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Entry version 156 (18 Sep 2019)
Sequence version 1 (01 Feb 1995)
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Protein

Genome polyprotein

Gene
N/A
Organism
Tick-borne powassan virus (strain LB) (POWV) (Powassan virus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

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.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 immune 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. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_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 <a href="http://www.uniprot.org/help/function_section">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 sitei1543Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1567Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1627Charge 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>Sitei1950Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1953Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2525mRNA cap bindingPROSITE-ProRule annotation1
Sitei2528mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2529mRNA cap bindingPROSITE-ProRule annotation1
Sitei2531mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2536mRNA cap bindingPROSITE-ProRule annotation1
Sitei2540mRNA cap bindingPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei2568S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2573For 2'-O-MTase activityBy similarity1
Sitei2573Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2598S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2599S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2616S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2617S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2643S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2644S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2658For 2'-O-MTase activityBy similarity1
Sitei2658Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2659S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2662mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2695For 2'-O-MTase activityBy similarity1
Sitei2695Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2726mRNA cap bindingPROSITE-ProRule annotation1
Sitei2728mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2731For 2'-O-MTase activityBy similarity1
Sitei2731Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2733S-adenosyl-L-methioninePROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi2951Zinc 1By similarity1
Metal bindingi2955Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2960Zinc 1By similarity1
Metal bindingi2963Zinc 1By similarity1
Metal bindingi3225Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3241Zinc 2By similarity1
Metal bindingi3360Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi1688 – 1695ATPPROSITE-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, 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

<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
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.15, EC:3.6.4.13)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
NS5
<p>This subsection of the <a href="http://www.uniprot.org/help/names_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>OrganismiTick-borne powassan virus (strain LB) (POWV) (Powassan virus)
<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 identifieri39008 [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 lineageiVirusesRiboviriaFlaviviridaeFlavivirus
<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 hostiDermacentor andersoni (Rocky mountain wood tick) [TaxID: 34620]
Homo sapiens (Human) [TaxID: 9606]
Ixodes cookei [TaxID: 35565]
Ixodes scapularis (Black-legged tick) (Deer tick) [TaxID: 6945]
Ixodes spinipalpis [TaxID: 34614]
Lepus americanus (Snowshoe hare) [TaxID: 48086]
Marmota monax (Woodchuck) [TaxID: 9995]
<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
  • UP000006848 <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 domaini1 – 96CytoplasmicSequence analysisAdd BLAST96
<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>Transmembranei97 – 117HelicalSequence analysisAdd BLAST21
Topological domaini118 – 243ExtracellularSequence analysisAdd BLAST126
Transmembranei244 – 260HelicalSequence analysisAdd BLAST17
Topological domaini261CytoplasmicSequence analysis1
Transmembranei262 – 278HelicalSequence analysisAdd BLAST17
Topological domaini279 – 726ExtracellularSequence analysisAdd BLAST448
Transmembranei727 – 747HelicalSequence analysisAdd BLAST21
Topological domaini748 – 754CytoplasmicSequence analysis7
Transmembranei755 – 775HelicalSequence analysisAdd BLAST21
Topological domaini776 – 1187ExtracellularSequence analysisAdd BLAST412
Transmembranei1188 – 1208HelicalSequence analysisBy similarityAdd BLAST21
Topological domaini1209 – 1233CytoplasmicSequence analysisBy similarityAdd BLAST25
Transmembranei1234 – 1253HelicalSequence analysisBy similarityAdd BLAST20
Topological domaini1254LumenalSequence analysisBy similarity1
Transmembranei1255 – 1275HelicalSequence analysisBy similarityAdd BLAST21
Topological domaini1276 – 1292CytoplasmicSequence analysisBy similarityAdd BLAST17
Transmembranei1293 – 1313HelicalSequence analysisBy similarityAdd BLAST21
Topological domaini1314 – 1327LumenalSequence analysisBy similarityAdd BLAST14
Transmembranei1328 – 1348HelicalSequence analysisBy similarityAdd BLAST21
Topological domaini1349 – 1359CytoplasmicSequence analysisBy similarityAdd BLAST11
Transmembranei1360 – 1378HelicalSequence analysisAdd BLAST19
Topological domaini1379 – 1382LumenalSequence analysis4
Transmembranei1383 – 1403HelicalSequence analysisAdd BLAST21
Topological domaini1404 – 1452CytoplasmicSequence analysisAdd BLAST49
<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>Intramembranei1453 – 1473HelicalSequence analysisAdd BLAST21
Topological domaini1474 – 2163CytoplasmicSequence analysisAdd BLAST690
Transmembranei2164 – 2184HelicalSequence analysisAdd BLAST21
Topological domaini2185 – 2190LumenalSequence analysis6
Intramembranei2191 – 2210HelicalSequence analysisAdd BLAST20
Topological domaini2211LumenalSequence analysis1
Transmembranei2212 – 2232HelicalSequence analysisAdd BLAST21
Topological domaini2233 – 2243CytoplasmicSequence analysisAdd BLAST11
Transmembranei2244 – 2264Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2265 – 2300LumenalSequence analysisAdd BLAST36
Intramembranei2301 – 2321HelicalSequence analysisAdd BLAST21
Topological domaini2322 – 2344LumenalSequence analysisAdd BLAST23
Intramembranei2345 – 2365HelicalSequence analysisAdd BLAST21
Topological domaini2366 – 2369LumenalSequence analysis4
Transmembranei2370 – 2390HelicalSequence analysisAdd BLAST21
Topological domaini2391 – 2433CytoplasmicSequence analysisAdd BLAST43
Transmembranei2434 – 2454HelicalSequence analysisAdd BLAST21
Topological domaini2455 – 2479LumenalSequence analysisAdd BLAST25
Transmembranei2480 – 2500HelicalSequence analysisAdd BLAST21
Topological domaini2501 – 3415CytoplasmicSequence analysisAdd BLAST915

