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Entry version 128 (07 Oct 2020)
Sequence version 1 (06 Dec 2005)
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Protein

Genome polyprotein

Gene
N/A
Organism
Kokobera virus (KOKV)
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

Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.By similarity
Inhibits RNA silencing by interfering with host Dicer.By similarity
Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.By similarity
Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.By similarity
Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).By similarity
Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response.By similarity
Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy similarity
displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (PubMed:18004778).PROSITE-ProRule annotation1 Publication
Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.By similarity
Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.By similarity
Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.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 hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala. EC:3.4.21.91

<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=340 mM for ATPase of serine protease NS31 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1543Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
    Active sitei1567Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
    Active sitei1627Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
    <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>Sitei1692Substrate binding1 Publication1
    Sitei1947Involved in NS3 ATPase and RTPase activitiesBy similarity1
    Sitei1950Involved in NS3 ATPase and RTPase activitiesBy similarity1
    Sitei1950Substrate binding1 Publication1
    Sitei1953Substrate binding1 Publication1
    Sitei2520mRNA cap bindingPROSITE-ProRule annotation1
    Sitei2523mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
    Sitei2524mRNA cap bindingPROSITE-ProRule annotation1
    Sitei2526mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
    Sitei2531mRNA cap bindingPROSITE-ProRule annotation1
    Sitei2535mRNA cap bindingPROSITE-ProRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei2563S-adenosyl-L-methioninePROSITE-ProRule annotation1
    Active sitei2568For 2'-O-MTase activityBy similarity1
    Sitei2568Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
    Binding sitei2593S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
    Binding sitei2594S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
    Binding sitei2611S-adenosyl-L-methioninePROSITE-ProRule annotation1
    Binding sitei2612S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
    Binding sitei2638S-adenosyl-L-methioninePROSITE-ProRule annotation1
    Binding sitei2639S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
    Active sitei2653For 2'-O-MTase activityBy similarity1
    Sitei2653Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
    Binding sitei2654S-adenosyl-L-methioninePROSITE-ProRule annotation1
    Active sitei2690For 2'-O-MTase activityBy similarity1
    Sitei2690Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
    Sitei2721mRNA cap bindingPROSITE-ProRule annotation1
    Sitei2723mRNA cap bindingPROSITE-ProRule annotation1
    Active sitei2726For 2'-O-MTase activityBy similarity1
    Sitei2726Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
    Binding sitei2728S-adenosyl-L-methioninePROSITE-ProRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi2947Zinc 1By similarity1
    Metal bindingi2951Zinc 1; via tele nitrogenBy similarity1
    Metal bindingi2956Zinc 1By similarity1
    Metal bindingi2959Zinc 1By similarity1
    Metal bindingi3222Zinc 2; via tele nitrogenBy similarity1
    Metal bindingi3238Zinc 2By similarity1
    Metal bindingi3356Zinc 2By similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1686 – 1693ATPPROSITE-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, Methyltransferase, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase
    Biological processActivation of host autophagy by virus, 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 STAT1 by virus, Inhibition of host STAT2 by virus, mRNA capping, mRNA processing, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus entry into host cell
    LigandATP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    S07.001

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 13 chains:
    Alternative name(s):
    Core protein
    Alternative name(s):
    Matrix protein
    Alternative name(s):
    Flavivirin protease NS2B regulatory subunit
    Non-structural protein 2B
    Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.151 Publication, EC:3.6.4.131 Publication)
    Alternative name(s):
    Flavivirin protease NS3 catalytic subunit
    Non-structural protein 3
    RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
    Alternative name(s):
    NS5
    <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>OrganismiKokobera virus (KOKV)
    <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 identifieri44024 [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 lineageiVirusesRiboviriaOrthornaviraeKitrinoviricotaFlasuviricetesAmarilloviralesFlaviviridaeFlavivirus
    <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 hostiCulex annulirostris (Common banded mosquito) [TaxID: 162997]
    Homo sapiens (Human) [TaxID: 9606]
    Ochlerotatus camptorhynchus [TaxID: 644619]
    Ochlerotatus vigilax [TaxID: 569589]
    <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
    • UP000124420 <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

