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UniProtKB - Q1X880 (POLG_YEFVU)

Entry version 120 (25 May 2022)
Sequence version 1 (02 May 2006)
Previous versions | rss
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Protein

Genome polyprotein

Gene
N/A
Organism
Yellow fever virus (isolate Uganda/A7094A4/1948) (YFV)
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 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. Also plays a role in virus assembly (By similarity).

PROSITE-ProRule annotationBy similarity

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.

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 (By similarity).

Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition.

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 sitei1537Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1561Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1622Charge 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>Sitei1945Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1948Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2520mRNA cap bindingPROSITE-ProRule annotation1
Sitei2523mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2524mRNA cap bindingPROSITE-ProRule annotation1
Sitei2526mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2531mRNA cap bindingPROSITE-ProRule annotation1
Sitei2535mRNA 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 sitei2563S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2568For 2'-O-MTase activityBy similarity1
Sitei2568Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2593S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2594S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2611S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2612S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2638S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2639S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2653For 2'-O-MTase activityBy similarity1
Sitei2653Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2654S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2657mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2689For 2'-O-MTase activityBy similarity1
Sitei2689Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2720mRNA cap bindingPROSITE-ProRule annotation1
Sitei2722mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2725For 2'-O-MTase activityBy similarity1
Sitei2725Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2727S-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 bindingi2946Zinc 1By similarity1
Metal bindingi2950Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2955Zinc 1By similarity1
Metal bindingi2958Zinc 1By similarity1
Metal bindingi3223Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3239Zinc 2By similarity1
Metal bindingi3358Zinc 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 bindingi1682 – 1689ATPPROSITE-ProRule annotation8

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionHelicase, Hydrolase, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase
Biological processActivation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host 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, GTP-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 14 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
Non-structural protein 2A-alpha
Short name:
NS2A-alpha
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>OrganismiYellow fever virus (isolate Uganda/A7094A4/1948) (YFV)
<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 identifieri407139 [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 luteocephalus (Mosquito) [TaxID: 299629]
Aedes simpsoni [TaxID: 7161]
Homo sapiens (Human) [TaxID: 9606]
Simiiformes [TaxID: 314293]
<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
  • UP000002486 <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 – 104CytoplasmicSequence analysisAdd BLAST104
<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>Transmembranei105 – 125HelicalSequence analysisAdd BLAST21
Topological domaini126 – 244ExtracellularSequence analysisAdd BLAST119
Transmembranei245 – 265HelicalSequence analysisAdd BLAST21
Topological domaini266 – 270CytoplasmicSequence analysis5
Transmembranei271 – 285HelicalSequence analysisAdd BLAST15
Topological domaini286 – 730ExtracellularSequence analysisAdd BLAST445
Transmembranei731 – 751HelicalSequence analysisAdd BLAST21
Topological domaini752 – 757ExtracellularSequence analysis6
Transmembranei758 – 778HelicalSequence analysisAdd BLAST21
Topological domaini779 – 1132ExtracellularBy similarityAdd BLAST354
Transmembranei1133 – 1153HelicalBy similarityAdd BLAST21
Topological domaini1154 – 1201CytoplasmicBy similarityAdd BLAST48
Transmembranei1202 – 1222HelicalBy similarityAdd BLAST21
Topological domaini1223 – 1287LumenalBy similarityAdd BLAST65
Transmembranei1288 – 1308HelicalBy similarityAdd BLAST21
Topological domaini1309 – 1355CytoplasmicBy similarityAdd BLAST47
Transmembranei1356 – 1376HelicalBy similarityAdd BLAST21
Topological domaini1377 – 1378LumenalBy similarity2
Transmembranei1379 – 1399HelicalSequence analysisAdd BLAST21
Topological domaini1400 – 1456CytoplasmicSequence analysisAdd BLAST57
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1457 – 1477HelicalSequence analysisAdd BLAST21
Topological domaini1478 – 2157CytoplasmicSequence analysisAdd BLAST680
Transmembranei2158 – 2178HelicalSequence analysisAdd BLAST21
Topological domaini2179 – 2186LumenalSequence analysis8
Intramembranei2187 – 2207HelicalSequence analysisAdd BLAST21
Topological domaini2208 – 2209LumenalSequence analysis2
Transmembranei2210 – 2230HelicalSequence analysisAdd BLAST21
Topological domaini2231 – 2241CytoplasmicSequence analysisAdd BLAST11
Transmembranei2242 – 2262Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2263 – 2293LumenalSequence analysisAdd BLAST31
Intramembranei2294 – 2314HelicalSequence analysisAdd BLAST21
Topological domaini2315 – 2360LumenalSequence analysisAdd BLAST46
Transmembranei2361 – 2380HelicalSequence analysisAdd BLAST20
Topological domaini2381 – 2421CytoplasmicSequence analysisAdd BLAST41
Transmembranei2422 – 2442HelicalSequence analysisAdd BLAST21
Topological domaini2443 – 2445LumenalSequence analysis3
Transmembranei2446 – 2466HelicalSequence analysisAdd BLAST21
Topological domaini2467 – 3411CytoplasmicSequence analysisAdd BLAST945

