Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 140 (18 Sep 2019)
Sequence version 1 (01 Feb 1994)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Genome polyprotein

Gene
N/A
Organism
Mosquito cell fusing agent (CFA flavivirus)
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

Capsid protein C: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions.By similarity
Peptide pr: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.By similarity
Protein prM: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Small envelope protein M: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.By similarity
Envelope protein E: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Non-structural protein 1: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. May play a role in viral genome replication. Assist membrane bending and envelopment of genomic RNA at the endoplasmic reticulum. Excreted as a hexameric lipoparticle that plays a role against host immune response.By similarity
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.By similarity
Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy similarity
Serine protease NS3: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.PROSITE-ProRule annotation
Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.By similarity
Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
Non-structural protein 4B: Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of a cellular antiviral state by blocking the IFN-alpha/beta pathway.By similarity
RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.By similarity

Caution

The cleavage sites are uncertain because this virus is very divergent from other flaviviruses.Curated

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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1506Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1530Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1589Charge 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>Sitei2468mRNA cap bindingPROSITE-ProRule annotation1
Sitei2471mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2472mRNA cap bindingPROSITE-ProRule annotation1
Sitei2474mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2479mRNA cap bindingPROSITE-ProRule annotation1
Sitei2483mRNA cap bindingPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei2497S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2502Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Active sitei2509For 2'-O-MTase activityBy similarity1
Binding sitei2527S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2528S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2545S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2546S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2572S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2573S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2587For 2'-O-MTase activityBy similarity1
Sitei2587Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2588S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2591mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2624For 2'-O-MTase activityBy similarity1
Sitei2624Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2655mRNA cap bindingPROSITE-ProRule annotation1
Sitei2657mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2660For 2'-O-MTase activityBy similarity1
Sitei2660Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2662S-adenosyl-L-methioninePROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi2881Zinc 1By similarity1
Metal bindingi2885Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2890Zinc 1By similarity1
Metal bindingi2893Zinc 1By similarity1
Metal bindingi3152Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3168Zinc 2By similarity1
Metal bindingi3287Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1640 – 1647ATPPROSITE-ProRule annotation8

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

GO - Biological processi

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

Molecular functionHelicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, RNA-binding, RNA-directed RNA polymerase, Transferase
Biological processActivation of host autophagy by virus, Host-virus interaction, Inhibition of host complement factors by virus, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host STAT1 by virus, Inhibition of host STAT2 by virus, mRNA capping, mRNA processing, Viral attachment to host cell, Viral immunoevasion, Viral RNA replication, Virus entry into host cell
LigandATP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
Capsid protein
Core protein
Alternative name(s):
Matrix protein
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.15, EC:3.6.4.13)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
NS5
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMosquito cell fusing agent (CFA flavivirus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri31658 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesRiboviriaFlaviviridaeFlavivirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiAedes [TaxID: 7158]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008238 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