    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 subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 103CytoplasmicSequence analysisAdd BLAST103
    <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>Transmembranei104 – 124HelicalSequence analysisAdd BLAST21
    Topological domaini125 – 245ExtracellularSequence analysisAdd BLAST121
    Transmembranei246 – 266HelicalSequence analysisAdd BLAST21
    Topological domaini267 – 271CytoplasmicSequence analysis5
    Transmembranei272 – 286HelicalCuratedAdd BLAST15
    Topological domaini287 – 739ExtracellularSequence analysisAdd BLAST453
    Transmembranei740 – 760HelicalSequence analysisAdd BLAST21
    Topological domaini761 – 766CytoplasmicSequence analysis6
    Transmembranei767 – 787HelicalSequence analysisAdd BLAST21
    Topological domaini788 – 1165ExtracellularSequence analysisAdd BLAST378
    Transmembranei1166 – 1186HelicalSequence analysisAdd BLAST21
    Topological domaini1187 – 1214CytoplasmicSequence analysisAdd BLAST28
    Transmembranei1215 – 1235HelicalSequence analysisAdd BLAST21
    Topological domaini1236 – 1242LumenalSequence analysis7
    Transmembranei1243 – 1263HelicalSequence analysisAdd BLAST21
    Topological domaini1264 – 1284CytoplasmicSequence analysisAdd BLAST21
    Transmembranei1285 – 1305HelicalSequence analysisAdd BLAST21
    Topological domaini1306 – 1335LumenalSequence analysisAdd BLAST30
    Transmembranei1336 – 1356HelicalSequence analysisAdd BLAST21
    Topological domaini1357 – 1363CytoplasmicSequence analysis7
    Transmembranei1364 – 1384HelicalSequence analysisAdd BLAST21
    Topological domaini1385 – 1387LumenalSequence analysis3
    Transmembranei1388 – 1408HelicalSequence analysisAdd BLAST21
    Topological domaini1409 – 1464CytoplasmicSequence analysisAdd BLAST56
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1465 – 1485HelicalSequence analysisAdd BLAST21
    Topological domaini1486 – 2158CytoplasmicSequence analysisAdd BLAST673
    Transmembranei2159 – 2179HelicalSequence analysisAdd BLAST21
    Topological domaini2180 – 2185LumenalSequence analysis6
    Intramembranei2186 – 2205HelicalSequence analysisAdd BLAST20
    Topological domaini2206LumenalSequence analysis1
    Transmembranei2207 – 2227HelicalSequence analysisAdd BLAST21
    Topological domaini2228 – 2242CytoplasmicSequence analysisAdd BLAST15
    Transmembranei2243 – 2257Helical; Note=Signal for NS4BCuratedAdd BLAST15
    Topological domaini2258 – 2293LumenalSequence analysisAdd BLAST36
    Intramembranei2294 – 2314HelicalSequence analysisAdd BLAST21
    Topological domaini2315 – 2336LumenalSequence analysisAdd BLAST22
    Transmembranei2337 – 2357HelicalSequence analysisAdd BLAST21
    Topological domaini2358CytoplasmicSequence analysis1
    Transmembranei2359 – 2379HelicalSequence analysisAdd BLAST21
    Topological domaini2380 – 2420LumenalSequence analysisAdd BLAST41
    Transmembranei2421 – 2441HelicalSequence analysisAdd BLAST21
    Topological domaini2442 – 3410CytoplasmicSequence analysisAdd BLAST969

    GO - Cellular componenti

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Host endoplasmic reticulum, Host membrane, Host nucleus, Membrane, Secreted, Virion

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1724M → T: Severe decrease in helicase activity. 1 Publication1