GO - Cellular componenti

Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000377241 – 3415Genome polyproteinAdd BLAST3415
ChainiPRO_00004052391 – 94Capsid protein CBy similarityAdd BLAST94
<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_000040514095 – 115ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST21
ChainiPRO_0000405141116 – 278Protein prMBy similarityAdd BLAST163
ChainiPRO_0000037725116 – 203Peptide prBy similarityAdd BLAST88
ChainiPRO_0000037726204 – 278Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037727279 – 775Envelope protein EBy similarityAdd BLAST497
ChainiPRO_0000037728776 – 1128Non-structural protein 1By similarityAdd BLAST353
ChainiPRO_00000377291129 – 1358Non-structural protein 2ABy similarityAdd BLAST230
ChainiPRO_00000377301359 – 1489Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00000377311490 – 2111Serine protease NS3By similarityAdd BLAST622
ChainiPRO_00000377322112 – 2237Non-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_00004051422238 – 2260Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00000377332261 – 2512Non-structural protein 4BBy similarityAdd BLAST252
ChainiPRO_00000377342513 – 3415RNA-directed RNA polymerase NS5By similarityAdd BLAST903

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_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 hostPROSITE-ProRule annotation1
<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 bondi281 ↔ 308By similarity
Disulfide bondi338 ↔ 399By similarity
Disulfide bondi338 ↔ 394By similarity
Disulfide bondi352 ↔ 383By similarity
Disulfide bondi370 ↔ 399By similarity
Disulfide bondi370 ↔ 394By similarity
Glycosylationi432N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotationBy similarity1
Disulfide bondi464 ↔ 568By similarity
Disulfide bondi585 ↔ 617By similarity
Disulfide bondi779 ↔ 790By similarity
Disulfide bondi830 ↔ 920By similarity
Glycosylationi860N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi955 ↔ 1000By similarity
Glycosylationi983N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi999N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi1057 ↔ 1106By similarity
Disulfide bondi1068 ↔ 1090By similarity
Disulfide bondi1089 ↔ 1093By 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 residuei2568PhosphoserineBy 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
Sitei94 – 95Cleavage; by viral protease NS3By similarity2
Sitei114 – 115Cleavage; by host signal peptidaseBy similarity2
Sitei115 – 116Cleavage; by host signal peptidaseBy similarity2
Sitei203 – 204Cleavage; by host furinBy similarity2
Sitei278 – 279Cleavage; by host signal peptidaseBy similarity2
Sitei775 – 776Cleavage; by host signal peptidaseBy similarity2
Sitei1128 – 1129Cleavage; by hostBy similarity2
Sitei1358 – 1359Cleavage; by viral protease NS3By similarity2
Sitei1489 – 1490Cleavage; by autolysisBy similarity2
Sitei2111 – 2112Cleavage; by autolysisBy similarity2
Sitei2237 – 2238Cleavage; by viral protease NS3By similarity2
Sitei2260 – 2261Cleavage; by host signal peptidaseBy similarity2
Sitei2512 – 2513Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q04538

<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: Homodimer; Homohexamer when secreted.

Interacts with envelope protein E. 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.

