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Entry version 71 (12 Aug 2020)
Sequence version 1 (10 Aug 2010)
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Protein

Genome polyprotein

Gene
N/A
Organism
Kyasanur forest disease virus (KFDV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

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.By similarity
Inhibits RNA silencing by interfering with host Dicer.By similarity
Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.By similarity
Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.By similarity
Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).By similarity
Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host 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.By similarity
Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.By similarity
Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala. EC:3.4.21.91

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 sitei1545Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1569Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1629Charge 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>Sitei1951Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1954Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2526mRNA cap bindingPROSITE-ProRule annotation1
Sitei2529mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2530mRNA cap bindingPROSITE-ProRule annotation1
Sitei2532mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2537mRNA cap bindingPROSITE-ProRule annotation1
Sitei2541mRNA 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 sitei2569S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2574For 2'-O-MTase activityBy similarity1
Sitei2574Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2599S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2600S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2617S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2618S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2644S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2645S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2659For 2'-O-MTase activityBy similarity1
Sitei2659Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2660S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2663mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2696For 2'-O-MTase activityBy similarity1
Sitei2696Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2727mRNA cap bindingPROSITE-ProRule annotation1
Sitei2729mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2732For 2'-O-MTase activityBy similarity1
Sitei2732Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2734S-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 bindingi2952Zinc 1By similarity1
Metal bindingi2956Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2961Zinc 1By similarity1
Metal bindingi2964Zinc 1By similarity1
Metal bindingi3226Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3242Zinc 2By similarity1
Metal bindingi3361Zinc 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 bindingi1690 – 1697ATPPROSITE-ProRule annotation8

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

GO - Biological processi

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

Molecular functionHelicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase
Biological processActivation of host autophagy by virus, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host STAT1 by virus, Inhibition of host STAT2 by virus, mRNA capping, mRNA processing, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus entry into host cell
LigandATP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

<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:3.6.1.15, EC:3.6.4.13)
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>OrganismiKyasanur forest disease virus (KFDV)
<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 identifieri33743 [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 hostiHomo sapiens (Human) [TaxID: 9606]
Hyalomma dromedarii (Camel tick) [TaxID: 34626]
Ornithodoros savignyi [TaxID: 69826]
Semnopithecus entellus (Hanuman langur) (Presbytis entellus) [TaxID: 88029]
<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
  • UP000133616 <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
  • UP000125499 Componenti: Genome
  • UP000130242 Componenti: Genome
  • UP000158026 Componenti: Genome
  • UP000127351 Componenti: Genome
  • UP000098523 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 – 99CytoplasmicSequence analysisAdd BLAST99
<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>Transmembranei100 – 120HelicalSequence analysisAdd BLAST21
Topological domaini121 – 243ExtracellularSequence analysisAdd BLAST123
Transmembranei244 – 261HelicalCuratedAdd BLAST18
Topological domaini262CytoplasmicSequence analysis1
Transmembranei263 – 281HelicalCuratedAdd BLAST19
Topological domaini282 – 728ExtracellularSequence analysisAdd BLAST447
Transmembranei729 – 749HelicalSequence analysisAdd BLAST21
Topological domaini750 – 756CytoplasmicSequence analysis7
Transmembranei757 – 777HelicalSequence analysisAdd BLAST21
Topological domaini778 – 1134ExtracellularSequence analysisAdd BLAST357
Transmembranei1135 – 1155HelicalSequence analysisAdd BLAST21
Topological domaini1156 – 1164LumenalSequence analysis9
Transmembranei1165 – 1185HelicalSequence analysisAdd BLAST21
Topological domaini1186 – 1189CytoplasmicSequence analysis4
Transmembranei1190 – 1210HelicalSequence analysisAdd BLAST21
Topological domaini1211 – 1235LumenalSequence analysisAdd BLAST25
Transmembranei1236 – 1256HelicalSequence analysisAdd BLAST21
Topological domaini1257 – 1295CytoplasmicSequence analysisAdd BLAST39
Transmembranei1296 – 1316HelicalSequence analysisAdd BLAST21
Topological domaini1317 – 1361LumenalSequence analysisAdd BLAST45
Transmembranei1362 – 1379HelicalSequence analysisAdd BLAST18
Topological domaini1380 – 1384CytoplasmicSequence analysis5
Transmembranei1385 – 1405HelicalSequence analysisAdd BLAST21
Topological domaini1406 – 1456LumenalSequence analysisAdd BLAST51
<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>Intramembranei1457 – 1477HelicalSequence analysisAdd BLAST21
Topological domaini1478 – 2162LumenalSequence analysisAdd BLAST685
Transmembranei2163 – 2183HelicalSequence analysisAdd BLAST21
Topological domaini2184 – 2191CytoplasmicSequence analysis8
Intramembranei2192 – 2211HelicalSequence analysisAdd BLAST20
Topological domaini2212LumenalSequence analysis1
Transmembranei2213 – 2233HelicalSequence analysisAdd BLAST21
Topological domaini2234 – 2246CytoplasmicSequence analysisAdd BLAST13
Transmembranei2247 – 2267HelicalSequence analysisAdd BLAST21
Topological domaini2268 – 2301LumenalSequence analysisAdd BLAST34
Intramembranei2302 – 2322HelicalSequence analysisAdd BLAST21
Topological domaini2323 – 2345LumenalSequence analysisAdd BLAST23
Intramembranei2346 – 2366HelicalSequence analysisAdd BLAST21
Topological domaini2367 – 2368LumenalSequence analysis2
Transmembranei2369 – 2389HelicalSequence analysisAdd BLAST21
Topological domaini2390 – 2432CytoplasmicSequence analysisAdd BLAST43
Transmembranei2433 – 2453HelicalSequence analysisAdd BLAST21
Topological domaini2454 – 2476LumenalSequence analysisAdd BLAST23
Transmembranei2477 – 2497HelicalSequence analysisAdd BLAST21
Topological domaini2498 – 3416CytoplasmicSequence analysisAdd BLAST919

