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Entry version 150 (12 Aug 2020)
Sequence version 2 (08 Feb 2011)
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Protein

Genome polyprotein

Gene
N/A
Organism
St. louis encephalitis virus (strain MS1-7)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.By similarity
Inhibits RNA silencing by interfering with host Dicer.By similarity
Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.By similarity
Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.By similarity
Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).By similarity
Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response.By similarity
Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy similarity
Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.PROSITE-ProRule annotation
Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.By similarity
Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.By similarity
Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.By similarity

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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1550Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1574Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1634Charge 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>Sitei1956Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1959Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2537mRNA cap bindingPROSITE-ProRule annotation1
Sitei2540mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2541mRNA cap bindingPROSITE-ProRule annotation1
Sitei2543mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2548mRNA cap bindingPROSITE-ProRule annotation1
Sitei2552mRNA 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 sitei2580S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2585For 2'-O-MTase activityBy similarity1
Sitei2585Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2610S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2611S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2628S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2629S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2655S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2656S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2670For 2'-O-MTase activityBy similarity1
Sitei2670Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2671S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2674mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2706For 2'-O-MTase activityBy similarity1
Sitei2706Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2737mRNA cap bindingPROSITE-ProRule annotation1
Sitei2739mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2742For 2'-O-MTase activityBy similarity1
Sitei2742Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2744S-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 bindingi2964Zinc 1By similarity1
Metal bindingi2968Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2973Zinc 1By similarity1
Metal bindingi2976Zinc 1By similarity1
Metal bindingi3241Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3257Zinc 2By similarity1
Metal bindingi3376Zinc 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 bindingi1693 – 1700ATPPROSITE-ProRule annotation8

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

GO - Biological processi

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

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

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S07.003

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.15, EC:3.6.4.13)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
NS5
<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>OrganismiSt. louis encephalitis virus (strain MS1-7)
<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 identifieri11081 [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 hostiAgelaius tricolor (Tricolored blackbird) [TaxID: 9191]
Cardinalis cardinalis (Northern cardinal) [TaxID: 98964]
Columba livia (Rock dove) [TaxID: 8932]
Culex nigripalpus [TaxID: 42429]
Culex pipiens (House mosquito) [TaxID: 7175]
Culex quinquefasciatus (Southern house mosquito) (Culex pungens) [TaxID: 7176]
Culex tarsalis (Encephalitis mosquito) [TaxID: 7177]
Cyanocitta cristata (Blue jay) [TaxID: 28727]
Euphagus cyanocephalus (Brewer's blackbird) [TaxID: 84817]
Haemorhous mexicanus (House finch) (Carpodacus mexicanus) [TaxID: 30427]
Homo sapiens (Human) [TaxID: 9606]
Mimus polyglottos (Northern mockingbird) [TaxID: 60713]
Passer domesticus (House sparrow) (Fringilla domestica) [TaxID: 48849]
Turdus migratorius (American robin) [TaxID: 9188]
Zenaida macroura (Mourning dove) [TaxID: 47245]