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

Capsid protein C :
Peptide pr :
Small envelope protein M :
Envelope protein E :
Non-structural protein 1 :
Non-structural protein 2A :
Serine protease subunit NS2B :
Serine protease NS3 :
Non-structural protein 4A :
Non-structural protein 4B :
RNA-directed RNA polymerase NS5 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 120CytoplasmicSequence analysisAdd BLAST120
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei121 – 141HelicalSequence analysisAdd BLAST21
Topological domaini142 – 245ExtracellularSequence analysisAdd BLAST104
Transmembranei246 – 262HelicalCuratedAdd BLAST17
Topological domaini263CytoplasmicCurated1
Transmembranei264 – 278HelicalCuratedAdd BLAST15
Topological domaini279 – 665ExtracellularSequence analysisAdd BLAST387
Transmembranei666 – 686HelicalSequence analysisAdd BLAST21
Topological domaini687 – 689CytoplasmicSequence analysis3
Transmembranei690 – 705HelicalSequence analysisAdd BLAST16
Topological domaini706 – 1138ExtracellularSequence analysisAdd BLAST433
Transmembranei1139 – 1159HelicalSequence analysisAdd BLAST21
Topological domaini1160 – 1178CytoplasmicSequence analysisAdd BLAST19
Transmembranei1179 – 1199HelicalSequence analysisAdd BLAST21
Topological domaini1200 – 1204LumenalSequence analysis5
Transmembranei1205 – 1225HelicalSequence analysisAdd BLAST21
Topological domaini1226 – 1231CytoplasmicSequence analysis6
Transmembranei1232 – 1252HelicalSequence analysisAdd BLAST21
Topological domaini1253 – 1261LumenalSequence analysis9
Transmembranei1262 – 1282HelicalSequence analysisAdd BLAST21
Topological domaini1283 – 1303CytoplasmicSequence analysisAdd BLAST21
Transmembranei1304 – 1324HelicalSequence analysisAdd BLAST21
Topological domaini1325 – 1326LumenalSequence analysis2
Transmembranei1327 – 1347HelicalSequence analysisAdd BLAST21
Topological domaini1348 – 1403CytoplasmicSequence analysisAdd BLAST56
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1404 – 1424HelicalSequence analysisAdd BLAST21
Topological domaini1425 – 2089CytoplasmicSequence analysisAdd BLAST665
Transmembranei2090 – 2110HelicalSequence analysisAdd BLAST21
Topological domaini2111 – 2145LumenalSequence analysisAdd BLAST35
Transmembranei2146 – 2166HelicalSequence analysisAdd BLAST21
Topological domaini2167 – 2178CytoplasmicSequence analysisAdd BLAST12
Transmembranei2179 – 2199Helical; Note=Signal for NS4Sequence analysisAdd BLAST21
Topological domaini2200 – 2242LumenalSequence analysisAdd BLAST43
Transmembranei2243 – 2263HelicalSequence analysisAdd BLAST21
Topological domaini2264 – 2302CytoplasmicSequence analysisAdd BLAST39
Intramembranei2303 – 2323HelicalSequence analysisAdd BLAST21
Topological domaini2324 – 2366CytoplasmicSequence analysisAdd BLAST43
Transmembranei2367 – 2387HelicalSequence analysisAdd BLAST21
Topological domaini2388 – 2412LumenalSequence analysisAdd BLAST25
Transmembranei2413 – 2433HelicalSequence analysisAdd BLAST21
Topological domaini2434 – 3341CytoplasmicSequence analysisAdd BLAST908

GO - Cellular componenti

Keywords - Cellular componenti

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

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000377141 – 116Capsid protein CBy similarityAdd BLAST116
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000441420117 – 136ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST20
ChainiPRO_0000441421137 – 278Protein prMBy similarityAdd BLAST142
ChainiPRO_0000441422137 – 221Peptide prBy similarityAdd BLAST85
ChainiPRO_0000037715222 – 278Small envelope protein MSequence analysisAdd BLAST57
ChainiPRO_0000037716279 – 705Envelope protein EBy similarityAdd BLAST427
ChainiPRO_0000037717706 – 1095Non-structural protein 1By similarityAdd BLAST390
ChainiPRO_00000377181096 – 1327Non-structural protein 2ABy similarityAdd BLAST232
ChainiPRO_00000377191328 – 1451Serine protease subunit NS2BBy similarityAdd BLAST124
ChainiPRO_00000377201452 – 2038Serine protease NS3By similarityAdd BLAST587
ChainiPRO_00000377212039 – 2173Non-structural protein 4ABy similarityAdd BLAST135
<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_00004414232174 – 2199Peptide 2kBy similarityAdd BLAST26
ChainiPRO_00000377222200 – 2457Non-structural protein 4BBy similarityAdd BLAST258
ChainiPRO_00000377232458 – 3341RNA-directed RNA polymerase NS5By similarityAdd BLAST884

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi157N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi243N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi339N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi399N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi411N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi575N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi611N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi794N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi896N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi993N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi1027N-linked (GlcNAc...) asparagine; by hostSequence analysis1

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

Genome polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
Protein prM: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.By similarity
Envelope protein E: N-glycosylated.By similarity
Non-structural protein 1: N-glycosylated. The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells.By similarity
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei116 – 117Cleavage; by viral protease NS3By similarity2
Sitei135 – 136Cleavage; by host signal peptidaseBy similarity2
Sitei705 – 706Cleavage; by host signal peptidaseBy similarity2
Sitei1095 – 1096Cleavage; by hostBy similarity2
Sitei1327 – 1328Cleavage; by viral protease NS3By similarity2
Sitei1451 – 1452Cleavage; by autolysisBy similarity2
Sitei2038 – 2039Cleavage; by autolysisBy similarity2
Sitei2173 – 2174Cleavage; by viral protease NS3By similarity2
Sitei2457 – 2458Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P33515

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

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

Capsid protein C: Homodimer. Protein prM: Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in the endoplasmic reticulum and Golgi. Non-structural protein 1: Forms homodimers as well as homohexamers. NS1 may interact with NS4A. Non-structural protein 2B:

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

Forms a heterodimer with NS2B.