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host endoplasmic reticulum, Host membrane, Host nucleus, Membrane, Secreted, 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_00004415011 – 3416Genome polyproteinAdd BLAST3416
ChainiPRO_00004415021 – 96Capsid protein CBy similarityAdd BLAST96
<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_000044150397 – 117ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST21
ChainiPRO_0000441504118 – 281Protein prMBy similarityAdd BLAST164
ChainiPRO_0000441505118 – 206Peptide prBy similarityAdd BLAST89
ChainiPRO_0000441506207 – 281Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000441507282 – 777Envelope protein EBy similarityAdd BLAST496
ChainiPRO_0000441508778 – 1130Non-structural protein 1By similarityAdd BLAST353
ChainiPRO_00004415091131 – 1360Non-structural protein 2ABy similarityAdd BLAST230
ChainiPRO_00004415101361 – 1491Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00004415111492 – 2112Serine protease NS3By similarityAdd BLAST621
ChainiPRO_00004415122113 – 2238Non-structural protein 4ABy similarityAdd BLAST126
<p>This subsection of the 'PTM / Processing' section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_00004415132239 – 2261Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004415142262 – 2513Non-structural protein 4BBy similarityAdd BLAST252
ChainiPRO_00004415152514 – 3416RNA-directed RNA polymerase NS5By similarityAdd BLAST903

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>Glycosylationi145N-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 bondi284 ↔ 311By similarity
Disulfide bondi341 ↔ 402By similarity
Disulfide bondi341 ↔ 397By similarity
Disulfide bondi355 ↔ 386By similarity
Disulfide bondi373 ↔ 402By similarity
Disulfide bondi373 ↔ 397By similarity
Glycosylationi435N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi467 ↔ 571By similarity
Disulfide bondi588 ↔ 619By similarity
Disulfide bondi781 ↔ 792By similarity
Disulfide bondi832 ↔ 922By similarity
Glycosylationi862N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi957 ↔ 1002By similarity
Glycosylationi985N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi1001N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi1059 ↔ 1108By similarity
Disulfide bondi1070 ↔ 1092By similarity
Disulfide bondi1091 ↔ 1095By 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 residuei2569PhosphoserineBy similarity1

