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UniProtKB - Q58HT7 (POLG_DEN4P)

Entry version 130 (25 May 2022)
Sequence version 1 (26 Apr 2005)
Previous versions | rss
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Protein

Genome polyprotein

Gene
N/A
Organism
Dengue virus type 4 (strain Philippines/H241/1956) (DENV-4)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.

By similarity

Inhibits RNA silencing by interfering with host Dicer.

By similarity

Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.

By similarity

Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.

By similarity

May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.

By similarity

Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.

By similarity

Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).

By similarity

Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease.

By similarity

Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune 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. Plays a role in the inhibition of the host innate immune response. Interacts with host MAVS and thereby prevents the interaction between DDX58 and MAVS. In turn, IFN-beta production is impaired. Interacts with host AUP1 which mediates induction of lipophagy in host cells and facilitates production of virus progeny particles (By similarity).

By similarity

Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.

By similarity

Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway.

By similarity

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).

May reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (By similarity).

By similarity

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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1525Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1549Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1609Charge 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>Sitei1931Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1934Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2501mRNA cap bindingPROSITE-ProRule annotation1
Sitei2504mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2505mRNA cap bindingPROSITE-ProRule annotation1
Sitei2507mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2512mRNA cap bindingPROSITE-ProRule annotation1
Sitei2516mRNA cap bindingPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei2543S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2548For 2'-O-MTase activityBy similarity1
Sitei2548Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2573S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2574S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2591S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2592S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2618S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2619S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2633For 2'-O-MTase activityBy similarity1
Sitei2633Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2634S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2637mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2668For 2'-O-MTase activityBy similarity1
Sitei2668Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2699mRNA cap bindingPROSITE-ProRule annotation1
Sitei2701mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2704For 2'-O-MTase activityBy similarity1
Sitei2704Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2706S-adenosyl-L-methioninePROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi2925Zinc 1By similarity1
Metal bindingi2929Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2934Zinc 1By similarity1
Metal bindingi2937Zinc 1By similarity1
Metal bindingi3200Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3216Zinc 2By similarity1
Metal bindingi3335Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1667 – 1674ATPPROSITE-ProRule annotation8

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionHelicase, Hydrolase, Ion channel, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase, Viral ion channel
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 MAVS by virus, Inhibition of host RLR pathway by virus, Inhibition of host STAT2 by virus, Inhibition of host TYK2 by virus, Ion transport, mRNA capping, mRNA processing, Transcription, Transcription regulation, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Protein family/group databases

