by host signal peptidaseSequence analysis2
    Sitei732 – 733Cleavage; by host signal peptidaseCurated2
    Sitei940 – 941Cleavage; by protease NS2-3PROSITE-ProRule annotation2
    Sitei?1564 – ?1565Cleavage; by serine protease NS3Sequence analysis2
    Sitei1615 – 1616Cleavage; by serine protease NS3Sequence analysis2
    Sitei1863 – 1864Cleavage; by serine protease NS3Sequence analysis2
    Sitei2274 – 2275Cleavage; by serine protease NS3Sequence analysis2

    Keywords - PTMi

    Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q69422

    <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

    NS4A interacts with NS3 serine protease and stabilizes its folding. NS3-NS4A complex is essential for the activation of the latter and allows membrane anchorage of NS3. NS3 interacts with human MAVS (Probable).

    1 Publication

    GO - Molecular functioni

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q69422

    <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

    12864
    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
    Q69422

    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_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>Domaini819 – 940Peptidase C18PROSITE-ProRule annotationAdd BLAST122
    Domaini941 – 1122Peptidase S29PROSITE-ProRule annotationAdd BLAST182
    Domaini1131 – 1281Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST151
    Domaini1284 – 1449Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
    Domaini2485 – 2603RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

    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>Motifi1228 – 1231DECH box4

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi172 – 199Cys-richAdd BLAST28
    Compositional biasi677 – 681Poly-Ala5
    Compositional biasi2145 – 2186Pro-richAdd BLAST42
    Compositional biasi2232 – 2235Poly-Thr4

    <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 N-terminal one-third of serine protease NS3 contains the protease activity. This region contains a zinc atom that does not belong to the active site, but may play a structural rather than a catalytic role. This region is essential for the activity of protease NS2-3, maybe by contributing to the folding of the latter. The helicase activity is located in the C-terminus of NS3 (By similarity).By similarity

    Keywords - Domaini

    SH3-binding, Transmembrane, Transmembrane helix

    Phylogenomic databases

    Database of Orthologous Groups

    More...
    OrthoDBi
    754at10239

    Family and domain databases

    Database of protein disorder

    More...
    DisProti
    DP00674

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.20.25.210, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011492 DEAD_Flavivir
    IPR002521 HCV_core_C
    IPR002519 HCV_env
    IPR002518 HCV_NS2
    IPR000745 HCV_NS4a
    IPR001490 HCV_NS4b
    IPR002868 HCV_NS5a
    IPR013193 HCV_NS5a_1B_dom
    IPR014001 Helicase_ATP-bd
    IPR001650 Helicase_C
    IPR013192 NS5A_1a
    IPR038170 NS5A_1a_sf
    IPR027417 P-loop_NTPase
    IPR009003 Peptidase_S1_PA
    IPR004109 Peptidase_S29_NS3
    IPR007094 RNA-dir_pol_PSvirus
    IPR002166 RNA_pol_HCV

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF07652 Flavi_DEAD, 1 hit
    PF01542 HCV_core, 1 hit
    PF01539 HCV_env, 1 hit
    PF01538 HCV_NS2, 1 hit
    PF01006 HCV_NS4a, 1 hit
    PF01001 HCV_NS4b, 1 hit
    PF01506 HCV_NS5a, 1 hit
    PF08300 HCV_NS5a_1a, 1 hit
    PF08301 HCV_NS5a_1b, 1 hit
    PF02907 Peptidase_S29, 1 hit
    PF00998 RdRP_3, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00487 DEXDc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50494 SSF50494, 1 hit
    SSF52540 SSF52540, 2 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51693 HCV_NS2_PRO, 1 hit
    PS51192 HELICASE_ATP_BIND_1, 1 hit
    PS51194 HELICASE_CTER, 1 hit
    PS51822 HV_PV_NS3_PRO, 1 hit
    PS50507 RDRP_SSRNA_POS, 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>. 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_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.