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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei97 – 98Cleavage; by viral protease NS3By similarity2
Sitei118 – 119Cleavage; by host signal peptidaseBy similarity2
Sitei206 – 207Cleavage; by host furinBy similarity2
Sitei281 – 282Cleavage; by host signal peptidaseBy similarity2
Sitei777 – 778Cleavage; by host signal peptidaseBy similarity2
Sitei1130 – 1131Cleavage; by hostBy similarity2
Sitei1360 – 1361Cleavage; by viral protease NS3By similarity2
Sitei1491 – 1492Cleavage; by autolysisBy similarity2
Sitei2112 – 2113Cleavage; by autolysisBy similarity2
Sitei2238 – 2239Cleavage; by viral protease NS3By similarity2
Sitei2261 – 2262Cleavage; by host signal peptidaseBy similarity2
Sitei2513 – 2514Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

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

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

Homodimer (By similarity).

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

By similarity

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

By similarity

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

Interacts with protein prM (By similarity).

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

By similarity

Homodimer; Homohexamer when secreted (By similarity).

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

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

By similarity

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

By similarity

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

By similarity

Forms a heterodimer with NS2B (By similarity).

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

Interacts with NS4B (By similarity).

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

By similarity

Interacts with serine protease NS3 (By similarity).

By similarity

Homodimer.

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

GO - Molecular functioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

More...
SMRi
D7RF80

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%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>Domaini1492 – 1671Peptidase S7PROSITE-ProRule annotationAdd BLAST180
Domaini1677 – 1833Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1844 – 2002Helicase C-terminalPROSITE-ProRule annotationAdd BLAST159
Domaini2514 – 2778mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3042 – 3191RdRp 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>Regioni379 – 392Fusion peptideBy similarityAdd BLAST14
Regioni1412 – 1451Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni2732 – 2736Interaction with host SCRIBBy 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>Motifi1781 – 1784DEAH boxPROSITE-ProRule annotation4

<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

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
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
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
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.