Interacts with host SCRIB; this interaction targets NS5 to the cell membrane periphery and nucleus, thereby allowing efficient host nuclear STAT1 inhibition.

By similarity

GO - Molecular functioni

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

3D structure databases

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

More...
SMRi
Q04538

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_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>Domaini1490 – 1669Peptidase S7PROSITE-ProRule annotationAdd BLAST180
Domaini1675 – 1832Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST158
Domaini1842 – 2001Helicase C-terminalPROSITE-ProRule annotationAdd BLAST160
Domaini2513 – 2777mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3041 – 3190RdRp catalyticPROSITE-ProRule annotationAdd BLAST150

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>Regioni376 – 389Fusion peptideBy similarityAdd BLAST14
Regioni1410 – 1449Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni2731 – 2735Interaction with host SCRIBBy 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>Motifi1780 – 1783DEAH boxPROSITE-ProRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1746 – 1749Poly-Ser4
Compositional biasi1971 – 1974Poly-Asp4

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

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

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

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12149 Flavi_E_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.60.260.50, 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
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR013756 GlyE_cen_dom_subdom2
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR014756 Ig_E-set
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
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
PF00948 Flavi_NS1, 1 hit
PF01005 Flavi_NS2A, 1 hit
PF01350 Flavi_NS4A, 1 hit
PF01349 Flavi_NS4B, 1 hit
PF00972 Flavi_NS5, 1 hit
PF01570 Flavi_propep, 1 hit
PF01728 FtsJ, 1 hit
PF00949 Peptidase_S7, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF003817 Gen_Poly_FLV, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
SSF53335 SSF53335, 1 hit
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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