    Q69422-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPVISTQTSP VPAPRTRKNK QTQASYPVSI KTSVERGQRA KRKVQRDARP
    60 70 80 90 100
    RNYKIAGIHD GLQTLAQAAL PAHGWGRQDP RHKSRNLGIL LDYPLGWIGD
    110 120 130 140 150
    VTTHTPLVGP LVAGAVVRPV CQIVRLLEDG VNWATGWFGV HLFVVCLLSL
    160 170 180 190 200
    ACPCSGARVT DPDTNTTILT NCCQRNQVIY CSPSTCLHEP GCVICADECW
    210 220 230 240 250
    VPANPYISHP SNWTGTDSFL ADHIDFVMGA LVTCDALDIG ELCGACVLVG
    260 270 280 290 300
    DWLVRHWLIH IDLNETGTCY LEVPTGIDPG FLGFIGWMAG KVEAVIFLTK
    310 320 330 340 350
    LASQVPYAIA TMFSSVHYLA VGALIYYASR GKWYQLLLAL MLYIEATSGN
    360 370 380 390 400
    PIRVPTGCSI AEFCSPLMIP CPCHSYLSEN VSEVICYSPK WTRPVTLEYN
    410 420 430 440 450
    NSISWYPYTI PGARGCMVKF KNNTWGCCRI RNVPSYCTMG TDAVWNDTRN
    460 470 480 490 500
    TYEACGVTPW LTTAWHNGSA LKLAILQYPG SKEMFKPHNW MSGHLYFEGS
    510 520 530 540 550
    DTPIVYFYDP VNSTLLPPER WARLPGTPPV VRGSWLQVPQ GFYSDVKDLA
    560 570 580 590 600
    TGLITKDKAW KNYQVLYSAT GALSLTGVTT KAVVLILLGL CGSKYLILAY
    610 620 630 640 650
    LCYLSLCFGR ASGYPLRPVL PSQSYLQAGW DVLSKAQVAP FALIFFICCY
    660 670 680 690 700
    LRCRLRYAAL LGFVPMAAGL PLTFFVAAAA AQPDYDWWVR LLVAGLVLWA
    710 720 730 740 750
    GRDRGPRIAL LVGPWPLVAL LTLLHLATPA SAFDTEIIGG LTIPPVVALV
    760 770 780 790 800
    VMSRFGFFAH LLPRCALVNS YLWQRWENWF WNVTLRPERF LLVLVCFPGA
    810 820 830 840 850
    TYDTLVTFCV CHVALLCLTS SAASFFGTDS RVRAHRMLVR LGKCHAWYSH
    860 870 880 890 900
    YVLKFFLLVF GENGVFFYKH LHGDVLPNDF ASKLPLQEPF FPFEGKARVY
    910 920 930 940 950
    RNEGRRLACG DTVDGLPVVA RLGDLVFAGL AMPPDGWAIT APFTLQCLSE
    960 970 980 990 1000
    RGTLSAMAVV MTGIDPRTWT GTIFRLGSLA TSYMGFVCDN VLYTAHHGSK
    1010 1020 1030 1040 1050
    GRRLAHPTGS IHPITVDAAN DQDIYQPPCG AGSLTRCSCG ETKGYLVTRL
    1060 1070 1080 1090 1100
    GSLVEVNKSD DPYWCVCGAL PMAVAKGSSG APILCSSGHV IGMFTAARNS
    1110 1120 1130 1140 1150
    GGSVSQIRVR PLVCAGYHPQ YTAHATLDTK PTVPNEYSVQ ILIAPTGSGK
    1160 1170 1180 1190 1200
    STKLPLSYMQ EKYEVLVLNP SVATTASMPK YMHATYGVNP NCYFNGKCTN
    1210 1220 1230 1240 1250
    TGASLTYSTY GMYLTGACSR NYDVIICDEC HATDATTVLG IGKVLTEAPS
    1260 1270 1280 1290 1300
    KNVRLVVLAT ATPPGVIPTP HANITEIQLT DEGTIPFHGK KIKEENLKKG
    1310 1320 1330 1340 1350
    RHLIFEATKK HCDELANELA RKGITAVSYY RGCDISKIPE GDCVVVATDA
    1360 1370 1380 1390 1400
    LCTGYTGDFD SVYDCSLMVE GTCHVDLDPT FTMGVRVCGV SAIVKGQRRG
    1410 1420 1430 1440 1450
    RTGRGRAGIY YYVDGSCTPS GMVPECNIVE AFDAAKAWYG LSSTEAQTIL
    1460 1470 1480 1490 1500
    DTYRTQPGLP AIGANLDEWA DLFSMVNPEP SFVNTAKRTA DNYVLLTAAQ
    1510 1520 1530 1540 1550
    LQLCHQYGYA APNDAPRWQG ARLGKKPCGV LWRLDGADAC PGPEPSEVTR
    1560 1570 1580 1590 1600
    YQMCFTEVNT SGTAALAVGV GVAMAYLAID TFGATCVRRC WSITSVPTGA
    1610 1620 1630 1640 1650
    TVAPVVDEEE IVEECASFIP LEAMVAAIDK LKSTITTTSP FTLETALEKL
    1660 1670 1680 1690 1700
    NTFLGPHAAT ILAIIEYCCG LVTLPDNPFA SCVFAFIAGI TTPLPHKIKM
    1710 1720 1730 1740 1750
    FLSLFGGAIA SKLTDARGAL AFMMAGAAGT ALGTWTSVGF VFDMLGGYAA
    1760 1770 1780 1790 1800
    ASSTACLTFK CLMGEWPTMD QLAGLVYSAF NPAAGVVGVL SACAMFALTT
    1810 1820 1830 1840 1850
    AGPDHWPNRL LTMLARSNTV CNEYFIATRD IRRKILGILE ASTPWSVISA
    1860 1870 1880 1890 1900
    CIRWLHTPTE DDCGLIAWGL EIWQYVCNFF VICFNVLKAG VQSMVNIPGC
    1910 1920 1930 1940 1950
    PFYSCQKGYK GPWIGSGMLQ ARCPCGAELI FSVENGFAKL YKGPRTCSNY
    1960 1970 1980 1990 2000
    WRGAVPVNAR LCGSARPDPT DWTSLVVNYG VRDYCKYEKL GDHIFVTAVS
    2010 2020 2030 2040 2050
    SPNVCFTQVP PTLRAAVAVD GVQVQCYLGE PKTPWTTSAC CYGPDGKGKT
    2060 2070 2080 2090 2100
    VKLPFRVDGH TPGVRMQLNL RDALETNDCN SINNTPSDEA AVSALVFKQE
    2110 2120 2130 2140 2150
    LRRTNQLLEA ISAGVDTTKL PAPSIEEVVV RKRQFRARTG SLTLPPPPRS
    2160 2170 2180 2190 2200
    VPGVSCPESL QRSDPLEGPS NLPSSPPVLQ LAMPMPLLGA GECNPFTAIG
    2210 2220 2230 2240 2250
    CAMTETGGGP DDLPSYPPKK EVSEWSDGSW STTTTASSYV TGPPYPKIRG
    2260 2270 2280 2290 2300
    KDSTQSAPAK RPTKKKLGKS EFSCSMSYTW TDVISFKTAS KVLSATRAIT
    2310 2320 2330 2340 2350
    SGFLKQRSLV YVTEPRDAEL RKQKVTINRQ PLFPPSYHKQ VRLAKEKASK
    2360 2370 2380 2390 2400
    VVGVMWDYDE VAAHTPSKSA KSHITGLRGT DVRSGAARKA VLDLQKCVEA
    2410 2420 2430 2440 2450
    GEIPSHYRQT VIVPKEEVFV KTPQKPTKKP PRLISYPHLE MRCVEKMYYG
    2460 2470 2480 2490 2500
    QVAPDVVKAV MGDAYGFVDP RTRVKRLLSM WSPDAVGATC DTVCFDSTIT
    2510 2520 2530 2540 2550
    PEDIMVETDI YSAAKLSDQH RAGIHTIARQ LYAGGPMIAY DGREIGYRRC
    2560 2570 2580 2590 2600
    RSSGVYTTSS SNSLTCWLKV NAAAEQAGMK NPRFLICGDD CTVIWKSAGA
    2610 2620 2630 2640 2650
    DADKQAMRVF ASWMKVMGAP QDCVPQPKYS LEELTSCSSN VTSGITKSGK
    2660 2670 2680 2690 2700
    PYYFLTRDPR IPLGRCSAEG LGYNPSAAWI GYLIHHYPCL WVSRVLAVHF
    2710 2720 2730 2740 2750
    MEQMLFEDKL PETVTFDWYG KNYTVPVEDL PSIIAGVHGI EAFSVVRYTN
    2760 2770 2780 2790 2800
    AEILRVSQSL TDMTMPPLRA WRKKARAVLA SAKRRGGAHA KLARFLLWHA
    2810 2820 2830 2840 2850
    TSRPLPDLDK TSVARYTTFN YCDVYSPEGD VFVTPQRRLQ KFLVKYLAVI
    2860
    VFALGLIAVG LAIS
    Length:2,864
    Mass (Da):312,705
    Last modified:November 1, 1996 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5F5A7D8FAF0CDE81
    GO

