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Entry version 91 (12 Aug 2020)
Sequence version 1 (28 Jul 2009)
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Protein

Genome polyprotein

Gene
N/A
Organism
Wesselsbron virus (WSLV)
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 sitei1531Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1555Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1616Charge 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
Sitei2512mRNA cap bindingPROSITE-ProRule annotation1
Sitei2515mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2516mRNA cap bindingPROSITE-ProRule annotation1
Sitei2518mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2523mRNA cap bindingPROSITE-ProRule annotation1
Sitei2527mRNA 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 sitei2555S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2560For 2'-O-MTase activityBy similarity1
Sitei2560Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2585S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2586S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2603S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2604S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2631S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2645For 2'-O-MTase activityBy similarity1
Sitei2645Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2646S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2649mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2681For 2'-O-MTase activityBy similarity1
Sitei2681Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2712mRNA cap bindingPROSITE-ProRule annotation1
Sitei2714mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2717For 2'-O-MTase activityBy similarity1
Sitei2717Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2719S-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 bindingi2938Zinc 1By similarity1
Metal bindingi2942Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2947Zinc 1By similarity1
Metal bindingi2950Zinc 1By similarity1
Metal bindingi3215Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3231Zinc 2By similarity1
Metal bindingi3350Zinc 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 bindingi1677 – 1684ATPPROSITE-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>OrganismiWesselsbron virus (WSLV)
<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 identifieri164416 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesRiboviriaFlaviviridaeFlavivirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiAedes [TaxID: 7158]
Capra hircus (Goat) [TaxID: 9925]
Homo sapiens (Human) [TaxID: 9606]
Ovis aries (Sheep) [TaxID: 9940]
<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
  • UP000123687 <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 – 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 – 239ExtracellularSequence analysisAdd BLAST119
Transmembranei240 – 260HelicalSequence analysisAdd BLAST21
Topological domaini261 – 265CytoplasmicSequence analysis5
Transmembranei266 – 280HelicalCuratedAdd BLAST15
Topological domaini281 – 720ExtracellularSequence analysisAdd BLAST440
Transmembranei721 – 741HelicalSequence analysisAdd BLAST21
Topological domaini742 – 749CytoplasmicSequence analysis8
Transmembranei750 – 770HelicalSequence analysisAdd BLAST21
Topological domaini771 – 1126ExtracellularSequence analysisAdd BLAST356
Transmembranei1127 – 1147HelicalSequence analysisAdd BLAST21
Topological domaini1148 – 1184CytoplasmicSequence analysisAdd BLAST37
Transmembranei1185 – 1205HelicalSequence analysisAdd BLAST21
Topological domaini1206 – 1283LumenalSequence analysisAdd BLAST78
Transmembranei1284 – 1304HelicalSequence analysisAdd BLAST21
Topological domaini1305 – 1350CytoplasmicSequence analysisAdd BLAST46
Transmembranei1351 – 1371HelicalSequence analysisAdd BLAST21
Topological domaini1372 – 1373LumenalSequence analysis2
Transmembranei1374 – 1394HelicalSequence analysisAdd BLAST21
Topological domaini1395 – 1450CytoplasmicSequence analysisAdd BLAST56
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1451 – 1471HelicalSequence analysisAdd BLAST21
Topological domaini1472 – 2154CytoplasmicSequence analysisAdd BLAST683
Transmembranei2155 – 2175HelicalSequence analysisAdd BLAST21
Topological domaini2176 – 2181LumenalSequence analysis6
Intramembranei2182 – 2200HelicalCuratedAdd BLAST19
Topological domaini2201LumenalSequence analysis1
Transmembranei2202 – 2222HelicalSequence analysisAdd BLAST21
Topological domaini2223 – 2234CytoplasmicSequence analysisAdd BLAST12
Transmembranei2235 – 2255Helical; Note=Signal for NS4BCuratedAdd BLAST21
Topological domaini2256 – 2286LumenalSequence analysisAdd BLAST31
Intramembranei2287 – 2307HelicalSequence analysisAdd BLAST21
Topological domaini2308 – 2355LumenalSequence analysisAdd BLAST48
Transmembranei2356 – 2376HelicalSequence analysisAdd BLAST21
Topological domaini2377 – 2419CytoplasmicSequence analysisAdd BLAST43
Transmembranei2420 – 2440HelicalSequence analysisAdd BLAST21
Topological domaini2441 – 2468LumenalSequence analysisAdd BLAST28
Transmembranei2469 – 2489HelicalSequence analysisAdd BLAST21
Topological domaini2490 – 3405CytoplasmicSequence analysisAdd BLAST916

