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Entry version 121 (11 Dec 2019)
Sequence version 1 (06 Dec 2005)
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Protein

Genome polyprotein

Gene
N/A
Organism
Bussuquara virus (BUSV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_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 sitei1554Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1578Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1638Charge 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>Sitei1961Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1964Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2537mRNA cap bindingPROSITE-ProRule annotation1
Sitei2540mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2541mRNA cap bindingPROSITE-ProRule annotation1
Sitei2543mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2548mRNA cap bindingPROSITE-ProRule annotation1
Sitei2552mRNA cap bindingPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_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 sitei2580S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2585For 2'-O-MTase activityBy similarity1
Sitei2585Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2610S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2611S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2628S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2629S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2655S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2656S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2670For 2'-O-MTase activityBy similarity1
Sitei2670Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2671S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2674mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2705For 2'-O-MTase activityBy similarity1
Sitei2705Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2736mRNA cap bindingPROSITE-ProRule annotation1
Sitei2738mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2741For 2'-O-MTase activityBy similarity1
Sitei2741Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2743S-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 bindingi2962Zinc 1By similarity1
Metal bindingi2966Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2971Zinc 1By similarity1
Metal bindingi2974Zinc 1By similarity1
Metal bindingi3240Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3256Zinc 2By similarity1
Metal bindingi3375Zinc 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 bindingi1697 – 1704ATPPROSITE-ProRule annotation8

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

GO - Biological processi

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

Molecular functionHelicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase
Biological processActivation of host autophagy by virus, 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:3.6.1.15By similarity, EC:3.6.4.13By similarity)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
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>OrganismiBussuquara virus (BUSV)
<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 identifieri64304 [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 hostiHomo sapiens (Human) [TaxID: 9606]
<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
  • UP000120303 <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

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 – 111CytoplasmicSequence analysisAdd BLAST111
<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>Transmembranei112 – 132HelicalSequence analysisAdd BLAST21
Topological domaini133 – 250ExtracellularSequence analysisAdd BLAST118
Transmembranei251 – 271HelicalSequence analysisAdd BLAST21
Topological domaini272 – 277CytoplasmicSequence analysis6
Transmembranei278 – 292HelicalCuratedAdd BLAST15
Topological domaini293 – 745ExtracellularSequence analysisAdd BLAST453
Transmembranei746 – 766HelicalSequence analysisAdd BLAST21
Topological domaini767 – 772CytoplasmicSequence analysis6
Transmembranei773 – 793HelicalSequence analysisAdd BLAST21
Topological domaini794 – 1218ExtracellularSequence analysisAdd BLAST425
Transmembranei1219 – 1239HelicalSequence analysisAdd BLAST21
Topological domaini1240 – 1249CytoplasmicSequence analysis10
Transmembranei1250 – 1270HelicalSequence analysisAdd BLAST21
Topological domaini1271 – 1278LumenalSequence analysis8
Transmembranei1279 – 1299HelicalSequence analysisAdd BLAST21
Topological domaini1300 – 1308CytoplasmicSequence analysis9
Transmembranei1309 – 1329HelicalSequence analysisAdd BLAST21
Topological domaini1330 – 1342LumenalSequence analysisAdd BLAST13
Transmembranei1343 – 1363HelicalSequence analysisAdd BLAST21
Topological domaini1364 – 1373CytoplasmicSequence analysis10
Transmembranei1374 – 1394HelicalSequence analysisAdd BLAST21
Transmembranei1399 – 1419HelicalSequence analysisAdd BLAST21
Topological domaini1420 – 1475CytoplasmicSequence analysisAdd BLAST56
<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>Intramembranei1476 – 1496HelicalSequence analysisAdd BLAST21
Topological domaini1497 – 2172CytoplasmicSequence analysisAdd BLAST676
Transmembranei2173 – 2193HelicalSequence analysisAdd BLAST21
Topological domaini2194 – 2197LumenalSequence analysis4
Intramembranei2198 – 2218HelicalSequence analysisAdd BLAST21
Topological domaini2219 – 2220LumenalSequence analysis2
Transmembranei2221 – 2241HelicalSequence analysisAdd BLAST21
Topological domaini2242 – 2256CytoplasmicSequence analysisAdd BLAST15
Transmembranei2257 – 2271Helical; Note=Signal for NS4BCuratedAdd BLAST15
Topological domaini2272 – 2309LumenalSequence analysisAdd BLAST38
Intramembranei2310 – 2330HelicalSequence analysisAdd BLAST21
Topological domaini2331 – 2378LumenalSequence analysisAdd BLAST48
Transmembranei2379 – 2399HelicalSequence analysisAdd BLAST21
Topological domaini2400 – 2437CytoplasmicSequence analysisAdd BLAST38
Transmembranei2438 – 2458HelicalSequence analysisAdd BLAST21
Topological domaini2459 – 2494LumenalSequence analysisAdd BLAST36
Transmembranei2495 – 2515HelicalSequence analysisAdd BLAST21
Topological domaini2516 – 3429CytoplasmicSequence analysisAdd BLAST914