Interacts with NS4B.

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

Interacts with serine protease NS3. RNA-directed RNA polymerase NS5: interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation.

By similarity

GO - Molecular functioni

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

3D structure databases

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

More...
SMRi
P33515

Database of comparative protein structure models

More...
ModBasei
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1452 – 1630Peptidase S7PROSITE-ProRule annotationAdd BLAST179
Domaini1627 – 1780Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST154
Domaini1793 – 1947Helicase C-terminalPROSITE-ProRule annotationAdd BLAST155
Domaini2454 – 2706mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST253
Domaini2970 – 3117RdRp catalyticPROSITE-ProRule annotationAdd BLAST148

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>Regioni55 – 97Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST43
Regioni371 – 384Involved in fusionBy similarityAdd BLAST14

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>Motifi1729 – 1732DECH box4

<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

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.98.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011492 DEAD_Flavivir
IPR001157 Flavi_NS1
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
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
PF07652 Flavi_DEAD, 1 hit
PF00869 Flavi_glycoprot, 1 hit
PF00948 Flavi_NS1, 1 hit
PF00972 Flavi_NS5, 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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 3 hits
SSF53335 SSF53335, 1 hit
SSF56983 SSF56983, 1 hit

PROSITE; a protein domain and family database

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

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

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

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

P33515-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRKDLEARG KAPGRDSSTP FWGREGRRKD KDKGGESPSN RQVTLKTPIQ
60 70 80 90 100
SGRRAGKRQR VGLLGRLGVG WGSFLQEDIV QALIHMALVL HALFASIDRR
110 120 130 140 150
IRSLSRRVTA LESRRTTGNP MTLAFILGFL TVLCGCVVID MQVSTTRGTE
160 170 180 190 200
IFEGETNRTD YLHLLKLPAD GCWSGILVTK KCPKVTDLAK DLESTDCGST
210 220 230 240 250
WTEFTLRYRR CVVKKREKRS REPPKADLLA EMEIIAFKTI RENKTIFIVA
260 270 280 290 300
LLCVAIAKRW PTWVVILLAI GTWTTVKGEF VEPLYTLKAE QMTMLQTIVR
310 320 330 340 350
PEEGYVVATP NGLLEFKTGP AEIYGGQWLR ELLADCHVNA SYSTDVCPGG
360 370 380 390 400
SQLNMADIMA KERVCSTQPY NRGWGTGCFK WGIGFVGTCV ELHCDRGFNV
410 420 430 440 450
SSIARSAIVM NVTASFHSVS DTQQMVGDIP LTFRFAKLGN AAMTCRLESE
460 470 480 490 500
QLLLDYYHVT GSSHEGLFLR SQVDSWPGVH STASGRHGME KVVVWGDARS
510 520 530 540 550
NEILVKNVIE PSLSWEDAIA THGGFRDISF VCQIMLDKLV SGAFRDCPGP
560 570 580 590 600
KISTFSQDGF GYSGVVITTL TASSNETCSL SLTCHGCLLQ STKMIFLAGK