MEROPS protease database

More...MEROPSi		S07.001

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Capsid protein C
Alternative name(s):
Core protein
Protein prM
Peptide pr
Small envelope protein M
Alternative name(s):
Matrix protein
Envelope protein E
Non-structural protein 1
Short name:
NS1
Non-structural protein 2A
Short name:
NS2A
Serine protease subunit NS2B
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
Non-structural protein 4A
Short name:
NS4A
Peptide 2k
Non-structural protein 4B
Short name:
NS4B
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
Non-structural protein 5
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDengue virus type 4 (strain Philippines/H241/1956) (DENV-4)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri408686 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiViruses › Riboviria › Orthornavirae › Kitrinoviricota › Flasuviricetes › Amarillovirales › Flaviviridae › Flavivirus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160]
Aedes polynesiensis (Polynesian tiger mosquito) [TaxID: 188700]
Homo sapiens (Human) [TaxID: 9606]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000275 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 100CytoplasmicSequence analysisAdd BLAST100
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei101 – 117HelicalSequence analysisAdd BLAST17
Topological domaini118 – 237ExtracellularSequence analysisAdd BLAST120
Transmembranei238 – 258HelicalSequence analysisAdd BLAST21
Topological domaini259 – 265CytoplasmicSequence analysis7
Transmembranei266 – 279HelicalSequence analysisAdd BLAST14
Topological domaini280 – 723ExtracellularSequence analysisAdd BLAST444
Transmembranei724 – 746HelicalSequence analysisAdd BLAST23
Topological domaini747 – 750CytoplasmicSequence analysis4
Transmembranei751 – 771HelicalSequence analysisAdd BLAST21
Topological domaini772 – 1194ExtracellularSequence analysisAdd BLAST423
Transmembranei1195 – 1218HelicalSequence analysisAdd BLAST24
Topological domaini1219 – 1224LumenalSequence analysis6
Transmembranei1225 – 1243HelicalSequence analysisAdd BLAST19
Topological domaini1244 – 1267CytoplasmicSequence analysisAdd BLAST24
Transmembranei1268 – 1288HelicalSequence analysisAdd BLAST21
Topological domaini1289LumenalSequence analysis1
Transmembranei1290 – 1308HelicalSequence analysisAdd BLAST19
Topological domaini1309 – 1316LumenalSequence analysis8
Transmembranei1317 – 1337HelicalSequence analysisAdd BLAST21
Topological domaini1338 – 1345CytoplasmicSequence analysis8
Transmembranei1346 – 1366HelicalSequence analysisAdd BLAST21
Topological domaini1367 – 1369LumenalSequence analysis3
Transmembranei1370 – 1390HelicalSequence analysisAdd BLAST21
Topological domaini1391 – 1437CytoplasmicSequence analysisAdd BLAST47
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1438 – 1458HelicalSequence analysisAdd BLAST21
Topological domaini1459 – 2146CytoplasmicSequence analysisAdd BLAST688
Transmembranei2147 – 2167HelicalSequence analysisAdd BLAST21
Topological domaini2168 – 2169LumenalSequence analysis2
Intramembranei2170 – 2190HelicalSequence analysisAdd BLAST21
Topological domaini2191LumenalSequence analysis1
Transmembranei2192 – 2212HelicalSequence analysisAdd BLAST21
Topological domaini2213 – 2225CytoplasmicSequence analysisAdd BLAST13
Transmembranei2226 – 2246Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2247 – 2270LumenalSequence analysisAdd BLAST24
Intramembranei2271 – 2291HelicalSequence analysisAdd BLAST21
Topological domaini2292 – 2301LumenalSequence analysis10
Intramembranei2302 – 2322HelicalSequence analysisAdd BLAST21
Topological domaini2323 – 2343LumenalSequence analysisAdd BLAST21
Transmembranei2344 – 2364HelicalSequence analysisAdd BLAST21
Topological domaini2365 – 2409CytoplasmicSequence analysisAdd BLAST45
Transmembranei2410 – 2430HelicalSequence analysisAdd BLAST21
Topological domaini2431 – 2455LumenalSequence analysisAdd BLAST25
Transmembranei2456 – 2476HelicalSequence analysisAdd BLAST21
Topological domaini2477 – 3387CytoplasmicSequence analysisAdd BLAST911

Keywords - Cellular componenti

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

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004052271 – 3387Genome polyproteinAdd BLAST3387
ChainiPRO_00002681031 – 99Capsid protein CBy similarityAdd BLAST99
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000268104100 – 113ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST14
ChainiPRO_0000268105114 – 279Protein prMBy similarityAdd BLAST166
ChainiPRO_0000268106114 – 204Peptide prBy similarityAdd BLAST91
ChainiPRO_0000268107205 – 279Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000268108280 – 774Envelope protein EBy similarityAdd BLAST495
ChainiPRO_0000268109775 – 1126Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00002681101127 – 1344Non-structural protein 2ABy similarityAdd BLAST218
ChainiPRO_00002681111345 – 1474Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00002681121475 – 2092Serine protease NS3By similarityAdd BLAST618
ChainiPRO_00002681132093 – 2219Non-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_00002681142220 – 2242Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00002681152243 – 2487Non-structural protein 4BBy similarityAdd BLAST245
ChainiPRO_00002681162488 – 3387RNA-directed RNA polymerase NS5By similarityAdd BLAST900

