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Entry version 132 (29 Sep 2021)
Sequence version 1 (06 Dec 2005)
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Protein

Genome polyprotein

Gene
N/A
Organism
Kokobera virus (KOKV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

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

By similarity

Inhibits RNA silencing by interfering with host Dicer.

By similarity

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

By similarity

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

By similarity

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

By similarity

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

By similarity

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

By similarity

Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response.

By similarity

Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).

PROSITE-ProRule annotationBy similarity

displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (PubMed:18004778).

PROSITE-ProRule annotation1 Publication

Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.

By similarity

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

By similarity

Induces the formation of ER-derived membrane vesicles where the viral replication takes place. Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway. Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment.

By similarity

Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway.

By similarity

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

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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=340 mM for ATPase of serine protease NS31 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1543Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1567Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1627Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1692Substrate binding1 Publication1
Sitei1947Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1950Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1950Substrate binding1 Publication1
Sitei1953Substrate binding1 Publication1
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_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 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
Active sitei2690For 2'-O-MTase activityBy similarity1
Sitei2690Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2721mRNA cap bindingPROSITE-ProRule annotation1
Sitei2723mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2726For 2'-O-MTase activityBy similarity1
Sitei2726Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2728S-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 bindingi2947Zinc 1By similarity1
Metal bindingi2951Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2956Zinc 1By similarity1
Metal bindingi2959Zinc 1By similarity1
Metal bindingi3222Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3238Zinc 2By similarity1
Metal bindingi3356Zinc 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 bindingi1686 – 1693ATPPROSITE-ProRule annotation8

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

GO - Biological processi

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

Molecular functionHelicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Transferase
Biological processActivation of host autophagy by virus, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host STAT1 by virus, Inhibition of host STAT2 by virus, mRNA capping, mRNA processing, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus entry into host cell
LigandATP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.21.91, 10317

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_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.151 Publication, EC:3.6.4.131 Publication)
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>OrganismiKokobera virus (KOKV)
<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 identifieri44024 [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 lineageiVirusesRiboviriaOrthornaviraeKitrinoviricotaFlasuviricetesAmarilloviralesFlaviviridaeFlavivirus
<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 hostiCulex annulirostris (Common banded mosquito) [TaxID: 162997]
Homo sapiens (Human) [TaxID: 9606]
Ochlerotatus camptorhynchus [TaxID: 644619]
Ochlerotatus vigilax [TaxID: 569589]
<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
  • UP000124420 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 103CytoplasmicSequence analysisAdd BLAST103
<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>Transmembranei104 – 124HelicalSequence analysisAdd BLAST21
Topological domaini125 – 245ExtracellularSequence analysisAdd BLAST121
Transmembranei246 – 266HelicalSequence analysisAdd BLAST21
Topological domaini267 – 271CytoplasmicSequence analysis5
Transmembranei272 – 286HelicalCuratedAdd BLAST15
Topological domaini287 – 739ExtracellularSequence analysisAdd BLAST453
Transmembranei740 – 760HelicalSequence analysisAdd BLAST21
Topological domaini761 – 766CytoplasmicSequence analysis6
Transmembranei767 – 787HelicalSequence analysisAdd BLAST21
Topological domaini788 – 1165ExtracellularSequence analysisAdd BLAST378
Transmembranei1166 – 1186HelicalSequence analysisAdd BLAST21
Topological domaini1187 – 1214CytoplasmicSequence analysisAdd BLAST28
Transmembranei1215 – 1235HelicalSequence analysisAdd BLAST21
Topological domaini1236 – 1242LumenalSequence analysis7
Transmembranei1243 – 1263HelicalSequence analysisAdd BLAST21
Topological domaini1264 – 1284CytoplasmicSequence analysisAdd BLAST21
Transmembranei1285 – 1305HelicalSequence analysisAdd BLAST21
Topological domaini1306 – 1335LumenalSequence analysisAdd BLAST30
Transmembranei1336 – 1356HelicalSequence analysisAdd BLAST21
Topological domaini1357 – 1363CytoplasmicSequence analysis7
Transmembranei1364 – 1384HelicalSequence analysisAdd BLAST21
Topological domaini1385 – 1387LumenalSequence analysis3
Transmembranei1388 – 1408HelicalSequence analysisAdd BLAST21
Topological domaini1409 – 1464CytoplasmicSequence 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>Intramembranei1465 – 1485HelicalSequence analysisAdd BLAST21
Topological domaini1486 – 2158CytoplasmicSequence analysisAdd BLAST673
Transmembranei2159 – 2179HelicalSequence analysisAdd BLAST21
Topological domaini2180 – 2185LumenalSequence analysis6
Intramembranei2186 – 2205HelicalSequence analysisAdd BLAST20
Topological domaini2206LumenalSequence analysis1
Transmembranei2207 – 2227HelicalSequence analysisAdd BLAST21
Topological domaini2228 – 2242CytoplasmicSequence analysisAdd BLAST15
Transmembranei2243 – 2257Helical; Note=Signal for NS4BCuratedAdd BLAST15
Topological domaini2258 – 2293LumenalSequence analysisAdd BLAST36
Intramembranei2294 – 2314HelicalSequence analysisAdd BLAST21
Topological domaini2315 – 2336LumenalSequence analysisAdd BLAST22
Transmembranei2337 – 2357HelicalSequence analysisAdd BLAST21
Topological domaini2358CytoplasmicSequence analysis1
Transmembranei2359 – 2379HelicalSequence analysisAdd BLAST21
Topological domaini2380 – 2420LumenalSequence analysisAdd BLAST41
Transmembranei2421 – 2441HelicalSequence analysisAdd BLAST21
Topological domaini2442 – 3410CytoplasmicSequence analysisAdd BLAST969

