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Entry version 178 (12 Aug 2020)
Sequence version 1 (01 Apr 1993)
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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 2 (strain 16681-PDK53) (DENV-2)
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
Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease.By similarity
Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune 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.PROSITE-ProRule annotation
Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired.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.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). May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (By similarity).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

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 sitei1526Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1550Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1610Charge 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>Sitei1932Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1935Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2505mRNA cap bindingPROSITE-ProRule annotation1
Sitei2508mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2509mRNA cap bindingPROSITE-ProRule annotation1
Sitei2511mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2516mRNA cap bindingPROSITE-ProRule annotation1
Sitei2520mRNA 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 sitei2547S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2552For 2'-O-MTase activityBy similarity1
Sitei2552Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2577S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2578S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2595S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2596S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2622S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2623S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2637For 2'-O-MTase activityBy similarity1
Sitei2637Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2638S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2641mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2672For 2'-O-MTase activityBy similarity1
Sitei2672Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2703mRNA cap bindingPROSITE-ProRule annotation1
Sitei2705mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2708For 2'-O-MTase activityBy similarity1
Sitei2708Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2710S-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 bindingi2929Zinc 1By similarity1
Metal bindingi2933Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2938Zinc 1By similarity1
Metal bindingi2941Zinc 1By similarity1
Metal bindingi3203Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3219Zinc 2By similarity1
Metal bindingi3338Zinc 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 bindingi1668 – 1675ATPPROSITE-ProRule annotation8

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

GO - Biological processi

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

Molecular functionHelicase, Hydrolase, Ion channel, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase, Viral ion channel
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 MAVS by virus, Inhibition of host RLR pathway by virus, Inhibition of host STAT2 by virus, Inhibition of host TYK2 by virus, Ion transport, mRNA capping, mRNA processing, Transcription, Transcription regulation, Transport, 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