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi182N-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 bondi282 ↔ 309By similarity
Disulfide bondi339 ↔ 400By similarity
Glycosylationi346N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi353 ↔ 384By similarity
Disulfide bondi371 ↔ 395By similarity
Disulfide bondi464 ↔ 564By similarity
Disulfide bondi581 ↔ 612By similarity
Disulfide bondi778 ↔ 789By similarity
Disulfide bondi829 ↔ 917By similarity
Glycosylationi904N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi953 ↔ 997By similarity
Glycosylationi981N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi1054 ↔ 1103By similarity
Disulfide bondi1065 ↔ 1087By similarity
Disulfide bondi1086 ↔ 1090By similarity
Glycosylationi2297N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2301N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi2453N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
<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 residuei2543PhosphoserineBy similarity1

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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei99 – 100Cleavage; by viral protease NS3By similarity2
Sitei113 – 114Cleavage; by host signal peptidaseBy similarity2
Sitei204 – 205Cleavage; by host furinSequence analysisBy similarity2
Sitei279 – 280Cleavage; by host signal peptidaseBy similarity2
Sitei774 – 775Cleavage; by host signal peptidaseBy similarity2
Sitei1126 – 1127Cleavage; by hostBy similarity2
Sitei1344 – 1345Cleavage; by viral protease NS3By similarity2
Sitei1474 – 1475Cleavage; by autolysisBy similarity2
Sitei2092 – 2093Cleavage; by autolysisBy similarity2
Sitei2219 – 2220Cleavage; by viral protease NS3By similarity2
Sitei2242 – 2243Cleavage; by host signal peptidaseBy similarity2
Sitei2487 – 2488Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

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

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

Homodimer.

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

By similarity

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

By similarity

Homodimer; in the endoplasmic reticulum and Golgi.

Interacts with protein prM.

Interacts with non-structural protein 1.

By similarity

Homodimer; Homohexamer when secreted.

Interacts with envelope protein E.

By similarity

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

By similarity

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

By similarity

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.

By similarity

Interacts with host MAVS; this interaction inhibits the synthesis of IFN-beta.

Interacts with host AUP1; the interaction occurs in the presence of Dengue virus NS4B and induces lipophagy which facilitates production of virus progeny particles (By similarity).

By similarity

Interacts with serine protease NS3.

By similarity

Homodimer.

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

Interacts with serine protease NS3 (By similarity).

Interacts with host PAF1 complex; the interaction may prevent the recruitment of the PAF1 complex to interferon-responsive genes, and thus reduces the immune response (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

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

Secondary structure

13387
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q58HT7

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

More...SMRi		Q58HT7

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1475 – 1652Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1654 – 1810Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1820 – 1987Helicase C-terminalAdd BLAST168
Domaini2489 – 2751mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST263
Domaini3016 – 3166RdRp catalyticPROSITE-ProRule annotationAdd BLAST151

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>Regioni36 – 71Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni377 – 390Fusion peptideBy similarityAdd BLAST14
Regioni1397 – 1436Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1658 – 1661Important for RNA-bindingBy similarity4

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>Motifi1758 – 1761DEAH boxPROSITE-ProRule annotation4
Motifi2564 – 2567SUMO-interacting motifBy similarity4

<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		cd20761, capping_2-OMTase_Flaviviridae, 1 hit
cd12149, Flavi_E_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.930, 1 hit
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.40.10.10, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit
3.30.387.10, 1 hit
3.30.67.10, 1 hit
3.40.50.150, 1 hit
3.40.50.300, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011492, DEAD_Flavivir
IPR043502, DNA/RNA_pol_sf
IPR000069, Env_glycoprot_M_flavivir
IPR038302, Env_glycoprot_M_sf_flavivir
IPR013755, Flav_gly_cen_dom_subdom1
IPR001122, Flavi_capsidC
IPR037172, Flavi_capsidC_sf
IPR027287, Flavi_E_Ig-like
IPR026470, Flavi_E_Stem/Anchor_dom
IPR038345, Flavi_E_Stem/Anchor_dom_sf
IPR001157, Flavi_NS1
IPR000752, Flavi_NS2A
IPR000487, Flavi_NS2B
IPR000404, Flavi_NS4A
IPR001528, Flavi_NS4B
IPR002535, Flavi_propep
IPR038688, Flavi_propep_sf
IPR000336, Flavivir/Alphavir_Ig-like_sf
IPR001850, Flavivirus_NS3_S7
IPR014412, Gen_Poly_FLV
IPR011998, Glycoprot_cen/dimer
IPR036253, Glycoprot_cen/dimer_sf
IPR038055, Glycoprot_E_dimer_dom
IPR013756, GlyE_cen_dom_subdom2
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR014756, Ig_E-set
IPR026490, mRNA_cap_0/1_MeTrfase
IPR027417, P-loop_NTPase
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR000208, RNA-dir_pol_flavivirus
IPR007094, RNA-dir_pol_PSvirus
IPR002877, rRNA_MeTrfase_FtsJ_dom
IPR029063, SAM-dependent_MTases