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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004051601 – 3412Genome polyproteinAdd BLAST3412
ChainiPRO_00002615301 – 101Capsid protein CBy similarityAdd BLAST101
<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_0000261531102 – 121ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST20
ChainiPRO_0000261532122 – 285Protein prMBy similarityAdd BLAST164
ChainiPRO_0000261533122 – 210Peptide prBy similarityAdd BLAST89
ChainiPRO_0000261534211 – 285Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000261535286 – 778Envelope protein EBy similarityAdd BLAST493
ChainiPRO_0000261536779 – 1130Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00002615371131 – 1354Non-structural protein 2ABy similarityAdd BLAST224
ChainiPRO_00002615381131 – 1320Non-structural protein 2A-alphaBy similarityAdd BLAST190
ChainiPRO_00002615391355 – 1484Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00002615401485 – 2107Serine protease NS3By similarityAdd BLAST623
ChainiPRO_00002615412108 – 2233Non-structural protein 4ABy similarityAdd BLAST126
<p>This subsection of the 'PTM / Processing' section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_00002615422234 – 2256Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00002615432257 – 2507Non-structural protein 4BBy similarityAdd BLAST251
ChainiPRO_00002615442508 – 3412RNA-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%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>Glycosylationi134N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi150N-linked (GlcNAc...) asparagine; by hostSequence analysis1
<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 bondi288 ↔ 315By similarity
Disulfide bondi345 ↔ 406By similarity
Disulfide bondi345 ↔ 401By similarity
Disulfide bondi359 ↔ 390By similarity
Disulfide bondi377 ↔ 406By similarity
Disulfide bondi377 ↔ 401By similarity
Disulfide bondi467 ↔ 568By similarity
Disulfide bondi585 ↔ 615By similarity
Disulfide bondi782 ↔ 793By similarity
Disulfide bondi833 ↔ 921By similarity
Glycosylationi908N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi957 ↔ 1002By similarity
Glycosylationi986N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi1058 ↔ 1107By similarity
Disulfide bondi1069 ↔ 1091By similarity
Disulfide bondi1090 ↔ 1094By 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 residuei2563PhosphoserineBy 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. The nascent capsid protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature capsid protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Specific enzymatic cleavages in vivo yield mature proteins peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. 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
Polyubiquitinated; ubiquitination is probably mediated by host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is not ISGylated or sumoylated.By similarity
Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei101 – 102Cleavage; by viral protease NS3By similarity2
Sitei121 – 122Cleavage; by host signal peptidaseBy similarity2
Sitei210 – 211Cleavage; by host furinBy similarity2
Sitei285 – 286Cleavage; by host signal peptidaseBy similarity2
Sitei778 – 779Cleavage; by host signal peptidaseBy similarity2
Sitei1130 – 1131Cleavage; by hostBy similarity2
Sitei1354 – 1355Cleavage; by viral protease NS3By similarity2
Sitei1484 – 1485Cleavage; by autolysisBy similarity2
Sitei2107 – 2108Cleavage; by autolysisBy similarity2
Sitei2233 – 2234Cleavage; by viral protease NS3By similarity2
Sitei2256 – 2257Cleavage; by host signal peptidaseBy similarity2
Sitei2507 – 2508Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		Q1X880

<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 (By similarity).

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

By similarity

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

By similarity

Homodimer; in the endoplasmic reticulum and Golgi (By similarity).