    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 varianti395V → I. 1
    Natural varianti703D → N. 1
    Natural varianti706P → H. 1
    Natural varianti727A → V. 1
    Natural varianti791L → F. 1
    Natural varianti804T → A. 1
    Natural varianti940T → M. 1
    Natural varianti1879F → L. 1
    Natural varianti1895V → A. 1
    Natural varianti1919L → P. 1
    Natural varianti1945R → K. 1
    Natural varianti1966R → G. 1
    Natural varianti1973T → P. 1
    Natural varianti1979Y → C. 1
    Natural varianti1990L → M. 1
    Natural varianti2052K → Q. 1
    Natural varianti2082I → T. 1
    Natural varianti2095L → P. 1
    Natural varianti2097F → I. 1
    Natural varianti2174S → P. 1
    Natural varianti2196F → L. 1
    Natural varianti2201C → R. 1
    Natural varianti2203M → V. 1
    Natural varianti2221E → G. 1
    Natural varianti2228G → E. 1
    Natural varianti2233T → A. 1
    Natural varianti2244P → L. 1
    Natural varianti2268G → E. 1
    Natural varianti2271E → K. 1
    Natural varianti2833V → I. 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
    U22304 Genomic RNA Translation: AAC54059.1
    AF179612 Genomic RNA Translation: AAF01368.1
    AJ277947 Genomic RNA Translation: CAC33083.1
    AJ428955 Genomic RNA Translation: CAD21957.1
    AY534873 Genomic RNA Translation: AAS45125.1
    AY534874 Genomic RNA Translation: AAS45126.1
    AY534875 Genomic RNA Translation: AAS45127.1
    AY534876 Genomic RNA Translation: AAS45128.1
    AY534877 Genomic RNA Translation: AAS45129.1
    AY534878 Genomic RNA Translation: AAS45130.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_056931.1, NC_001655.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1403460