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_00004415911 – 3405Genome polyproteinAdd BLAST3405
ChainiPRO_00004415921 – 99Capsid protein CBy similarityAdd BLAST99
<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_0000441593100 – 116ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST17
ChainiPRO_0000441594117 – 280Protein prMBy similarityAdd BLAST164
ChainiPRO_0000441595117 – 205Peptide prBy similarityAdd BLAST89
ChainiPRO_0000441596206 – 280Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000441597281 – 770Envelope protein EBy similarityAdd BLAST490
ChainiPRO_0000441598771 – 1123Non-structural protein 1By similarityAdd BLAST353
ChainiPRO_00004415991124 – 1349Non-structural protein 2ABy similarityAdd BLAST226
ChainiPRO_00004416001124 – 1315Non-structural protein 2A-alphaBy similarityAdd BLAST192
ChainiPRO_00004416011350 – 1479Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00004416021480 – 2102Serine protease NS3By similarityAdd BLAST623
ChainiPRO_00004416032103 – 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_00004416042229 – 2251Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004416052252 – 2499Non-structural protein 4BBy similarityAdd BLAST248
ChainiPRO_00004416062500 – 3405RNA-directed RNA polymerase NS5By similarityAdd BLAST906

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 bondi283 ↔ 310By similarity
Disulfide bondi340 ↔ 401By similarity
Disulfide bondi340 ↔ 396By similarity
Disulfide bondi354 ↔ 385By similarity
Disulfide bondi372 ↔ 401By similarity
Disulfide bondi372 ↔ 396By similarity
Disulfide bondi462 ↔ 560By similarity
Disulfide bondi577 ↔ 607By similarity
Disulfide bondi774 ↔ 785By similarity
Disulfide bondi825 ↔ 913By similarity
Glycosylationi900N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi949 ↔ 994By similarity
Glycosylationi978N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi1051 ↔ 1100By similarity
Disulfide bondi1062 ↔ 1084By similarity
Disulfide bondi1083 ↔ 1087By 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 residuei2555PhosphoserineBy 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
Sitei99 – 100Cleavage; by viral protease NS3By similarity2
Sitei116 – 117Cleavage; by host signal peptidaseBy similarity2
Sitei205 – 206Cleavage; by host furinBy similarity2
Sitei280 – 281Cleavage; by host signal peptidaseBy similarity2
Sitei770 – 771Cleavage; by host signal peptidaseBy similarity2
Sitei1123 – 1124Cleavage; by hostBy similarity2
Sitei1349 – 1350Cleavage; by viral protease NS3By similarity2
Sitei1479 – 1480Cleavage; by autolysisBy similarity2
Sitei2102 – 2103Cleavage; by autolysisBy similarity2
Sitei2228 – 2229Cleavage; by viral protease NS3By similarity2
Sitei2251 – 2252Cleavage; by host signal peptidaseBy similarity2
Sitei2499 – 2500Cleavage; 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).

By similarity

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

By similarity

Homodimer; Homohexamer when secreted.

Interacts with envelope protein E (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 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).

