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Protein

Genome polyprotein

Gene
N/A
Organism
Yellow fever virus (strain 17D vaccine) (YFV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-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
Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.1 Publication
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. 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 similarity1 Publication
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. Also plays a role in virus assembly (PubMed:18199634).PROSITE-ProRule annotation1 Publication
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: 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 (PubMed:15956546).By similarity1 Publication
RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:19850911). NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions (PubMed:19850911). 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 (PubMed:25211074). IFN-I induces binding of NS5 to host IFN-activated transcription factor STAT2, preventing its transcriptional activity. Host TRIM23 is the E3 ligase that interacts with and polyubiquitinates NS5 to promote its binding to STAT2 and trigger IFN-I signaling inhibition (PubMed:25211074).2 Publications

<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

<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>pH dependencei

Optimum pH is 9.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1537Charge relay system; for serine protease NS3 activity1
Active sitei1561Charge relay system; for serine protease NS3 activity1
Active sitei1622Charge relay system; for serine protease NS3 activity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1945Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1948Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2519mRNA cap bindingPROSITE-ProRule annotation1 Publication1
Sitei2522mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1 Publication1
Sitei2523mRNA cap bindingPROSITE-ProRule annotation1 Publication1
Sitei2525mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1 Publication1
Sitei2530mRNA cap bindingPROSITE-ProRule annotation1
Sitei2534mRNA cap bindingPROSITE-ProRule annotation1 Publication1
<p>This subsection of the ‘Function’ 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 sitei2562S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2567For 2'-O-MTase activityBy similarity1
Sitei2567Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2592S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2593S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2610S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2611S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2637S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2638S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2652For 2'-O-MTase activityBy similarity1
Sitei2652Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1 Publication1
Binding sitei2653S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2656mRNA cap bindingPROSITE-ProRule annotation1 Publication1
Active sitei2688For 2'-O-MTase activityBy similarity1
Sitei2688Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2719mRNA cap bindingPROSITE-ProRule annotation1 Publication1
Sitei2721mRNA cap bindingPROSITE-ProRule annotation1 Publication1
Active sitei2724For 2'-O-MTase activityBy similarity1
Sitei2724Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2726S-adenosyl-L-methioninePROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 bindingi2945Zinc 1By similarity1
Metal bindingi2949Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2954Zinc 1By similarity1
Metal bindingi2957Zinc 1By similarity1
Metal bindingi3222Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3238Zinc 2By similarity1
Metal bindingi3357Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1682 – 1689ATPPROSITE-ProRule annotation8