    <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_00004415161 – 3410Genome polyproteinAdd BLAST3410
    ChainiPRO_00004415171 – 102Capsid protein CBy similarityAdd BLAST102
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000441518103 – 119ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST17
    ChainiPRO_0000441519120 – 286Protein prMBy similarityAdd BLAST167
    ChainiPRO_0000441520120 – 211Peptide prBy similarityAdd BLAST92
    ChainiPRO_0000441521212 – 286Small envelope protein MBy similarityAdd BLAST75
    ChainiPRO_0000441522287 – 787Envelope protein EBy similarityAdd BLAST501
    ChainiPRO_0000441523788 – 1138Non-structural protein 1By similarityAdd BLAST351
    ChainiPRO_00004415241139 – 1362Non-structural protein 2ABy similarityAdd BLAST224
    ChainiPRO_00004415251363 – 1492Serine protease subunit NS2BBy similarityAdd BLAST130
    ChainiPRO_00004415261493 – 2108Serine protease NS3By similarityAdd BLAST616
    ChainiPRO_00004415272109 – 2234Non-structural protein 4ABy similarityAdd BLAST126
    <p>This subsection of the 'PTM / Processing' section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_00004415282235 – 2257Peptide 2kBy similarityAdd BLAST23
    ChainiPRO_00004415292258 – 2507Non-structural protein 4BBy similarityAdd BLAST250
    ChainiPRO_00004415302508 – 3410RNA-directed RNA polymerase NS5By similarityAdd BLAST903

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bondi289 ↔ 316By similarity
    Disulfide bondi346 ↔ 407By similarity
    Disulfide bondi346 ↔ 402By similarity
    Disulfide bondi360 ↔ 391By similarity
    Disulfide bondi378 ↔ 407By similarity
    Disulfide bondi378 ↔ 402By similarity
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi440N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
    Disulfide bondi476 ↔ 574By similarity
    Disulfide bondi591 ↔ 622By similarity
    Disulfide bondi791 ↔ 802By similarity
    Disulfide bondi842 ↔ 928By similarity
    Glycosylationi915N-linked (GlcNAc...) asparagine; by hostBy similarity1
    Disulfide bondi964 ↔ 1009By similarity
    Disulfide bondi1066 ↔ 1115By similarity
    Disulfide bondi1077 ↔ 1099By similarity
    Disulfide bondi1077 ↔ 1098By similarity
    Disulfide bondi1098 ↔ 1102By similarity
    Disulfide bondi1099 ↔ 1102By similarity
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2563PhosphoserineBy similarity1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
    Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.By similarity
    N-glycosylated.By similarity
    N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.By similarity
    Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei102 – 103Cleavage; by viral protease NS3By similarity2
    Sitei121 – 122Cleavage; by host signal peptidaseBy similarity2
    Sitei211 – 212Cleavage; by host furinBy similarity2
    Sitei286 – 287Cleavage; by host signal peptidaseBy similarity2
    Sitei787 – 788Cleavage; by host signal peptidaseBy similarity2
    Sitei1138 – 1139Cleavage; by hostBy similarity2
    Sitei1362 – 1363Cleavage; by viral protease NS3By similarity2
    Sitei1492 – 1493Cleavage; by autolysisBy similarity2
    Sitei2108 – 2109Cleavage; by autolysisBy similarity2
    Sitei2234 – 2235Cleavage; by viral protease NS3By similarity2
    Sitei2257 – 2258Cleavage; by host signal peptidaseSequence analysis2
    Sitei2507 – 2508Cleavage; by viral protease NS3By similarity2

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

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

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

    Homodimer (By similarity).

    Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway (By similarity).

    By similarity

    Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi.

    By similarity

    Homodimer; in the endoplasmic reticulum and Golgi (By similarity).

    Interacts with protein prM (By similarity).

    Interacts with non-structural protein 1 (By similarity).

    By similarity

    Homodimer; Homohexamer when secreted (By similarity).

    Interacts with envelope protein E (By similarity). NS1 interacts with NS4B (By similarity).

    Interacts with host complement protein CFH; this interaction leads to the degradation of C3 (By similarity).

    By similarity

    Interacts (via N-terminus) with serine protease NS3.

    By similarity

    Forms a heterodimer with serine protease NS3 (By similarity). May form homooligomers (By similarity).

    By similarity

    Forms a heterodimer with NS2B (By similarity).

    Interacts with non-structural protein 2A (via N-terminus) (By similarity).

    Interacts with NS4B (By similarity).

    Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity).

    By similarity

    Interacts with serine protease NS3 (By similarity).

    By similarity

    Homodimer (By similarity).

    Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation (By similarity).

