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Protein

Genome polyprotein

Gene
N/A
Organism
Japanese encephalitis virus (strain SA-14)
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

Capsid protein C: 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
Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.By similarity
Peptide pr: 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
Protein prM: 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
Small envelope protein M: 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
Envelope protein E: 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
Non-structural protein 1: 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
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response.By similarity
Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy similarity
Serine protease NS3: 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
Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.By similarity
Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
Non-structural protein 4B: 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
RNA-directed RNA polymerase NS5: 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 (PubMed:16731929). Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:16731929).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 ‘Function’ 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 sitei1555Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1579Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1639Charge 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>Sitei1962Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1965Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2540mRNA cap bindingPROSITE-ProRule annotation1
Sitei2543mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2544mRNA cap bindingPROSITE-ProRule annotation1
Sitei2546mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2551mRNA cap bindingPROSITE-ProRule annotation1
Sitei2555mRNA cap bindingPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 sitei2583S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2588For 2'-O-MTase activityBy similarity1
Sitei2588Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2613S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2614S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2631S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2632S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2658S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2659S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2673For 2'-O-MTase activityBy similarity1
Sitei2673Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2674S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2677mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2709For 2'-O-MTase activityBy similarity1
Sitei2709Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2740mRNA cap bindingPROSITE-ProRule annotation1
Sitei2742mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2745For 2'-O-MTase activityBy similarity1
Sitei2745Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2747S-adenosyl-L-methioninePROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 bindingi2967Zinc 11 Publication1
Metal bindingi2971Zinc 1; via tele nitrogen1 Publication1
Metal bindingi2976Zinc 11 Publication1
Metal bindingi2979Zinc 11 Publication1
Metal bindingi3244Zinc 2; via tele nitrogen1 Publication1
Metal bindingi3260Zinc 21 Publication1
Metal bindingi3379Zinc 21 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi1698 – 1705ATPPROSITE-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 processActivation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host STAT1 by virus, Inhibition of host STAT2 by virus, Inhibition of host TYK2 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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.4.12 2787
3.6.4.13 2787

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_and_taxonomy_section">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
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_and_taxonomy_section">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>OrganismiJapanese encephalitis virus (strain SA-14)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri11073 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 hostiArdeidae (herons) [TaxID: 8899]
Bos taurus (Bovine) [TaxID: 9913]
Culex gelidus [TaxID: 308713]
Culex tritaeniorhynchus (Mosquito) [TaxID: 7178]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000008380 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