<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 domaini2 – 108CytoplasmicSequence analysisAdd BLAST107
<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>Transmembranei109 – 129HelicalSequence analysisAdd BLAST21
Topological domaini130 – 247ExtracellularSequence analysisAdd BLAST118
Transmembranei248 – 268HelicalSequence analysisAdd BLAST21
Topological domaini269 – 273CytoplasmicSequence analysis5
Transmembranei274 – 288HelicalCuratedAdd BLAST15
Topological domaini289 – 741ExtracellularSequence analysisAdd BLAST453
Transmembranei742 – 762HelicalSequence analysisAdd BLAST21
Topological domaini763 – 768CytoplasmicSequence analysis6
Transmembranei769 – 789HelicalSequence analysisAdd BLAST21
Topological domaini790 – 1214ExtracellularSequence analysisAdd BLAST425
Transmembranei1215 – 1235HelicalSequence analysisAdd BLAST21
Topological domaini1236 – 1245CytoplasmicSequence analysis10
Transmembranei1246 – 1266HelicalSequence analysisAdd BLAST21
Topological domaini1267 – 1288LumenalSequence analysisAdd BLAST22
Transmembranei1289 – 1303HelicalSequence analysisAdd BLAST15
Topological domaini1304CytoplasmicSequence analysis1
Transmembranei1305 – 1325HelicalSequence analysisAdd BLAST21
Topological domaini1326 – 1339LumenalSequence analysisAdd BLAST14
Transmembranei1340 – 1360HelicalSequence analysisAdd BLAST21
Topological domaini1361 – 1369CytoplasmicSequence analysis9
Transmembranei1370 – 1390HelicalSequence analysisAdd BLAST21
Topological domaini1391 – 1393LumenalSequence analysis3
Transmembranei1394 – 1414HelicalSequence analysisAdd BLAST21
Topological domaini1415 – 1471CytoplasmicSequence analysisAdd BLAST57
<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>Intramembranei1472 – 1492HelicalSequence analysisAdd BLAST21
Topological domaini1493 – 2167CytoplasmicSequence analysisAdd BLAST675
Transmembranei2168 – 2188HelicalSequence analysisAdd BLAST21
Topological domaini2189 – 2193LumenalSequence analysis5
Intramembranei2194 – 2214HelicalSequence analysisAdd BLAST21
Topological domaini2215LumenalSequence analysis1
Transmembranei2216 – 2236HelicalSequence analysisAdd BLAST21
Topological domaini2237 – 2251CytoplasmicSequence analysisAdd BLAST15
Transmembranei2252 – 2266Helical; Note=Signal for NS4BSequence analysisAdd BLAST15
Topological domaini2267 – 2308LumenalSequence analysisAdd BLAST42
Intramembranei2309 – 2329HelicalSequence analysisAdd BLAST21
Topological domaini2330 – 2376LumenalSequence analysisAdd BLAST47
Transmembranei2377 – 2397HelicalSequence analysisAdd BLAST21
Topological domaini2398 – 2440CytoplasmicSequence analysisAdd BLAST43
Transmembranei2441 – 2461HelicalSequence analysisAdd BLAST21
Topological domaini2462 – 2466LumenalSequence analysis5
Transmembranei2467 – 2487HelicalSequence analysisAdd BLAST21
Topological domaini2488 – ›3412CytoplasmicSequence analysisAdd BLAST›925

GO - Cellular componenti

Keywords - Cellular componenti

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

<p>This section 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_00004051431 – ›3412Genome polyproteinAdd BLAST›3412
ChainiPRO_00000377351 – 103Capsid protein CBy similarityAdd BLAST103
<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_0000405144104 – 121ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST18
ChainiPRO_0000405145122 – 288Protein prMBy similarityAdd BLAST167
ChainiPRO_0000037736122 – 213Peptide prBy similarityAdd BLAST92
ChainiPRO_0000037737214 – 288Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037738289 – 789Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000037739790 – 1141Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000377401142 – 1368Non-structural protein 2ABy similarityAdd BLAST227
ChainiPRO_00000377411369 – 1499Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000377421500 – 2117Serine protease NS3By similarityAdd BLAST618
ChainiPRO_00004051462118 – 2243Non-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_00004051472244 – 2266Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004051482267 – 2524Non-structural protein 4BBy similarityAdd BLAST258
ChainiPRO_00004051492525 – ›3412RNA-directed RNA polymerase NS5By similarityAdd BLAST›888

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>Glycosylationi136N-linked (GlcNAc...) asparagine; by hostBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi291 ↔ 318By similarity
Disulfide bondi348 ↔ 409By similarity
Disulfide bondi348 ↔ 404By similarity
Disulfide bondi362 ↔ 393By similarity
Disulfide bondi380 ↔ 409By similarity
Disulfide bondi380 ↔ 404By similarity
Disulfide bondi478 ↔ 576By similarity
Disulfide bondi593 ↔ 624By similarity
Disulfide bondi793 ↔ 804By similarity
Disulfide bondi844 ↔ 932By similarity
Glycosylationi919N-linked (GlcNAc...) asparagine; by hostBy similarity1
Glycosylationi964N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi968 ↔ 1012By similarity
Glycosylationi996N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi1069 ↔ 1118By similarity
Disulfide bondi1080 ↔ 1102By similarity
Disulfide bondi1080 ↔ 1101By similarity
Disulfide bondi1101 ↔ 1105By similarity
Disulfide bondi1102 ↔ 1105By 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 residuei2580PhosphoserineBy similarity1