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_00004414551 – 3429Genome polyproteinAdd BLAST3429
ChainiPRO_00004414561 – 107Capsid protein CBy similarityAdd BLAST107
<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_0000441457108 – 125ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST18
ChainiPRO_0000441458126 – 292Protein prMBy similarityAdd BLAST167
ChainiPRO_0000441459126 – 217Peptide prBy similarityAdd BLAST92
ChainiPRO_0000441460218 – 292Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000441461293 – 793Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000441462794 – 1145Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00004414631146 – 1372Non-structural protein 2ABy similarityAdd BLAST227
ChainiPRO_00004414641373 – 1503Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00004414651504 – 2121Serine protease NS3By similarityAdd BLAST618
ChainiPRO_00004414662122 – 2248Non-structural protein 4ABy similarityAdd BLAST127
<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_00004414672249 – 2271Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004414682272 – 2524Non-structural protein 4BBy similarityAdd BLAST253
ChainiPRO_00004414692525 – 3429RNA-directed RNA polymerase NS5By similarityAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi156N-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 bondi295 ↔ 322By similarity
Disulfide bondi352 ↔ 413By similarity
Disulfide bondi352 ↔ 408By similarity
Disulfide bondi366 ↔ 397By similarity
Disulfide bondi384 ↔ 413By similarity
Disulfide bondi384 ↔ 408By similarity
Disulfide bondi481 ↔ 582By similarity
Disulfide bondi599 ↔ 630By similarity
Disulfide bondi797 ↔ 808By similarity
Disulfide bondi848 ↔ 936By similarity
Glycosylationi923N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi972 ↔ 1016By similarity
Glycosylationi1000N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi1073 ↔ 1122By similarity
Disulfide bondi1084 ↔ 1106By similarity
Disulfide bondi1084 ↔ 1105By similarity
Disulfide bondi1105 ↔ 1109By similarity
Disulfide bondi1106 ↔ 1109By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2580PhosphoserineBy similarity1

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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei106 – 107Cleavage; by viral protease NS3By similarity2
Sitei126 – 127Cleavage; by host signal peptidaseBy similarity2
Sitei217 – 218Cleavage; by host furinBy similarity2
Sitei292 – 293Cleavage; by host signal peptidaseBy similarity2
Sitei793 – 794Cleavage; by host signal peptidaseBy similarity2
Sitei1145 – 1146Cleavage; by hostBy similarity2
Sitei1372 – 1373Cleavage; by viral protease NS3By similarity2
Sitei1503 – 1504Cleavage; by autolysisBy similarity2
Sitei2121 – 2122Cleavage; by autolysisBy similarity2
Sitei2248 – 2249Cleavage; by viral protease NS3By similarity2
Sitei2271 – 2272Cleavage; by host signal peptidaseBy similarity2
Sitei2524 – 2525Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

<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. NS1 interacts with NS4B.

Interacts with host complement protein CFH; this interaction leads to the degradation of C3. Non-structural protein 2A:

Interacts (via N-terminus) with serine protease NS3. Non-structural protein 2B:

Forms a heterodimer with serine protease NS3. May form homooligomers. Serine protease NS3:

Forms a heterodimer with NS2B.

Interacts with NS4B.

Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity. Non-structural protein 4B:

Interacts with serine protease NS3. RNA-directed RNA polymerase NS5: Homodimer.

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

Interacts with serine protease NS3.