Capsid protein C :
Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A :
Serine protease NS3 :
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 – 109CytoplasmicSequence analysisAdd BLAST108
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei110 – 130HelicalSequence analysisAdd BLAST21
Topological domaini131 – 253ExtracellularSequence analysisAdd BLAST123
Transmembranei254 – 274HelicalSequence analysisAdd BLAST21
Topological domaini275 – 279CytoplasmicSequence analysis5
Transmembranei280 – 294HelicalCuratedAdd BLAST15
Topological domaini295 – 746ExtracellularSequence analysisAdd BLAST452
Transmembranei747 – 767HelicalSequence analysisAdd BLAST21
Topological domaini768 – 773CytoplasmicSequence analysis6
Transmembranei774 – 794HelicalSequence analysisAdd BLAST21
Topological domaini795 – 1219ExtracellularSequence analysisAdd BLAST425
Transmembranei1220 – 1240HelicalSequence analysisAdd BLAST21
Topological domaini1241 – 1250CytoplasmicSequence analysis10
Transmembranei1251 – 1271HelicalSequence analysisAdd BLAST21
Topological domaini1272LumenalSequence analysis1
Transmembranei1273 – 1293HelicalSequence analysisAdd BLAST21
Topological domaini1294 – 1309CytoplasmicSequence analysisAdd BLAST16
Transmembranei1310 – 1330HelicalSequence analysisAdd BLAST21
Topological domaini1331 – 1341LumenalSequence analysisAdd BLAST11
Transmembranei1342 – 1362HelicalSequence analysisAdd BLAST21
Topological domaini1363 – 1374CytoplasmicSequence analysisAdd BLAST12
Transmembranei1375 – 1395HelicalSequence analysisAdd BLAST21
Topological domaini1396 – 1398LumenalSequence analysis3
Transmembranei1399 – 1419HelicalSequence analysisAdd BLAST21
Topological domaini1420 – 1476CytoplasmicSequence analysisAdd BLAST57
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Intramembranei1477 – 1497HelicalSequence analysisAdd BLAST21
Topological domaini1498 – 2173CytoplasmicSequence analysisAdd BLAST676
Transmembranei2174 – 2194HelicalSequence analysisAdd BLAST21
Topological domaini2195 – 2199LumenalSequence analysis5
Intramembranei2200 – 2220HelicalSequence analysisAdd BLAST21
Topological domaini2221LumenalSequence analysis1
Transmembranei2222 – 2242HelicalSequence analysisAdd BLAST21
Topological domaini2243 – 2257CytoplasmicSequence analysisAdd BLAST15
Transmembranei2258 – 2278Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2279 – 2311LumenalSequence analysisAdd BLAST33
Intramembranei2312 – 2332HelicalSequence analysisAdd BLAST21
Topological domaini2333 – 2368LumenalSequence analysisAdd BLAST36
Transmembranei2369 – 2389HelicalSequence analysisAdd BLAST21
Topological domaini2390 – 2444CytoplasmicSequence analysisAdd BLAST55
Transmembranei2445 – 2465HelicalSequence analysisAdd BLAST21
Topological domaini2466 – 2469LumenalSequence analysis4
Transmembranei2470 – 2490HelicalSequence analysisAdd BLAST21
Topological domaini2491 – 3432CytoplasmicSequence analysisAdd BLAST942

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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1703G → A: Complete loss of both the ATPase and helicase activities. 1 Publication1
Mutagenesisi1704K → D, E, H, N, Q or R: Complete loss of both the ATPase and helicase activities. 1 Publication1
Mutagenesisi1705T → A: Complete loss of both the ATPase and helicase activities. 1 Publication1
Mutagenesisi1961Q → A: 80% loss of ATPase activity. 1 Publication1
Mutagenesisi1962R → A: 90% loss of ATPase activity. 1 Publication1
Mutagenesisi1965R → A: Complete loss of ATPase activity. 1 Publication1
Mutagenesisi1968R → A: Complete loss of ATPase activity. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004051881 – 3432Genome polyproteinAdd BLAST3432
ChainiPRO_00000378361 – 105Capsid protein CBy similarityAdd BLAST105
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_0000405189106 – 127ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST22
ChainiPRO_0000405190128 – 294Protein prMBy similarityAdd BLAST167
ChainiPRO_0000037837128 – 219Peptide prBy similarityAdd BLAST92
ChainiPRO_0000037838220 – 294Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037839295 – 794Envelope protein EBy similarityAdd BLAST500
ChainiPRO_0000037840795 – 1146Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00000378411147 – 1373Non-structural protein 2ABy similarityAdd BLAST227
ChainiPRO_00000378421374 – 1504Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000378431505 – 2123Serine protease NS3By similarityAdd BLAST619
ChainiPRO_00000378442124 – 2249Non-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_00004051912250 – 2272Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000378452273 – 2527Non-structural protein 4BBy similarityAdd BLAST255
ChainiPRO_00000378462528 – 3432RNA-directed RNA polymerase NS5By similarityAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi142N-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 bondi297 ↔ 324By similarity
Disulfide bondi354 ↔ 415By similarity
Disulfide bondi354 ↔ 410By similarity
Disulfide bondi368 ↔ 399By similarity
Disulfide bondi386 ↔ 415By similarity
Disulfide bondi386 ↔ 410By similarity
Glycosylationi448N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi484 ↔ 581By similarity
Disulfide bondi598 ↔ 629By similarity
Disulfide bondi798 ↔ 809By similarity
Disulfide bondi849 ↔ 937By similarity
Glycosylationi924N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi973 ↔ 1017By similarity
Glycosylationi1001N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi1074 ↔ 1123By similarity
Disulfide bondi1085 ↔ 1106By similarity
Disulfide bondi1107 ↔ 1110By 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 residuei2583PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Genome polyprotein: 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
Protein prM: 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
Envelope protein E: N-glycosylated.By similarity
Non-structural protein 1: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.By similarity
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei105 – 106Cleavage; by viral protease NS3Sequence analysis2
Sitei127 – 128Cleavage; by host signal peptidaseBy similarity2
Sitei219 – 220Cleavage; by host furinBy similarity2
Sitei294 – 295Cleavage; by host signal peptidaseSequence analysis2
Sitei794 – 795Cleavage; by host signal peptidaseSequence analysis2
Sitei1146 – 1147Cleavage; by hostBy similarity2
Sitei1373 – 1374Cleavage; by viral protease NS3Sequence analysis2
Sitei1504 – 1505Cleavage; by autolysisSequence analysis2
Sitei2123 – 2124Cleavage; by autolysisSequence analysis2
Sitei2249 – 2250Cleavage; by viral protease NS3Sequence analysis2
Sitei2272 – 2273Cleavage; by host signal peptidaseSequence analysis2
Sitei2527 – 2528Cleavage; by viral protease NS3Sequence analysis2