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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei103 – 104Cleavage; by viral protease NS3By similarity2
Sitei121 – 122Cleavage; by host signal peptidaseBy similarity2
Sitei213 – 214Cleavage; by host furinBy similarity2
Sitei288 – 289Cleavage; by host signal peptidaseBy similarity2
Sitei789 – 790Cleavage; by host signal peptidaseBy similarity2
Sitei1141 – 1142Cleavage; by hostBy similarity2
Sitei1368 – 1369Cleavage; by viral protease NS3By similarity2
Sitei1499 – 1500Cleavage; by autolysisBy similarity2
Sitei2117 – 2118Cleavage; by autolysisBy similarity2
Sitei2243 – 2244Cleavage; by viral protease NS3By similarity2
Sitei2266 – 2267Cleavage; by host signal peptidaseBy similarity2
Sitei2524 – 2525Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P09732

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

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

Homodimer (By similarity).

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

By similarity

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

By similarity

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

Interacts with protein prM (By similarity).

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

By similarity

Homodimer; Homohexamer when secreted (By similarity).

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

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

By similarity

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

By similarity

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

By similarity

Forms a heterodimer with NS2B (By similarity).

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

Interacts with NS4B (By similarity).

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

By similarity

Interacts with serine protease NS3 (By similarity).

By similarity

Homodimer.

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

Interacts with serine protease NS3.

By similarity

GO - Molecular functioni

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

3D structure databases

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

More...
SMRi
P09732

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Domaini1500 – 1677Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1680 – 1836Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1847 – 2011Helicase C-terminalPROSITE-ProRule annotationAdd BLAST165
Domaini2525 – 2790mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3054 – 3206RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 15Interaction with host EXOC1By similarityAdd BLAST14
Regioni37 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni386 – 399Fusion peptideBy similarityAdd BLAST14
Regioni1422 – 1461Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1684 – 1687Important for RNA-bindingBy similarity4
Regioni2162 – 2166Regulates the ATPase activity of NS3 helicaseBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1784 – 1787DEAH boxPROSITE-ProRule annotation4

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The transmembrane domains of the small envelope protein M and envelope protein E contain an endoplasmic reticulum retention signal.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the N-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type methyltransferase family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12149, Flavi_E_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.930, 1 hit
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.40.10.10, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit

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
IPR001122, Flavi_capsidC
IPR037172, Flavi_capsidC_sf
IPR027287, Flavi_E_Ig-like
IPR026470, Flavi_E_Stem/Anchor_dom
IPR038345, Flavi_E_Stem/Anchor_dom_sf
IPR001157, Flavi_NS1
IPR000752, Flavi_NS2A
IPR000487, Flavi_NS2B
IPR000404, Flavi_NS4A
IPR001528, Flavi_NS4B
IPR002535, Flavi_propep
IPR038688, Flavi_propep_sf
IPR000336, Flavivir/Alphavir_Ig-like_sf
IPR001850, Flavivirus_NS3_S7
IPR014412, Gen_Poly_FLV
IPR011998, Glycoprot_cen/dimer
IPR036253, Glycoprot_cen/dimer_sf
IPR038055, Glycoprot_E_dimer_dom
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR014756, Ig_E-set
IPR026490, mRNA_cap_0/1_MeTrfase
IPR027417, P-loop_NTPase
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR000208, RNA-dir_pol_flavivirus
IPR007094, RNA-dir_pol_PSvirus
IPR002877, rRNA_MeTrfase_FtsJ_dom
IPR029063, SAM-dependent_MTases