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

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.50 6740
3.6.4.13 6740

<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 14 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Non-structural protein 2A-alpha1 Publication
Short name:
NS2A-alpha
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.911 Publication, 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):
Non-structural protein 5
<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>OrganismiYellow fever virus (strain 17D vaccine) (YFV)
<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 identifieri11090 [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 lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirus
<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 aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes luteocephalus (Mosquito) [TaxID: 299629]
Aedes simpsoni [TaxID: 7161]
Homo sapiens (Human) [TaxID: 9606]
Simiiformes [TaxID: 314293]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_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
  • UP000180883 <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
  • UP000158765 Componenti: Genome
  • UP000180940 Componenti: Genome
  • UP000119912 Componenti: Genome
  • UP000181442 Componenti: Genome
  • UP000158778 Componenti: Genome
  • UP000138083 Componenti: Genome
  • UP000000360 Componenti: Genome
  • UP000180827 Componenti: Genome
  • UP000141075 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 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 – 104CytoplasmicSequence analysisAdd BLAST104
<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>Transmembranei105 – 125HelicalSequence analysisAdd BLAST21
Topological domaini126 – 244ExtracellularSequence analysisAdd BLAST119
Transmembranei245 – 265HelicalSequence analysisAdd BLAST21
Topological domaini266 – 270CytoplasmicSequence analysis5
Transmembranei271 – 285HelicalSequence analysisAdd BLAST15
Topological domaini286 – 730ExtracellularSequence analysisAdd BLAST445
Transmembranei731 – 751HelicalSequence analysisAdd BLAST21
Topological domaini752 – 757ExtracellularSequence analysis6
Transmembranei758 – 778HelicalSequence analysisAdd BLAST21
Topological domaini779 – 1132ExtracellularSequence analysisAdd BLAST354
Transmembranei1133 – 1153HelicalSequence analysisAdd BLAST21
Topological domaini1154 – 1201CytoplasmicSequence analysisAdd BLAST48
Transmembranei1202 – 1222HelicalSequence analysisAdd BLAST21
Topological domaini1223 – 1287LumenalSequence analysisAdd BLAST65
Transmembranei1288 – 1308HelicalSequence analysisAdd BLAST21
Topological domaini1309 – 1355CytoplasmicSequence analysisAdd BLAST47
Transmembranei1356 – 1376HelicalSequence analysisAdd BLAST21
Topological domaini1377 – 1378LumenalSequence analysis2
Transmembranei1379 – 1399HelicalSequence analysisAdd BLAST21
Topological domaini1400 – 1456CytoplasmicSequence analysisAdd BLAST57
<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>Intramembranei1457 – 1477HelicalSequence analysisAdd BLAST21
Topological domaini1478 – 2157CytoplasmicSequence analysisAdd BLAST680
Transmembranei2158 – 2178HelicalSequence analysisAdd BLAST21
Topological domaini2179 – 2186LumenalSequence analysis8
Intramembranei2187 – 2207HelicalSequence analysisAdd BLAST21
Topological domaini2208 – 2209LumenalSequence analysis2
Transmembranei2210 – 2230HelicalSequence analysisAdd BLAST21
Topological domaini2231 – 2241CytoplasmicSequence analysisAdd BLAST11
Transmembranei2242 – 2262Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2263 – 2293LumenalSequence analysisAdd BLAST31
Intramembranei2294 – 2314HelicalSequence analysisAdd BLAST21
Topological domaini2315 – 2360LumenalSequence analysisAdd BLAST46
Transmembranei2361 – 2381HelicalSequence analysisAdd BLAST21
Topological domaini2382 – 2421CytoplasmicSequence analysisAdd BLAST40
Transmembranei2422 – 2442HelicalSequence analysisAdd BLAST21
Topological domaini2443 – 2445LumenalSequence analysis3
Transmembranei2446 – 2466HelicalSequence analysisAdd BLAST21
Topological domaini2467 – 3411CytoplasmicSequence analysisAdd BLAST945