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF003817, Gen_Poly_FLV, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR04240, flavi_E_stem, 1 hit

PROSITE; a protein domain and family database

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

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

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

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

Q58HT7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNQRKKVVRP PFNMLKRERN RVSTPQGLVK RFSTGLFSGK GPLRMVLAFI 
        60         70         80         90        100
TFLRVLSIPP TAGILKRWGQ LKKNKAIKIL TGFRKEIGRM LNILNGRKRS 
       110        120        130        140        150
TMTLLCLIPT AMAFHLSTRD GEPLMIVARH ERGRPLLFKT TEGINKCTLI 
       160        170        180        190        200
AMDLGEMCED TVTYECPLLV NTEPEDIDCW CNLTSAWVMY GTCTQSGERR 
       210        220        230        240        250
REKRSVALTP HSGMGLETRA ETWMSSEGAW KHAQRVESWI LRNPGFALLA 
       260        270        280        290        300
GFMAYMIGQT GIQRTVFFVL MMLVAPSYGM RCVGVGNRDF VEGVSGGAWV 
       310        320        330        340        350
DLVLEHGGCV TTMAQGKPTL DFELIKTTAK EVALLRTYCI EASISNITTA 
       360        370        380        390        400
TRCPTQGEPY LKEEQDQQYI CRRDVVDRGW GNGCGLFGKG GVVTCAKFSC 
       410        420        430        440        450
SGKITGNLVQ IENLEYTVVV TVHNGDTHAV GNDIPNHGVT ATITPRSPSV 
       460        470        480        490        500
EVKLPDYGEL TLDCEPRSGI DFNEMILMKM KKKTWLVHKQ WFLDLPLPWA 
       510        520        530        540        550
AGADTSEVHW NYKERMVTFK VPHAKRQDVT VLGSQEGAMH SALTGATEVD 
       560        570        580        590        600
SGDGNHMFAG HLKCKVRMEK LRIKGMSYTM CSGKFSIDKE MAETQHGTTV 
       610        620        630        640        650
VKVKYEGAGA PCKVPIEIRD VNKEKVVGRI ISSTPFAEYT NSVTNIELEP 
       660        670        680        690        700
PFGDSYIVIG VGDSALTLHW FRKGSSIGKM LESTYRGAKR MAILGETAWD 
       710        720        730        740        750
FGSVGGLLTS LGKAVHQVFG SVYTTMFGGV SWMVRILIGF LVLWIGTNSR 
       760        770        780        790        800
NTSMAMTCIA VGGITLFLGF TVHADTGCAV SWSGKELKCG SGIFVIDNVH 
       810        820        830        840        850
TWTEQYKFQP ESPARLASAI LNAHEDGVCG IRSTTRLENI MWKQITNELN 
       860        870        880        890        900
YVLWEGGHDL TVVAGDVKGV LSKGKRALAP PVNDLKYSWK TWGKAKIFTP 
       910        920        930        940        950
EAKNSTFLID GPDTSECPNE RRAWNFLEVE DYGFGMFTTN IWMKFREGSS 
       960        970        980        990       1000
EVCDHRLMSA AIKDQKAVHA DMGYWIESSK NQTWQIEKAS LIEVKTCLWP 
      1010       1020       1030       1040       1050