    By similarity

    GO - Molecular functioni

    <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

    13410
    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
    Q32ZD5

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q32ZD5

    <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>Domaini1493 – 1670Peptidase S7PROSITE-ProRule annotationAdd BLAST178
    Domaini1673 – 1829Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
    Domaini1839 – 2006Helicase C-terminalPROSITE-ProRule annotationAdd BLAST168
    Domaini2508 – 2773mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
    Domaini3036 – 3187RdRp catalyticPROSITE-ProRule annotationAdd BLAST152

    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>Regioni2 – 15Interaction with host EXOC1By similarityAdd BLAST14
    Regioni38 – 73Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
    Regioni384 – 397Fusion peptideBy similarityAdd BLAST14
    Regioni1415 – 1454Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
    Regioni1677 – 1680Important for RNA-bindingBy similarity4
    Regioni2153 – 2157Regulates the ATPase activity of NS3 helicaseBy similarity5

    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>Motifi1777 – 1780DEAH boxPROSITE-ProRule annotation4

    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 biasi1086 – 1089Poly-ThrSequence analysis4

    <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 transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.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

    In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd12149, Flavi_E_C, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.10.930, 1 hit
    1.10.8.970, 1 hit
    1.20.1280.260, 1 hit
    2.40.10.10, 1 hit
    2.60.260.50, 1 hit
    2.60.40.350, 1 hit
    2.60.98.10, 1 hit
    3.30.387.10, 1 hit
    3.30.67.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011492, DEAD_Flavivir
    IPR043502, DNA/RNA_pol_sf
    IPR000069, Env_glycoprot_M_flavivir
    IPR038302, Env_glycoprot_M_sf_flavivir
    IPR013755, Flav_gly_cen_dom_subdom1
    IPR001122, Flavi_capsidC
    IPR037172, Flavi_capsidC_sf
    IPR027287, Flavi_E_Ig-like
    IPR026470, Flavi_E_Stem/Anchor_dom
    IPR038345, Flavi_E_Stem/Anchor_dom_sf
    IPR001157, Flavi_NS1
    IPR000752, Flavi_NS2A
    IPR000487, Flavi_NS2B
    IPR000404, Flavi_NS4A
    IPR001528, Flavi_NS4B
    IPR002535, Flavi_propep
    IPR038688, Flavi_propep_sf
    IPR000336, Flavivir/Alphavir_Ig-like_sf
    IPR001850, Flavivirus_NS3_S7
    IPR014412, Gen_Poly_FLV
    IPR011998, Glycoprot_cen/dimer
    IPR036253, Glycoprot_cen/dimer_sf
    IPR038055, Glycoprot_E_dimer_dom
    IPR013756, GlyE_cen_dom_subdom2
    IPR014001, Helicase_ATP-bd
    IPR001650, Helicase_C
    IPR014756, Ig_E-set
    IPR026490, mRNA_cap_0/1_MeTrfase
    IPR027417, P-loop_NTPase
    IPR009003, Peptidase_S1_PA
    IPR043504, Peptidase_S1_PA_chymotrypsin
    IPR000208, RNA-dir_pol_flavivirus
    IPR007094, RNA-dir_pol_PSvirus
    IPR002877, rRNA_MeTrfase_FtsJ_dom
    IPR029063, SAM-dependent_MTases

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01003, Flavi_capsid, 1 hit
    PF07652, Flavi_DEAD, 1 hit
    PF02832, Flavi_glycop_C, 1 hit
    PF00869, Flavi_glycoprot, 1 hit
    PF01004, Flavi_M, 1 hit
    PF00948, Flavi_NS1, 1 hit
    PF01005, Flavi_NS2A, 1 hit
    PF01002, Flavi_NS2B, 1 hit
    PF01350, Flavi_NS4A, 1 hit
    PF01349, Flavi_NS4B, 1 hit
    PF00972, Flavi_NS5, 1 hit
    PF01570, Flavi_propep, 1 hit
    PF01728, FtsJ, 1 hit
    PF00949, Peptidase_S7, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF003817, Gen_Poly_FLV, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00487, DEXDc, 1 hit
    SM00490, HELICc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF101257, SSF101257, 1 hit
    SSF50494, SSF50494, 1 hit
    SSF52540, SSF52540, 2 hits
    SSF53335, SSF53335, 1 hit
    SSF56672, SSF56672, 1 hit
    SSF56983, SSF56983, 1 hit
    SSF81296, SSF81296, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR04240, flavi_E_stem, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51527, FLAVIVIRUS_NS2B, 1 hit
    PS51528, FLAVIVIRUS_NS3PRO, 1 hit
    PS51192, HELICASE_ATP_BIND_1, 1 hit
    PS51194, HELICASE_CTER, 1 hit
    PS50507, RDRP_SSRNA_POS, 1 hit
    PS51591, RNA_CAP01_NS5_MT, 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.

