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Entry version 82 (12 Aug 2020)
Sequence version 1 (03 Nov 2009)
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Protein

Genome polyprotein

Gene
N/A
Organism
Edge Hill virus (EHV)
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. Also plays a role in virus assembly (By similarity).PROSITE-ProRule annotationBy similarity
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.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 (By similarity). 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. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition.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 sitei1532Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1556Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1617Charge 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>Sitei1940Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1943Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2511mRNA cap bindingPROSITE-ProRule annotation1
Sitei2514mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2515mRNA cap bindingPROSITE-ProRule annotation1
Sitei2517mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2522mRNA cap bindingPROSITE-ProRule annotation1
Sitei2526mRNA 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 sitei2554S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2559For 2'-O-MTase activityBy similarity1
Sitei2559Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2584S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2585S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2602S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2603S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2629S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2630S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2644For 2'-O-MTase activityBy similarity1
Sitei2644Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2645S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2648mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2680For 2'-O-MTase activityBy similarity1
Sitei2680Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2711mRNA cap bindingPROSITE-ProRule annotation1
Sitei2713mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2716For 2'-O-MTase activityBy similarity1
Sitei2716Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2718S-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 bindingi2936Zinc 1By similarity1
Metal bindingi2940Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2945Zinc 1By similarity1
Metal bindingi2948Zinc 1By similarity1
Metal bindingi3213Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3229Zinc 2By similarity1
Metal bindingi3348Zinc 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 bindingi1678 – 1685ATPPROSITE-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, GTP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S07.001

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 14 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Non-structural protein 2A-alpha
Short name:
NS2A-alpha
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>OrganismiEdge Hill virus (EHV)
<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 identifieri64296 [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 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
  • UP000136711 <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 – 104CytoplasmicSequence analysisAdd BLAST104
<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>Transmembranei105 – 125HelicalSequence analysisAdd BLAST21
Topological domaini126 – 240ExtracellularSequence analysisAdd BLAST115
Transmembranei241 – 261HelicalSequence analysisAdd BLAST21
Topological domaini262 – 266CytoplasmicSequence analysis5
Transmembranei267 – 281HelicalCuratedAdd BLAST15
Topological domaini282 – 725ExtracellularSequence analysisAdd BLAST444
Transmembranei726 – 746HelicalSequence analysisAdd BLAST21
Topological domaini747 – 753ExtracellularSequence analysis7
Transmembranei754 – 774HelicalSequence analysisAdd BLAST21
Topological domaini775 – 1122ExtracellularSequence analysisAdd BLAST348
Transmembranei1123 – 1143HelicalSequence analysisAdd BLAST21
Topological domaini1144 – 1198CytoplasmicSequence analysisAdd BLAST55
Transmembranei1199 – 1219HelicalSequence analysisAdd BLAST21
Topological domaini1220 – 1287LumenalSequence analysisAdd BLAST68
Transmembranei1288 – 1308HelicalSequence analysisAdd BLAST21
Topological domaini1309 – 1352CytoplasmicSequence analysisAdd BLAST44
Transmembranei1353 – 1373HelicalSequence analysisAdd BLAST21
Topological domaini1374 – 1376LumenalSequence analysis3
Transmembranei1377 – 1397HelicalSequence analysisAdd BLAST21
Topological domaini1398 – 1447CytoplasmicSequence analysisAdd BLAST50
<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 – 2154CytoplasmicSequence analysisAdd BLAST686
Transmembranei2155 – 2175HelicalSequence analysisAdd BLAST21
Topological domaini2176 – 2181LumenalSequence analysis6
Intramembranei2182 – 2200HelicalSequence analysisAdd BLAST19
Topological domaini2201LumenalSequence analysis1
Transmembranei2202 – 2222HelicalCuratedAdd BLAST21
Topological domaini2223 – 2235CytoplasmicSequence analysisAdd BLAST13
Transmembranei2236 – 2250Helical; Note=Signal for NS4BCuratedAdd BLAST15
Topological domaini2251 – 2285CytoplasmicSequence analysisAdd BLAST35
Intramembranei2286 – 2306HelicalSequence analysisAdd BLAST21
Topological domaini2307 – 2354LumenalSequence analysisAdd BLAST48
Transmembranei2355 – 2375HelicalSequence analysisAdd BLAST21
Topological domaini2376 – 2418CytoplasmicSequence analysisAdd BLAST43
Transmembranei2419 – 2439HelicalSequence analysisAdd BLAST21
Topological domaini2440 – 2467LumenalSequence analysisAdd BLAST28
Transmembranei2468 – 2488HelicalSequence analysisAdd BLAST21
Topological domaini2489 – 3401CytoplasmicSequence analysisAdd BLAST913