GO - Cellular componenti

Keywords - Cellular componenti

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

<p>This section 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>Mutagenesisi98 – 101RKRR → AAAA: Complete loss of NS2B-NS3 cleavage. 4
Mutagenesisi98 – 101RKRR → AKAA: Complete loss of NS2B-NS3 cleavage. 4
Mutagenesisi98 – 101RKRR → AKRA: Reduces NS2B-NS3 cleavage efficiency. 4
Mutagenesisi98 – 100RKR → AAA: Complete loss of NS2B-NS3 cleavage. 3
Mutagenesisi98 – 100RKR → AKA: Complete loss of NS2B-NS3 cleavage. 3
Mutagenesisi98 – 99RK → AA: Reduces NS2B-NS3 cleavage efficiency. 2
Mutagenesisi99 – 101KRR → ARA: Complete loss of NS2B-NS3 cleavage. 1 Publication3
Mutagenesisi99 – 100KR → AA: Complete loss of NS2B-NS3 cleavage. 2
Mutagenesisi100 – 101RR → AA: Reduces NS2B-NS3 cleavage efficiency. 2
Mutagenesisi116 – 121LLMTGG → VPQAQA: Complete loss of infectious virus production. Enhances signal peptidase cleavage in vitro of nascent capsid protein C. 1 Publication6
Mutagenesisi908N → A: Reduces viral RNA accumulation and NS1 secretion. 1 Publication1
Mutagenesisi910S → A: Reduces viral RNA accumulation and NS1 secretion. 1 Publication1
Mutagenesisi986N → A: No effect. 1 Publication1
Mutagenesisi988T → A: No effect. 1 Publication1
Mutagenesisi1077R → A: Blocks RNA replication. 1 Publication1
Mutagenesisi1152 – 1154RKR → AAA: Defective in infectious particle production; almost no effect on viral replication. 1 Publication3
Mutagenesisi1229 – 1231RER → AAA: Defective in infectious particle production; almost no effect on viral replication. 1 Publication3
Mutagenesisi1319 – 1321QKT → RRS: Increases NS2A-alpha processing, complete loss of NS2A. 3
Mutagenesisi1319Q → A: Almost no effect on viral replication. 1 Publication1
Mutagenesisi1319Q → S: Complete loss of cleavage and NS2A alpha. Complete loss of infectivity. 1 Publication1
Mutagenesisi1320K → E, I, Q or S: Complete loss of cleavage and NS2A-alpha processing. Complete loss of infectivity. 1 Publication1
Mutagenesisi1320K → R: No effect on NS2A-alpha processing. 1 Publication1
Mutagenesisi1321T → V: Complete loss of cleavage and NS2A alpha synthesis. Complete loss of infectivity. 1 Publication1
Mutagenesisi1351F → C, I or V: Enhances NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1351F → G: No effect on NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1352G → A or K: Enhances NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1352G → E or V: Reduces NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1353R → H, K, R or T: Reduces NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1353R → L or P: Complete loss of NS2A-NS2B cleavage. 1 Publication1
Mutagenesisi1354R → I, N, S or T: Complete loss of NS2A-NS2B cleavage. 1 Publication1
Mutagenesisi1354R → K: Reduces of NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1355S → D, K, R or V: Complete loss of NS2A-NS2B cleavage. 1 Publication1
Mutagenesisi1355S → G: Reduces of NS2A-NS2B cleavage efficiency. 1 Publication1
Mutagenesisi1406 – 1409ELKK → ALAA: Complete loss of polyprotein cleavage. 1 Publication4
Mutagenesisi1537H → A: Complete loss NS3 protease activity. 1 Publication1
Mutagenesisi1561D → A or N: Complete loss NS3 protease activity. 1 Publication1
Mutagenesisi1622S → A: Complete loss NS3 protease activity. 1 Publication1
Mutagenesisi1622S → C: Diminishes NS3 protease activity. 1 Publication1
Mutagenesisi1833W → A: Complete loss of production of infectious virus particles. 1 Publication1
Mutagenesisi2107R → A, L, M, T or V: Reduces NS4A-NS4B cleavage efficiency. 1 Publication1
Mutagenesisi2107R → E: Complete loss of NS4A-NS4B cleavage. 2 Publications1
Mutagenesisi2107R → K: No effect on NS4A-NS4B cleavage efficiency. 1 Publication1
Mutagenesisi2107R → P: Complete loss of NS4A-NS4B cleavage. 1 Publication1
Mutagenesisi2234S → A or T: No effect on NS4A-NS4B cleavage. 1 Publication1
Mutagenesisi2234S → I or P: No effect on NS4A-NS4B cleavage. 1 Publication1
Mutagenesisi2505R → A, I, L, Q, S or T: No effect on NS4B-NS5 cleavage efficiency. 1 Publication1
Mutagenesisi2505R → P: Reduces NS4B-NS5 cleavage efficiency. 1 Publication1
Mutagenesisi2506R → E: Complete loss of NS4B-NS5 cleavage. 2 Publications1
Mutagenesisi2506R → H, N or Q: Reduces NS4B-NS5 cleavage efficiency. 1 Publication1
Mutagenesisi2506R → K: No effect on NS4B-NS5 cleavage efficiency. 1 Publication1
Mutagenesisi2506R → Y: Complete loss of NS4B-NS5 cleavage. 1 Publication1
Mutagenesisi2507G → A or S: Reduces NS4B-NS5 cleavage efficiency. 1
Mutagenesisi2507G → E, K, L, M, N or V: Reduces NS4B-NS5 cleavage efficiency. 1
Mutagenesisi2512K → R: Completet loss of NS5 binding to STAT2 after IFN-I stimulation. 1 Publication1
Mutagenesisi2562S → A: Complete loss of 2'-O-MTase 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004051531 – 3411Genome polyproteinAdd BLAST3411
ChainiPRO_00000377541 – 101Capsid protein C1 PublicationAdd BLAST101
<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_0000261384102 – 121ER anchor for the capsid protein C, removed in mature form by serine protease NS31 PublicationAdd BLAST20
ChainiPRO_0000261385122 – 285Protein prMBy similarityAdd BLAST164
ChainiPRO_0000037755122 – 210Peptide prBy similarityAdd BLAST89
ChainiPRO_0000037756211 – 285Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000037757286 – 778Envelope protein EBy similarityAdd BLAST493
ChainiPRO_0000037758779 – 1130Non-structural protein 11 PublicationAdd BLAST352
ChainiPRO_00000377591131 – 1354Non-structural protein 2ABy similarityAdd BLAST224
ChainiPRO_00002613861131 – 1320Non-structural protein 2A-alpha1 PublicationAdd BLAST190
ChainiPRO_00000377601355 – 1484Serine protease subunit NS2B1 PublicationAdd BLAST130
ChainiPRO_00000377611485 – 2107Serine protease NS32 PublicationsAdd BLAST623
ChainiPRO_00000377622108 – 2233Non-structural protein 4A1 PublicationAdd 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_00002613872234 – 2256Peptide 2k1 PublicationAdd BLAST23
ChainiPRO_00000377632257 – 2506Non-structural protein 4B1 PublicationAdd BLAST250
ChainiPRO_00000377642507 – 3411RNA-directed RNA polymerase NS52 PublicationsAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi134N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi150N-linked (GlcNAc...) asparagine; by hostSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi288 ↔ 315By similarity
Disulfide bondi345 ↔ 406By similarity
Disulfide bondi345 ↔ 401By similarity
Disulfide bondi359 ↔ 390By similarity
Disulfide bondi377 ↔ 406By similarity
Disulfide bondi377 ↔ 401By similarity
Disulfide bondi467 ↔ 568By similarity
Disulfide bondi585 ↔ 615By similarity
Disulfide bondi782 ↔ 793By similarity
Disulfide bondi833 ↔ 921By similarity
Glycosylationi908N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi957 ↔ 1002By similarity
Glycosylationi986N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi1058 ↔ 1107By similarity
Disulfide bondi1069 ↔ 1091By similarity
Disulfide bondi1090 ↔ 1094By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2562Phosphoserine1 Publication1