    Q32ZD5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTKKPGRPGR NRAVNMLKRG ASRALGPMIK LKRMLFGLLD GRGPLRMVLA
    60 70 80 90 100
    ILAFFRFTAL KPTAGLLKRW GMMDKVHALS LLKGFKKDLA SMTDFVHLPK
    110 120 130 140 150
    KKSGVSIIGR MLVFSFTAAV RVTLENGMSL MKIQKADVGK VITIRTDRGE
    160 170 180 190 200
    NRCIVQAMDV GEDCEDTMKY LCPAIENPSE PDDIDCWCDK ADAMVTYGRC
    210 220 230 240 250
    SKTRHSRRSR RSTNIAGHAD SRLDSRGSVW MDTKKATSYL TKAESWALRN
    260 270 280 290 300
    PGYALVAAVL GWSLGTSNAQ KVIFTVMILL IAPAYSIRCV GVENRDFIEG
    310 320 330 340 350
    VSGGTWVDVV LEHGGCVTIM APDKPTIDLE LTSTIAKSMA VTRTYCVQAQ
    360 370 380 390 400
    VSELSVETRC PTMGEAHNSK SSDAAYVCKK GFSDRGWGNG CGLFGKGSME
    410 420 430 440 450
    TCAKFSCQTK AEGRIIQREN LEYTIHMNVH ASQETGHFMN DTIASENKHG
    460 470 480 490 500
    AKISITATGP SRTADLGDYG MVTLDCEPRA GLDFDNLYLL TLGRNSWLVN
    510 520 530 540 550
    RDWFHDVNLP WIGGAEGHWK NRESLVEFGK THATKREVLA LGSQEGTLQV
    560 570 580 590 600
    ALAGAMIAKF GSNVATINSG HLKCRLKLDK LKIKGTTYHM CKGSFAFTKT
    610 620 630 640 650
    PSDTGHGTVL LELTYSGSDG PCRVPISMSV SLSNIEPVGR MVTVNPIVLS
    660 670 680 690 700
    SSPQKTIMIE VEPPFGDSFI IAGTGEPRAH YHWRKSGSSI GAAFATTIKG
    710 720 730 740 750
    ARRLAVIGDD AWDFGSVGGI LNSVGKALHQ IFGGMFRTLF GGMSWFTQIM
    760 770 780 790 800
    IGALCCWLGI NARDRTIAVT FLAVGGVLVF LATSVNADSG CALDLKRKEF
    810 820 830 840 850
    KCGNGIFVFN DAEAWSHSYR YHPSTPKKLA GSIVRAIEEG QCGVRSVGRL
    860 870 880 890 900
    EHEMWRANAR EINAILLENE KNLSVVVLES EYYRKAKNLM PIGDEMPFGW
    910 920 930 940 950
    KSWGKKFFEE PQLQNQTFVV DGRVGKECPE EKRSWNNFRI EDFGFGVFTT
    960 970 980 990 1000
    SVWMEQRTEY TEDCDQKVIG AAVKGELAAH SDLGYWIESR SKNGSWELER
    1010 1020 1030 1040 1050
    AYLLESKSCS WPATHTLWNG GVEESELIIP KSRAGPVSHH NTRKGYHNQI
    1060 1070 1080 1090 1100
    KGPWHLTPLE IRFESCPGTT VVTTEECGNR GPSLRTTTTS GKVISEWCCR
    1110 1120 1130 1140 1150
    SCTMPPLSFR TADGCWYGME IRPLKEREET MVKSHVSAGR GDGVDNLSLG
    1160 1170 1180 1190 1200
    LLVLTIALQE VMRKRILGRH ITWMVIAVFM AMILGGLSYR DLGRYLVLVG
    1210 1220 1230 1240 1250