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    vg:1403460

    <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
    U22304 Genomic RNA Translation: AAC54059.1
    AF179612 Genomic RNA Translation: AAF01368.1
    AJ277947 Genomic RNA Translation: CAC33083.1
    AJ428955 Genomic RNA Translation: CAD21957.1
    AY534873 Genomic RNA Translation: AAS45125.1
    AY534874 Genomic RNA Translation: AAS45126.1
    AY534875 Genomic RNA Translation: AAS45127.1
    AY534876 Genomic RNA Translation: AAS45128.1
    AY534877 Genomic RNA Translation: AAS45129.1
    AY534878 Genomic RNA Translation: AAS45130.1
    RefSeqiNP_056931.1, NC_001655.1

    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
    2LZPNMR-A734-764[»]
    2LZQNMR-A764-789[»]
    2MKBNMR-A845-869[»]
    SMRiQ69422
    ModBaseiSearch...
    PDBe-KBiSearch...

    Chemistry databases

    BindingDBiQ69422
    ChEMBLiCHEMBL5981

    Protein family/group databases

    MEROPSiC18.002

    Proteomic databases

    PRIDEiQ69422

    Genome annotation databases

    GeneIDi1403460
    KEGGivg:1403460

    Phylogenomic databases

    OrthoDBi754at10239

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:Q69422

    Family and domain databases

    DisProtiDP00674
    Gene3Di2.20.25.210, 1 hit
    InterProiView protein in InterPro
    IPR011492 DEAD_Flavivir
    IPR002521 HCV_core_C
    IPR002519 HCV_env
    IPR002518 HCV_NS2
    IPR000745 HCV_NS4a
    IPR001490 HCV_NS4b
    IPR002868 HCV_NS5a
    IPR013193 HCV_NS5a_1B_dom
    IPR014001 Helicase_ATP-bd
    IPR001650 Helicase_C
    IPR013192 NS5A_1a
    IPR038170 NS5A_1a_sf
    IPR027417 P-loop_NTPase
    IPR009003 Peptidase_S1_PA
    IPR004109 Peptidase_S29_NS3
    IPR007094 RNA-dir_pol_PSvirus
    IPR002166 RNA_pol_HCV
    PfamiView protein in Pfam
    PF07652 Flavi_DEAD, 1 hit
    PF01542 HCV_core, 1 hit
    PF01539 HCV_env, 1 hit
    PF01538 HCV_NS2, 1 hit
    PF01006 HCV_NS4a, 1 hit
    PF01001 HCV_NS4b, 1 hit
    PF01506 HCV_NS5a, 1 hit
    PF08300 HCV_NS5a_1a, 1 hit
    PF08301 HCV_NS5a_1b, 1 hit
    PF02907 Peptidase_S29, 1 hit
    PF00998 RdRP_3, 1 hit
    SMARTiView protein in SMART
    SM00487 DEXDc, 1 hit
    SUPFAMiSSF50494 SSF50494, 1 hit
    SSF52540 SSF52540, 2 hits
    PROSITEiView protein in PROSITE
    PS51693 HCV_NS2_PRO, 1 hit
    PS51192 HELICASE_ATP_BIND_1, 1 hit
    PS51194 HELICASE_CTER, 1 hit
    PS51822 HV_PV_NS3_PRO, 1 hit
    PS50507 RDRP_SSRNA_POS, 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_GBVB
    <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: Q69422
    Secondary accession number(s): Q6QLR5
    , Q6QLR6, Q6QLR7, Q6QLR8, Q6QLR9, Q6QLS0, Q8JKE4, Q999T0, Q9QEW5
    <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: July 5, 2005
    Last sequence update: November 1, 1996
    Last modified: September 18, 2019
    This is version 158 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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    UniProt is an ELIXIR core data resource
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