By similarity

GO - Molecular functioni

<p>This section provides information on 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>Domaini1504 – 1680Peptidase S7PROSITE-ProRule annotationAdd BLAST177
Domaini1684 – 1840Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1850 – 2020Helicase C-terminalPROSITE-ProRule annotationAdd BLAST171
Domaini2525 – 2788mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST264
Domaini3052 – 3205RdRp catalyticPROSITE-ProRule annotationAdd BLAST154

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>Regioni38 – 73Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni390 – 403Fusion peptideBy similarityAdd BLAST14
Regioni1426 – 1465Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1688 – 1691Important for RNA-bindingBy similarity4

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili859 – 887Sequence analysisAdd BLAST29

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>Motifi1788 – 1791DEAH 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 biasi283 – 286Poly-LeuSequence analysis4
Compositional biasi2473 – 2477Poly-AlaSequence analysis5

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

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

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

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

Keywords - Domaini

Coiled coil, 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
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR001122 Flavi_capsidC
IPR037172 Flavi_capsidC_sf
IPR027287 Flavi_E_Ig-like
IPR026470 Flavi_E_Stem/Anchor_dom
IPR038345 Flavi_E_Stem/Anchor_dom_sf
IPR001157 Flavi_NS1
IPR000752 Flavi_NS2A
IPR000487 Flavi_NS2B
IPR000404 Flavi_NS4A
IPR001528 Flavi_NS4B
IPR002535 Flavi_propep
IPR038688 Flavi_propep_sf
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR014756 Ig_E-set
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR000208 RNA-dir_pol_flavivirus
IPR007094 RNA-dir_pol_PSvirus
IPR002877 rRNA_MeTrfase_FtsJ_dom
IPR029063 SAM-dependent_MTases

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF003817 Gen_Poly_FLV, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR04240 flavi_E_stem, 1 hit

PROSITE; a protein domain and family database

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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. 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.