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_00004414701 – 3401Genome polyproteinAdd BLAST3401
ChainiPRO_00004414711 – 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_0000441472101 – 117ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST17
ChainiPRO_0000441473118 – 281Protein prMBy similarityAdd BLAST164
ChainiPRO_0000441474118 – 206Peptide prBy similarityAdd BLAST89
ChainiPRO_0000441475207 – 281Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000441476282 – 774Envelope protein EBy similarityAdd BLAST493
ChainiPRO_0000441477775 – 1126Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00004414781127 – 1351Non-structural protein 2ABy similarityAdd BLAST225
ChainiPRO_00004414791127 – 1317Non-structural protein 2A-alphaBy similarityAdd BLAST191
ChainiPRO_00004414801352 – 1480Serine protease subunit NS2BBy similarityAdd BLAST129
ChainiPRO_00004414811481 – 2102Serine protease NS3By similarityAdd BLAST622
ChainiPRO_00004414822103 – 2228Non-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_00004414832229 – 2251Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004414842252 – 2498Non-structural protein 4BBy similarityAdd BLAST247
ChainiPRO_00004414852499 – 3401RNA-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>Glycosylationi130N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi146N-linked (GlcNAc...) asparagine; by hostSequence analysis1
<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 bondi355 ↔ 386By similarity
Disulfide bondi373 ↔ 397By similarity
Disulfide bondi462 ↔ 564By similarity
Disulfide bondi581 ↔ 611By similarity
Disulfide bondi778 ↔ 789By similarity
Disulfide bondi829 ↔ 916By similarity
Glycosylationi904N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi952 ↔ 997By similarity
Glycosylationi981N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi1054 ↔ 1103By similarity
Disulfide bondi1065 ↔ 1087By similarity
Disulfide bondi1086 ↔ 1090By 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 residuei2554PhosphoserineBy 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. The nascent capsid protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature capsid protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Specific enzymatic cleavages in vivo yield mature proteins peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. 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
Polyubiquitinated; ubiquitination is probably mediated by host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is not ISGylated or sumoylated.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
Sitei117 – 118Cleavage; by host signal peptidaseBy similarity2
Sitei206 – 207Cleavage; by host furinBy similarity2
Sitei281 – 282Cleavage; by host signal peptidaseBy similarity2
Sitei774 – 775Cleavage; by host signal peptidaseBy similarity2
Sitei1126 – 1127Cleavage; by hostBy similarity2
Sitei1351 – 1352Cleavage; by viral protease NS3By similarity2
Sitei1480 – 1481Cleavage; by hostBy similarity2
Sitei2102 – 2103Cleavage; by autolysisBy similarity2
Sitei2228 – 2229Cleavage; by viral protease NS3By similarity2
Sitei2251 – 2252Cleavage; by host signal peptidaseBy similarity2
Sitei2498 – 2499Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

<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). NS3 interacts with host PDCD6IP; this interaction contributes to virion release (By similarity).

By similarity

Interacts with serine protease NS3 (By similarity).

By similarity

Homodimer (By similarity).

Interacts with host STAT2; this interaction prevents the establishment of cellular antiviral state (By similarity).

Interacts with serine protease NS3 (By similarity).

Interacts with host TRIM23; this interaction leads to NS5 ubiquitination (By similarity).