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P27395

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Capsid protein C: Homodimer. Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway. Protein prM: Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in the endoplasmic reticulum and Golgi. Interacts with protein prM. Interacts with non-structural protein 1. Non-structural protein 1: Homohexamer when secreted. NS1 interacts with NS4B. Interacts with host complement protein CFH; this interaction leads to the degradation of C3. Non-structural protein 2A: Interacts (via N-terminus) with serine protease NS3. Non-structural protein 2B: Forms a heterodimer with serine protease NS3. May form homooligomers. Serine protease NS3: Forms a heterodimer with NS2B. Interacts with NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity. Non-structural protein 4B: Interacts with serine protease NS3. RNA-directed RNA polymerase NS5: 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

Secondary structure

13432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P27395

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

More...
SMRi
P27395

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P27395

<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_and_domains_section">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>Domaini1505 – 1682Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1685 – 1841Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1852 – 2017Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini2528 – 2793mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3057 – 3209RdRp 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
Regioni392 – 405Fusion peptideBy similarityAdd BLAST14
Regioni1427 – 1466Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1689 – 1692Important for RNA-bindingBy similarity4
Regioni2168 – 2172Regulates 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>Motifi1789 – 1792DEAH 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

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
VOG0900007N

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
2.60.260.50, 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
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
IPR037172 Flavi_capsidC_sf
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR013756 GlyE_cen_dom_subdom2
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR014756 Ig_E-set
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
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
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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by ribosomal frameshifting. AlignAdd to basket
Isoform Genome polyprotein (identifier: P27395-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MTKKPGGPGK NRAINMLKRG LPRVFPLVGV KRVVMSLLDG RGPVRFVLAL
60 70 80 90 100
ITFFKFTALA PTKALLGRWK AVEKSVAMKH LTSFKRELGT LIDAVNKRGR
110 120 130 140 150