Q32ZE0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARKPGRPGG NRVVNMLKRT AANAASPLGL AKRLLGDAFA GRGPLRVILA
60 70 80 90 100
VVAFFRFTAI KMSPALLKKW GTVEKGAAIA IMKSFKKEIG SMLDVVARRK
110 120 130 140 150
TKNKGKRSVE SSALLVLLTA CLALGFKVVT GPEGPIMDVT KKDVGKALEI
160 170 180 190 200
PFQNFNNTCW VMAMDVGHPC EDTIEYECPS LDIGAEPNDI DCWCDTMPMR
210 220 230 240 250
VRYGRCTKGS IPKRSRRNAV FPQHTENVLA TRQETWMNTD VIMKHLIKVE
260 270 280 290 300
TWALRNPGFA LVAITLGWML GSNRSQKIIF TILLLLVAPA YNMRCIGVEN
310 320 330 340 350
RDFVEGLSGG TWVDVVLEHG GCVTVRVEGK PTLDFELVQT KATGLAAVRA
360 370 380 390 400
YCYQAKVSDI QISAACPAVQ LTENSKATDS NYLCRRGVTN RGWNNGCGLF
410 420 430 440 450
GKGDIHTCVK FKCEKKAAGF SIGKENLEYE VRASVHNSIG ADKFSNELAD
460 470 480 490 500
GEPHTQKMKF SPLSPSAEKS FGDYGTLGMD CEPQSGLDFG QLYLMTIESK
510 520 530 540 550
SWLVNRDWYH DLHLPYTVGS GSQWNNREAL VEFQEPHATK QEVLALGSQE
560 570 580 590 600
GALHSALAGA IMANRETSSP HALLLTAGHL KCRIKMDKMV IKGITYGQCS
610 620 630 640 650
GTFKMEKHPA DTGHGTVVLD VSYQGDDAPC KIPIVITSNL AEVEPVGRLV
660 670 680 690 700
SAHPVITAKN VRTMLEVEPP YGDSYIVIGV GDGRLKQHWF KKGSVIGGAF
710 720 730 740 750
STTMKGAKRL AVLGDAAWDF GSVGGVFNSL GKAVHQLFGG IFRTLFGGMS
760 770 780 790 800
WLSRLMIGAL CLWIGINARD HSIAVTMLSV GGILIFLSIN VSADTGCVVD
810 820 830 840 850
IERKELKCGS GIFIMNDIEA WRDEYAFHPS GPKALAASVV EAFSQGVCGV
860 870 880 890 900
RSVNRLEHKM WESIADELNA ILEENEREIT IVVKDMENPA QKGKMRLRPV
910 920 930 940 950
EKELKYGWKK WGASFFKRAS RKNATFLVDG PSGEECPNSN RAWNSFFIED
960 970 980 990 1000
FGFGVFKTSV WLGLNEQMTE VCDTKMIGTG VKNDRAVHSD LGYWIESRKN
1010 1020 1030 1040 1050
LTWEISRARL IETKACIWPR SHTLWSDGIE ETQLIIPKSL GGPRSRHNMR
1060 1070 1080 1090 1100
SGYKTQINGP WDQIPLDIKF EECPGTSVTV TPNCGGRGPS ARSTTASGKV
1110 1120 1130 1140 1150
IADWCCRDCI LPPLTFRSGE TCWYAMEIRP VSEREETLIR SKVSAGDGNE
1160 1170 1180 1190 1200
IDTFSLGLLV AMLVTQEGLR KRWATRHIMV ASLTMLAAMV TGHITYRDLL
1210 1220 1230 1240 1250
RYVVLLGATF AQINDGGDVM HLALVAVFKV QPGFLLGFLL RRRWTPRESM
1260 1270 1280 1290 1300
LLAISACFLH LVFSELSTDI TTLAHNFSLA LLILRAIIQT DVSSVTLPVL
1310 1320 1330 1340 1350
SMMAPSFQLS VLGTFRMAVA VYVIVNLMMS KRNDAVKKAA PSVVAAALGQ
1360 1370 1380 1390 1400
FGMVNATAAL GTLYVLEKHG KRSWPPSEIF SAVGVLCALV GALGNVQSTP
1410 1420 1430 1440 1450
LAGPMAACGL LIAAYVVTGK STDIEIERAG LISWSEDAEV SGSSPRVDVA
1460 1470 1480 1490 1500
LDENGDFSLI DGQGPSLESV ILKTALVAFS GLFPVSIPFC AAAWYLHGKS
1510 1520 1530 1540 1550
GRRAGALWDI PAPREVKKGS TENGVYRILA NRLFGKTQVG VGVMHEGVFH
1560 1570 1580 1590 1600
TMWHVTRGAA LKSGEGRLDP YWGDVKKDLI SYGGPWKLEG RWDGVSEVQL
1610 1620 1630 1640 1650
IAVPPKEKAK NVQTTPGVFK TPHGEIGAIV LDFPAGSSGS PIINKLGEVI
1660 1670 1680 1690 1700
GLYGNGLMMG DAYASSIAQA EVEDEPDTPN CLPPDVTHKK KLTVLDLHPG
1710 1720 1730 1740 1750
AGKTRKVLPK LLQEALEKRL RTVVLAPTRV VAAEMAEALK GMPIRYQTAA
1760 1770 1780 1790 1800
VTSSHSGNEI IDLMCHATFT SRLMQPHRVP NYNLYIMDEA HFTDPASIAA
1810 1820 1830 1840 1850
RGFIATKVSL GEAAAVFMTA TPPGSDNPFP ASNAPITDTE AQIPDKAWST
1860 1870 1880 1890 1900
GFDWITEYGG KTVWFVPSVR MGNEIAACLT KAKKKVIQLS RRTFNTEYPK
1910 1920 1930 1940 1950
CKQGDWDFVV TTDISEMGAN FKATRVIDSR RAIKPSIMQD QEERVVLSGP
1960 1970 1980 1990 2000
TPISPASAAQ RRGRVGRNPN QLGDEYVFSG LTQANDEGNA CWTEARMLLD
2010 2020 2030 2040 2050
NIHMQNGLIA QLYGPEQDKC FATDGEFKLR EKERATFLEF LKADLPVWLS
2060 2070 2080 2090 2100
FKAASSGVQY HDRKWCFDGP DNNLVLEDNV PVEIWTKSGE RKKLKPRWSD
2110 2120 2130 2140 2150