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01003, Flavi_capsid, 1 hit
PF07652, Flavi_DEAD, 1 hit
PF02832, Flavi_glycop_C, 1 hit
PF00869, Flavi_glycoprot, 1 hit
PF01004, Flavi_M, 1 hit
PF00948, Flavi_NS1, 1 hit
PF01005, Flavi_NS2A, 1 hit
PF01002, Flavi_NS2B, 1 hit
PF01350, Flavi_NS4A, 1 hit
PF01349, Flavi_NS4B, 1 hit
PF00972, Flavi_NS5, 1 hit
PF01570, Flavi_propep, 1 hit
PF01728, FtsJ, 1 hit
PF00949, Peptidase_S7, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF003817, Gen_Poly_FLV, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF101257, SSF101257, 1 hit
SSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 2 hits
SSF53335, SSF53335, 1 hit
SSF56672, SSF56672, 1 hit
SSF56983, SSF56983, 1 hit
SSF81296, SSF81296, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR04240, flavi_E_stem, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51527, FLAVIVIRUS_NS2B, 1 hit
PS51528, FLAVIVIRUS_NS3PRO, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51591, RNA_CAP01_NS5_MT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Fragment.

<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.

P09732-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKKPGKPGR NRVVNMLKRG VSRVNPLTGL KRILGSLLDG RGPVRFILAI
60 70 80 90 100
LTFFRFTALQ PTEALKRRWR AVDKRTALKH LNGFKRDLGS MLDTINRRPS
110 120 130 140 150
KKRGGTRSLL GLAALIGLAS SLQLSTYQGK VLMSINKTDA QSAINIPSAN
160 170 180 190 200
GANTCIVRAL DVGVMCKNDI TYLCPVLSAG NDPEDIDCWC DVEEVWVHYG
210 220 230 240 250
RCTRMGHSRR SRRSISVQHH GDSTLATKNT PWLDTVKTTK YLTKVENWVL
260 270 280 290 300
RNPGYALVAL AIGWMLGSNN TQRVVFVIML MLIAPAYSFN CLGTSNRDFV
310 320 330 340 350
EGASGATWID LVLEGGSCVT VMAPEKPTLD FKVMKMEATE LATVREYCYE
360 370 380 390 400
ATLDTLSTVA RCPTTGEAHN TKRSDPTFVC KRDVVDRGWG NGCGLFGKGS
410 420 430 440 450
IDTCAKFTCK NKATGKTILR ENIKYEVAIF VHGSTDSTSH GNYFEQIGKN
460 470 480 490 500
QAARFTISPQ APSFTANMGE YGTVTIDCEA RSGINTEDYY VFTVKEKSWL
510 520 530 540 550
VNRDWFHDLN LPWTSPATTD WRNRETLVEF EEPHATKQTV VALGSQEGAL
560 570 580 590 600
HTALAGAIPA TVSSSTLTLQ SGHLKCRAKL DKVKIKGTTY GMCDSAFTFS
610 620 630 640 650
KNPADTGHGT VIVELQYTGS NGPCRVPISV TANLMDLTPV GRLVTVNPFI
660 670 680 690 700
STGGANNKVM IEVEPPFGDS YIVVGRGTTQ INYHWHKEGS SIGKALATTW
710 720 730 740 750