KQNKRGGNEG SIMWLASLAV VIACAGAMKL SNFQGKLLMT INNTDIADVI
160 170 180 190 200
VIPTSKGENR CWVRAIDVGY MCEDTITYEC PKLTMGNDPE DVDCWCDNQE
210 220 230 240 250
VYVQYGRCTR TRHSKRSRRS VSVQTHGESS LVNKKEAWLD STKATRYLMK
260 270 280 290 300
TENWIIRNPG YAFLAAVLGW MLGSNNGQRV VFTILLLLVA PAYSFNCLGM
310 320 330 340 350
GNRDFIEGAS GATWVDLVLE GDSCLTIMAN DKPTLDVRMI NIEASQLAEV
360 370 380 390 400
RSYCYHASVT DISTVARCPT TGEAHNEKRA DSSYVCKQGF TDRGWGNGCG
410 420 430 440 450
LFGKGSIDTC AKFSCTSKAI GRTIQPENIK YEVGIFVHGT TTSENHGNYS
460 470 480 490 500
AQVGASQAAK FTVTPNAPSI TLKLGDYGEV TLDCEPRSGL NTEAFYVMTV
510 520 530 540 550
GSKSFLVHRE WFHDLALPWT SPSSTAWRNR ELLMEFEGAH ATKQSVVALG
560 570 580 590 600
SQEGGLHQAL AGAIVVEYSS SVKLTSGHLK CRLKMDKLAL KGTTYGMCTE
610 620 630 640 650
KFSFAKNPVD TGHGTVVIEL SYSGSDGPCK IPIVSVASLN DMTPVGRLVT
660 670 680 690 700
VNPFVATSSA NSKVLVEMEP PFGDSYIVVG RGDKQINHHW HKAGSTLGKA
710 720 730 740 750
FSTTLKGAQR LAALGDTAWD FGSIGGVFNS IGRAVHQVFG GAFRTLFGGM
760 770 780 790 800
SWITQGLMGA LLLWMGVNAR DRSIALAFLA TGGVLVFLAT NVHADTGCAI
810 820 830 840 850
DITRKEMRCG SGIFVHNDVE AWVDRYKYLP ETPRSLAKIV HKAHKEGVCG
860 870 880 890 900
VRSVTRLEHQ MWEAVRDELN VLLKENAVDL SVVVNKPVGR YRSAPKRLSM
910 920 930 940 950
TQEKFEMGWK AWGKSILFAP ELANSTFVVD GPETKECPDE HRAWNSMQIE
960 970 980 990 1000
DFGFGITSTR VWLKIREEST DECDGAIIGT AVKGHVAVHS DLSYWIESRY
1010 1020 1030 1040 1050
NDTWKLERAV FGEVKSCTWP ETHTLWGDDV EESELIIPHT IAGPKSKHNR
1060 1070 1080 1090 1100
REGYKTQNQG PWDENGIVLD FDYCPGTKVT ITEDCSKRGP SVRTTTDSGK
1110 1120 1130 1140 1150
LITDWCCRSC SLPPLRFRTE NGCWYGMEIR PVMHDETTLV RSQVDAFKGE
1160 1170 1180 1190 1200
MVDPFQLGLL VMFLATQEVL RKRWTARLTI PAVLGVLLVL MLGGITYTDL
1210 1220 1230 1240 1250
ARYVVLVAAA FAEANSGGDV LHLALIAVFK IQPAFLVMNM LSTRWTNQEN
1260 1270 1280 1290 1300
VILVLGAAFF QLASVDLQIG VHGILNAAAI AWMIVRAITF PTTSSVTMPV
1310 1320 1330 1340 1350
LALLTPGMRA LYLDTYRIIL LVIGICSLLH ERKKTMAKKK GAVLLGLALT
1360 1370 1380 1390 1400
STGWFSPTTI AAGLMVCNPN KKRGWPATEF LSAVGLMFAI VGGLAELDIE
1410 1420 1430 1440 1450
SMSIPFMLAG LMAVSYVVSG KATDMWLERA ADISWEMDAA ITGSSRRLDV
1460 1470 1480 1490 1500
KLDDDGDFHL IDDPGVPWKV WVLRMSCIGL AALTPWAIVP AAFGYWLTLK
1510 1520 1530 1540 1550
TTKRGGVFWD TPSPKPCSKG DTTTGVYRIM ARGILGTYQA GVGVMYENVF
1560 1570 1580 1590 1600
HTLWHTTRGA AIMSGEGKLT PYWGSVREDR IAYGGPWRFD RKWNGTDDVQ
1610 1620 1630 1640 1650
VIVVEPGKAA VNIQTKPGVF RTPFGEVGAV SLDYPRGTSG SPILDSNGDI
1660 1670 1680 1690 1700
IGLYGNGVEL GDGSYVSAIV QGDRQEEPVP EAYTPNMLRK RQMTVLDLHP
1710 1720 1730 1740 1750
GSGKTRKILP QIIKDAIQQR LRTAVLAPTR VVAAEMAEAL RGLPVRYQTS
1760 1770 1780 1790 1800
AVQREHQGNE IVDVMCHATL THRLMSPNRV PNYNLFVMDE AHFTDPASIA
1810 1820 1830 1840 1850
ARGYIATKVE LGEAAAIFMT ATPPGTTDPF PDSNAPIHDL QDEIPDRAWS
1860 1870 1880 1890 1900
SGYEWITEYA GKTVWFVASV KMGNEIAMCL QRAGKKVIQL NRKSYDTEYP
1910 1920 1930 1940 1950
KCKNGDWDFV ITTDISEMGA NFGASRVIDC RKSVKPTILE EGEGRVILGN
1960 1970 1980 1990 2000
PSPITSASAA QRRGRVGRNP NQVGDEYHYG GATSEDDSNL AHWTEAKIML
2010 2020 2030 2040 2050