By similarity

GO - Molecular functioni

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

3D structure databases

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

More...
SMRi
C8XPB2

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>Domaini1481 – 1661Peptidase S7PROSITE-ProRule annotationAdd BLAST181
Domaini1665 – 1821Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1816 – 1995Helicase C-terminalPROSITE-ProRule annotationAdd BLAST180
Domaini2499 – 2763mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3026 – 3178RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni379 – 392Fusion peptideBy similarityAdd BLAST14
Regioni1404 – 1443Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1669 – 1672Important 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>Motifi1769 – 1772DEAH boxPROSITE-ProRule annotation4
Motifi2869 – 2902Nuclear localization signalBy similarityAdd BLAST34

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 biasi702 – 705Poly-SerSequence analysis4
Compositional biasi2862 – 2866Poly-ProSequence analysis5

<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
1.10.8.970, 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.

C8XPB2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPVRPRNKPK GVNVMAAGKV AQKIKNKLKS KAKAIGNISK GLRGFILFIL
60 70 80 90 100
AQIFWARKLT PRVRTMWKKV DKAKATRVLK GIRNIATQLI TGLAGRKKRR
110 120 130 140 150
SMTHGIILSL GVTMVIGASL HHHGGRYLLN VTHADLGKTF TIGSGNCTAN
160 170 180 190 200
IVEAGSWCSD SMEYECVTLA EAEEPDDIDC WCRGVERVRV TYGRCKNGLD
210 220 230 240 250
SRRSRRAAVI TAHIDKGLTT RQEKWLSTSM GERQIQRIER WMMRNPFYAA
260 270 280 290 300
ISLLLAWWVG SDIKQKVLIA FLVLAIGPAY STHCVGIPKR DFVQGVQGNT
310 320 330 340 350
WVNLVLDQGS CVTLSSDNKP SVDIWLDSIF ISSPVLVRRV SHTATISDTK
360 370 380 390 400
VQTACPTNGE AKLEEEASAE YECKKTYSDR GWGNGCGLFG KGSIVACAKY
410 420 430 440 450
TSTGHMDVYE IDSTKIEYVT KAQVHAGMKH DDTTMVKEVK FEPTTGSMDV
460 470 480 490 500
EFTGYGTLGL ECHVQTMVDM ANYYLVVMGQ EAWLVHKQWV EDITLPWKIG
510 520 530 540 550
EGGFWRDKHY MVEFTEPHAT TMTVMVLGAQ EGALRTALAG AMVVTYTDSS
560 570 580 590 600
GTKKFSLKGG HVSCKARMNG LVLKGSTYTM CKGGFSFVKT PTDTGHGTAV
610 620 630 640 650
MQVKVSKGTP CRIPVQAVDS SNGGTNRATL ITANPIAATT EDEVMIELSP
660 670 680 690 700
PYGESYIMIG TGDDKLTYHW HKSGSTIGSL FTETYKGAQR MAIIGDDAWD
710 720 730 740 750
FSSSSNFFNS IGKALHTVFG NVFHSIFGGL SWITKIILGG MFLWLGVNSR
760 770 780 790 800
NQTMCMVLMA VGGILLFMTL GVSGEVGCSL DIKRRELKCG DGLFLFNDVN
810 820 830 840 850
DWTHKYKFHP EDPKLLASLI KKSHQEGRCG LSSVNEVEHR MWNSIKTEIN
860 870 880 890 900
AMFEENGVDL SVVVKDSKLH YKMGSHAFPK VEEGLSLGWK NWGKSLVFEP