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1724M → T: Severe decrease in helicase activity. 1 Publication1

<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_00004415161 – 3410Genome polyproteinAdd BLAST3410
ChainiPRO_00004415171 – 102Capsid protein CBy similarityAdd BLAST102
<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_0000441518103 – 119ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST17
ChainiPRO_0000441519120 – 286Protein prMBy similarityAdd BLAST167
ChainiPRO_0000441520120 – 211Peptide prBy similarityAdd BLAST92
ChainiPRO_0000441521212 – 286Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000441522287 – 787Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000441523788 – 1138Non-structural protein 1By similarityAdd BLAST351
ChainiPRO_00004415241139 – 1362Non-structural protein 2ABy similarityAdd BLAST224
ChainiPRO_00004415251363 – 1492Serine protease subunit NS2BBy similarityAdd BLAST130
ChainiPRO_00004415261493 – 2108Serine protease NS3By similarityAdd BLAST616
ChainiPRO_00004415272109 – 2234Non-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_00004415282235 – 2257Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004415292258 – 2507Non-structural protein 4BBy similarityAdd BLAST250
ChainiPRO_00004415302508 – 3410RNA-directed RNA polymerase NS5By similarityAdd BLAST903

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi289 ↔ 316By similarity
Disulfide bondi346 ↔ 407By similarity
Disulfide bondi346 ↔ 402By similarity
Disulfide bondi360 ↔ 391By similarity
Disulfide bondi378 ↔ 407By similarity
Disulfide bondi378 ↔ 402By similarity
<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>Glycosylationi440N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi476 ↔ 574By similarity
Disulfide bondi591 ↔ 622By similarity
Disulfide bondi791 ↔ 802By similarity
Disulfide bondi842 ↔ 928By similarity
Glycosylationi915N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi964 ↔ 1009By similarity
Disulfide bondi1066 ↔ 1115By similarity
Disulfide bondi1077 ↔ 1099By similarity
Disulfide bondi1077 ↔ 1098By similarity
Disulfide bondi1098 ↔ 1102By similarity
Disulfide bondi1099 ↔ 1102By 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_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei102 – 103Cleavage; by viral protease NS3By similarity2
Sitei121 – 122Cleavage; by host signal peptidaseBy similarity2
Sitei211 – 212Cleavage; by host furinBy similarity2
Sitei286 – 287Cleavage; by host signal peptidaseBy similarity2
Sitei787 – 788Cleavage; by host signal peptidaseBy similarity2
Sitei1138 – 1139Cleavage; by hostBy similarity2
Sitei1362 – 1363Cleavage; by viral protease NS3By similarity2
Sitei1492 – 1493Cleavage; by autolysisBy similarity2
Sitei2108 – 2109Cleavage; by autolysisBy similarity2
Sitei2234 – 2235Cleavage; by viral protease NS3By similarity2
Sitei2257 – 2258Cleavage; by host signal peptidaseSequence analysis2
Sitei2507 – 2508Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

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

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

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

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). NS1 interacts with NS4B (By similarity).

Interacts with host complement protein CFH; this interaction leads to the degradation of C3 (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).

By similarity

Interacts with serine protease NS3 (By similarity).

By similarity

Homodimer (By similarity).

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).