Q04538-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMTTSKGKGG GPPRRKLKVT ANKSRPATSP MPKGFVLSRM LGILWHAVTG
60 70 80 90 100
TARPPVLKMF WKTVPLRQAE AVLKKIKRVI GNLMQSLHMR GRRRSGVDWT
110 120 130 140 150
WIFLTMALMT MAMATTIHRD REGYMVMRAS GRDAASQVRV QNGTCVILAT
160 170 180 190 200
DMGEWCEDSI TYSCVTIDQE EEPVDVDCFC RGVDRVKLEY GRCGRQAGSR
210 220 230 240 250
GKRSVVIPTH AQKDMVGRGH AWLKGDNIRD HVTRVEGWMW KNKLLTAAIV
260 270 280 290 300
ALAWLMVDSW MARVTVILLA LSLGPVYATR CTHLENRDFV TGTQGTTRVS
310 320 330 340 350
LVLELGGCVT ITAEGKPSID VWLEDIFQES PAETREYCLH AKLTNTKVEA
360 370 380 390 400
RCPTTGPATL PEEHQANMVC KRDQSDRGWG NHCGFFGKGS IVACAKFECE
410 420 430 440 450
EAKKAVGHVY DSTKITYVVK VEPHTGDYLA ANETNSNRKS AQFTVASEKV
460 470 480 490 500
ILRLGDYGDV SLTCKVASGI DVAQTVVMSL DSSKDHLPSA WQVHRDWFED
510 520 530 540 550
LALPWKHKDN QDWNSVEKLV EFGPPHAVKM DVFNLGDQTA VLLKSLAGVP
560 570 580 590 600
LASVEGQKYH LKSGHVTCDV GLEKLKLKGT TYSMCDKAKF KWKRVPVDSG
610 620 630 640 650
HDTVVMEVSY TGSDKPCRIP VRAVAHGVPA VNVAMLITPN PTIETNGGGF
660 670 680 690 700
IEMQLPPGDN IIYVGDLSQQ WFQKGSTIGR MFEKTRRGLE RLSVVGEHAW
710 720 730 740 750
DFGSVGGVLS SVGKAIHTVL GGAFNTLFGG VGFIPKMLLG VALVWLGLNA
760 770 780 790 800
RNPTMSMTFL AVGALTLMMT MGVGADYGCA IDPERMEIRC GEGLVVWKEV
810 820 830 840 850
SEWYDGYAYH PESPDTLAQA LREAFERGVC GVVPQNRLEM AMWRSTAPEL
860 870 880 890 900
NLVLSEGEAN LTIVVDKTDP ADYRGGTPMV LKKTGKESKV SWKSWGKSIL
910 920 930 940 950
WSVPDSPRRM MMGVDGVGEC PLYRRATGVF TVAEFGVGLR TKVFLDLRGE
960 970 980 990 1000
ASKECDTGVM GAAVKNGKAI HTDQSMWMSS FRNDTGTYIH ELILTDLRNC
1010 1020 1030 1040 1050
TWPASHTIDN DGVLDSHLFL PVTLAGPRSK YNRIPGYSEQ VRGPWDQTPL
1060 1070 1080 1090 1100
RVVRDHCPGT SVRIDSHCDK RGASVRSTTE SGKIIPEWCC RACELPPVTF
1110 1120 1130 1140 1150
RSGTDCWYAM EIRPVHSQGG LVRSMVVADN GALLSEGGVP GLVAVFVLME
1160 1170 1180 1190 1200
FLLRRRPGSV TSILWGGILM LGLLVTGLVR VEEIVRYVIA VGVTFHLELG
1210 1220 1230 1240 1250
PETMVLVMLQ AVFNMRTCYL MGFLVKRVIT TREVVTVYFL LLVLEMGIPE
1260 1270 1280 1290 1300
MNFGHLWEWA DALAMGLLII KASAMEDRRG LGFLLAGLMT QRHLVAVHHG
1310 1320 1330 1340 1350
LMVFLTVALA VVGRNIYNGQ KERKGLCFTV PLASLLGGSG SGLRMLALWE
1360 1370 1380 1390 1400
CLGGRGRRSL SEPLTVVGVM LAMASGLLRH SSQEALLALS AGSFLILMLI
1410 1420 1430 1440 1450
LGTRRLQLTA EWAGVVEWNP ELVNEGGEVS LKVRQDAMGN LHLTEVEREE
1460 1470 1480 1490 1500
RRLALWLVFG LLASAYHWSG ILVTMGAWTV YELFSSTRRT DLVFSGQLPD
1510 1520 1530 1540 1550
QGEKRSFDIK EGVYRIYAPG LFWGYRQIGV GYGTKGVLHT MWHVTRGAAL
1560 1570 1580 1590 1600
SVEGATSGPY WADVREDVVC YGGAWGLDKK WGGEVVQVHA FPPDSGHKIH
1610 1620 1630 1640 1650
QCQPGKLNLE GGRVLGAIPI DLPRGTSGSP IINAQGDVLG LYGNGLKSND
1660 1670 1680 1690 1700
VYISSIAQGN VEKSRPEMPL AVQGGKWTSK GSITVLDMHP GSGKTHRVLP
1710 1720 1730 1740 1750
ELIRECIDKR LRTVVLAPTR VVLKEMERAL QGKRVKFHSA AVDNASSSSG
1760 1770 1780 1790 1800
AIVDVMCHAT YVNRRLLPQG RQNWEVAIMD EAHWTDPHSI AARGHLYSLA
1810 1820 1830 1840 1850
KENRCALVLM TATPPGKSEA FPESKGAIVS EEKPIPEGEW RDGFDWITEF
1860 1870 1880 1890 1900
EGRTAWFVPS IAKGGAIART LRQKGKSVIC LNSKTFDKDY GRVHEEKPDF
1910 1920 1930 1940 1950
VVTTDISEMG ANLDVNRVID GRTNIKPEEI DGKVELIGTR RVTTASAAQR
1960 1970 1980 1990 2000
RGRVGRHEGR TDLYVYSGQC DDDDSSLVQW KEAQILLDNI TTVRGPVATF
2010 2020 2030 2040 2050
YGPEQGKMLE VAGHFRLTEE KRKHFRHLLT NCDFTPWLAW HVAANTACVT
2060 2070 2080 2090 2100
DRKWTWEGPD ENAIDGPGGE LVTFRSPNGA ERKLKPIWKD SRMFREGRDV
2110 2120 2130 2140 2150
ADFIQYASGR RSAVDILTGL GGVPDLLRLR CTAAWDVVYT LLNETPGSRA
2160 2170 2180 2190 2200
MKMAERDAPE AMLTLLEVAV LGIATLGVVW CFIVRTSVSR MVLGTLVLAV
2210 2220 2230 2240 2250
ALILLWLGGM DYGTMAGVAL IFYLLLTVLQ PEPGKQRSGE DNRLAFLLIG
2260 2270 2280 2290 2300
LGSVVGLVAA NELGYLEQTK TDISGLFRRE DQGGMVWDAW TNIDIQPARS
2310 2320 2330 2340 2350