DNIHMPNGLV AQLYGPEREK AFTMDGEYRL RGEEKKNFLE LLRTADLPVW
2060 2070 2080 2090 2100
LAYKVASNGI QYTDRKWCFD GPRTNAILED NTEVEIVTRM GERKILKPRW
2110 2120 2130 2140 2150
LDARVYADHQ ALKWFKDFAA GKRSAVSFIE VLGRMPEHFM GKTREALDTM
2160 2170 2180 2190 2200
YLVATAEKGG KAHRMALEEL PDALETITLI VAITVMTGGF FLLMMQRKGI
2210 2220 2230 2240 2250
GKMGLGALVL TLATFFLWAA EVPGTKIAGT LLIALLLMVV LIPEPEKQRS
2260 2270 2280 2290 2300
QTDNQLAVFL ICVLTVVGVV AANEYGMLEK TKADLKSMFG GKTQASGLTG
2310 2320 2330 2340 2350
LPSMALDLRP ATAWALYGGS TVVLTPLLKH LITSEYVTTS LASINSQAGS
2360 2370 2380 2390 2400
LFVLPRGVPF TDLDLTVGLV FLGCWGQITL TTFLTAMVLA TLHYGYMLPG
2410 2420 2430 2440 2450
WQAEALRAAQ RRTAAGIMKN AVVDGMVATD VPELERTTPL MQKKVGQVLL
2460 2470 2480 2490 2500
IGVSVAAFLV NPNVTTVREA GVLVTAATLT LWDNGASAVW NSTTATGLCH
2510 2520 2530 2540 2550
VMRGSYLAGG SIAWTLIKNA DKPSLKRGRP GGRTLGEQWK EKLNAMSREE
2560 2570 2580 2590 2600
FFKYRREAII EVDRTEARRA RRENNIVGGH PVSRGSAKLR WLVEKGFVSP
2610 2620 2630 2640 2650
IGKVIDLGCG RGGWSYYAAT LKKVQEVRGY TKGGAGHEEP MLMQSYGWNL
2660 2670 2680 2690 2700
VSLKSGVDVF YKPSEPSDTL FCDIGESSPS PEVEEQRTLR VLEMTSDWLH
2710 2720 2730 2740 2750
RGPREFCIKV LCPYMPKVIE KMEVLQRRFG GGLVRLPLSR NSNHEMYWVS
2760 2770 2780 2790 2800
GAAGNVVHAV NMTSQVLLGR MDRTVWRGPK YEEDVNLGSG TRAVGKGEVH
2810 2820 2830 2840 2850
SNQEKIKKRI QKLKEEFATT WHKDPEHPYR TWTYHGSYEV KATGSASSLV
2860 2870 2880 2890 2900
NGVVELMSKP WDAIANVTTM AMTDTTPFGQ QRVFKEKVDT KAPEPPAGAK
2910 2920 2930 2940 2950
EVLNETTNWL WAHLSREKRP RLCTKEEFIK KVNSNAALGA VFAEQNQWST
2960 2970 2980 2990 3000
AREAVDDPRF WEMVDEEREN HLRGECHTCI YNMMGKREKK PGEFGKAKGS
3010 3020 3030 3040 3050
RAIWFMWLGA RYLEFEALGF LNEDHWLSRE NSGGGVEGSG VQKLGYILRD
3060 3070 3080 3090 3100
IAGKQGGKMY ADDTAGWDTR ITRTDLENEA KVLELLDGEH RMLARAIIEL
3110 3120 3130 3140 3150
TYRHKVVKVM RPAAEGKTVM DVISREDQRG SGQVVTYALN TFTNIAVQLV
3160 3170 3180 3190 3200
RLMEAEGVIG PQHLEQLPRK TKIAVRTWLF ENGEERVTRM AISGDDCVVK
3210 3220 3230 3240 3250
PLDDRFATAL HFLNAMSKVR KDIQEWKPSH GWHDWQQVPF CSNHFQEIVM
3260 3270 3280 3290 3300
KDGRSIVVPC RGQDELIGRA RISPGAGWNV KDTACLAKAY AQMWLLLYFH
3310 3320 3330 3340 3350
RRDLRLMANA ICSAVPVDWV PTGRTSWSIH SKGEWMTTED MLQVWNRVWI
3360 3370 3380 3390 3400
EENEWMMDKT PITSWTDVPY VGKREDIWCG SLIGTRSRAT WAENIYAAIN
3410 3420 3430
QVRAVIGKEN YVDYMTSLRR YEDVLIQEDR VI
Length:3,432
Mass (Da):380,211
Last modified:August 1, 1992 - 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:i11B9423735B1B5FE
GO
Isoform Structural polyprotein (identifier: P0DOH7-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0DOH7.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Product of a -1 ribosomal frameshifting.By similarity
Length:1,198
Mass (Da):131,562
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA46249 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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
M55506 Genomic RNA Translation: AAA46248.1
M55506 Genomic RNA Translation: AAA46249.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...
PIRi
A35519 GNWVJS