Interacts with NS1 (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
C5H431

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>Domaini1480 – 1659Peptidase S7PROSITE-ProRule annotationAdd BLAST180
Domaini1664 – 1820Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1831 – 1992Helicase C-terminalPROSITE-ProRule annotationAdd BLAST162
Domaini2500 – 2764mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3028 – 3180RdRp 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>Regioni378 – 391Fusion peptideBy similarityAdd BLAST14
Regioni1402 – 1441Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1668 – 1671Important 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>Motifi1768 – 1771DEAH boxPROSITE-ProRule annotation4
Motifi2871 – 2904Nuclear 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 biasi2816 – 2819Poly-SerSequence analysis4
Compositional biasi2864 – 2868Poly-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.

C5H431-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATKGMNKSR ARSRGVNMVA ARVKNLAVKV KNKTKQSARG LRGFLLFLVA
60 70 80 90 100
QIFWARKLTP QVKRLWRMVD KVQGLRILKN IRNIVTNLMK GLAGRKKKRS
110 120 130 140 150
LTVPLVLLLI PLIAYSATVT RQRGLGLLLN VTFADVGKTY EVEGGNCSVN
160 170 180 190 200
TLDAGKWCED YVEYECVTLS EGEEPDDLDC WCYGVDNVRV TYGRCKSGGS
210 220 230 240 250
RRSRRSAVIT PHVDKGLTTR QEKWLPTKIG EQQLQKVEKW IMRNPLYALG
260 270 280 290 300
AVALAYFVGT SNVQRVVIAI LLLGIGPAYS THCLGIPKRD FIRGLDGNTW
310 320 330 340 350
VSVVLEQGSC VTLIADNKPS VDIWLSSIVV DTPTLVRKVC YASSVTGSKA
360 370 380 390 400
TGACPTMGDA HMSEEGNEEW ECKRSYSDRG WGNGCGLFGK GSIVACAKFS
410 420 430 440 450
CTHEMEVYQI DATKIEYTIS AQVHSGAKKD DWENHTKLVT FVPTTGTSTV
460 470 480 490 500
AFTGYGNFGL ECHVQMMVDL SNSYLVKVGT DAWLVNKQWV HDITLPWQSG
510 520 530 540 550
TGGHWRDKHF MVDFEEPHAV TMKALVLGSQ EGALRTALSG AMVVELNSNR
560 570 580 590 600
YSLKGGHVTC KAYMNNLILK GSTYSMCKRG MSFAKQPVET DHGTAVMQIK
610 620 630 640 650
VTTGAPCRIP VIAADSMAGT ENRGSVITTN PIAASNNDEV LVEISPPFGE
660 670 680 690 700
SYIIVGNGDD KLTYHWQRSG STIGNLFTET MKGAQRMIIT GEHSWDFGST
710 720 730 740 750
GGFFSSIAKA VHTVFGAAFH AIFGGLSWIT KILIGGLLIW LGLNSRSSSM
760 770 780 790 800
SMGFICIGAL LLVLATGVGA EVGCSLSWKQ REMKCGDGVF VFKDSDDWFS
810 820 830 840 850
KYQYIPEDPK TMATLIHQAH QDGLCGLSSV SDLEHRMWYS RVDEINAILD
860 870 880 890 900
ENEVDLTVVV QESDAVYLRG SHAFPRPKSE LKYGWKTWGK NIIFNPSRKN
910 920 930 940 950
GTFIIDGKSK AECPFNKRVW NSIRVEEFGT GVYQTRVFMR PEFDYTKLCD
960 970 980 990 1000
TGTLGAAVKG SVSAHGDPMF WMESEEINGT WMITTLEALN YRECEWPSSH