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

Secondary structure

13410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q32ZD5

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q32ZD5

<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>Domaini1493 – 1670Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1673 – 1829Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1839 – 2006Helicase C-terminalPROSITE-ProRule annotationAdd BLAST168
Domaini2508 – 2773mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3036 – 3187RdRp catalyticPROSITE-ProRule annotationAdd BLAST152

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>Regioni2 – 15Interaction with host EXOC1By similarityAdd BLAST14
Regioni38 – 73Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni384 – 397Fusion peptideBy similarityAdd BLAST14
Regioni1415 – 1454Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1677 – 1680Important for RNA-bindingBy similarity4
Regioni2153 – 2157Regulates the ATPase activity of NS3 helicaseBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1777 – 1780DEAH boxPROSITE-ProRule annotation4

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

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

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

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

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...
CDDi
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
3.40.50.300, 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
SSF101257, SSF101257, 1 hit
SSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 2 hits
SSF53335, SSF53335, 1 hit
SSF56672, SSF56672, 1 hit
SSF56983, SSF56983, 1 hit
SSF81296, SSF81296, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR04240, flavi_E_stem, 1 hit

PROSITE; a protein domain and family database

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

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

Q32ZD5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTKKPGRPGR NRAVNMLKRG ASRALGPMIK LKRMLFGLLD GRGPLRMVLA
60 70 80 90 100
ILAFFRFTAL KPTAGLLKRW GMMDKVHALS LLKGFKKDLA SMTDFVHLPK
110 120 130 140 150
KKSGVSIIGR MLVFSFTAAV RVTLENGMSL MKIQKADVGK VITIRTDRGE
160 170 180 190 200
NRCIVQAMDV GEDCEDTMKY LCPAIENPSE PDDIDCWCDK ADAMVTYGRC
210 220 230 240 250
SKTRHSRRSR RSTNIAGHAD SRLDSRGSVW MDTKKATSYL TKAESWALRN
260 270 280 290 300
PGYALVAAVL GWSLGTSNAQ KVIFTVMILL IAPAYSIRCV GVENRDFIEG
310 320 330 340 350
VSGGTWVDVV LEHGGCVTIM APDKPTIDLE LTSTIAKSMA VTRTYCVQAQ
360 370 380 390 400
VSELSVETRC PTMGEAHNSK SSDAAYVCKK GFSDRGWGNG CGLFGKGSME
410 420 430 440 450
TCAKFSCQTK AEGRIIQREN LEYTIHMNVH ASQETGHFMN DTIASENKHG
460 470 480 490 500
AKISITATGP SRTADLGDYG MVTLDCEPRA GLDFDNLYLL TLGRNSWLVN
510 520 530 540 550
RDWFHDVNLP WIGGAEGHWK NRESLVEFGK THATKREVLA LGSQEGTLQV
560 570 580 590 600
ALAGAMIAKF GSNVATINSG HLKCRLKLDK LKIKGTTYHM CKGSFAFTKT
610 620 630 640 650
PSDTGHGTVL LELTYSGSDG PCRVPISMSV SLSNIEPVGR MVTVNPIVLS
660 670 680 690 700
SSPQKTIMIE VEPPFGDSFI IAGTGEPRAH YHWRKSGSSI GAAFATTIKG
710 720 730 740 750
ARRLAVIGDD AWDFGSVGGI LNSVGKALHQ IFGGMFRTLF GGMSWFTQIM
760 770 780 790 800
IGALCCWLGI NARDRTIAVT FLAVGGVLVF LATSVNADSG CALDLKRKEF
810 820 830 840 850
KCGNGIFVFN DAEAWSHSYR YHPSTPKKLA GSIVRAIEEG QCGVRSVGRL
860 870 880 890 900
EHEMWRANAR EINAILLENE KNLSVVVLES EYYRKAKNLM PIGDEMPFGW
910 920 930 940 950
KSWGKKFFEE PQLQNQTFVV DGRVGKECPE EKRSWNNFRI EDFGFGVFTT
960 970 980 990 1000
SVWMEQRTEY TEDCDQKVIG AAVKGELAAH SDLGYWIESR SKNGSWELER
1010 1020 1030 1040 1050
AYLLESKSCS WPATHTLWNG GVEESELIIP KSRAGPVSHH NTRKGYHNQI
1060 1070 1080 1090 1100
KGPWHLTPLE IRFESCPGTT VVTTEECGNR GPSLRTTTTS GKVISEWCCR
1110 1120 1130 1140 1150
SCTMPPLSFR TADGCWYGME IRPLKEREET MVKSHVSAGR GDGVDNLSLG
1160 1170 1180 1190 1200
LLVLTIALQE VMRKRILGRH ITWMVIAVFM AMILGGLSYR DLGRYLVLVG