KGAQRLAVLG DTAWDFGSIG GVFNSIGKAV HQVFGGAFRT LFGGMSWITQ
760 770 780 790 800
GLLGALLLWM GLQARDRSIS LTLLAVGGIL IFLATSVQAD SGCAIDLQRR
810 820 830 840 850
ELKCGGGIFV YNDVEKWKSD YKYFPLTPTG LAHVIQEAHA NGICGIRSTS
860 870 880 890 900
RLEHLMWENI QRELNAIFED NEIDLSVVVQ EDPKYYKRAP RRLKKLEDEL
910 920 930 940 950
DYGWKKWGKT LFVEPRLGNN TFVVDGPETK ECPTANRAWN SFKVEDFGFG
960 970 980 990 1000
MVFTRLWLTI REENTTECDS AIIGTAIKGD RAVHSDLSYW IESKKNETWQ
1010 1020 1030 1040 1050
LERAVMGEVK SCTWPETHTL WGDGVVESEM IIPVTLGGPK SHHNKRNGYH
1060 1070 1080 1090 1100
TQTKGPWSEG EITLDFDYCP GTTVTVTEHC GNRGASLRTT TASGKLVTDW
1110 1120 1130 1140 1150
CCRSCSLPPL RYTTKDGCWY GMEIRPVKEE EAKLVKSRVT AGVAGGMEPF
1160 1170 1180 1190 1200
QLGLLVAFIA TQEVLKRRWT GKLTLTSLAV CLALLIFGNL TYMDLVRYLV
1210 1220 1230 1240 1250
LVGTAFAEMN TGGDVIHLAL VAVFKVQPAF LAGLFLRMQW SNQENILMVI
1260 1270 1280 1290 1300
GAAFLQMAAN DLKLEVLPIL NAMSIAWMLI RAMKEGKVAM YALPILCALT
1310 1320 1330 1340 1350
PGMRMAGLDV IRCLLLIIGI VTLLNERRES VAKKKGGYLL AAALCQAGVC
1360 1370 1380 1390 1400
SPLIMMGGLI LAHPNGKRSW PASEVLTGVG LMCALAGGLL EFEETSMVVP
1410 1420 1430 1440 1450
FAIAGLMYIT YTVSGKAAEM WIEKAADITW EQNAEITGTS PRLDVDLDSH
1460 1470 1480 1490 1500
GNFKLLNDPG APVHLFALRF ILLGLSARFH WFIPFGVLGF WLLGKHSKRG
1510 1520 1530 1540 1550
GALWDVPSPK VYPKCETKPG IYRIMTRGIL GTFQAGVGVM HEGVFHTMWH
1560 1570 1580 1590 1600
ATEGAVLRNG EGRLDPYAGD VRNDLISYGG PWKLSATWDG TEEVQMIAVA
1610 1620 1630 1640 1650
PGKPAINVQT TPGVFKTPFG TIGAVTLDFP KGTSGSPIIN KKGEIIGLYG
1660 1670 1680 1690 1700
NGVLIGQGEY VSGIIQGERT EEPIPDAYNE EMLRKRKLTV LELHPGAGKT
1710 1720 1730 1740 1750
RKVLPQIIKD CIQKRLRTAV LAPTRVVACE IAEALKGLPI RYLTPAVRNE
1760 1770 1780 1790 1800
HQGNEIVDVM CHATLTQKLL TPTRVPNYQV YIMDEAHFID PASIAARGYI
1810 1820 1830 1840 1850
STKVELGEAA AIFMTATPPG TNDPFPDSNS PILDVEAQVP DKAWSTGYEW
1860 1870 1880 1890 1900
ITNFTGRTVW FVPSVKSGNE IAICLQKAGK RVIQLNRKSF DTEYPKTKNN
1910 1920 1930 1940 1950
EWDFVVTTDI SEMGANFGAH RVIDSRKCVK PVILEDDDRV ILNGPMAITS
1960 1970 1980 1990 2000
ASAAQRRGRI GRNPSQIGDE YHYGGATNED DHDLANWTEA KILLDNIYLP
2010 2020 2030 2040 2050
NGLVAQMYQP ERDKVFTMDG EFRLRGEERK NFVELMRNGD LPVWLAYKVA
2060 2070 2080 2090 2100
SNGHSYQDRS WCFTGQTNNT ILEDNNEVEV FTKTGDRKIL RPKWMDARVC
2110 2120 2130 2140 2150
CDYQALKSFK EFAAGKRSAL GMMEVMGRMP NHFWEKTVAA ADTLYLLGTS
