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Protein

Genome polyprotein

Gene
N/A
Organism
West Nile virus (WNV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

Capsid protein C: 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 (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins (By similarity). Can migrate to the cell nucleus where it modulates host functions (By similarity). Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (PubMed:23522008).By similarity1 Publication
Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.By similarity
Peptide pr: 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
Protein prM: 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
Small envelope protein M: 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
Envelope protein E: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes (PubMed:15367621). Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM (By similarity). 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 (By similarity). The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers (By similarity). prM-E cleavage is inefficient, and many virions are only partially matured (By similarity). These uncleaved prM would play a role in immune evasion (By similarity).By similarity
Non-structural protein 1: 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
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response.By similarity
Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy similarity
Serine protease NS3: 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.PROSITE-ProRule annotation
Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.By similarity
Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
Non-structural protein 4B: 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
RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:17267492). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed:17267492). 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 (By similarity). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).By similarity1 Publication

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

  • Selective 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1552Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1576Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1636Charge 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>Sitei1959Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1962Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2538mRNA cap bindingPROSITE-ProRule annotation1
Sitei2541mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2542mRNA cap bindingPROSITE-ProRule annotation1
Sitei2544mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2549mRNA cap bindingPROSITE-ProRule annotation1 Publication1
Sitei2553mRNA cap bindingPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 sitei2581S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2586For 2'-O-MTase activityBy similarity1
Sitei2586Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2611S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2612S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2629S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2630S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2656S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2657S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2671For 2'-O-MTase activityBy similarity1
Sitei2671Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2672S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2675mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2707For 2'-O-MTase activityBy similarity1
Sitei2707Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2738mRNA cap bindingPROSITE-ProRule annotation1
Sitei2740mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2743For 2'-O-MTase activityBy similarity1
Sitei2743Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2745S-adenosyl-L-methioninePROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 bindingi2965Zinc 1By similarity1
Metal bindingi2969Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2974Zinc 1By similarity1
Metal bindingi2977Zinc 1By similarity1
Metal bindingi3242Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3258Zinc 2By similarity1
Metal bindingi3377Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1695 – 1702ATPPROSITE-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, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase
Biological processActivation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, 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 JAK1 by virus, Inhibition of host STAT1 by virus, Inhibition of host STAT2 by virus, Inhibition of host TYK2 by virus, mRNA capping, mRNA processing, Transcription, Transcription regulation, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.48 6687
3.4.21.91 6687

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S07.003

<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 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:3.6.1.15By similarity, EC:3.6.4.13By similarity)
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_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>OrganismiWest Nile virus (WNV)
<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 identifieri11082 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirus
<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 hostiAedes [TaxID: 7158]
Amblyomma variegatum (Tropical bont tick) [TaxID: 34610]
Aves [TaxID: 8782]
Culex [TaxID: 53527]
Homo sapiens (Human) [TaxID: 9606]
Hyalomma marginatum [TaxID: 34627]
Mansonia uniformis [TaxID: 308735]
Mimomyia [TaxID: 308737]
Rhipicephalus [TaxID: 34630]
<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
  • UP000008600 <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

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

Capsid protein C :
Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A :
Serine protease NS3 :
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :

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 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 domaini2 – 105CytoplasmicSequence analysisAdd BLAST104
<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>Transmembranei106 – 126HelicalSequence analysisAdd BLAST21
Topological domaini127 – 248ExtracellularSequence analysisAdd BLAST122
Transmembranei249 – 269HelicalSequence analysisAdd BLAST21
Topological domaini270 – 275CytoplasmicSequence analysis6
Transmembranei276 – 290HelicalCuratedAdd BLAST15
Topological domaini291 – 739ExtracellularSequence analysisAdd BLAST449
Transmembranei740 – 760HelicalSequence analysisAdd BLAST21
Topological domaini761 – 766CytoplasmicSequence analysis6
Transmembranei767 – 787HelicalSequence analysisAdd BLAST21
Topological domaini788 – 1212ExtracellularSequence analysisAdd BLAST425
Transmembranei1213 – 1233HelicalSequence analysisAdd BLAST21
Topological domaini1234 – 1243CytoplasmicSequence analysis10
Transmembranei1244 – 1264HelicalSequence analysisAdd BLAST21
Topological domaini1265 – 1278LumenalSequence analysisAdd BLAST14
Transmembranei1279 – 1299HelicalSequence analysisAdd BLAST21
Topological domaini1300 – 1307CytoplasmicSequence analysis8
Transmembranei1308 – 1328HelicalSequence analysisAdd BLAST21
Topological domaini1329 – 1340LumenalSequence analysisAdd BLAST12
Transmembranei1341 – 1361HelicalSequence analysisAdd BLAST21
Topological domaini1362 – 1371CytoplasmicSequence analysis10
Transmembranei1372 – 1392HelicalSequence analysisAdd BLAST21
Topological domaini1393 – 1395LumenalSequence analysis3
Transmembranei1396 – 1416HelicalSequence analysisAdd BLAST21
Topological domaini1417 – 1473CytoplasmicSequence analysisAdd BLAST57
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Intramembranei1474 – 1494HelicalSequence analysisAdd BLAST21
Topological domaini1495 – 2170CytoplasmicSequence analysisAdd BLAST676
Transmembranei2171 – 2191HelicalSequence analysisAdd BLAST21
Topological domaini2192 – 2196LumenalSequence analysis5
Intramembranei2197 – 2217HelicalSequence analysisAdd BLAST21
Topological domaini2218LumenalSequence analysis1
Transmembranei2219 – 2239HelicalSequence analysisAdd BLAST21
Topological domaini2240 – 2254CytoplasmicSequence analysisAdd BLAST15
Transmembranei2255 – 2275Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2276 – 2309LumenalSequence analysisAdd BLAST34
Intramembranei2310 – 2330HelicalSequence analysisAdd BLAST21
Topological domaini2331 – 2377LumenalSequence analysisAdd BLAST47
Transmembranei2378 – 2398HelicalSequence analysisAdd BLAST21
Topological domaini2399 – 2441CytoplasmicSequence analysisAdd BLAST43
Transmembranei2442 – 2462HelicalSequence analysisAdd BLAST21
Topological domaini2463 – 2467LumenalSequence analysis5
Transmembranei2468 – 2488HelicalSequence analysisAdd BLAST21
Topological domaini2489 – 3430CytoplasmicSequence analysisAdd BLAST942

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host endoplasmic reticulum, Host membrane, Host nucleus, Membrane, Secreted, 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>Mutagenesisi14V → A: Loss of interaction between capsid protein C and host EXOC1. 1 Publication1
Mutagenesisi2586K → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. 1 Publication1
Mutagenesisi2671D → A: Lethal for the virus. Complete loss of 2'-O and N-7 methyltransferase activies. 1 Publication1
Mutagenesisi2707K → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. 1 Publication1
Mutagenesisi2743E → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5419

<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_00004414181 – 3430Genome polyproteinAdd BLAST3430
ChainiPRO_00000377431 – 105Capsid protein C1 PublicationAdd BLAST105
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_0000037744106 – 123ER anchor for the capsid protein C, removed in mature form by serine protease NS31 PublicationAdd BLAST18
ChainiPRO_0000405150124 – 290Protein prM1 PublicationAdd BLAST167
ChainiPRO_0000405151124 – 215Peptide pr1 PublicationAdd BLAST92
ChainiPRO_0000037745216 – 290Small envelope protein M1 PublicationAdd BLAST75
ChainiPRO_0000037746291 – 787Envelope protein E1 PublicationAdd BLAST497
ChainiPRO_0000037747788 – 1139Non-structural protein 11 PublicationAdd BLAST352
ChainiPRO_00000377481140 – 1370Non-structural protein 2A1 PublicationAdd BLAST231
ChainiPRO_00000377491371 – 1501Serine protease subunit NS2B1 PublicationAdd BLAST131
ChainiPRO_00000377501502 – 2120Serine protease NS31 PublicationAdd BLAST619
ChainiPRO_00000377512121 – 2246Non-structural protein 4A1 PublicationAdd 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_00004051522247 – 2269Peptide 2k1 PublicationAdd BLAST23
ChainiPRO_00000377522270 – 2525Non-structural protein 4B1 PublicationAdd BLAST256
ChainiPRO_00000377532526 – 3430RNA-directed RNA polymerase NS51 PublicationAdd BLAST905