1210 1220 1230 1240 1250
AAFAERNSGG DLLHLVLVAT FKVKPMALLG FVLGGRWCRR QSLLLSIGAV
1260 1270 1280 1290 1300
LVNFALEFQG GYFELVDSLA LALLFVKAVV QTDTTSVSLP LLAALAPAGC
1310 1320 1330 1340 1350
YTVLGTHRFI MLTLVLVTFL GCKKTASVKK AGTAAVGVVL GMVGMKTIPM
1360 1370 1380 1390 1400
LGMLMVTSRA RRSWPLHEAM AAVGILCALF GALAETEVDL AGPLAAAGLI
1410 1420 1430 1440 1450
VMAYVISGRS NDLSIKKVED VKWSDEAEVT GESVSYHVSL DVRGDPTLTE
1460 1470 1480 1490 1500
DSGPGLEKVL LKVGLMAISG IYPVAIPFAL GAWFFLEKRC KRAGALWDIP
1510 1520 1530 1540 1550
SPREAKPAKV EDGVYRIFSR KLFGESQIGA GVMVKGTFHT MWHVTRGAVL
1560 1570 1580 1590 1600
KAGEGLLEPA WADVRKDLIC YGGNWKLEEH WDGNEEVQLI ALEPGKKVRH
1610 1620 1630 1640 1650
IQTKPGIFKT SEGEIGALDL DCMAGTSGSP IVNKNGEVVG LYGNGVLIKG
1660 1670 1680 1690 1700
DRYVSAISQK ENVGQEDGAE IEDNWFRKRE LTVLDLHPGA GKTRRVLPQL
1710 1720 1730 1740 1750
VREAVKKRLR TVILAPTRVV ASEMYEALRG EPIRYMTPAV QSERTGNEIV
1760 1770 1780 1790 1800
DFMCHSTFTM KLFQGVRVPN YNLYIMDEAH FLDPASVAAR GYIETRVSMG
1810 1820 1830 1840 1850
DAGAIFMTAT PPGTTEAFPP SNSPIIDEET RIPDKAWNSG YEWIIEFDGR
1860 1870 1880 1890 1900
TVWFVHSIKQ GAEIGTCLQK AGKKVLYLNR KTFESEYPKC KSEKWDFVIT
1910 1920 1930 1940 1950
TDISEMGANF KADRVIDPRK TIKPILLDGR VSMQGPIAIT PASAAQRRGR
1960 1970 1980 1990 2000
IGRNPEKLGD IYAYSGNVSS DNEGHVSWTE ARMLLDNVHV QGGVVAQLYT
2010 2020 2030 2040 2050
PEREKTEAYE GEFKLKTNQR KVFSELIRTG DLPVWLAFQV ASANVEYHDR
2060 2070 2080 2090 2100
KWCFDGPNEH LLLENNQEIE VWTRQGQRRV LKPRWLDGRI TSDHLNLKSF
2110 2120 2130 2140 2150
KEFASGKRSA LSILDLIAVL PSHLNLRLQE ALDTAAILSR SEPGSRSYKA
2160 2170 2180 2190 2200
ALENSPEMIE TFLLCALVCL MTIGLVVVLV RGKGPGKLAF GMVSIGVMTW
2210 2220 2230 2240 2250
LLWSAGVDPG KIAAAVILVF LLLVVLIPEP EKQRSVQDNQ LAMLMLLIAT
2260 2270 2280 2290 2300
ILGGVAANEM GWLEKTKADL SWVVRGRSST TTPVVELDMK PATAWTLYAL
2310 2320 2330 2340 2350
ATTLLTPLFQ HLIVTKYANI SLMAIASQAG TLFSMDSGIP FSSIELSVPL
2360 2370 2380 2390 2400
LALGCWTQIT PCSLILACVL LSTHYAILLP GMQAQAARDA QRRTAAGIMK
2410 2420 2430 2440 2450
NAVVDGIVAT DIPPLDGAGP LTEKKLGQLL LFAAAVTGVV ITRSPRSWSE
2460 2470 2480 2490 2500
LGVLGSAVGS TLIEGSAGKF WNATTVTAMC NLFRGSYLAG VPLTYTIIRN
2510 2520 2530 2540 2550
SNPSNKRGGG IGETLGEKWK ARLNQMNTLE FHRYRRSHIM EVDREPARAA
2560 2570 2580 2590 2600
LKSGDFTRGA AVSRGSAKLR WMHERGYIRL HDKVVDLGCG RGGWCYYSAT
2610 2620 2630 2640 2650
VKEVKEVKGY TKGGRGHEEP VLTQSYGWNI VQMKSGVDVF YKEAEPCDVV
2660 2670 2680 2690 2700
LCDIGECSSS PAVEADRSTK VLELAERWLE RNDGADFCIK VLCPYMPEVV
2710 2720 2730 2740 2750
EKLSKLQLRY GGCLVRNPLS RNSTHEMYWV SGYKGNLIGV INSTSALLLR
2760 2770 2780 2790 2800
RMEIKFAEPR YEEDVNLSCG TRAVSIAPPK FDYKKIGQRV ERLKAEHMST
2810 2820 2830 2840 2850
WHYDCEHPYR TWAYHGSYVV KPSGSASSQV NGVVKLLSKP WDVSSEVTGM
2860 2870 2880 2890 2900
SMTDTTPFGQ QRVFKEKVDT KAPEPPAGAE MASVIVSEWL WKRLNREKKP
2910 2920 2930 2940 2950
RLCTKEEFVR KVRGNAALGP VFEEENQWKD AAEAVQDPGF WNLVDMERKN
2960 2970 2980 2990 3000
HLEGKCETCV YNMMGKREKK RGEFGKAKGS RAIWYMWLGA RFLEFEALGF
3010 3020 3030 3040 3050
LNEDHWMSRG NSGGGVEGLG IQKLGYVMRE IGEKGGILYA DDTAGWDTRI
3060 3070 3080 3090 3100
TECDLRNEAH IMEYMENEHR KLARAIFELT YKHKVVKVMR PGKGVPLMDI
3110 3120 3130 3140 3150
ISREDQRGSG QVVTYALNTF TNLVVQLIRM AEAECVLTPE DLHEMSQSAK
3160 3170 3180 3190 3200
LRLLKWLKEE GWERLTRMAV SGDDCVVAAP DARFGAALTF LNAMSKIRKD
3210 3220 3230 3240 3250
IKEWTPSKGW KNWEEVPFCS HHFHRLQMKD GRELVVPCRS QDELIGRARV
3260 3270 3280 3290 3300
TQGPGDLMSS ACLAKAYAQM WQLLYFHRRD LRLMGNAICS AVPVDWVPTG
3310 3320 3330 3340 3350
RTTWSIHGKG EWMTSENMLE VWNRVWIEEN EHMEDKTPVR EWTDIPYLGK
3360 3370 3380 3390 3400
REDPWCGSYI GYRPRSTWAE NIKVPVNVIR VKIGGNKYQD YLGTQKRYES
3410
EKRVEFRGVL
Length:3,410
Mass (Da):378,066
Last modified:December 6, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i09A5AAC11C68907C
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
AY632541 Genomic RNA Translation: AAV34157.1