<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. The nascent capsid protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature capsid protein C is cleaved at a site upstream of this hydrophobic domain by NS3. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. Non-structural protein 2A-alpha, a C-terminally truncated form of non-structural protein 2A, results from partial cleavage by NS3. Specific enzymatic cleavages in vivo yield mature proteins peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.7 Publications
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
Polyubiquitinated; ubiquitination is probably mediated by host TRIM23 and is prerequisite for NS5-STAT2 interaction. NS5 is not ISGylated or sumoylated.1 Publication
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei101 – 102Cleavage; by viral protease NS31 Publication2
Sitei121 – 122Cleavage; by host signal peptidase1 Publication2
Sitei210 – 211Cleavage; by host furinBy similarity2
Sitei285 – 286Cleavage; by host signal peptidaseBy similarity2
Sitei778 – 779Cleavage; by host signal peptidase1 Publication2
Sitei1130 – 1131Cleavage; by hostBy similarity2
Sitei1320 – 1321Cleavage; by viral protease NS31 Publication2
Sitei1354 – 1355Cleavage; by viral protease NS32 Publications2
Sitei1484 – 1485Cleavage; by autolysis2 Publications2
Sitei2107 – 2108Cleavage; by autolysis3 Publications2
Sitei2233 – 2234Cleavage; by viral protease NS31 Publication2
Sitei2256 – 2257Cleavage; by host signal peptidaseBy similarity2
Sitei2506 – 2507Cleavage; by viral protease NS33 Publications2