    AAFAERNSGG DLLHLVLVAT FKVKPMALLG FVLGGRWCRR QSLLLSIGAV
    1260 1270 1280 1290 1300
    LVNFALEFQG GYFELVDSLA LALLFVKAVV QTDTTSVSLP LLAALAPAGC
    1310 1320 1330 1340 1350
    YTVLGTHRFI MLTLVLVTFL GCKKTASVKK AGTAAVGVVL GMVGMKTIPM
    1360 1370 1380 1390 1400
    LGMLMVTSRA RRSWPLHEAM AAVGILCALF GALAETEVDL AGPLAAAGLI
    1410 1420 1430 1440 1450
    VMAYVISGRS NDLSIKKVED VKWSDEAEVT GESVSYHVSL DVRGDPTLTE
    1460 1470 1480 1490 1500
    DSGPGLEKVL LKVGLMAISG IYPVAIPFAL GAWFFLEKRC KRAGALWDIP
    1510 1520 1530 1540 1550
    SPREAKPAKV EDGVYRIFSR KLFGESQIGA GVMVKGTFHT MWHVTRGAVL
    1560 1570 1580 1590 1600
    KAGEGLLEPA WADVRKDLIC YGGNWKLEEH WDGNEEVQLI ALEPGKKVRH
    1610 1620 1630 1640 1650
    IQTKPGIFKT SEGEIGALDL DCMAGTSGSP IVNKNGEVVG LYGNGVLIKG
    1660 1670 1680 1690 1700
    DRYVSAISQK ENVGQEDGAE IEDNWFRKRE LTVLDLHPGA GKTRRVLPQL
    1710 1720 1730 1740 1750
    VREAVKKRLR TVILAPTRVV ASEMYEALRG EPIRYMTPAV QSERTGNEIV
    1760 1770 1780 1790 1800
    DFMCHSTFTM KLFQGVRVPN YNLYIMDEAH FLDPASVAAR GYIETRVSMG
    1810 1820 1830 1840 1850
    DAGAIFMTAT PPGTTEAFPP SNSPIIDEET RIPDKAWNSG YEWIIEFDGR
    1860 1870 1880 1890 1900
    TVWFVHSIKQ GAEIGTCLQK AGKKVLYLNR KTFESEYPKC KSEKWDFVIT
    1910 1920 1930 1940 1950
    TDISEMGANF KADRVIDPRK TIKPILLDGR VSMQGPIAIT PASAAQRRGR
    1960 1970 1980 1990 2000
    IGRNPEKLGD IYAYSGNVSS DNEGHVSWTE ARMLLDNVHV QGGVVAQLYT
    2010 2020 2030 2040 2050
    PEREKTEAYE GEFKLKTNQR KVFSELIRTG DLPVWLAFQV ASANVEYHDR
    2060 2070 2080 2090 2100
    KWCFDGPNEH LLLENNQEIE VWTRQGQRRV LKPRWLDGRI TSDHLNLKSF
    2110 2120 2130 2140 2150
    KEFASGKRSA LSILDLIAVL PSHLNLRLQE ALDTAAILSR SEPGSRSYKA
    2160 2170 2180 2190 2200
    ALENSPEMIE TFLLCALVCL MTIGLVVVLV RGKGPGKLAF GMVSIGVMTW
    2210 2220 2230 2240 2250
    LLWSAGVDPG KIAAAVILVF LLLVVLIPEP EKQRSVQDNQ LAMLMLLIAT
    2260 2270 2280 2290 2300
    ILGGVAANEM GWLEKTKADL SWVVRGRSST TTPVVELDMK PATAWTLYAL
    2310 2320 2330 2340 2350
    ATTLLTPLFQ HLIVTKYANI SLMAIASQAG TLFSMDSGIP FSSIELSVPL
    2360 2370 2380 2390 2400
    LALGCWTQIT PCSLILACVL LSTHYAILLP GMQAQAARDA QRRTAAGIMK