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>Glycosylationi138N-linked (GlcNAc...) asparagine; by hostBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi293 ↔ 3201 Publication
Disulfide bondi350 ↔ 411By similarity
Disulfide bondi350 ↔ 4061 Publication
Disulfide bondi364 ↔ 3951 Publication
Disulfide bondi382 ↔ 4111 Publication
Disulfide bondi382 ↔ 406By similarity
Disulfide bondi476 ↔ 5741 Publication
Disulfide bondi591 ↔ 6221 Publication
Disulfide bondi791 ↔ 802By similarity
Disulfide bondi842 ↔ 930By similarity
Glycosylationi917N-linked (GlcNAc...) asparagine; by hostBy similarity1
Glycosylationi962N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi966 ↔ 1010By similarity
Glycosylationi994N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi1067 ↔ 1116By similarity
Disulfide bondi1078 ↔ 1099By similarity
Disulfide bondi1100 ↔ 1103By 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 residuei2581PhosphoserineBy similarity1

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

Genome polyprotein: Specific enzymatic cleavages 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 similarity1 Publication
Protein prM: 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
Envelope protein E: Not N-glycosylated.1 Publication
Non-structural protein 1: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.By similarity
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei105 – 106Cleavage; by viral protease NS31 Publication2
Sitei123 – 124Cleavage; by host signal peptidase1 Publication2
Sitei215 – 216Cleavage; by host furin1 Publication2
Sitei290 – 291Cleavage; by host signal peptidase1 Publication2
Sitei787 – 788Cleavage; by host signal peptidase1 Publication2
Sitei1139 – 1140Cleavage; by host1 Publication2
Sitei1370 – 1371Cleavage; by viral protease NS31 Publication2
Sitei1501 – 1502Cleavage; by autolysis1 Publication2
Sitei2120 – 2121Cleavage; by autolysis1 Publication2
Sitei2246 – 2247Cleavage; by viral protease NS31 Publication2
Sitei2269 – 2270Cleavage; by host signal peptidase1 Publication2
Sitei2525 – 2526Cleavage; by viral protease NS31 Publication2

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P06935

<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

Capsid protein C: Homodimer (By similarity). Interacts (via N-terminus) with host EXOC1 (via C-terminus) (PubMed:19889084, PubMed:23522008); this interaction results in EXOC1 degradation through the proteasome degradation pathway (PubMed:23522008). Protein prM: Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi (By similarity). Envelope protein E: Homodimer; in the endoplasmic reticulum and Golgi (By similarity). Non-structural protein 1: Homodimer; Homohexamer when secreted (By similarity). NS1 interacts with NS4B (By similarity). Interacts with host complement protein CFH; this interaction leads to the degradation of C3 (By similarity). Non-structural protein 2A: Interacts (via N-terminus) with serine protease NS3 (By similarity). Non-structural protein 2B: Forms a heterodimer with serine protease NS3. May form homooligomers (By similarity). Serine protease NS3: Forms a heterodimer with NS2B. Interacts with NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity). Non-structural protein 4B: Interacts with serine protease NS3. Interacts with NS1 (By similarity). RNA-directed RNA polymerase NS5: 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 similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P06935, 4 interactors

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P06935

<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

13430
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

More...
DisProti
DP00673

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P06935

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

More...
SMRi
P06935

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P06935

<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>Domaini1502 – 1679Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1682 – 1838Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1849 – 2014Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini2526 – 2791mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3055 – 3207RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

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 EXOC11 PublicationAdd BLAST14
Regioni37 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni388 – 401Fusion peptideBy similarityAdd BLAST14
Regioni1424 – 1463Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1686 – 1689Important for RNA-bindingBy similarity4
Regioni2165 – 2169Regulates 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>Motifi1786 – 1789DEAH 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 biasi281 – 284Poly-Leu4
Compositional biasi2675 – 2678Poly-Ser4

<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

Transmembrane, Transmembrane helix

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
VOG09000016

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
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
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
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
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
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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