2160 2170 2180 2190 2200
EANSRAHKEA LAELPDSLET LLLIGMLCVM SMGTFIFLMN RKGVGKMGLG
2210 2220 2230 2240 2250
AFVMTLATAL LWAAEVPGTQ IAGVLLIVFL LMIVLIPEPE KQRSQTDNQL
2260 2270 2280 2290 2300
AVFLICIMTL MGVVAANEMG LLEKTKSDIA KLFGSQPGSV GFATRTTPWD
2310 2320 2330 2340 2350
ISLDIKPATA WALYAAATMV MTPLIKHLIT TQYVNFSLTA IASQAGVLLG
2360 2370 2380 2390 2400
LTNGMPFTAM DLSVPLLVLG CWNQMTLPSL AVAVMLLAIH YAFMIPGWQA
2410 2420 2430 2440 2450
EAMRAAQRRT AAGIMKNAVV DGIVATDIPD LSPATPMTEK KMGQILLIAA
2460 2470 2480 2490 2500
AVLAVLVRPG ICSIKEFGVL GSAALVTLIE GTAGVVWNCT TAVGLCNLMR
2510 2520 2530 2540 2550
GGWLAGMSIT WTVYKNVDKP KGKRGGGKGA TLGEIWKSRL NQLTRAEFMA
2560 2570 2580 2590 2600
YRKDGIVEVD RAPARKARRE GRLTGGHPVS RGSAKLRWIT ERGFVKPMGK
2610 2620 2630 2640 2650
VVDLGCGRGG WSYYCATLKH VQEVKGFTKG GPGHEEPQLM QSYGWNLVHM
2660 2670 2680 2690 2700
KSGVDVFHKP AEPADTVLCD IGESNPSCEV EEARTARVLD MVEEWLKKGA
2710 2720 2730 2740 2750
TEFCIKVLCP YTPKIIEKLE KLQRKYGGGL VRVPLSRNST HEMYWVSGAA
2760 2770 2780 2790 2800
GNIIHAVSMT SQVLMGRMDK QNRSGPRYEE DVNLGSGTRS VGKLTEKPDL
2810 2820 2830 2840 2850
RKVGERIRRL REEYQQTWTY DHNNPYRTWN YHGSYEVKPT GSASSMVNGV
2860 2870 2880 2890 2900
VRLLSKPWDM ITNVTTMAMT DTTPFGQQRV FKEKVDTKAP EPPLGVAQIM
2910 2920 2930 2940 2950
DVTTDWLWDF VAREKKPRVC TPEEFKAKVN SHAALGAMFE EQNQWSSARE
2960 2970 2980 2990 3000
AVEDPKFWEM VDEEREAHLK GECHTCIYNM MGKREKKTGE FGKAKGSRAI
3010 3020 3030 3040 3050
WYMWLGARFL EFEALGFLNE DHWMSRENSY GGVEGKGLQK LGYILQEISQ
3060 3070 3080 3090 3100
IPGGKMYADD TAGWDTRITK EDLKNEAKIT KRMEERHRKL AEAIIDLTYR
3110 3120 3130 3140 3150
HKVVKVMRPG PDGKTYMDVI SREDQRGSGQ VVTYALNTFT NLAVQLIRCM
3160 3170 3180 3190 3200
EAEGVVDEDD ITRVRLGRLA KAVEWLRKNG PERLSRMAVS GDDCVVKPID
3210 3220 3230 3240 3250
DRFATALHFL NNMSKIRKDI QEWKPSTGWH NWQEVPFCSH HFNELMLKDG
3260 3270 3280 3290 3300
RTIVVPCRSQ DELIGRARIS PGAGWNVKET ACLSKSYAQM WLLMYFHRRD
3310 3320 3330 3340 3350
LRMMANAICS AVPVNWVPTG RTTWSIHGKG EWMTTEDMLS VWNRVWIEEN
3360 3370 3380 3390 3400
EYMKDKTPLA AWNDIPYLGK REDIWCGSLI GTRTRATWAE NIYAPIMQIR
3410
NLIGEEEYRD YM
Length:3,412
Mass (Da):378,483
Last modified:February 8, 2011 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF89336D9D434A11F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei34121