    2410 2420 2430 2440 2450
    NAVVDGIVAT DIPPLDGAGP LTEKKLGQLL LFAAAVTGVV ITRSPRSWSE
    2460 2470 2480 2490 2500
    LGVLGSAVGS TLIEGSAGKF WNATTVTAMC NLFRGSYLAG VPLTYTIIRN
    2510 2520 2530 2540 2550
    SNPSNKRGGG IGETLGEKWK ARLNQMNTLE FHRYRRSHIM EVDREPARAA
    2560 2570 2580 2590 2600
    LKSGDFTRGA AVSRGSAKLR WMHERGYIRL HDKVVDLGCG RGGWCYYSAT
    2610 2620 2630 2640 2650
    VKEVKEVKGY TKGGRGHEEP VLTQSYGWNI VQMKSGVDVF YKEAEPCDVV
    2660 2670 2680 2690 2700
    LCDIGECSSS PAVEADRSTK VLELAERWLE RNDGADFCIK VLCPYMPEVV
    2710 2720 2730 2740 2750
    EKLSKLQLRY GGCLVRNPLS RNSTHEMYWV SGYKGNLIGV INSTSALLLR
    2760 2770 2780 2790 2800
    RMEIKFAEPR YEEDVNLSCG TRAVSIAPPK FDYKKIGQRV ERLKAEHMST
    2810 2820 2830 2840 2850
    WHYDCEHPYR TWAYHGSYVV KPSGSASSQV NGVVKLLSKP WDVSSEVTGM
    2860 2870 2880 2890 2900
    SMTDTTPFGQ QRVFKEKVDT KAPEPPAGAE MASVIVSEWL WKRLNREKKP
    2910 2920 2930 2940 2950
    RLCTKEEFVR KVRGNAALGP VFEEENQWKD AAEAVQDPGF WNLVDMERKN
    2960 2970 2980 2990 3000
    HLEGKCETCV YNMMGKREKK RGEFGKAKGS RAIWYMWLGA RFLEFEALGF
    3010 3020 3030 3040 3050
    LNEDHWMSRG NSGGGVEGLG IQKLGYVMRE IGEKGGILYA DDTAGWDTRI
    3060 3070 3080 3090 3100
    TECDLRNEAH IMEYMENEHR KLARAIFELT YKHKVVKVMR PGKGVPLMDI
    3110 3120 3130 3140 3150
    ISREDQRGSG QVVTYALNTF TNLVVQLIRM AEAECVLTPE DLHEMSQSAK
    3160 3170 3180 3190 3200
    LRLLKWLKEE GWERLTRMAV SGDDCVVAAP DARFGAALTF LNAMSKIRKD
    3210 3220 3230 3240 3250
    IKEWTPSKGW KNWEEVPFCS HHFHRLQMKD GRELVVPCRS QDELIGRARV
    3260 3270 3280 3290 3300
    TQGPGDLMSS ACLAKAYAQM WQLLYFHRRD LRLMGNAICS AVPVDWVPTG
    3310 3320 3330 3340 3350
    RTTWSIHGKG EWMTSENMLE VWNRVWIEEN EHMEDKTPVR EWTDIPYLGK
    3360 3370 3380 3390 3400
    REDPWCGSYI GYRPRSTWAE NIKVPVNVIR VKIGGNKYQD YLGTQKRYES
    3410
    EKRVEFRGVL
    Length:3,410
    Mass (Da):378,066
    Last modified:December 6, 2005 - 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:i09A5AAC11C68907C
    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
    AY632541 Genomic RNA Translation: AAV34157.1

