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UniProtKB - P27395 (POLG_JAEV1)

Entry version 165 (07 Oct 2020)
Sequence version 1 (01 Aug 1992)
Previous versions | rss
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Protein

Genome polyprotein

Gene
N/A
Organism
Japanese encephalitis virus (strain SA-14) (JEV)
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 pH 6.0. 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 (PubMed:7897348). May have membrane-destabilizing activity and form viroporins (By similarity).By similarity1 Publication
Displays three enzymatic activities: serine protease, NTPase and RNA helicase (PubMed:18201743, PubMed:7897348). 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 (Probable). NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).PROSITE-ProRule annotation1 Publication2 Publications
Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity).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 (By similarity). Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway (By similarity). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (By similarity).By similarity
Replicates the viral (+) and (-) RNA genome (PubMed:24293643). 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 similarity2 Publications

Miscellaneous

Strain SA-14 is classified as genotype III.Curated

<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.1 Publication EC:3.4.21.91

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+, Mg2+Note: For RNA-directed RNA polymerase NS5 activity; Mn2+ is more effective than Mg2+.1 Publication

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 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 <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 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 <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 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 <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 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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%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:
Capsid protein C
Alternative name(s):
Core protein
Protein prM
Peptide pr
Small envelope protein M
Alternative name(s):
Matrix protein
Envelope protein E
Non-structural protein 1
Short name:
NS1
Non-structural protein 2A
Short name:
NS2A
Serine protease subunit NS2B
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.911 Publication, EC:3.6.1.151 Publication, EC:3.6.4.131 Publication)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
Non-structural protein 4A
Short name:
NS4A
Peptide 2k
Non-structural protein 4B
Short name:
NS4B
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
Non-structural protein 5
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiJapanese encephalitis virus (strain SA-14) (JEV)
<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 identifieri11073 [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 lineageiViruses › Riboviria › Orthornavirae › Kitrinoviricota › Flasuviricetes › Amarillovirales › Flaviviridae › Flavivirus ›
<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 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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008380 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 109CytoplasmicSequence analysisAdd BLAST108
<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>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%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>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

Complete GO annotation on QuickGO ...

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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1379E → A: No effect on human SPCS1 binding. 1 Publication1
Mutagenesisi1385G → A: Reduces human SPCS1 binding. 1 Publication1
Mutagenesisi1405P → A: Slightly reduces human SPCS1 binding. 1 Publication1
Mutagenesisi1410G → A: Slightly reduces human SPCS1 binding. 1 Publication1
Mutagenesisi1420G → A: Slightly reduces human SPCS1 binding. 1 Publication1
Mutagenesisi1485P → A: Reduces SPCS1 human binding. 1 Publication1
Mutagenesisi1488I → A: Slightly reduces human SPCS1 binding. 1 Publication1
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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004051881 – 3432Genome polyproteinAdd BLAST3432
ChainiPRO_00000378361 – 105Capsid protein CAdd BLAST105
<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_0000405189106 – 127ER anchor for the capsid protein C, removed in mature form by serine protease NS3Add BLAST22
ChainiPRO_0000405190128 – 294Protein prMAdd BLAST167
ChainiPRO_0000037837128 – 219Peptide prAdd BLAST92
ChainiPRO_0000037838220 – 294Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037839295 – 794Envelope protein EAdd BLAST500
ChainiPRO_0000037840795 – 1146Non-structural protein 1Add BLAST352
ChainiPRO_00000378411147 – 1373Non-structural protein 2AAdd BLAST227
ChainiPRO_00000378421374 – 1504Serine protease subunit NS2BAdd BLAST131
ChainiPRO_00000378431505 – 2123Serine protease NS3Add BLAST619
ChainiPRO_00000378442124 – 2249Non-structural protein 4AAdd 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 2kAdd BLAST23
ChainiPRO_00000378452273 – 2527Non-structural protein 4BAdd BLAST255
ChainiPRO_00000378462528 – 3432RNA-directed RNA polymerase NS5Add BLAST905

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>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%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 (PubMed:7897348). 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 similarity1 Publication
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
Sitei105 – 106Cleavage; by viral protease NS3By similarity2
Sitei127 – 128Cleavage; by host signal peptidaseBy similarity2
Sitei219 – 220Cleavage; by host furinBy similarity2
Sitei294 – 295Cleavage; by host signal peptidaseBy similarity2
Sitei794 – 795Cleavage; by host signal peptidaseBy similarity2
Sitei1146 – 1147Cleavage; by hostBy similarity2
Sitei1373 – 1374Cleavage; by viral protease NS3By similarity2
Sitei1504 – 1505Cleavage; by autolysisBy similarity2
Sitei2123 – 2124Cleavage; by autolysisBy similarity2
Sitei2249 – 2250Cleavage; by viral protease NS3By similarity2
Sitei2272 – 2273Cleavage; by host signal peptidaseBy similarity2
Sitei2527 – 2528Cleavage; by viral protease NS3By similarity2

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%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

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 (PubMed:7897348). May form homooligomers.

Interacts with human SPCS1 (PubMed:29593046). Serine protease NS3:

Forms a heterodimer with NS2B (PubMed:7897348).

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 similarity2 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

<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

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

More...SMRi		P27395

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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%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>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
Regioni1374 – 1423Interaction with human SPCS11 PublicationAdd BLAST50
Regioni1427 – 1466Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1458 – 1505Interaction with human SPCS11 PublicationAdd BLAST48
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

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
3.30.387.10, 1 hit
3.30.67.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011492, DEAD_Flavivir
IPR043502, DNA/RNA_pol_sf
IPR000069, Env_glycoprot_M_flavivir
IPR038302, Env_glycoprot_M_sf_flavivir
IPR013755, Flav_gly_cen_dom_subdom1
IPR001122, Flavi_capsidC
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
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>Sequences (2)i

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

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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 <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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.
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. Truncated N-terminus.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[»]
SMRiP27395
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiS07.003

Proteomic databases

PRIDEiP27395

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
2.40.10.10, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit
3.30.387.10, 1 hit
3.30.67.10, 1 hit
InterProiView protein in InterPro
IPR011492, DEAD_Flavivir
IPR043502, DNA/RNA_pol_sf
IPR000069, Env_glycoprot_M_flavivir
IPR038302, Env_glycoprot_M_sf_flavivir
IPR013755, Flav_gly_cen_dom_subdom1
IPR001122, Flavi_capsidC
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
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_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%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: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 7, 2020
This is version 165 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

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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