<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:3.6.1.15By 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):
Non-structural protein 5
<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>OrganismiDengue virus type 2 (strain 16681-PDK53) (DENV-2)
<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 identifieri31635 [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 lineageiVirusesRiboviriaFlaviviridaeFlavivirus
<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 hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes furcifer (Mosquito) [TaxID: 299627]
Aedes taylori (Mosquito) [TaxID: 299628]
Erythrocebus patas (Red guenon) (Cercopithecus patas) [TaxID: 9538]
Homo sapiens (Human) [TaxID: 9606]
<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
  • UP000008390 <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 – 101CytoplasmicSequence analysisAdd BLAST101
<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>Transmembranei102 – 122HelicalSequence analysisAdd BLAST21
Topological domaini123 – 242ExtracellularSequence analysisAdd BLAST120
Transmembranei243 – 260HelicalSequence analysisAdd BLAST18
Topological domaini261CytoplasmicSequence analysis1
Transmembranei262 – 280HelicalSequence analysisAdd BLAST19
Topological domaini281 – 727ExtracellularSequence analysisAdd BLAST447
Transmembranei728 – 748HelicalSequence analysisAdd BLAST21
Topological domaini749 – 752CytoplasmicSequence analysis4
Transmembranei753 – 773HelicalSequence analysisAdd BLAST21
Topological domaini774 – 1195ExtracellularSequence analysisAdd BLAST422
Transmembranei1196 – 1220HelicalSequence analysisAdd BLAST25
Topological domaini1221 – 1226CytoplasmicSequence analysis6
Transmembranei1227 – 1245HelicalSequence analysisAdd BLAST19
Topological domaini1246 – 1269LumenalSequence analysisAdd BLAST24
Transmembranei1270 – 1290HelicalSequence analysisAdd BLAST21
Topological domaini1291CytoplasmicSequence analysis1
Transmembranei1292 – 1310HelicalSequence analysisAdd BLAST19
Topological domaini1311 – 1317LumenalSequence analysis7
Transmembranei1318 – 1338HelicalSequence analysisAdd BLAST21
Topological domaini1339 – 1346CytoplasmicSequence analysis8
Transmembranei1347 – 1367HelicalSequence analysisAdd BLAST21
Topological domaini1368 – 1370LumenalSequence analysis3
Transmembranei1371 – 1391HelicalSequence analysisAdd BLAST21
Topological domaini1392 – 1447CytoplasmicSequence 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>Intramembranei1448 – 1468HelicalSequence analysisAdd BLAST21
Topological domaini1469 – 2147CytoplasmicSequence analysisAdd BLAST679
Transmembranei2148 – 2168HelicalSequence analysisAdd BLAST21
Topological domaini2169 – 2170LumenalSequence analysis2
Intramembranei2171 – 2191HelicalSequence analysisAdd BLAST21
Topological domaini2192LumenalSequence analysis1
Transmembranei2193 – 2213HelicalSequence analysisAdd BLAST21
Topological domaini2214 – 2228CytoplasmicSequence analysisAdd BLAST15
Transmembranei2229 – 2249Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2250 – 2274LumenalSequence analysisAdd BLAST25
Intramembranei2275 – 2295HelicalSequence analysisAdd BLAST21
Topological domaini2296 – 2316LumenalSequence analysisAdd BLAST21
Intramembranei2317 – 2337HelicalSequence analysisAdd BLAST21
Topological domaini2338 – 2347LumenalSequence analysis10
Transmembranei2348 – 2368HelicalSequence analysisAdd BLAST21
Topological domaini2369 – 2413CytoplasmicSequence analysisAdd BLAST45
Transmembranei2414 – 2434HelicalSequence analysisAdd BLAST21
Topological domaini2435 – 2459LumenalSequence analysisAdd BLAST25
Transmembranei2460 – 2480HelicalSequence analysisAdd BLAST21
Topological domaini2481 – 3391CytoplasmicSequence analysisAdd BLAST911