    NCBI Reference Sequences

    More...
    RefSeqi
    YP_001040007.1, NC_009029.2

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    5075791

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    vg:5075791

    <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
    AY632541 Genomic RNA Translation: AAV34157.1
    RefSeqiYP_001040007.1, NC_009029.2

    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
    2V6IX-ray2.10A1678-2108[»]
    2V6JX-ray2.30A1678-2108[»]
    SMRiQ32ZD5
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein family/group databases

    MEROPSiS07.001

    Genome annotation databases

    GeneIDi5075791
    KEGGivg:5075791

    Miscellaneous databases

    EvolutionaryTraceiQ32ZD5

    Family and domain databases

    CDDicd12149, Flavi_E_C, 1 hit
    Gene3Di1.10.10.930, 1 hit
    1.10.8.970, 1 hit
    1.20.1280.260, 1 hit
    2.40.10.10, 1 hit
    2.60.260.50, 1 hit
    2.60.40.350, 1 hit
    2.60.98.10, 1 hit
    3.30.387.10, 1 hit
    3.30.67.10, 1 hit
    InterProiView protein in InterPro
    IPR011492, DEAD_Flavivir
    IPR043502, DNA/RNA_pol_sf
    IPR000069, Env_glycoprot_M_flavivir
    IPR038302, Env_glycoprot_M_sf_flavivir
    IPR013755, Flav_gly_cen_dom_subdom1
    IPR001122, Flavi_capsidC
    IPR037172, Flavi_capsidC_sf
    IPR027287, Flavi_E_Ig-like
    IPR026470, Flavi_E_Stem/Anchor_dom
    IPR038345, Flavi_E_Stem/Anchor_dom_sf
    IPR001157, Flavi_NS1
    IPR000752, Flavi_NS2A
    IPR000487, Flavi_NS2B
    IPR000404, Flavi_NS4A
    IPR001528, Flavi_NS4B
    IPR002535, Flavi_propep
    IPR038688, Flavi_propep_sf
    IPR000336, Flavivir/Alphavir_Ig-like_sf
    IPR001850, Flavivirus_NS3_S7
    IPR014412, Gen_Poly_FLV
    IPR011998, Glycoprot_cen/dimer
    IPR036253, Glycoprot_cen/dimer_sf
    IPR038055, Glycoprot_E_dimer_dom
    IPR013756, GlyE_cen_dom_subdom2
    IPR014001, Helicase_ATP-bd
    IPR001650, Helicase_C
    IPR014756, Ig_E-set
    IPR026490, mRNA_cap_0/1_MeTrfase
    IPR027417, P-loop_NTPase
    IPR009003, Peptidase_S1_PA
    IPR043504, Peptidase_S1_PA_chymotrypsin
    IPR000208, RNA-dir_pol_flavivirus
    IPR007094, RNA-dir_pol_PSvirus
    IPR002877, rRNA_MeTrfase_FtsJ_dom
    IPR029063, SAM-dependent_MTases
    PfamiView protein in Pfam
    PF01003, Flavi_capsid, 1 hit
    PF07652, Flavi_DEAD, 1 hit
    PF02832, Flavi_glycop_C, 1 hit
    PF00869, Flavi_glycoprot, 1 hit
    PF01004, Flavi_M, 1 hit
    PF00948, Flavi_NS1, 1 hit
    PF01005, Flavi_NS2A, 1 hit
    PF01002, Flavi_NS2B, 1 hit
    PF01350, Flavi_NS4A, 1 hit
    PF01349, Flavi_NS4B, 1 hit
    PF00972, Flavi_NS5, 1 hit
    PF01570, Flavi_propep, 1 hit
    PF01728, FtsJ, 1 hit
    PF00949, Peptidase_S7, 1 hit
    PIRSFiPIRSF003817, Gen_Poly_FLV, 1 hit
    SMARTiView protein in SMART
    SM00487, DEXDc, 1 hit
    SM00490, HELICc, 1 hit
    SUPFAMiSSF101257, SSF101257, 1 hit
    SSF50494, SSF50494, 1 hit
    SSF52540, SSF52540, 2 hits
    SSF53335, SSF53335, 1 hit
    SSF56672, SSF56672, 1 hit
    SSF56983, SSF56983, 1 hit
    SSF81296, SSF81296, 1 hit
    TIGRFAMsiTIGR04240, flavi_E_stem, 1 hit
    PROSITEiView protein in PROSITE
    PS51527, FLAVIVIRUS_NS2B, 1 hit
    PS51528, FLAVIVIRUS_NS3PRO, 1 hit
    PS51192, HELICASE_ATP_BIND_1, 1 hit
    PS51194, HELICASE_CTER, 1 hit
    PS50507, RDRP_SSRNA_POS, 1 hit
    PS51591, RNA_CAP01_NS5_MT, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <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_KOKV
    <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: Q32ZD5
    <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: September 27, 2017
    Last sequence update: December 6, 2005
    Last modified: October 7, 2020
    This is version 128 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

    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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