NCBI Reference Sequences

More...
RefSeqi
YP_001040007.1, NC_009029.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5075791

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:5075791

<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
AY632541 Genomic RNA Translation: AAV34157.1
RefSeqiYP_001040007.1, NC_009029.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V6IX-ray2.10A1678-2108[»]
2V6JX-ray2.30A1678-2108[»]
SMRiQ32ZD5
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiS07.001

Genome annotation databases

GeneIDi5075791
KEGGivg:5075791

Enzyme and pathway databases

BRENDAi3.4.21.91, 10317

Miscellaneous databases

EvolutionaryTraceiQ32ZD5

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
3.40.50.300, 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
SUPFAMiSSF101257, SSF101257, 1 hit
SSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 2 hits
SSF53335, SSF53335, 1 hit
SSF56672, SSF56672, 1 hit
SSF56983, SSF56983, 1 hit
SSF81296, SSF81296, 1 hit
TIGRFAMsiTIGR04240, flavi_E_stem, 1 hit
PROSITEiView protein in PROSITE
PS51527, FLAVIVIRUS_NS2B, 1 hit
PS51528, FLAVIVIRUS_NS3PRO, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit
PS51591, RNA_CAP01_NS5_MT, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_KOKV
<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: Q32ZD5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2017
Last sequence update: December 6, 2005
Last modified: September 29, 2021
This is version 132 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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

Keywords - Technical termi

3D-structure

Documents

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