GO - Cellular componenti

Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004052141 – 3391Genome polyproteinAdd BLAST3391
ChainiPRO_00000379361 – 100Capsid protein CBy similarityAdd BLAST100
<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_0000037937101 – 114ER anchor for the Capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST14
PropeptideiPRO_0000441419101 – 114ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST14
ChainiPRO_0000308279115 – 280Protein prMBy similarityAdd BLAST166
ChainiPRO_0000308280115 – 205Peptide prBy similarityAdd BLAST91
ChainiPRO_0000037938206 – 280Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037939281 – 775Envelope protein EBy similarityAdd BLAST495
ChainiPRO_0000037940776 – 1127Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000379411128 – 1345Non-structural protein 2ABy similarityAdd BLAST218
ChainiPRO_00000379431346 – 1475Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00003084651476 – 2093Serine protease NS3By similarityAdd BLAST618
ChainiPRO_00000379442094 – 2220Non-structural protein 4ABy similarityAdd BLAST127
<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_00003082812221 – 2243Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000379452244 – 2491Non-structural protein 4BBy similarityAdd BLAST248
ChainiPRO_00000379462492 – 3391RNA-directed RNA polymerase NS5By similarityAdd BLAST900

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi183N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
<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 bondi283 ↔ 310By similarity
Disulfide bondi340 ↔ 401By similarity
Glycosylationi347N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi354 ↔ 385By similarity
Disulfide bondi372 ↔ 396By similarity
Glycosylationi433N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi465 ↔ 565By similarity
Disulfide bondi582 ↔ 613By similarity
Disulfide bondi779 ↔ 790By similarity
Disulfide bondi830 ↔ 918By similarity
Glycosylationi905N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi954 ↔ 998By similarity
Glycosylationi982N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi1055 ↔ 1104By similarity
Disulfide bondi1066 ↔ 1088By similarity
Disulfide bondi1087 ↔ 1091By similarity
Glycosylationi1134N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2301N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2305N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2457N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
<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 residuei2547PhosphoserineBy 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
Sumoylation of RNA-directed RNA polymerase NS5 increases NS5 protein stability allowing proper viral RNA replication.By similarity
Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei100 – 101Cleavage; by viral protease NS3By similarity2
Sitei114 – 115Cleavage; by host signal peptidaseBy similarity2
Sitei205 – 206Cleavage; by host furinSequence analysisBy similarity2
Sitei280 – 281Cleavage; by host signal peptidaseBy similarity2
Sitei775 – 776Cleavage; by host signal peptidaseBy similarity2
Sitei1127 – 1128Cleavage; by hostBy similarity2
Sitei1345 – 1346Cleavage; by viral protease NS3By similarity2
Sitei1475 – 1476Cleavage; by autolysisBy similarity2
Sitei2093 – 2094Cleavage; by autolysisBy similarity2
Sitei2220 – 2221Cleavage; by viral protease NS3By similarity2
Sitei2243 – 2244Cleavage; by host signal peptidaseBy similarity2
Sitei2491 – 2492Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P29991

<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.

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

By similarity

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

By similarity

Homodimer; in the endoplasmic reticulum and Golgi.

Interacts with protein prM.

Interacts with non-structural protein 1.

By similarity

Homodimer; Homohexamer when secreted.

Interacts with envelope protein E.

By similarity

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

By similarity

Forms a heterodimer with serine protease NS3. May form homooligomers.

By similarity

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.

Interacts with host SHFL.

By similarity

Interacts with host MAVS; this interaction inhibits the synthesis of IFN-beta.

Interacts with host SHFL (By similarity). May interact with host SRPRA and SEC61G (By similarity).

By similarity

Interacts with serine protease NS3.

By similarity

Homodimer.

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

Interacts with serine protease NS3 (By similarity).

Interacts with host PAF1 complex; the interaction may prevent the recruitment of the PAF1 complex to interferon-responsive genes, and thus reduces the immune response (By similarity).

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

<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

13391
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
P29991

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
P29991

<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>Domaini1476 – 1653Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1655 – 1811Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1821 – 1988Helicase C-terminalAdd BLAST168
Domaini2493 – 2755mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST263
Domaini3020 – 3169RdRp catalyticPROSITE-ProRule annotationAdd BLAST150

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>Regioni1 – 15Interaction with host EXOC1By similarityAdd BLAST15
Regioni37 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni378 – 391Fusion peptideBy similarityAdd BLAST14
Regioni1398 – 1437Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1659 – 1662Important for RNA-bindingBy similarity4

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>Motifi1759 – 1762DEAH boxPROSITE-ProRule annotation4
Motifi2568 – 2571SUMO-interacting motifBy similarity4

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 biasi97 – 100Poly-Arg4
Compositional biasi1434 – 1437Poly-Glu4
Compositional biasi2148 – 2154Poly-Leu7
Compositional biasi3383 – 3386Poly-Glu4

<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

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.