KTHTLWSNGV LESQMLIPKA YAGPFSQHNY RQGYATQTVG PWHLGKLEID 
      1060       1070       1080       1090       1100
FGECPGTTVT IQEDCDHRGP SLRTTTASGK LVTQWCCRSC TMPPLRFLGE 
      1110       1120       1130       1140       1150
DGCWYGMEIR PLSEKEENMV KSQVSAGQGT SETFSMGLLC LTLFVEECLR 
      1160       1170       1180       1190       1200
RRVTRKHMIL VVVTTLCAII LGGLTWMDLL RALIMLGDTM SGRMGGQIHL 
      1210       1220       1230       1240       1250
AIMAVFKMSP GYVLGIFLRK LTSRETALMV IGMAMTTVLS IPHDLMEFID 
      1260       1270       1280       1290       1300
GISLGLILLK MVTHFDNTQV GTLALSLTFI RSTMPLVMAW RTIMAVLFVV 
      1310       1320       1330       1340       1350
TLIPLCRTSC LQKQSHWVEI TALILGAQAL PVYLMTLMKG ASKRSWPLNE 
      1360       1370       1380       1390       1400
GIMAVGLVSL LGSALLKNDV PLAGPMVAGG LLLAAYVMSG SSADLSLEKA 
      1410       1420       1430       1440       1450
ANVQWDEMAD ITGSSPIIEV KQDEDGSFSI RDIEETNMIT LLVKLALITV 
      1460       1470       1480       1490       1500
SGLYPLAIPV TMTLWYMWQV KTQRSGALWD VPSPAAAQKA TLTEGVYRIM 
      1510       1520       1530       1540       1550
QRGLFGKTQV GVGIHMEGVF HTMWHVTRGS VICHETGRLE PSWADVRNDM 
      1560       1570       1580       1590       1600
ISYGGGWRLG DKWDKEEDVQ VLAIEPGKNP KHVQTKPGLF KTLTGEIGAV 
      1610       1620       1630       1640       1650
TLDFKPGTSG SPIINRKGKV IGLYGNGVVT KSGDYVSAIT QAERTGEPDY 
      1660       1670       1680       1690       1700
EVDEDIFRKK RLTIMDLHPG AGKTKRILPS IVREALKRRL RTLILAPTRV 
      1710       1720       1730       1740       1750
VAAEMEEALR GLPIRYQTPA VKSEHTGREI VDLMCHATFT TRLLSSTRVP 
      1760       1770       1780       1790       1800
NYNLIVMDEA HFTDPSSVAA RGYISTRVEM GEAAAIFMTA TPPGATDPFP 
      1810       1820       1830       1840       1850
QSNSPIEDIE REIPERSWNT GFDWITDYQG KTVWFVPSIK AGNDIANCLR 
      1860       1870       1880       1890       1900
KSGKKVIQLS RKTFDTEYPK TKLTDWDFVV TTDISEMGAN FRAGRVIDPR 
      1910       1920       1930       1940       1950
RCLKPVISTD GPERVILAGP IPVTPASAAQ RRGRIGRNPA QEDDQYVFSG 
      1960       1970       1980       1990       2000
DPLKNDEDHA HWTEAKMLLD NIYTPEGIIP TLFGPEREKN QAIDGEFRLR 
      2010       2020       2030       2040       2050
GEQRKTFVEL MRRGDLPVWL SYKVASAGIS YKDREWCFTG ERNNQILEEN 
      2060       2070       2080       2090       2100
MEVEIWTREG EKKKLRPKWL DARVYADPMA LKDFKEFASG RKSITLDILT 
      2110       2120       2130       2140       2150
EIASLPTYLS SRAKLALDNI VMLHTTERGG KAYQHALNEL PESLETLMLV 
      2160       2170       2180       2190       2200
ALLGAMTAGI FLFFMQGKGI GKLSMGLIAI AVASGLLWVA EIQPQWIAAS 
      2210       2220       2230       2240       2250
IILEFFLMVL LIPEPEKQRT PQDNQLIYVI LTILTIIGLI AANEMGLIEK 