D7RF80-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKGAVLKGK GGGPPRRVPK ETAKKTRQGP GRLPNGLVLM RMMGVLWHMV
60 70 80 90 100
AGTARNPILK RFWATVPVRQ AIAALRKIRK TVGLLLDSLN KRRGKRRSTT
110 120 130 140 150
GLLTPILLAC LATLVFSATV RRERTGNMVI RAEGKDAATQ VEVMNGTCTI
160 170 180 190 200
LATDMGSWCD DSIMYECVTI DSGEEPVDVD CFCKGVERVS LEYGRCGKPA
210 220 230 240 250
GGRNRRSVSI PVHAHSDLTG RGHKWLKGDS VKTHLTRVEG WVWKNKFLTA
260 270 280 290 300
AFCAVVWMVT DSLPTRFIVI TVALCLAPTY ATRCTHLQNR DFVSGTQGTT
310 320 330 340 350
RVSLVLELGG CVTLTAEGKP SVDVWLDDIH QENPAKTREY CLHAKLANSK
360 370 380 390 400
VAARCPAMGP ATLPEEHQAS TVCRRDQSDR GWGNHCGLFG KGSIVACAKF
410 420 430 440 450
SCEAKKKATG YVYDVNKITY VVKVEPHTGD YLAANESHSN RKTASFTTQS
460 470 480 490 500
EKTILTLGDY GDISLTCRVT SGVDPAQTVV LELDKTAEHL PKAWQVHRDW
510 520 530 540 550
FEDLSLPWRH GGAQEWNHAD RLVEFGEPHA VKMDIFNLGD QTGILLKSLA
560 570 580 590 600
GVPVANIEGS KYHLQSGHVT CDVGLEKLKM KGMTYTVCEG SKFAWKRPPT
610 620 630 640 650
DSGHDTVVME VTYTGSKPCR IPVRAVAHGE PNVNVASLIT PNPSMETTGG
660 670 680 690 700
GFVELQLPPG DNIIYVGELS HQWFQKGSTI GRVLEKTRRG IERLTVVGEH
710 720 730 740 750
AWDFGSVGGM LSSVGKALHT AFGAAFNTIF GGVGFLPRIL LGVALAWLGL
760 770 780 790 800
NSRNPTLSVG FLITGGLVLT MTLGVGADMG CAIDANRMEL RCGEGLVVWR
810 820 830 840 850
EVTDWYDGYA FHPESPSVLA ASLKEAYEEG ICGIVPQNRL EMAMWRRVEA
860 870 880 890 900
VLNLALAESD ANLTVVVDKR DPSDYRGGKV GTLRRSGKEM KTSWKGWSQS
910 920 930 940 950
FVWSVPEAPR RFMVGVEGAG ECPLDKRRTG VFTVAEFGMG MRTKVFLDLR
960 970 980 990 1000
ETASSDCDTG VMGAAVKSGH AVHTDQSLWM RSHRNATGVF ISELIVTDLR
1010 1020 1030 1040 1050
NCTWPASHTL DNAGVVDSKL FLPAGLAGPR SHYNHIPGYA EQVKGPWSQT
1060 1070 1080 1090 1100
PLRVVREPCP GTAVKIDQSC DKRGASLRST TESGKAIPEW CCRTCELPPV
1110 1120 1130 1140 1150
TFRSGTDCWY AMEIRPVHQQ GGLVRSMVLA DNGAMLSEGG VPGIVAVFVV
1160 1170 1180 1190 1200
LELVIRRRPT TGSSVVWCGM VVLGLVVTGL VTIEGLCRYV VAVGILMSME
1210 1220 1230 1240 1250
LGPEIVALVL LQAVFDMRTG LLVAFAVKRA YTTREAVATY FLLLVLELGF
1260 1270 1280 1290 1300
PEASLSNIWK WADSLAMGAL ILQACGQEGR TRVGYLLAAM MTQKDMVIIH
1310 1320 1330 1340 1350
TGLTIFLSAA TAMAVWSMIK GQRDQKGLSW ATPLAGLLGG EGVGLRLLAF
1360 1370 1380 1390 1400
RKLAERRNRR SFSEPLTVVG VMLTVASGMV RHTSQEALCA LVAGAFLLLM
1410 1420 1430 1440 1450
MVLGTRKMQL TAEWCGEVEW NPDLVNEGGE VNLKVRQDAM GNLHLTEVEK
1460 1470 1480 1490 1500
EERAMALWLL AGLVASAFHW AGILIVLAVW TLFEMLGSGR RSELVFSGQE
1510 1520 1530 1540 1550
TRTERNRPFE IKDGAYRIYS PGLLWGHRQI GVGYGAKGVL HTMWHVTRGA
1560 1570 1580 1590 1600
ALVVDEAISG PYWADVREDV VCYGGAWSLE SRWRGETVQV HAFPPGRPQE
1610 1620 1630 1640 1650
THQCQPGELI LENGRKLGAV PIDLSKGTSG SPIINAQGEV VGLYGNGLKT
1660 1670 1680 1690 1700
NEAYVSSIAQ GEAEKSRPEI PLSVQGTGWM SKGQITVLDM HPGSGKTHRV
1710 1720 1730 1740 1750
LPELVRQCAD RGMRTLVLAP TRVVLKEMER ALAGKKVRFH SPAVEGQTTA
1760 1770 1780 1790 1800
GAIVDVMCHA TYVHRRLLPQ GRQNWEVAIM DEAHWTDPHS IAARGHLYSL