WGTYVLIVSL FTPYMLHQLQ TKIQRLVNSS VAAGTQAMRD LGGGTPFFGV
2360 2370 2380 2390 2400
AGHVVALGVT SLVGATPTSL ALGVALAALH LAVVTSGLEA ELTQRAHRAF
2410 2420 2430 2440 2450
FSAMVKNPMV DGEIINPIPD GDPKPALYER KMSLFLAIGL CIAAVALNRT
2460 2470 2480 2490 2500
AAAMTEAGAV AVAALGQLLR PEEESWWTMP MACGMAGLVR GSLWGLLPVL
2510 2520 2530 2540 2550
HRIWLRTQGA RRGGAEGSTL GDIWKQRLNS CTKEEFFAYR RTGVMETNRD
2560 2570 2580 2590 2600
QARELLRRGE TNMGLAVSRG CAKLAWLEER GYATLKGEVV DLGCGRGGWS
2610 2620 2630 2640 2650
YYAASRPSVM AVRAYTIGGK GHEAPRLVTS LGWNLIKFRS GMDVFSMATT
2660 2670 2680 2690 2700
RADTILCDIG ESSPDPEKEG ARSRRVILLM EQWKARNPDA AAVFKVLAPY
2710 2720 2730 2740 2750
RPEVLEALHR FQLQWGGGLV RVPFSRNSTH EMYYSTAVTG NLVNSVNVLS
2760 2770 2780 2790 2800
RKLLARFGET RGPIQVPEID LGTGTRCVTL AEDKVKPRDV AERIGALREQ
2810 2820 2830 2840 2850
YSESWHEDKE HPYRTWQYWG SYRTPATGSA ASLINGVVKL LSWPWNARED
2860 2870 2880 2890 2900
VTRMAMTDTT AFGQQRVFKE KVDTKAQEPQ PGTRVIMRAV SDWLLEHLSR
2910 2920 2930 2940 2950
RAKVRMCTKD EFIAKVRSNA ALGAWSDEQN KWSSAKEAVE DPEFWKLVDE
2960 2970 2980 2990 3000
ERSRHLKGQC RHCVYNMMGK REKKLGEFGV AKGSRAIWYM WLGSRFLEFE
3010 3020 3030 3040 3050
VLGFLNEEHW ASREVSGAGV EGTSLNYLGW LLRELGMKDG GKLYADDTAG
3060 3070 3080 3090 3100
WDTRITNADL EDEEQILRYM EGEHHVLAKT ILEKAYHAKV VKVARPSPQG
3110 3120 3130 3140 3150
GCVMDVITRR DQRGSGQVVT YALNTITNMK VQLIRMMEGE GVIGPADSQD
3160 3170 3180 3190 3200
PRLKRVETWL KEHGVERLGR MLVSGDDCVV KPIDDRFGKA LYFLNDMAKV
3210 3220 3230 3240 3250
RKDVGEWEPS MGFTEWEEVP FCSHHFHELV MKDGRSLIVP CRDQDELVGR
3260 3270 3280 3290 3300
ARVSPGCGWS VRETACLSKA YGQMWLLNYF HRRDLRTLGF AICSAVPVSW
3310 3320 3330 3340 3350
VPMGRTTWSI HASGEWMTTE DMLRIWNKVW ILDNPHMEDK QTVDEWRDIP
3360 3370 3380 3390 3400
YLPKTQDLVC SSLVGRKERA EWAKNIWGSV EKVRKLIGPE DYRDYLSSMD
3410
RHDLHWELKL ESSII
Length:3,415
Mass (Da):378,570
Last modified:February 1, 1995 - 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:iE71092FE64049F46
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L06436 Genomic RNA Translation: AAA02739.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A46105

NCBI Reference Sequences

More...
RefSeqi
NP_620099.1, NC_003687.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
940442

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:940442

<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
L06436 Genomic RNA Translation: AAA02739.1
PIRiA46105
RefSeqiNP_620099.1, NC_003687.1

3D structure databases

SMRiQ04538
ModBaseiSearch...

Proteomic databases

PRIDEiQ04538

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi940442
KEGGivg:940442

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
Gene3Di1.10.8.970, 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
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR013756 GlyE_cen_dom_subdom2
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR014756 Ig_E-set
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
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
PF00948 Flavi_NS1, 1 hit
PF01005 Flavi_NS2A, 1 hit
PF01350 Flavi_NS4A, 1 hit
PF01349 Flavi_NS4B, 1 hit
PF00972 Flavi_NS5, 1 hit
PF01570 Flavi_propep, 1 hit
PF01728 FtsJ, 1 hit
PF00949 Peptidase_S7, 1 hit
PIRSFiPIRSF003817 Gen_Poly_FLV, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
SSF53335 SSF53335, 1 hit
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_POWVL
<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: Q04538
<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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 18, 2019
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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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