      2260       2270       2280       2290       2300
TKTDFGFYQV KTETTILDVD LRPASAWTLY AVATTILTPM LRHTIENTSA 
      2310       2320       2330       2340       2350
NLSLAAIANQ AAVLMGLGKG WPLHRMDLGV PLLAMGCYSQ VNPTTLIASL 
      2360       2370       2380       2390       2400
VMLLVHYAII GPGLQAKATR EAQKRTAAGI MKNPTVDGIT VIDLEPISYD 
      2410       2420       2430       2440       2450
PKFEKQLGQV MLLVLCAGQL LLMRTTWAFC EVLTLATGPV LTLWEGNPGR 
      2460       2470       2480       2490       2500
FWNTTIAVST ANIFRGSYLA GAGLAFSLIK NAQTPRRGTG TTGETLGEKW 
      2510       2520       2530       2540       2550
KRQLNSLDRK EFEEYKRSGI LEVDRTEAKS ALKDGSKIKH AVSRGSSKIR 
      2560       2570       2580       2590       2600
WIVERGMVKP KGKVVDLGCG RGGWSYYMAT LKNVTEVKGY TKGGPGHEEP 
      2610       2620       2630       2640       2650
IPMATYGWNL VKLHSGVDVF YKPTEQVDTL LCDIGESSSN PTIEEGRTLR 
      2660       2670       2680       2690       2700
VLKMVEPWLS SKPEFCIKVL NPYMPTVIEE LEKLQRKHGG SLVRCPLSRN 
      2710       2720       2730       2740       2750
STHEMYWVSG VSGNIVSSVN TTSKMLLNRF TTRHRKPTYE KDVDLGAGTR 
      2760       2770       2780       2790       2800
SVSTETEKPD MTIIGRRLQR LQEEHKETWH YDQENPYRTW AYHGSYEAPS 
      2810       2820       2830       2840       2850
TGSASSMVNG VVKLLTKPWD VIPMVTQLAM TDTTPFGQQR VFKEKVDTRT 
      2860       2870       2880       2890       2900
PQPKPGTRMV MTTTANWLWA LLGKKKNPRL CTREEFISKV RSNAAIGAVF 
      2910       2920       2930       2940       2950
QEEQGWTSAS EAVNDSRFWE LVDKERALHQ EGKCESCVYN MMGKREKKLG 
      2960       2970       2980       2990       3000
EFGRAKGSRA IWYMWLGARF LEFEALGFLN EDHWFGRENS WSGVEGEGLH 
      3010       3020       3030       3040       3050
RLGYILEDID KKDGDLIYAD DTAGWDTRIT EDDLLNEELI TEQMAPHHKI 
      3060       3070       3080       3090       3100
LAKAIFKLTY QNKVVKVLRP TPKGAVMDII SRKDQRGSGQ VGTYGLNTFT 
      3110       3120       3130       3140       3150
NMEVQLIRQM EAEGVITQDD MHNPKGLKER VEKWLKECGV DRLKRMAISG 
      3160       3170       3180       3190       3200
DDCVVKPLDE RFSTSLLFLN DMGKVRKDIP QWEPSKGWKN WQEVPFCSHH 
      3210       3220       3230       3240       3250
FHKIFMKDGR SLVVPCRNQD ELIGRARISQ GAGWSLRETA CLGKAYAQMW 
      3260       3270       3280       3290       3300
SLMYFHRRDL RLASMAICSA VPTEWFPTSR TTWSIHAHHQ WMTTEDMLKV 
      3310       3320       3330       3340       3350
WNRVWIEDNP NMTDKTPVHS WEDIPYLGKR EDLWCGSLIG LSSRATWAKN 
      3360       3370       3380 
IHTAITQVRN LIGKEEYVDY MPVMKRYSAP FESEGVL
Length:3,387
Mass (Da):378,408
Last modified:April 26, 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:i83A0CECAB088E1A8
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
AY947539 Genomic RNA Translation: AAX48017.1