1810 1820 1830 1840 1850
AKENRCALVL MTATPPGRGD PFPESNGAIM SEERAIPDGE WREGFDWITE
1860 1870 1880 1890 1900
YEGRTAWFVP SISKGGAVAR TLRQRGKSVI CLNSKTFEKD YLRVREEKPD
1910 1920 1930 1940 1950
FVVTTDISEM GANLDVSRVI DGRTNIKPEE VDGKVELTGT RKVTTASAAQ
1960 1970 1980 1990 2000
RRGRVGRTSG RTDEYIYSGQ CDDDDTSLVQ WKEAQILLDN ITTLRGPVAT
2010 2020 2030 2040 2050
FYGPEQVKMP EVAGHYRLNE EKRKHFRHLM TQCDFTPWLA WHVATNTSNV
2060 2070 2080 2090 2100
LDRSWTWQGP EENAIDGADG DLVRFKTPGG SERVLQPVWK DCRMFREGRD
2110 2120 2130 2140 2150
VKDFILYASG RRSVGDVLGG LAGVPGLLRH RCASALDVVY TLLNENPGSR
2160 2170 2180 2190 2200
AMRMAERDAP EAFLTIVEVA VLGVATLGIL WCFVARASVS RMFLGTVVLF
2210 2220 2230 2240 2250
AALFLLWIGG VDYGHMAGIA LIFYTLLTVL QPEPGKQRSS DDNRLAYFLL
2260 2270 2280 2290 2300
GLFSLAGLVT ANEMGMLDKT KADLAGLVWR GEQRHPAWEE WTNVDIQPAR
2310 2320 2330 2340 2350
SWGTYVLIVS LFTPYMLHQL QTKIQQLVNS SVASGAQAMR DLGGGTPFFG
2360 2370 2380 2390 2400
VAGHVIALGV TSLVGATPMS LGLGVALAAF HLAIVASGLE AELTQRAHRV
2410 2420 2430 2440 2450
FFSAMVKNPM VDGDVINPFP DGETKPALYE RRMSLILAIA LCMGSVVLNR
2460 2470 2480 2490 2500
TAASMTEAGA VGLAALGQLV HPETETLWTM PMACGMAGLV RGSFWGLLPM
2510 2520 2530 2540 2550
GHRLWLRTTG TRRGGAEGET LGDIWKRRLN GCSREEFFQY RRSGVMETER
2560 2570 2580 2590 2600
DKARELLKRG ETNMGLAVSR GTAKLAWLEE RGYATLKGEV VDLGCGRGGW
2610 2620 2630 2640 2650
SYYAASRPAV MGVKAYTIGG KGHEVPRLIT SLGWNLIKFR TGMDVYSLEA
2660 2670 2680 2690 2700
HRADTILCDI GESSPDPLAE GERSRRVILL MEKWKLRNPD ASCVFKVLAP
2710 2720 2730 2740 2750
YRPEVLEALH RFQLQWGGGL VRVPFSRNST HEMYFSTAIS GNIINSVNTQ
2760 2770 2780 2790 2800
SRKLLARFGD QRGPTKVPEV DLGTGTRCVV LAEDKVREAD VAERIAALKT
2810 2820 2830 2840 2850
QYGDSWHVDK EHPYRTWQYW GSYKTEATGS AASLINGVVK LLSWPWNARE
2860 2870 2880 2890 2900
DVVRMAMTDT TAFGQQRVFK EKVDTKAQEP QVGTKIIMRA VNDWIFERLA
2910 2920 2930 2940 2950
GKKTPRLCTR EEFIAKVRSN AALGAWSDEQ NRWPNAREAV EDPEFWRLVD
2960 2970 2980 2990 3000
EERERHLGGR CAQCVYNMMG KREKKLGEFG VAKGSRAIWY MWLGSRYLEF
3010 3020 3030 3040 3050
EALGFLNEDH WASRDLSGAG VEGTSLNYLG WHLKKLSELE GGLFYADDTA
3060 3070 3080 3090 3100
GWDTRITNAD LEDEEQILRY LEGEHRTLAK TILEKAYHAK VVKVARPSSS
3110 3120 3130 3140 3150
GGCVMDIITR RDQRGSGQVV TYALNTLTNI KVQLIRMMEG EGVIGPSDSQ
3160 3170 3180 3190 3200
DPRLLRVEAW LKEHGEERLT RMLVSGDDCV VRPIDDRFGK ALYFLNDMAK
3210 3220 3230 3240 3250
VRKDIGEWEP SEGYSSWEEV PFCSHHFHEL TMKDGRVIIV PCRDQDELVG
3260 3270 3280 3290 3300
RARVSPGCGW SVRETACLSK AYGQMWLLSY FHRRDLRTLG LAICSAVPID
3310 3320 3330 3340 3350
WVPQGRTTWS IHASGAWMTT EDMLEVWNRV WILDNPFMGD KGKVREWRDI
3360 3370 3380 3390 3400
PYLPKSQDGL CSSLVGRRER AEWAKNIWGS VEKVRRMIGP ERYADYLSCM
3410
DRHELHWDLK LESNII
Length:3,416
Mass (Da):377,417
Last modified:August 10, 2010 - 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:iDEB3FDE2DC0DA5C2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti404A → T in AFF18436 (PubMed:21991403).Curated1