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

P06935-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKKPGGPGK NRAVNMLKRG MPRGLSLIGL KRAMLSLIDG KGPIRFVLAL
60 70 80 90 100
LAFFRFTAIA PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRST
110 120 130 140 150
KQKKRGGTAG FTILLGLIAC AGAVTLSNFQ GKVMMTVNAT DVTDVITIPT
160 170 180 190 200
AAGKNLCIVR AMDVGYLCED TITYECPVLA AGNDPEDIDC WCTKSSVYVR
210 220 230 240 250
YGRCTKTRHS RRSRRSLTVQ THGESTLANK KGAWLDSTKA TRYLVKTESW
260 270 280 290 300
ILRNPGYALV AAVIGWMLGS NTMQRVVFAI LLLLVAPAYS FNCLGMSNRD
310 320 330 340 350
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLADVRSYC
360 370 380 390 400
YLASVSDLST RAACPTMGEA HNEKRADPAF VCKQGVVDRG WGNGCGLFGK
410 420 430 440 450
GSIDTCAKFA CTTKATGWII QKENIKYEVA IFVHGPTTVE SHGKIGATQA
460 470 480 490 500
GRFSITPSAP SYTLKLGEYG EVTVDCEPRS GIDTSAYYVM SVGEKSFLVH
510 520 530 540 550
REWFMDLNLP WSSAGSTTWR NRETLMEFEE PHATKQSVVA LGSQEGALHQ
560 570 580 590 600
ALAGAIPVEF SSNTVKLTSG HLKCRVKMEK LQLKGTTYGV CSKAFKFART
610 620 630 640 650
PADTGHGTVV LELQYTGTDG PCKVPISSVA SLNDLTPVGR LVTVNPFVSV
660 670 680 690 700
ATANSKVLIE LEPPFGDSYI VVGRGEQQIN HHWHKSGSSI GKAFTTTLRG
710 720 730 740 750
AQRLAALGDT AWDFGSVGGV FTSVGKAIHQ VFGGAFRSLF GGMSWITQGL
760 770 780 790 800
LGALLLWMGI NARDRSIAMT FLAVGGVLLF LSVNVHADTG CAIDIGRQEL
810 820 830 840 850
RCGSGVFIHN DVEAWMDRYK FYPETPQGLA KIIQKAHAEG VCGLRSVSRL
860 870 880 890 900
EHQMWEAIKD ELNTLLKENG VDLSVVVEKQ NGMYKAAPKR LAATTEKLEM
910 920 930 940 950
GWKAWGKSII FAPELANNTF VIDGPETEEC PTANRAWNSM EVEDFGFGLT
960 970 980 990 1000
STRMFLRIRE TNTTECDSKI IGTAVKNNMA VHSDLSYWIE SGLNDTWKLE
1010 1020 1030 1040 1050
RAVLGEVKSC TWPETHTLWG DGVLESDLII PITLAGPRSN HNRRPGYKTQ
1060 1070 1080 1090 1100
NQGPWDEGRV EIDFDYCPGT TVTISDSCEH RGPAARTTTE SGKLITDWCC
1110 1120 1130 1140 1150
RSCTLPPLRF QTENGCWYGM EIRPTRHDEK TLVQSRVNAY NADMIDPFQL
1160 1170 1180 1190 1200
GLMVVFLATQ EVLRKRWTAK ISIPAIMLAL LVLVFGGITY TDVLRYVILV
1210 1220 1230 1240 1250
GAAFAEANSG GDVVHLALMA TFKIQPVFLV ASFLKARWTN QESILLMLAA
1260 1270 1280 1290 1300
AFFQMAYYDA KNVLSWEVPD VLNSLSVAWM ILRAISFTNT SNVVVPLLAL
1310 1320 1330 1340 1350
LTPGLKCLNL DVYRILLLMV GVGSLIKEKR SSAAKKKGAC LICLALASTG
1360 1370 1380 1390 1400
VFNPMILAAG LMACDPNRKR GWPATEVMTA VGLMFAIVGG LAELDIDSMA
1410 1420 1430 1440 1450
IPMTIAGLMF AAFVISGKST DMWIERTADI TWESDAEITG SSERVDVRLD
1460 1470 1480 1490 1500
DDGNFQLMND PGAPWKIWML RMACLAISAY TPWAILPSVI GFWITLQYTK
1510 1520 1530 1540 1550
RGGVLWDTPS PKEYKKGDTT TGVYRIMTRG LLGSYQAGAG VMVEGVFHTL
1560 1570 1580 1590 1600
WHTTKGAALM SGEGRLDPYW GSVKEDRLCY GGPWKLQHKW NGHDEVQMIV
1610 1620 1630 1640 1650
VEPGKNVKNV QTKPGVFKTP EGEIGAVTLD YPTGTSGSPI VDKNGDVIGL
1660 1670 1680 1690 1700
YGNGVIMPNG SYISAIVQGE RMEEPAPAGF EPEMLRKKQI TVLDLHPGAG
1710 1720 1730 1740 1750
KTRKILPQII KEAINKRLRT AVLAPTRVVA AEMSEALRGL PIRYQTSAVH
1760 1770 1780 1790 1800
REHSGNEIVD VMCHATLTHR LMSPHRVPNY NLFIMDEAHF TDPASIAARG