P29991-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNDQRKEAKN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLYMAL
60 70 80 90 100
VAFLRFLTIP PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR
110 120 130 140 150
SAGMIIMLIP TVMAFHLTTR NGEPHMIVSR QEKGKSLLFK TEVGVNMCTL
160 170 180 190 200
MAMDLGELCE DTITYKCPLL RQNEPEDIDC WCNSTSTWVT YGTCTTMGEH
210 220 230 240 250
RREKRSVALV PHVGMGLETR TETWMSSEGA WKHVQRIETW ILRHPGFTMM
260 270 280 290 300
AAILAYTIGT THFQRALILI LLTAVTPSMT MRCIGMSNRD FVEGVSGGSW
310 320 330 340 350
VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT
360 370 380 390 400
ESRCPTQGEP SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFR
410 420 430 440 450
CKKNMEGKVV QPENLEYTIV ITPHSGEEHA VGNDTGKHGK EIKITPQSSI
460 470 480 490 500
TEAELTGYGT ITMECSPRTG LDFNEIVLLQ MENKAWLVHR QWFLDLPLPW
510 520 530 540 550
LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM HTALTGATEI
560 570 580 590 600
QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI
610 620 630 640 650
VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE
660 670 680 690 700
PPFGDSYIII GVEPGQLKLN WFKKGSSIGQ MFETTMRGAK RMAILGDTAW
710 720 730 740 750
DFGSLGGVFT SIGKALHQVF GAIYGAAFSG VSWTMKILIG VIITWIGMNS
760 770 780 790 800
RSTSLSVTLV LVGIVTLYLG VMVQADSGCV VSWKNKELKC GSGIFITDNV
810 820 830 840 850
HTWTEQYKFQ PESPSKLASA IQKAHEEDIC GIRSVTRLEN LMWKQITPEL
860 870 880 890 900
NHILSENEVK LTIMTGDIKG IMQAGKRSLR PQPTELKYSW KTWGKAKMLS
910 920 930 940 950
TESHNQTFFI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLKEKQ
960 970 980 990 1000
DVFCDSKLMS AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKNCHW
1010 1020 1030 1040 1050
PKSHTLWSNG VLESEMIIPK NLAGPVSKHN YRPGYHTQIT GPWHLGKLEM
1060 1070 1080 1090 1100
DFDFCDGTTV VVTEDCGNRG PSLRTTTASG KLITEWCCRS CTLPPLRYRG
1110 1120 1130 1140 1150
EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QVDNFSLGVL GMALFLEEML
1160 1170 1180 1190 1200
RTRVGTKHAI LLVAVSFVTL IIGNRSFRDL GRVMVMVGAT MTDDIGMGVT
1210 1220 1230 1240 1250
YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLSSQ STIPETILEL
1260 1270 1280 1290 1300
TDALALGMMV LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA
1310 1320 1330 1340 1350
VVSVSPLFLT SSQQKTDWIP LALTIKGLNP TAIFLTTLSR TSKKRSWPLN
1360 1370 1380 1390 1400
EAIMAVGMVS ILASSLLKND IPMTGPLVAG GLLTVCYVLT GRSADLELER
1410 1420 1430 1440 1450
AADVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL TILIRRGLLV
1460 1470 1480 1490 1500
ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPMGK AELEDGAYRI
1510 1520 1530 1540 1550
KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD
1560 1570 1580 1590 1600
LISYGGGWKL EGEWKEGEEV QVLALDPGKN PRAVQTKPGL FKTNAGTIGA
1610 1620 1630 1640 1650
VSLDFSPGTS GSPIIDKKGK VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN
1660 1670 1680 1690 1700
PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP AIVREAIKRG LRTLILAPTR
1710 1720 1730 1740 1750
VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF TMRLLSPVRV
1760 1770 1780 1790 1800
PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
1810 1820 1830 1840 1850
PQSNAPIIDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KAGNDIAACL
1860 1870 1880 1890 1900
RKNGKKVIQL SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP
1910 1920 1930 1940 1950
RRCMKPVILT DGEERVILAG PMPVTHSSAA QRRGRIGRNP KNENDQYIYM
1960 1970 1980 1990 2000
GEPLENDEDC AHWKEAKMLL DNINTPEGII PSMFEPEREK VDAIDGEYRL
2010 2020 2030 2040 2050
RGEARTTFVD LMRRGDLPVW LAYRVAAEGI NYADRRWCFD GVKNNQILEE
2060 2070 2080 2090 2100
NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA GRKSLTLNLI