Sequence conflicti404A → T in AFF18435 (PubMed:21991403).Curated1
Sequence conflicti511G → E in ACA50033 (Ref. 2) Curated1
Sequence conflicti511G → E in AFF18436 (PubMed:21991403).Curated1
Sequence conflicti511G → E in AFF18435 (PubMed:21991403).Curated1
Sequence conflicti797V → A in AFF18436 (PubMed:21991403).Curated1
Sequence conflicti797V → A in AFF18435 (PubMed:21991403).Curated1
Sequence conflicti1063A → T in AFF18436 (PubMed:21991403).Curated1
Sequence conflicti1063A → T in AFF18435 (PubMed:21991403).Curated1
Sequence conflicti1163S → T in AAQ91607 (PubMed:17169393).Curated1
Sequence conflicti1163S → T in ACA50033 (Ref. 2) Curated1
Sequence conflicti1163S → T in AFF18434 (PubMed:21991403).Curated1
Sequence conflicti1163S → T in AFF18436 (PubMed:21991403).Curated1
Sequence conflicti1163S → T in AFF18435 (PubMed:21991403).Curated1
Sequence conflicti1843E → V in AAQ91607 (PubMed:17169393).Curated1
Sequence conflicti2187A → T in AAQ91607 (PubMed:17169393).Curated1
Sequence conflicti2187A → T in ACA50033 (Ref. 2) Curated1
Sequence conflicti2187A → T in AFF18434 (PubMed:21991403).Curated1
Sequence conflicti2187A → T in AFF18436 (PubMed:21991403).Curated1
Sequence conflicti2187A → T in AFF18435 (PubMed:21991403).Curated1
Sequence conflicti2304T → A in AAQ91607 (PubMed:17169393).Curated1
Sequence conflicti3077T → N in AFF18436 (PubMed:21991403).Curated1
Sequence conflicti3077T → N in AFF18435 (PubMed:21991403).Curated1

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
AY323490 Genomic RNA Translation: AAQ91607.1
EU480689 Genomic RNA Translation: ACA50033.1
JF416958 Genomic RNA Translation: AFF18434.1
JF416960 Genomic RNA Translation: AFF18436.1
JF416959 Genomic RNA Translation: AFF18435.1
HM055369 Genomic RNA Translation: ADH95737.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY323490 Genomic RNA Translation: AAQ91607.1
EU480689 Genomic RNA Translation: ACA50033.1
JF416958 Genomic RNA Translation: AFF18434.1
JF416960 Genomic RNA Translation: AFF18436.1
JF416959 Genomic RNA Translation: AFF18435.1
HM055369 Genomic RNA Translation: ADH95737.1

3D structure databases

SMRiD7RF80
ModBaseiSearch...

Family and domain databases

Gene3Di1.10.8.970, 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
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
SUPFAMiSSF50494, 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

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_KFDV
<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: D7RF80
Secondary accession number(s): B1PMU9
, H8Y6L3, H8Y6L4, H8Y6L5, Q14F58
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2017
Last sequence update: August 10, 2010
Last modified: August 12, 2020
This is version 71 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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