1810 1820 1830 1840 1850
YIATKVELGE AAAIFMTATP PGTSDPFPES NAPISDMQTE IPDRAWNTGY
1860 1870 1880 1890 1900
EWITEYVGKT VWFVPSVKMG NEIALCLQRA GKKVIQLNRK SYETEYPKCK
1910 1920 1930 1940 1950
NDDWDFVITT DISEMGANFK ASRVIDSRKS VKPTIIEEGD GRVILGEPSA
1960 1970 1980 1990 2000
ITAASAAQRR GRIGRNPSQV GDEYCYGGHT NEDDSNFAHW TEARIMLDNI
2010 2020 2030 2040 2050
NMPNGLVAQL YQPEREKVYT MDGEYRLRGE ERKNFLEFLR TADLPVWLAY
2060 2070 2080 2090 2100
KVAAAGISYH DRKWCFDGPR TNTILEDNNE VEVITKLGER KILRPRWADA
2110 2120 2130 2140 2150
RVYSDHQALK SFKDFASGKR SQIGLVEVLG RMPEHFMVKT WEALDTMYVV
2160 2170 2180 2190 2200
ATAEKGGRAH RMALEELPDA LQTIVLIALL SVMSLGVFFL LMQRKGIGKI
2210 2220 2230 2240 2250
GLGGVILGAA TFFCWMAEVP GTKIAGMLLL SLLLMIVLIP EPEKQRSQTD
2260 2270 2280 2290 2300
NQLAVFLICV LTLVGAVAAN EMGWLDKTKN DIGSLLGHRP EARETTLGVE
2310 2320 2330 2340 2350
SFLLDLRPAT AWSLYAVTTA VLTPLLKHLI TSDYINTSLT SINVQASALF
2360 2370 2380 2390 2400
TLARGFPFVD VGVSALLLAV GCWGQVTLTV TVTAAALLFC HYAYMVPGWQ
2410 2420 2430 2440 2450
AEAMRSAQRR TAAGIMKNVV VDGIVATDVP ELERTTPVMQ KKVGQIILIL
2460 2470 2480 2490 2500
VSMAAVVVNP SVRTVREAGI LTTAAAVTLW ENGASSVWNA TTAIGLCHIM
2510 2520 2530 2540 2550
RGGWLSCLSI MWTLIKNMEK PGLKRGGAKG RTLGEVWKER LNHMTKEEFT
2560 2570 2580 2590 2600
RYRKEAITEV DRSAAKHARR EGNITGGHPV SRGTAKLRWL VERRFLEPVG
2610 2620 2630 2640 2650
KVVDLGCGRG GWCYYMATQK RVQEVKGYTK GGPGHEEPQL VQSYGWNIVT
2660 2670 2680 2690 2700
MKSGVDVFYR PSEASDTLLC DIGESSSSAE VEEHRTVRVL EMVEDWLHRG
2710 2720 2730 2740 2750
PKEFCIKVLC PYMPKVIEKM ETLQRRYGGG LIRNPLSRNS THEMYWVSHA
2760 2770 2780 2790 2800
SGNIVHSVNM TSQVLLGRME KKTWKGPQFE EDVNLGSGTR AVGKPLLNSD
2810 2820 2830 2840 2850
TSKIKNRIER LKKEYSSTWH QDANHPYRTW NYHGSYEVKP TGSASSLVNG
2860 2870 2880 2890 2900
VVRLLSKPWD TITNVTTMAM TDTTPFGQQR VFKEKVDTKA PEPPEGVKYV
2910 2920 2930 2940 2950
LNETTNWLWA FLARDKKPRM CSREEFIGKV NSNAALGAMF EEQNQWKNAR
2960 2970 2980 2990 3000
EAVEDPKFWE MVDEEREAHL RGECNTCIYN MMGKREKKPG EFGKAKGSRA
3010 3020 3030 3040 3050
IWFMWLGARF LEFEALGFLN EDHWLGRKNS GGGVEGLGLQ KLGYILKEVG
3060 3070 3080 3090 3100
TKPGGKVYAD DTAGWDTRIT KADLENEAKV LELLDGEHRR LARSIIELTY
3110 3120 3130 3140 3150
RHKVVKVMRP AADGKTVMDV ISREDQRGSG QVVTYALNTF TNLAVQLVRM
3160 3170 3180 3190 3200
MEGEGVIGPD DVEKLGKGKG PKVRTWLFEN GEERLSRMAV SGDDCVVKPL
3210 3220 3230 3240 3250
DDRFATSLHF LNAMSKVRKD IQEWKPSTGW YDWQQVPFCS NHFTELIMKD
3260 3270 3280 3290 3300
GRTLVVPCRG QDELIGRARI SPGAGWNVRD TACLAKSYAQ MWLLLYFHRR
3310 3320 3330 3340 3350
DLRLMANAIC SAVPANWVPT GRTTWSIHAK GEWMTTEDML AVWNRVWIEE
3360 3370 3380 3390 3400
NEWMEDKTPV ERWSDVPYSG KREDIWCGSL IGTRTRATWA ENIHVAINQV
3410 3420 3430
RSVIGEEKYV DYMSSLRRYE DTIVVEDTVL
Length:3,430
Mass (Da):380,110
Last modified:October 24, 2003 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i42D71B7CB12DC45B
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
M12294 Genomic RNA Translation: AAA48498.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A25256 GNWVWV