Interacts with protein prM (By similarity).

Interacts with non-structural protein 1 (By similarity).

By similarity

Homodimer; Homohexamer when secreted (By similarity).

Interacts with envelope protein E (By similarity).

By similarity

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

By similarity

Forms a heterodimer with serine protease NS3 (By similarity). May form homooligomers (By similarity).

By similarity

Forms a heterodimer with NS2B (By similarity).

Interacts with non-structural protein 2A (via N-terminus) (By similarity).

Interacts with NS4B (By similarity).

Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity). NS3 interacts with host PDCD6IP; this interaction contributes to virion release (By similarity).

By similarity

Interacts with serine protease NS3 (By similarity).

By similarity

Homodimer (By similarity).

Interacts with host STAT2; this interaction prevents the establishment of cellular antiviral state (By similarity).

Interacts with serine protease NS3 (By similarity).

Interacts with host TRIM23; this interaction leads to NS5 ubiquitination (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

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q1X880

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

More...SMRi		Q1X880

Database of comparative protein structure models

More...ModBasei		Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%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>Domaini1485 – 1665Peptidase S7PROSITE-ProRule annotationAdd BLAST181
Domaini1669 – 1825Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1820 – 1997Helicase C-terminalAdd BLAST178
Domaini2508 – 2772mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3036 – 3188RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni38 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST35
Regioni383 – 396Fusion peptideBy similarityAdd BLAST14
Regioni1407 – 1446Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1673 – 1676Important for RNA-bindingBy similarity4
Regioni1942 – 1961DisorderedSequence analysisAdd BLAST20

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>Motifi1773 – 1776DEAH boxPROSITE-ProRule annotation4
Motifi2879 – 2912Nuclear localization signalBy similarityAdd BLAST34

<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
2.60.260.50, 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
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		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.