Keywords - Coding sequence diversityi

Ribosomal frameshifting

<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
M55506 Genomic RNA Translation: AAA46248.1
M55506 Genomic RNA Translation: AAA46249.1 Different initiation.
PIRiA35519 GNWVJS

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
2Z83X-ray1.80A1685-2123[»]
3P54X-ray2.10A295-700[»]
4HDGX-ray2.38A/B2799-3432[»]
4HDHX-ray2.28A/B2799-3432[»]
4K6MX-ray2.60A/B2528-3432[»]
4MTPX-ray3.65A/B/C/D2799-3432[»]
5MV1X-ray2.25A295-700[»]
5MV2X-ray2.10A295-700[»]
5O19X-ray2.10A965-1146[»]
5O36X-ray2.60A965-1158[»]
5OW2X-ray1.98A/B1-105[»]
5WSNelectron microscopy4.30B/D/F220-293[»]
5YWOelectron microscopy4.70B/D/F220-293[»]
5YWPelectron microscopy4.60B/D/F220-293[»]
ProteinModelPortaliP27395
SMRiP27395
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS07.003

Proteomic databases

PRIDEiP27395

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG0900007N

Enzyme and pathway databases

BRENDAi3.6.4.12 2787
3.6.4.13 2787

Miscellaneous databases

EvolutionaryTraceiP27395

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
2.60.260.50, 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
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
IPR037172 Flavi_capsidC_sf
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR013756 GlyE_cen_dom_subdom2
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR014756 Ig_E-set
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
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
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit
TIGRFAMsiTIGR04240 flavi_E_stem, 1 hit
PROSITEiView protein in PROSITE
PS51527 FLAVIVIRUS_NS2B, 1 hit
PS51528 FLAVIVIRUS_NS3PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51591 RNA_CAP01_NS5_MT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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<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_JAEV1
<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: P27395
Secondary accession number(s): Q82920
, Q82921, Q82922, Q82923, Q82924, Q82925, Q82926, Q82927, Q82928
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: December 5, 2018
This is version 156 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Complete proteome

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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