2110 2120 2130 2140 2150
TEMGRLPTFM TQKARNALDN LAVLHTAEAG GRAYNHALSE LPETLETLLL
2160 2170 2180 2190 2200
LTLLATVTGG IFLFLMSARG IGKMTLGMCC IITASILLWY AQIQPHWIAA
2210 2220 2230 2240 2250
SIILEFFLIV LLIPEPEKQR TPQDNQLTYV VIAILTVVAA TMANEMGFLE
2260 2270 2280 2290 2300
KTKKDLGLGS IATQQPESNI LDIDLRPASA WTLYAVATTF VTPMLRHSIE
2310 2320 2330 2340 2350
NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG CYSQVNPTTL
2360 2370 2380 2390 2400
TAALFLLVAH YAIIGPALQA KASREAQKRA AAGIMKNPTV DGITVIDLDP
2410 2420 2430 2440 2450
IPYDPKFEKQ LGQVMLLVLC VTQVLMMRTT WALCEALTLA TGPISTLSEG
2460 2470 2480 2490 2500
NPGRFWNTTI AVSMANIFRG SYLAGAGLLF SIMKNTTNTR RVTGNIGETL
2510 2520 2530 2540 2550
GEKWKSRLNA LGKSEFQIYK KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS
2560 2570 2580 2590 2600
AKLRWFVERN MVTPEGKVVD LGCGRGGWSY YCGGLKNVRE VKGLTKGGPG
2610 2620 2630 2640 2650
HEEPIPMSTY GWNLVRLQSG VDVFFIPPEK CDTLLCDIGE SSPNPTVEAG
2660 2670 2680 2690 2700
RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMEALQR KYGGALVRNP
2710 2720 2730 2740 2750
LSRNSTHEMY WVSNASGNIV SSVNMISRML INRFTMRYKK ATYEPDVDLG
2760 2770 2780 2790 2800
SGTRNIGIES EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY
2810 2820 2830 2840 2850
ETKQTGSASS MVNGVFRLLT KPWDVVPMVT QMAMTDTTPF GQQRVFKEKV
2860 2870 2880 2890 2900
DTRTQEPKEG TKKLMKITAE WLWKELGKKK TPRMCTREEF TRKVRSNAAL
2910 2920 2930 2940 2950
GAIFTDENKW KSAREAVEDS RFWELVDKER NLHLEGKCET CVYNIMGKRE
2960 2970 2980 2990 3000
KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RENSLSGVEG
3010 3020 3030 3040 3050
EGLHKLGYIL RDVSKKEGGA MYADDTAGWD TRITLEDLKN EEMVTNHMEG
3060 3070 3080 3090 3100
EHKKLAEAIF KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL
3110 3120 3130 3140 3150
NTFTNMEAQL IRQMEGEGVF KSIQHLTITE EIAVQNWLAR VGRERLSRMA
3160 3170 3180 3190 3200
ISGDDCVVKP LDDRLPSALT ALNDMGKIRK DIQQWEPSRG WNDWTQVPFC
3210 3220 3230 3240 3250
SHHFHELIMK DGRVLVVPCR NQDELIGRAR ISQGAGWSLR ETACLGKSYA
3260 3270 3280 3290 3300
QMWSLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA KHEWMTTEDM
3310 3320 3330 3340 3350
LTVWNRVWIQ ENPWMEDKTP VESWEEIPYL GKREDQWCGS LIGLTSRATW
3360 3370 3380 3390
AKNIQAAINQ VRSLIGNEEY TDYMPSMKRF RREEEEAGVL W
Length:3,391
Mass (Da):379,884
Last modified:April 1, 1993 - 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:i5EE11A74081C5177
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
M84728 Genomic RNA Translation: AAA73186.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B42451, GNWV26

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84728 Genomic RNA Translation: AAA73186.1
PIRiB42451, GNWV26

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
2R29X-ray3.00A578-674[»]
3EVGX-ray2.20A2493-2757[»]
6FLAX-ray2.90I577-677[»]
SMRiP29991
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP29991, 107 interactors

Proteomic databases

PRIDEiP29991

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P29991, 1 sequenced antibody

Miscellaneous databases

EvolutionaryTraceiP29991

Protein Ontology

More...
PROi
PR:P29991

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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ProtoNeti
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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_DEN27
<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: P29991
<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: April 1, 1993
Last sequence update: April 1, 1993
Last modified: August 12, 2020
This is version 178 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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