1010 1020 1030 1040 1050
TLDGAKVVES DMFMPRSLAG PISKHNHIPG YKVQTSGPWH NVPLEIKREE
1060 1070 1080 1090 1100
CPGTTVVVDE KCDDRAKSVR STTDSGKIIP EWCCRSCTMP PVSFWGPDGC
1110 1120 1130 1140 1150
WYSMEVRPKH TNEAHLVKSW VVASKGDVDP FSLGLLMLFL CSDMFLMKRF
1160 1170 1180 1190 1200
SMRAILVGSL VMLGAMTLGS LSYLDLLRYA ITVGMYMAEI NSGGDVTHLA
1210 1220 1230 1240 1250
LLAVFRVRAG FVSMLALKRL WSPREGFVAT CGIVMVQLAL GDILSTDIME
1260 1270 1280 1290 1300
WLNAAGMAVL IIKSIVEPKR CNAVLPLLCL LTPLTVAEIQ RAVMFVCSIV
1310 1320 1330 1340 1350
IFVTVWQTDS VSTRKTIPLV ALTVCSFFKW TSPFLGIVCY LAFTRLPQRS
1360 1370 1380 1390 1400
WPLGETMAAV GLVGVLAGMG LKDMNGMLGP VAVGGVLLIV MSLSGKVDGL
1410 1420 1430 1440 1450
VIKKVADVTW DEDAEISGAS HRYDVEQTDT GEFKLRNEEP APWIQVAVLT
1460 1470 1480 1490 1500
IAILSAATHP ACLAVVTIGW FAWQKTTTRS GVLWDIPTVV PPEEVSYLED
1510 1520 1530 1540 1550
GVYTINQNSF LGLAQKGVGV VKDGVFHTMW HVTRGAFLLH AGKRMTPSWA
1560 1570 1580 1590 1600
NVKEDLISYG GGWKLDAKWD GSEEVQLIAV SPGKVPVNVQ TTPSVFQLKN
1610 1620 1630 1640 1650
GKEIGAVNLD YPSGTSGSPI LNKNGDVIGL YGNGILIGNN TYVSAIAQSD
1660 1670 1680 1690 1700
SVEEGGTEQL QDIPTMLKKG MLTVLDFHPG AGKTRIYLPQ ILKECEKLKL
1710 1720 1730 1740 1750
KTLVLAPTRV VLSEMREAMP KMSIKYHTQA FSNTSTGKEI IDAMCHATLT
1760 1770 1780 1790 1800
HRMLEPTRVT NWEVVIMDEA HFMDPASIAA RGWAAHRSRA RECATIFMSA
1810 1820 1830 1840 1850
TPPGTSNEFP ESNGMIEDVK KDVPSEPWTK GHEWILEDRR PTAWFLPSIR
1860 1870 1880 1890 1900
IANSIANCLR KADRTVVVLN RKTFEKEYPT IKSKKPDFIL ATDIAEMGAN
1910 1920 1930 1940 1950
LKVERVIDCR TAYKPILVDD ATKVMVKGPL RISASSAAQR RGRIGRDPNR
1960 1970 1980 1990 2000
DTDTYIYGDS TTEDNGHYVC WTEGSMLLDN MEIRNGMIAP LYGVEGTKTT
2010 2020 2030 2040 2050
TSPGETRLRE DQRKVFRELV KRLDMPVWFS WQVAKAGLKV QDRSWCFDGE
2060 2070 2080 2090 2100
DDNTLLNDNG EPILARSPGG AKKPLKPRWV DTRVCSDNAS LIDFIKFAEG
2110 2120 2130 2140 2150
RRSASGILLG LQGFPEFLSG KMREAIDTVT VLYTSDTGSR AYKHALAMMP
2160 2170 2180 2190 2200
EATTIFLLVM LAIICTSGVI MFFLAPKGLS RMSMAMMTML VSAYLMSLGG
2210 2220 2230 2240 2250
MNPVQISCVM LVFFIFMVVL IPEPGTQRST YDNQIIYLLV GVLSLILLVA
2260 2270 2280 2290 2300
ANEMELLEKT KRDIFGAVVV EEAKRWTFPE FDLRPGAAWT VYVGLVTPGN
2310 2320 2330 2340 2350
PMLHHWIKID YGNISLSGIT QNAQVLGLMD RGIPFIKMNM SVVILLLSAW
2360 2370 2380 2390 2400
NGITLLPLFA GMGAAALHWG FILPGLRAQA AKAAQKRVYH GVAKNPVVDG
2410 2420 2430 2440 2450
NPTVDIDDAP GMPAMYEKKL ALVILLALSI LNLVLTRTPF ATAEMVVLGS
2460 2470 2480 2490 2500
AAVGPLIEGD TNAYWNGPIA VAFSGLMRGN YYATIGLAYN GWLAKQTRRG
2510 2520 2530 2540 2550