910 920 930 940 950
KQSNVSFIID GTSEDCPFTN RIWNAFVVEE FGIGMFTTNV FLTHKVDFTK
960 970 980 990 1000
QCDASLLGAG VKGDVAVHGD PTLWMESRKE NGTWQLHTIQ MNGLRECFWP
1010 1020 1030 1040 1050
QTHTIHGSSV MESAMFLPKQ YGGPVSHHNH YTGYAVQTAG PWNVQPLIVK
1060 1070 1080 1090 1100
RETCPGTQVR VDEQCRDRGN SVRSTTSEGK IIPEWCCRSC TLPPVSFWGP
1110 1120 1130 1140 1150
DSCWYAMEIR PQNVHEEHLV RSWASAGTGM AESSLGLVAL FLFTDIFARK
1160 1170 1180 1190 1200
RMTRKFMVIG CLGVLSVMIV GGFTALDLIR YIIVVGQHFA SMNHGGDVAY
1210 1220 1230 1240 1250
LAIIAVGKLR PGLLMMYSFK AAWSPKERVM VALGLLVFQA VLGDFVHTGL
1260 1270 1280 1290 1300
WEWADAAGMC ILIIQGMATR KEKTYIMPIL ALLTPLSMEI IRKTGIFACV
1310 1320 1330 1340 1350
GLLGLSLWRG GDTTMRKGMP LLAGAATAAS GLTRASLSVV FILCATAASR
1360 1370 1380 1390 1400
RSWPIGEIMA IVGIVGTGFG MAVNDQASLA GPMLVFGLIM IVYATLGRAD
1410 1420 1430 1440 1450
GLTLKRVGDI TWEEEAVHSG SSTRYDVTLN EAGEFKLVHE EPVVWSHVVF
1460 1470 1480 1490 1500
LVVALIAASV HPIALVVVTI IWTYGKKHLR GGVLWDIPIA PPVEEAEPLE
1510 1520 1530 1540 1550
DGVYAILQSG LMGKAQAGVG VAQEGVFHTM WHVTRGGFLM VGGKRLTPHW
1560 1570 1580 1590 1600
ASVKRDLICY GGNWKLDGKW DGVEEVQLIA VAPGKAPTNV QTKPGVFRMA
1610 1620 1630 1640 1650
DGTEIGAVAL DYPSGTSGSP IVNEKGQVIG LYGNGIVIGG SGYVSSIAQI
1660 1670 1680 1690 1700
AGGEGVTEEP LLDTATMLRK GKLTVLDYHP GAGKTRIFLP YILKECVRRK
1710 1720 1730 1740 1750
LRTLVLAPTR VVLSEMREAL RDVAVKYHTQ AFQAAGTGRE LVDAMCHATL
1760 1770 1780 1790 1800
SHRMLESSRS VNWEVIIMDE AHYMDPTSIA ARGWAAHKAN NHESAVIFMT
1810 1820 1830 1840 1850
ATPPGSANEF PESNGEIEDL RRDIPTEPWN KGHEWILEDR RPTVWFLPSI
1860 1870 1880 1890 1900
RAANNIAACL RRSERSVVVL NRQTFETVYP TIKTKKPDFI LATDIAEMGA
1910 1920 1930 1940 1950
NLGVERVIDC RTSYKPVLTT DGRVVIKGPL RIPASAAAQR RGRVGRCKDR
1960 1970 1980 1990 2000
DTDSYVYSEE TSEDNGHYVC WTEASMLLDN MEVKGGMVAP LYDVEAQKTE
2010 2020 2030 2040 2050
MVPGEARLRD DQRKVFRTLI KRYDLPVWVS WQVAKSGLML EDRKWCFDGD
2060 2070 2080 2090 2100
DENTILNDNG EKILARSPGG QRKFLCPRWN DSRLYYDNAS LMSFLAFAEG
2110 2120 2130 2140 2150
RRSYLGVWHA VQMAPLKLGE KLTESLDTMV MLMRSEEGTR AYKLASTNAP
2160 2170 2180 2190 2200
EAVTILLMTG IVVACTLGVG LAFMWPKGVD KMSMGMITMS IAGYLMLQGG
2210 2220 2230 2240 2250
LTPVQVASVL LIFFIFMVVL IPEAGTQRSI NDNKTLYVLL GVALLIGAIT
2260 2270 2280 2290 2300
ANEMGYLEKT KRDLLGERVQ NEWKLELPMF DLRPGAAWSI YVGLATLVMP
2310 2320 2330 2340 2350
VLDHWIRTEY GSLSLTGIAQ QASILQAMDK GVPFFKLNMS VIVLLVSVWN
2360 2370 2380 2390 2400
NFSMLSVLCG VGLLGVHCAF VLPGLRAQAA KQAQRRVYHG VAKNPVVDGQ
2410 2420 2430 2440 2450
TTAEIETAPE MPPLYEKKLA LVLLGVVAIA NGVMVRSAFS MAETVVLLSA
2460 2470 2480 2490 2500
AVGPLLEGNT SAIWNGPMAV AMAGIMRGNY YAGIGLAYNL WILQSPKRGR
2510 2520 2530 2540 2550