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Virus Pathogen Resource

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY947539 Genomic RNA Translation: AAX48017.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AM0X-ray3.02Q/R/S/T574-674[»]
BMRBiQ58HT7
SMRiQ58HT7
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiS07.001

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		Q58HT7, 4 sequenced antibodies

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q58HT7

Family and domain databases

CDDicd20761, capping_2-OMTase_Flaviviridae, 1 hit
cd12149, Flavi_E_C, 1 hit
Gene3Di1.10.10.930, 1 hit
1.10.8.970, 1 hit
1.20.1280.260, 1 hit
2.40.10.10, 1 hit
2.60.260.50, 1 hit
2.60.40.350, 1 hit
2.60.98.10, 1 hit
3.30.387.10, 1 hit
3.30.67.10, 1 hit
3.40.50.150, 1 hit
3.40.50.300, 2 hits
InterProiView protein in InterPro
IPR011492, DEAD_Flavivir
IPR043502, DNA/RNA_pol_sf
IPR000069, Env_glycoprot_M_flavivir
IPR038302, Env_glycoprot_M_sf_flavivir
IPR013755, Flav_gly_cen_dom_subdom1
IPR001122, Flavi_capsidC
IPR037172, Flavi_capsidC_sf
IPR027287, Flavi_E_Ig-like
IPR026470, Flavi_E_Stem/Anchor_dom
IPR038345, Flavi_E_Stem/Anchor_dom_sf
IPR001157, Flavi_NS1
IPR000752, Flavi_NS2A
IPR000487, Flavi_NS2B
IPR000404, Flavi_NS4A
IPR001528, Flavi_NS4B
IPR002535, Flavi_propep
IPR038688, Flavi_propep_sf
IPR000336, Flavivir/Alphavir_Ig-like_sf
IPR001850, Flavivirus_NS3_S7
IPR014412, Gen_Poly_FLV
IPR011998, Glycoprot_cen/dimer
IPR036253, Glycoprot_cen/dimer_sf
IPR038055, Glycoprot_E_dimer_dom
IPR013756, GlyE_cen_dom_subdom2
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR014756, Ig_E-set
IPR026490, mRNA_cap_0/1_MeTrfase
IPR027417, P-loop_NTPase
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR000208, RNA-dir_pol_flavivirus
IPR007094, RNA-dir_pol_PSvirus
IPR002877, rRNA_MeTrfase_FtsJ_dom
IPR029063, SAM-dependent_MTases
PfamiView protein in Pfam
PF01003, Flavi_capsid, 1 hit
PF07652, Flavi_DEAD, 1 hit
PF02832, Flavi_glycop_C, 1 hit
PF00869, Flavi_glycoprot, 1 hit
PF01004, Flavi_M, 1 hit
PF00948, Flavi_NS1, 1 hit
PF01005, Flavi_NS2A, 1 hit
PF01002, Flavi_NS2B, 1 hit
PF01350, Flavi_NS4A, 1 hit
PF01349, Flavi_NS4B, 1 hit
PF00972, Flavi_NS5, 1 hit
PF01570, Flavi_propep, 1 hit
PF01728, FtsJ, 1 hit
PF00949, Peptidase_S7, 1 hit
PIRSFiPIRSF003817, Gen_Poly_FLV, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SUPFAMiSSF101257, SSF101257, 1 hit
SSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 2 hits
SSF53335, SSF53335, 1 hit
SSF56672, SSF56672, 1 hit
SSF56983, SSF56983, 1 hit
SSF81296, SSF81296, 1 hit
TIGRFAMsiTIGR04240, flavi_E_stem, 1 hit
PROSITEiView protein in PROSITE
PS51527, FLAVIVIRUS_NS2B, 1 hit
PS51528, FLAVIVIRUS_NS3PRO, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51591, RNA_CAP01_NS5_MT, 1 hit

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_DEN4P
<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: Q58HT7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: April 26, 2005
Last modified: May 25, 2022
This is version 130 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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

Keywords - Technical termi

3D-structure

Documents

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