610 620 630 640 650
TTSRAFVKCG NHTSTLLVGS TSVSIECALN PISQGWRLAR HVVDRYRRFG
660 670 680 690 700
VSGVAGVWQD LVGKFSVGAF FSNTALLVIL VLAALIDKRI AFLLVLGGYF
710 720 730 740 750
YYVRADLGCG IDTTRKTISC GSGVFVWKHL GVGISNDHAV ELEDYSFTDL
760 770 780 790 800
YIKDMFSWTT KPCLICEDAL QCVALRRAAF SAVGSMGSER VYVNDTLART
810 820 830 840 850
FKFSETAKRT ISVTINLIQY KFSSYVAHGR AEGDLGLLPT MYGSYPEKEA
860 870 880 890 900
DKVIRIVASR PDIRRLCGKA VSFQFKFTGF RRGLYGSNVQ VEVSKNSSTE
910 920 930 940 950
CPTYLAGVAV KNGRTVITDG MFWMESIVLD GVAQITSLEM RQSHRCVWPR
960 970 980 990 1000
EYTPDTLSDP SDQALFIPPA WGGPISRVNH IIGYKTQTDF PWNVSDITLI
1010 1020 1030 1040 1050
EGPAPGTKVK VDSRCHGRMH AQVIGPNDTE SWCCQSCTRI VHFRVGDLLY
1060 1070 1080 1090 1100
YPMEIQLGTM SEASEPNSKI FEEPIGEEPE PTVDDILKRY GKANAQSDFR
1110 1120 1130 1140 1150
RVSQRAGVWF DRSLLNLLCL AISLQLIGAK TRTSTLTRLF LTILAMALFG
1160 1170 1180 1190 1200
LPNLFSSVGL SAWVLLVASS SAQPQDLSMN LWIVLQTGSS AVLLLGYMIR
1210 1220 1230 1240 1250
RKLAMVLGVH HLVTLMCVQF LFSAVDRYQK YLYGLLELMA SVVLLSAYKS
1260 1270 1280 1290 1300
VLQALPPEVL CFSLVMGWKT ALSLATVVFL IFSLNAMYKY ACQYHNPRNG
1310 1320 1330 1340 1350
YRDSGANLWF WTVSLASAGG IWAAEKAHQP TVAAVLAFTM VVLFLYMEQT
1360 1370 1380 1390 1400
NVSMELEFIS AGETPEGVST ENDDGINIPD LKGRYGEDGI VVGAASSSGY
1410 1420 1430 1440 1450
LPELVFVFLL GFAVTSTSYF LGALYLLIAT STNLPVVIIR MLRMKLTASN
1460 1470 1480 1490 1500
RSDDLLGLGG PVETDLQTSF QDIPNGVYRI VVRSLFGDRQ RGAGFSKNGV
1510 1520 1530 1540 1550
FHTLMHVTRG EPVKWRGRVV VPHSGSALRD VVSYGGPWQL DTPTTTEDLV
1560 1570 1580 1590 1600
LMACKPDKTI EYHRYRPGVM SIDGEPVMFI SDDFGKGSSG SPFFINGEPV
1610 1620 1630 1640 1650
GFYGFGFYVN GIYRSTVAGG KPTDVTESLN CDSTRRFVTW HPGKGKTRKV
1660 1670 1680 1690 1700
IVEETKKNYD SNQRTVILTP TRVVMAEVVE ALNNSGMRSD KNLSYCTRNL
1710 1720 1730 1740 1750
ITVACHATFT KFVLSHGAKK VRVAMIIMDE CHFMDPMSIA ARGILEHLHG
1760 1770 1780 1790 1800
QGTKLIYLSA TPPGHAPDTG SNYAISDQSI SFPTWLSPAW IGNVQKSVGA
1810 1820 1830 1840 1850
KKTILFVPSH NQANTLASAI PGSVPLHRAN FSSNYAQAGD AATALVISTD
1860 1870 1880 1890 1900
ISEMGANLGV DLVIDTRRAL RPLVDSATRV KLVETNITTS SMIQRRGRTG
1910 1920 1930 1940 1950
RREPGTYVYP IDSQTEENPV SWVCWPEAQM ILDQLGMTFM LEEAAYSQPP
1960 1970 1980 1990 2000
GRFTLVGEDR MRFLKLMDRD DIPIWLAWHW AEAGDRRHSA LFQGAGTGKI
2010 2020 2030 2040 2050
IENRFGKQEY RPQYVDDRFE SIEWETRKVS IDFYMNCRGG PTLYEFFTVV
2060 2070 2080 2090 2100
DWTDIWRRTA SALWDLSDVM NGEVRDRYTT ERSLTVVMAF VLGVSIMLSC
2110 2120 2130 2140 2150
FIAVWALCFL FSLFRPKKAT YEQMPSSDPL SGGVLVSTPS VLYCMGVPLG
2160 2170 2180 2190 2200
FCVVITLAMF LVYPVLYKSI GNRSYMDSDL VKWVILGSCL ICGVLAWEMR
2210 2220 2230 2240 2250
MFPNIRSDLM ELVKAVKEPE EVVNSGPSFP SWEIAQGKGA TMLDSLQVFF
2260 2270 2280 2290 2300
FITVLSTKFL YWFQENWTAR MYAMKHPEMV SSIGGFRFDE IPFRAVLPSG
2310 2320 2330 2340 2350
FAIVAIASLP SVVVGLLAAG VFMAIMYCQN KWNATPKILT ALDARDQRHD
2360 2370 2380 2390 2400
RPTEITSRVP LENTRSIMYA FCLIFSLFWA FCTRSPGDFL RGSLVVGASM
2410 2420 2430 2440 2450