ARTYCDHGAL TAFKEFAGGR RSVTTGLLEG VGRLPEHLGQ RLKESIDTLY
2160 2170 2180 2190 2200
LAFTAEVGSR PHREAMQEMP AALETVLVFF LLMIMTGCTF FLLMRHKGIN
2210 2220 2230 2240 2250
KMGYGMVVMS AVGGLLWYGN VPAPKIAGIL LLTFLLMVVL IPNPEKQRSI
2260 2270 2280 2290 2300
QDNQLALVVL GCLMFLGGIA ANEMGMLERT KQDLAGVFHK TERKSTEFTL
2310 2320 2330 2340 2350
LTPPDLRPAT AWSIYAIGTT LITPLIHHMI TTHYANFSLM AMANQAGSLF
2360 2370 2380 2390 2400
GMQTGAPFSK MDWAVPAIVV GCWQQLTPAT LMTALVLLAV HYIYMIPGWQ
2410 2420 2430 2440 2450
AGAARAAQRR TAAGIMKNPV VDGLVVTDIP TLEEVDPLVE KKLGQYILLA
2460 2470 2480 2490 2500
VAIAAAVLRQ DLQSWSECAT LSAAAAATLW EGSPGKIWNA STACSLVNIF
2510 2520 2530 2540 2550
RGHTLAAVPF MFTILRNTGN TGKRGGVEGE TLGEKWKHLL NAMDKYEFSR
2560 2570 2580 2590 2600
YKVNGIFEVD REPARMALAN GLVTSGHAVS RGSAKLRWMV ERAAVRPTGR
2610 2620 2630 2640 2650
VIDLGCGRGG WSYYCATLKQ VQEVRGYTKG GPGHEEPRMV QSYGWNIVTL
2660 2670 2680 2690 2700
KSGVDVFHRP AEVGDTILCD IGESSATPEV EEARTLKVLE MVEPWLKNKP
2710 2720 2730 2740 2750
EFCIKVLCPY RPKVIERLSA LQRTYGGGLV RVPLSRNSTH EMYWTSGTAG
2760 2770 2780 2790 2800
NIINAVNLTS KVLLHRMEKK WIGPRYEKDV NLGSGTRAVI VKRKAPDMDK
2810 2820 2830 2840 2850
IGNRVKRLKE EHIATWCYDD MNPYRTWNYH GSYEVKPTGS ASSMINHVVK
2860 2870 2880 2890 2900
MLSKPWDTLN SVTSISMTDT TPFGQQRVFK EKVDTKAPEP PTGVAEVMDI
2910 2920 2930 2940 2950
ISDWTWRLLS RQKKPRLCTR DEFKAKVNNH AAMGSIFEEE HQWQTAKEAV
2960 2970 2980 2990 3000
EDPGFWALVD REREAHLAGR CETCVYNMMG KREKKLGEFG KAKGSRAIWY
3010 3020 3030 3040 3050
MWLGARFLEF EALGFLNEDH WLSRENSYAG VEGLGLQRLG YVLRDISRRP
3060 3070 3080 3090 3100
GGKMYADDTA GWDTRITEKD LDNEAKIIDQ MEGEHKQLAK AIMELTYRHK
3110 3120 3130 3140 3150
VVKVMRPGPG GKTYMDIISR EDQRGSGQVV TYALNTFTNM IVQLTRCAEA
3160 3170 3180 3190 3200
EGVLIPSMRE RKLTPAEHRA LLLWLDTEGV KRLKKMAISG DDCVVKGEDE
3210 3220 3230 3240 3250
RFATALYFLN AMAKVRKDIQ EWKPSSGWAD WQEVPFCSHH FKELQLKDGR
3260 3270 3280 3290 3300
TIVVPCRHQD ELVGRARVSP GAAWTVRESA GLAKAYAQMW KLMYFHRRDL
3310 3320 3330 3340 3350
RLMANAICSA VPKDWVPTGR TTWSIHGKGE WMTNEDMLEV WNRVWIRENP
3360 3370 3380 3390 3400
HVEDKTEVAD WKDVPYLGKR EDQWCGSLIG SRTRATWAEN IWVAVNQVRA
3410 3420
KIGKEEYSDH LSSQQRFENW GEVRFSGVL
Length:3,429
Mass (Da):379,101
Last modified:December 6, 2005 - 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:iA206F74156B24265
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
AY632536 Genomic RNA Translation: AAV34152.1

NCBI Reference Sequences

More...
RefSeqi
YP_001040004.1, NC_009026.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5075867

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:5075867

<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
AY632536 Genomic RNA Translation: AAV34152.1
RefSeqiYP_001040004.1, NC_009026.2

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Genome annotation databases

GeneIDi5075867
KEGGivg:5075867

Family and domain databases

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

ProtoNet; Automatic hierarchical classification of proteins

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_BUSV
<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: Q32ZE0
<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: September 27, 2017
Last sequence update: December 6, 2005
Last modified: December 11, 2019
This is version 121 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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