Q1X880-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF 
        60         70         80         90        100
FLFNILTGKK LTTHLKRLWR MLDPRQGLTV LRKVKRVVAS LMRGLSSRKR 
       110        120        130        140        150
RSSEMTMMPL LILSMVILGG GVTLVRKNRW LLLNVTAEDL GKTFSVGTGN 
       160        170        180        190        200
CTTNILEAKY WCPDSMEYNC PNLSPREEPD DIDCWCYGVE NVRVAYGRCD 
       210        220        230        240        250
AVGRSKRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ KIERWLVRNP 
       260        270        280        290        300
FFAVTALAIA YLVGNNKTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV 
       310        320        330        340        350
HGGTWVSASL EQDKCVTVMA PDKPSLDISL QTVAIDGPAE ARKVCYSAVL 
       360        370        380        390        400
THVKINDKCP STGEAHLAEE NDGDNACKRT YSDRGWGNGC GLFGKGSIVA 
       410        420        430        440        450
CAKFTCAKSM SLFEVDQTKI QYVIRAQLHV GAKQENWNTD IKTLKFDALS 
       460        470        480        490        500
GSQEAEFTGY GKATLECQVQ TAVDFGNSYI AEMEKDSWIV DRQWAQDLTL 
       510        520        530        540        550
PWQSGSGGIW REMHHLVEFE PPHAATIRVL ALGNQEGSLK TALTGAMRVT 
       560        570        580        590        600
KDENDNNLYK LHGGHVSCRV KLSALTLKGT SYKMCTDKMS FVKNPTDTGH 
       610        620        630        640        650
GTVVMQVKVP KGAPCKIPVI VADDLTAAVN KGILVTVNPI ASTNDDEVLI 
       660        670        680        690        700
EVNPPFGDSY IIVGTGDSRL TYQWHKEGSS IGKLFTQTMK GVERLAVMGD 
       710        720        730        740        750
AAWDFSSAGG FFTSVGKGIH TVFGSAFQGL FGGLSWITKV IMGAVLIWVG 
       760        770        780        790        800
INTRNMTMSM SMILVGVIMM FLSLGVGADQ GCAVNFGKRE LKCGDGIFVF 
       810        820        830        840        850
RDSDDWLTKY SYYPEDPVKL ASIIKASYEE GKCGLNSVDS LEHEMWRSRA 
       860        870        880        890        900
DEINAIFEEN EVDISIVVQD PKNIYQRGTH PFSRIRDGLQ YGWKTWGKNL 
       910        920        930        940        950
IFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGMGV FTTRVFMDAV 
       960        970        980        990       1000
FDYSVDCDGA ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM MHTLETLDYK 
      1010       1020       1030       1040       1050
ECEWPLTHTI GTSVEESDMF MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP 
      1060       1070       1080       1090       1100
LEVRREPCPG TSVVVDTSCD GRGKSTRSTT DSGKIIPEWC CRSCTMPPVS 
      1110       1120       1130       1140       1150
FHGSDGCWYP MEIRPMKTHE SHLVRSWVTA GEVHAVPFGL VSMMIAMEVV 
      1160       1170       1180       1190       1200
LRKRQGPKQM LVGGIILLGA MLVGQVTMLD LVKLIVAVGL HFHEINNGGD 
      1210       1220       1230       1240       1250
AMYMALIASF SIRPGLLIGF GLRTLWSPRE RLVMAFGAAM VEVALGGMMG 
      1260       1270       1280       1290       1300
GLWQYLNAVS LCVLTINAIS SRKASNTILP LMALLTPVTM YEVRMATMLF 
      1310       1320       1330       1340       1350
CTVVIVGVLH QNSKDTSMQK TIPIVALTLT SYMGLTQPFL GLCAYMSTQV 
      1360       1370       1380       1390       1400
FGRRSIPVNE ALAAAGLVGV LAGLAFQDME NFLGPIAVGG ILMMLVSVAG 
      1410       1420       1430       1440       1450
KVDGLELKKL GEVSWEEEAE ISGSSSRYDV ALSEQGEFKL LSEDKVPWDQ 
      1460       1470       1480       1490       1500
IVMTSLALVG AAIHPFALLL VLGGWVLHIK GARRSGDVLW DIPTPKVIEE 
      1510       1520       1530       1540       1550
CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLLRNGKK 
      1560       1570       1580       1590       1600
LVPSWASVKE DLVAYGGSWK LDGKWDGEEE VQLIAAVPGK AVVNVQTKPS 
      1610       1620       1630       1640       1650
LFKVRNGGEI GAVALDYPSG TSGSPIVNRS GEVVGLYGNG ILVGDNSFVS 
      1660       1670       1680       1690       1700
AISQTEVKEE SKEELQEIPT MLKKGMTTIL DFHPGAGKTR RFLPQILAEC 
      1710       1720       1730       1740       1750
ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG SGKEVIDAMC 
      1760       1770       1780       1790       1800
HATLTYRMLE PTRVVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT 
      1810       1820       1830       1840       1850
ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWTSGHEWI LADKRPTAWF 
      1860       1870       1880       1890       1900
LPSIRAANVM AASLRKAGKN VVVLNRKTFE KEYPTIKQKR PDFILATDIA 
      1910       1920       1930       1940       1950