WQILHPRSKI HDVMDFGSMV SAIGLLEMNY LFYRFMHIAA RALGAVAPFN
2460 2470 2480 2490 2500
QFRALEKSTT IGLGMKWKMT LNALDGDAFT RYKSRGVNET ERGDYVSRGG
2510 2520 2530 2540 2550
LKLNEIISKY EWRPSGRVVD LGCGRGGWSQ RAVMEETVSS ALGFTIGGAE
2560 2570 2580 2590 2600
KENPQRFVTK GYNLATLKTG VDVHRLTPFR CDTIMCDIGE SDPSPIKEKT
2610 2620 2630 2640 2650
RTLKVLQLLE NWLLVNPGAH FVCKILSPYS LEVLRKIESL QHLYNGRLVR
2660 2670 2680 2690 2700
LSHSRNSSVE MYYISGARSN VVRTTYMTLA ALMARFSRHL DSVVLPSPVL
2710 2720 2730 2740 2750
PKGTRADPAA SVASMNTSDM MDRVERLMNE NRGTWFEDQQ HPYKSFKYFG
2760 2770 2780 2790 2800
SFVTDDVKVG GQAVNPLVRK IMWPWETLTS VVGFSMTDVS TYSQQKVLRE
2810 2820 2830 2840 2850
KVDTVIPPHP QHIRRVNRTI TKHFIRLFKN RNLRPRILSK EEFVANVRND
2860 2870 2880 2890 2900
AAVGSWSRDV PWRDVQEAIQ DQCFWDLVGK ERALHLQGKC EMCIYNTMGK
2910 2920 2930 2940 2950
KEKKPSLAGE AKGSRTIWYM WLGSRFLEFE ALGFLNADHW VSREHFPGGV
2960 2970 2980 2990 3000
GGVGVNYFGY YLKDIASRGK YLIADDIAGW DTKISEEDLE DEEALLTALT
3010 3020 3030 3040 3050
EDPYHRALMA ATMRLAYQNI VAMFPRTHSK YGSGTVMDVV GRRDQRGSGQ
3060 3070 3080 3090 3100
VVTYALNTIT NGKVQVARVL ESEGLLQADE SVLDAWLEKH LEEALGNMVI
3110 3120 3130 3140 3150
AGDDVVVSTD NRDFSSALEY LELTGKTRKN VPQGAPSRME SNWEKVEFCS
3160 3170 3180 3190 3200
HHYHEMSLKD GRIIIAPCRH ENEVLGRSRL QKGGVVSISE SACMAKAYAQ
3210 3220 3230 3240 3250
MWALYYFHRR DLRLGFIAIS SAVPTNWFPL GRTSWSVHQY HEWMTTDDML
3260 3270 3280 3290 3300
RVWNDVWVHN NPWMLNKESI ESWDDIPYLH KKQDITCGSL IGVKERATWA
3310 3320 3330 3340
REIENSVISV RRIIDAETGV LNTYKDELSV MSRYRRGNDV I
Length:3,341
Mass (Da):373,267
Last modified:February 1, 1994 - 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:iBF0715F836F245ED
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
M91671 Genomic RNA Translation: AAA48509.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A42996

<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
M91671 Genomic RNA Translation: AAA48509.1
PIRiA42996

3D structure databases

SMRiP33515
ModBaseiSearch...

Proteomic databases

PRIDEiP33515

Family and domain databases

Gene3Di2.60.98.10, 1 hit
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR001157 Flavi_NS1
IPR001850 Flavivirus_NS3_S7
IPR014412 Gen_Poly_FLV
IPR011998 Glycoprot_cen/dimer
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
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
PF07652 Flavi_DEAD, 1 hit
PF00869 Flavi_glycoprot, 1 hit
PF00948 Flavi_NS1, 1 hit
PF00972 Flavi_NS5, 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
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 3 hits
SSF53335 SSF53335, 1 hit
SSF56983 SSF56983, 1 hit
PROSITEiView protein in PROSITE
PS51528 FLAVIVIRUS_NS3PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51591 RNA_CAP01_NS5_MT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_MCFA
<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: P33515
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 18, 2019
This is version 140 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again