KAAGVTLGEV WKRQLNMLGK QEFERYKVPD ITEVDRTAAR RYLKEGRTDV
2560 2570 2580 2590 2600
GISVSRGAAK IRWLHERGYL RITGRVLDLG CGRGGWSYYA AAQKEVMSVK
2610 2620 2630 2640 2650
GYTLGIEGHE KPIHMQTLGW NIVKFKDKSN VFTMPTEPSD TLLCDIGESS
2660 2670 2680 2690 2700
SNPLVERDRT MKVLENFERW KHVNTENFCV KVLAPYHPDV IEKLERLQLR
2710 2720 2730 2740 2750
FGGGIVRVPF SRNSTHEMYY ISGARNNITH MVNTTSRSLL RRMTRPSGKA
2760 2770 2780 2790 2800
IIEGDVFLPT GTRSVASEAG TIDHEALKLR VDQIKAEYSK TWTHDSNHPY
2810 2820 2830 2840 2850
RTWHYLGSYL CKATGSSSSM INGIVKMLSM PWDKFESVTL LAMTDTTPFG
2860 2870 2880 2890 2900
QQRVFKEKVD TKAPPPPPGT RAIMRVVNAW LFQHLARKKK PRICTREEFV
2910 2920 2930 2940 2950
AKVRSHAALG AYLEEQDKWK SASEAVQDPQ FWKLVDDERK LHLQGQCRTC
2960 2970 2980 2990 3000
VYNMMGKREK KPSEFGKAKG SRAIWYMWLG ARFLEFEALG FLNEDHWVSR
3010 3020 3030 3040 3050
ENSGGGVEGT GLQYLGYILK ELGGKTGGNM YADDTAGWDT RITEEDLEDE
3060 3070 3080 3090 3100
QEILKYMDEK HKKLAWAVTE LAYKNKVVKV MRPGPGGLTF MDIISRRDQR
3110 3120 3130 3140 3150
GSGQVVTYAL NTVTNLKVQL IRMAEAEHVI TNFDVDTVSQ KTLQDLRCWL
3160 3170 3180 3190 3200
DRFGADRLSR MAVSGDDCVV KPIDDQFADA LTHLNSMSKI RKDIDDWKPS
3210 3220 3230 3240 3250
QGWASWEDVP FCSHHFHELI LKDGRSIIAP CRDQDELIGR ARVSPGNGWM
3260 3270 3280 3290 3300
IRETACLSKA YAQMWLLMYF HRRDLRVMAN AINSTVPVDW VPTGRTTWSI
3310 3320 3330 3340 3350
HGKGEWMTTE DMLQVWNRVW IEDNPHQTDK TPITEWRDIP YLPKSIDKTC
3360 3370 3380 3390 3400
NSLVGTTQRA SWARDIKHTV HRIRGLVGNE KYTDYLATMD RFRELDESGP

GEVLW
Length:3,405
Mass (Da):378,677
Last modified:July 28, 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:i87F7F9ECD26AE1FC
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
EU707555 Genomic RNA Translation: ACH70606.1

NCBI Reference Sequences

More...
RefSeqi
YP_002922020.1, NC_012735.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7943824

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:7943824

<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
EU707555 Genomic RNA Translation: ACH70606.1
RefSeqiYP_002922020.1, NC_012735.1

3D structure databases

SMRiC5H431
ModBaseiSearch...

Protein family/group databases

MEROPSiS07.001

Genome annotation databases

GeneIDi7943824
KEGGivg:7943824

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_WSLV
<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: C5H431
<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: July 28, 2009
Last modified: August 12, 2020
This is version 91 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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