STTMTLGELW KRQLNLMGKR EFELYKITDI HEVDRSQAQA VMKAGIDNVG
2560 2570 2580 2590 2600
ISVSRGTSKL KWMVDRNYVE PLGRVVDLGC GRGGWSYLCA ASKRVSSVKA
2610 2620 2630 2640 2650
YTLGITGHEK PVNVQSLGWN IIKFKDKTDV FKMEPHACET LLCDIGESSS
2660 2670 2680 2690 2700
NPLVEMERTL KVIDNVERWM SPTTESYCFK VLAPYRPEVI ERLERFQLKY
2710 2720 2730 2740 2750
GGGIVRVPFS RNSTHEMYYV SGVKNNLTHM VSCVSRLLLR RMTHPDGRCK
2760 2770 2780 2790 2800
VEADVVFPTG TRNVASDLGP MDLSKVKDRV NRLRSEQGTW FQDDSHPYRT
2810 2820 2830 2840 2850
WHYLGSYVAK QSGSAATMVN GVVKMLSMPW DRIENVTQLA MTDTTPYGQQ
2860 2870 2880 2890 2900
RVFKEKVDTR APPPPPGTRA IMEVVNKWMF DFLAREKAPR ICTKEEFINK
2910 2920 2930 2940 2950
VRSNAALGNM LEEQDGWKDA ATAVQDPRFW ALVDRERQVH LEGRCETCIY
2960 2970 2980 2990 3000
NMMGKREKKP AEFGKAKGSR AIWYMWLGAR FLEFEALGFL NEDHWFGREN
3010 3020 3030 3040 3050
SLAGVEGVGL QYLGYVVKNV WEKSNGIMYA DDTAGWDTRV TEADLDDEQY
3060 3070 3080 3090 3100
LLSKMEGYHK KLASAVMNMT YKYKVVKVPR PGPGGKVFMD VIARQDQRGS
3110 3120 3130 3140 3150
GQVVTYPLNT GTNMKVQLIR MAEGEGVISR HDIERVTIKT LNALRVWLAE
3160 3170 3180 3190 3200
NGAERLSRMA VSGDDCVVAP LDERFGLALH HLNAMSKIRK DIDDWTESIP
3210 3220 3230 3240 3250
WRSWESVPFC SHHFHQLFLK DGRSIVVPCR DQDELVGRAR VSPGNGWKLK
3260 3270 3280 3290 3300
ETACLSKAYA QMWLLMYFHK RDLRLMGNAI CSSVPAHWVP TGRTTWSIHA
3310 3320 3330 3340 3350
HNEWISSERM LDVWNKVWIV DNPHMPDKTC IDDWRDVPYL PKSQDRLCGS
3360 3370 3380 3390 3400
LIGITARASW AENIRAVVNK IRGMIGNEVY SDHLSVMGRY TYSVQEVGTV

L
Length:3,401
Mass (Da):377,294
Last modified:November 3, 2009 - 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:i7CE3AD4F322122C2
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
DQ859060 Genomic RNA Translation: ABI54476.1

NCBI Reference Sequences

More...
RefSeqi
YP_009256192.1, NC_030289.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
27964207

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:27964207

<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
DQ859060 Genomic RNA Translation: ABI54476.1
RefSeqiYP_009256192.1, NC_030289.1

3D structure databases

SMRiC8XPB2
ModBaseiSearch...

Protein family/group databases

MEROPSiS07.001

Genome annotation databases

GeneIDi27964207
KEGGivg:27964207

Family and domain databases

CDDicd12149, Flavi_E_C, 1 hit
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_EHV
<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: C8XPB2
<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: November 3, 2009
Last modified: August 12, 2020
This is version 82 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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