EMGANLCVER VLDCRTAYKP VLVDEGRKVA IKGPLRISAS SAAQRRGRIG 
      1960       1970       1980       1990       2000
RNPNRDGDSY YYSEPTSEDN AHHVCWLEAS MLLDNMEVRG GMVAPLYGIE 
      2010       2020       2030       2040       2050
GTKTPVSPGE MRLRDDQRRV FRELVRGCDL PVWLSWQVAK AGLKTNDRKW 
      2060       2070       2080       2090       2100
CFEGPEEHEI LNDNGETVKC RSPGGAKKAL RPRWCDERVS SDQSALADFI 
      2110       2120       2130       2140       2150
KFAEGRRGAA EMLVVLTELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA 
      2160       2170       2180       2190       2200
LSMMPEAMTI VMLFILAGLL TSGMVIFFMS PKGMSRMSMA MGTMAGSGYL 
      2210       2220       2230       2240       2250
MFLGGVKPTH ISYVMLIFFV LMVVIIPEPG QQRSIQDNQV AYLIIGILTL 
      2260       2270       2280       2290       2300
LSVVAANELG MLEKTKEDFF GKRNIATSGG TIPWSWPDLD LKPGAAWTVY 
      2310       2320       2330       2340       2350
VGIVTMLSPM LHHWIKVEYG NLSLSGIAQS ASVLSFMDKG VPFMKMNISV 
      2360       2370       2380       2390       2400
VILLVSGWNS ITVIPLLCGV GGAMLHWTLI LPGIKAQQSK LAQKRVFHGV 
      2410       2420       2430       2440       2450
AKNPVVDGNP TADIEEAPEM PALYEKKLAL YLLLALSLMS VAMCRTPFSL 
      2460       2470       2480       2490       2500
AEGIVLSSAA LGPLIEGNTS LLWNGPMAVS MTGVMRGNYY AFVGVMYNLW 
      2510       2520       2530       2540       2550
KMKTGRRGSA NGKTLGEVWK RELNLLDKQQ FELYKRTDIT EVDRDMARRH 
      2560       2570       2580       2590       2600
LAEGKVDTGV AVSRGTAKLR WFHERGYVKL EGRVMDLGCG RGGWCYYAAA 
      2610       2620       2630       2640       2650
QKEVSGVKGY TLGRDGHEKP MNVQSLGWNI VTFKDKTDIH RLEPAKCETL 
      2660       2670       2680       2690       2700
LCDIGESSPS SVTEGERTLR VLETVEKWLA CGVDNFCVKV LAPYMPDVIE 
      2710       2720       2730       2740       2750
KLELLQRRFG GTVIRNPLSR NSTHEMYYVS GARSNITFTV NQTSRLLMRR 
      2760       2770       2780       2790       2800
MRRPTGKVTL EPDVILPIGT RSVETDKGPL DRGAIEERVE RIKTEYAATW 
      2810       2820       2830       2840       2850
FHDNDNPYRT WHYCGSYITK TSGSAASMIN GVIKILTFPW DRIEEVTRMA 
      2860       2870       2880       2890       2900
MTDTTPFGQQ RVFKEKVDTR AKDPPAGTRK IMRVVNRWLF RHLAREKKPR 
      2910       2920       2930       2940       2950
LCTKEEFIAK VRSHAAIGAF LEEQEQWKTA NEAVQDPKFW EMVDAERKLH 
      2960       2970       2980       2990       3000
QQGRCQSCVY NMMGKREKKL SEFGKAKGSR AIWYMWLGAR FLEFEALGFL 
      3010       3020       3030       3040       3050
NEDHWASREN SGGGVEGIGL QYLGYVIKDL STKEGGGFYA DDTAGWDTRI 
      3060       3070       3080       3090       3100
TEADLDDEQE IMSYMNAEQR KLAWAVMEMT YKNKVVKVLR PAPGGKAFMD 
      3110       3120       3130       3140       3150
IISRRDQRGS GQVVTYALNT ITNLKVQLIR MAEAEMVINH QHVNECDESA 
      3160       3170       3180       3190       3200
LARLDAWLAE NGCDRLARMA VSGDDCVVKP VDDRFGLALS HLNAMSKVRK 
      3210       3220       3230       3240       3250
DISEWQPSKG WTDWESVPFC SHHFHELVLK DGRKVVVPCR DQDELIGRGR 
      3260       3270       3280       3290       3300
VSPGNGWMIK ETACLSKAYA NMWSLMYFHK RDMRLLSFAV SSAVPTAWVP 
      3310       3320       3330       3340       3350
SGRTTWSVHG KGEWMTTEDM LDVWNRVWVL NNPHMKDKTT VKEWRDVPYL 
      3360       3370       3380       3390       3400
TKRQDKLCGS LIGMTNRATW ASHIHLVIHR IRNLIGQEKY TDYLTVMDRY 
      3410 
SVDADLQPGE LI
Length:3,412
Mass (Da):378,817
Last modified:May 2, 2006 - 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:iA4E981722EB79F52
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
AY968065 Genomic RNA Translation: AAY34248.1

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY968065 Genomic RNA Translation: AAY34248.1

3D structure databases

BMRBiQ1X880
SMRiQ1X880
ModBaseiSearch...

Protein family/group databases

MEROPSiS07.001

Proteomic databases

PRIDEiQ1X880

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
2.60.260.50, 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
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
SUPFAMiSSF50494, 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_YEFVU
<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: Q1X880
<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: November 28, 2006
Last sequence update: May 2, 2006
Last modified: May 25, 2022
This is version 120 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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