NCBI Reference Sequences

More...
RefSeqi
NP_041724.2, NC_001563.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
912267

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:912267

<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
M12294 Genomic RNA Translation: AAA48498.2
PIRiA25256 GNWVWV
RefSeqiNP_041724.2, NC_001563.2

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
2FP7X-ray1.68A1420-1466[»]
B1517-1688[»]
2G05model-D1675-2120[»]
2G2Gmodel-D1675-2120[»]
2GGVX-ray1.80A1419-1525[»]
B1503-1679[»]
2IJOX-ray2.30A1419-1482[»]
B1502-1685[»]
2P5PX-ray2.80A/B/C585-701[»]
2YOLX-ray3.20A1420-1465[»]
A1502-1671[»]
3E90X-ray2.45A/C1420-1463[»]
B/D1502-1685[»]
3I50X-ray3.00E291-688[»]
5IDKX-ray1.50A/B/C1420-1465[»]
DisProtiDP00673
ProteinModelPortaliP06935
SMRiP06935
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP06935, 4 interactors

Chemistry databases

BindingDBiP06935
ChEMBLiCHEMBL5419

Protein family/group databases

MEROPSiS07.003

Proteomic databases

PRIDEiP06935

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi912267
KEGGivg:912267

Phylogenomic databases

OrthoDBiVOG09000016

Enzyme and pathway databases

BRENDAi2.7.7.48 6687
3.4.21.91 6687

Miscellaneous databases

EvolutionaryTraceiP06935

Protein Ontology

More...
PROi
PR:P06935

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
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
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
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
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
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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<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_WNV
<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: P06935
<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: January 1, 1988
Last sequence update: October 24, 2003
Last modified: December 5, 2018
This is version 182 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

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