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti47I → M. 1
Natural varianti164V → I. 1
Natural varianti168N → D. 1
Natural varianti249 – 250VL → FC. 2
Natural varianti346E → K. 1
Natural varianti444F → S. 1
Natural varianti604A → T. 1
Natural varianti796D → S. 1
Natural varianti843I → Y. 1
Natural varianti955R → Q. 1

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
EF158050 Genomic RNA Translation: ABN11812.1
M16614 Genomic RNA Translation: AAA47786.1

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF158050 Genomic RNA Translation: ABN11812.1
M16614 Genomic RNA Translation: AAA47786.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FG0X-ray3.90A289-695[»]
SMRiP09732
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiS07.003

Proteomic databases

PRIDEiP09732

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P09732, 1 sequenced antibody

Family and domain databases

CDDicd12149, Flavi_E_C, 1 hit
Gene3Di1.10.10.930, 1 hit
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.40.10.10, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit
InterProiView protein in InterPro
IPR011492, DEAD_Flavivir
IPR043502, DNA/RNA_pol_sf
IPR000069, Env_glycoprot_M_flavivir
IPR038302, Env_glycoprot_M_sf_flavivir
IPR001122, Flavi_capsidC
IPR037172, Flavi_capsidC_sf
IPR027287, Flavi_E_Ig-like
IPR026470, Flavi_E_Stem/Anchor_dom
IPR038345, Flavi_E_Stem/Anchor_dom_sf
IPR001157, Flavi_NS1
IPR000752, Flavi_NS2A
IPR000487, Flavi_NS2B
IPR000404, Flavi_NS4A
IPR001528, Flavi_NS4B
IPR002535, Flavi_propep
IPR038688, Flavi_propep_sf
IPR000336, Flavivir/Alphavir_Ig-like_sf
IPR001850, Flavivirus_NS3_S7
IPR014412, Gen_Poly_FLV
IPR011998, Glycoprot_cen/dimer
IPR036253, Glycoprot_cen/dimer_sf
IPR038055, Glycoprot_E_dimer_dom
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR014756, Ig_E-set
IPR026490, mRNA_cap_0/1_MeTrfase
IPR027417, P-loop_NTPase
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR000208, RNA-dir_pol_flavivirus
IPR007094, RNA-dir_pol_PSvirus
IPR002877, rRNA_MeTrfase_FtsJ_dom
IPR029063, SAM-dependent_MTases
PfamiView protein in Pfam
PF01003, Flavi_capsid, 1 hit
PF07652, Flavi_DEAD, 1 hit
PF02832, Flavi_glycop_C, 1 hit
PF00869, Flavi_glycoprot, 1 hit
PF01004, Flavi_M, 1 hit
PF00948, Flavi_NS1, 1 hit
PF01005, Flavi_NS2A, 1 hit
PF01002, Flavi_NS2B, 1 hit
PF01350, Flavi_NS4A, 1 hit
PF01349, Flavi_NS4B, 1 hit
PF00972, Flavi_NS5, 1 hit
PF01570, Flavi_propep, 1 hit
PF01728, FtsJ, 1 hit
PF00949, Peptidase_S7, 1 hit
PIRSFiPIRSF003817, Gen_Poly_FLV, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SUPFAMiSSF101257, SSF101257, 1 hit
SSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 2 hits
SSF53335, SSF53335, 1 hit
SSF56672, SSF56672, 1 hit
SSF56983, SSF56983, 1 hit
SSF81296, SSF81296, 1 hit
TIGRFAMsiTIGR04240, flavi_E_stem, 1 hit
PROSITEiView protein in PROSITE
PS51527, FLAVIVIRUS_NS2B, 1 hit
PS51528, FLAVIVIRUS_NS3PRO, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51591, RNA_CAP01_NS5_MT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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_STEVM
<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: P09732
Secondary accession number(s): A3EZ58
, Q88781, Q88782, Q88783, Q88784, Q88785, Q88786, Q88787, Q88788
<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: July 1, 1989
Last sequence update: February 8, 2011
Last modified: August 12, 2020
This is version 150 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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

Keywords - Technical termi

3D-structure

Documents

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