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P03314

<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 (PubMed:12768036). Interacts (via N-terminus) with host EXOC1 (via C-terminus); this interaction results in EXOC1 degradation through the proteasome degradation pathway (By similarity). Protein prM: Forms heterodimers with envelope protein E in the endoplasmic reticulum and Golgi (By similarity). Envelope protein E: Homodimer; in the endoplasmic reticulum and Golgi. Interacts with protein prM. Interacts with non-structural protein 1 (By similarity). Non-structural protein 1: Homodimer; Homohexamer when secreted. Interacts with envelope protein E (By similarity). Non-structural protein 2A: Interacts (via N-terminus) with serine protease NS3 (PubMed:25694595). Non-structural protein 2B: Forms a heterodimer with serine protease NS3. May form homooligomers (By similarity). Serine protease NS3: Forms a heterodimer with NS2B (By similarity). Interacts with non-structural protein 2A (via N-terminus) (PubMed:25694595). Interacts with NS4B (By similarity). Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity). NS3 interacts with host PDCD6IP; this interaction contributes to virion release (PubMed:21044891). Non-structural protein 4B: Interacts with serine protease NS3 (By similarity). RNA-directed RNA polymerase NS5: Homodimer (By similarity). Interacts with host STAT2; this interaction prevents the establishment of cellular antiviral state (PubMed:25211074). Interacts with host TRIM23; this interaction leads to NS5 ubiquitination (PubMed:25211074).By similarity4 Publications

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

13411
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NA4electron microscopy-
1YKSX-ray1.80A1671-2107[»]
3EVAX-ray1.50A2507-2772[»]
3EVBX-ray1.85A2507-2772[»]
3EVCX-ray1.60A2507-2772[»]
3EVDX-ray1.50A2507-2772[»]
3EVEX-ray1.70A2507-2772[»]
3EVFX-ray1.45A2507-2772[»]
5FFMX-ray2.60A1671-2107[»]
5N6BX-ray1.71C/F2470-2478[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P03314

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

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SMRi
P03314

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P03314

<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>Domaini1485 – 1665Peptidase S7PROSITE-ProRule annotationAdd BLAST181
Domaini1669 – 1825Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1820 – 1997Helicase C-terminalAdd BLAST178
Domaini2507 – 2771mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3035 – 3187RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1773 – 1776DEAH boxPROSITE-ProRule annotation4
Motifi2878 – 2911Nuclear localization signalBy similarityAdd BLAST34

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi2656 – 2660Poly-Ser5

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

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

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

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12149 Flavi_E_C, 1 hit
cd00079 HELICc, 1 hit
cd06174 MFS, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
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

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
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
IPR020846 MFS_dom
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

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PIRSFi
PIRSF003817 Gen_Poly_FLV, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
SSF53335 SSF53335, 1 hit
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR04240 flavi_E_stem, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51527 FLAVIVIRUS_NS2B, 1 hit
PS51528 FLAVIVIRUS_NS3PRO, 1 hit
PS51192 HELICASE_ATP_BIND_1, 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>.<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.

P03314-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGRKAQGKT LGVNMVRRGV RSLSNKIKQK TKQIGNRPGP SRGVQGFIFF
60 70 80 90 100
FLFNILTGKK ITAHLKRLWK MLDPRQGLAV LRKVKRVVAS LMRGLSSRKR
110 120 130 140 150
RSHDVLTVQF LILGMLLMTG GVTLVRKNRW LLLNVTSEDL GKTFSVGTGN
160 170 180 190 200
CTTNILEAKY WCPDSMEYNC PNLSPREEPD DIDCWCYGVE NVRVAYGKCD
210 220 230 240 250
SAGRSRRSRR AIDLPTHENH GLKTRQEKWM TGRMGERQLQ KIERWFVRNP
260 270 280 290 300
FFAVTALTIA YLVGSNMTQR VVIALLVLAV GPAYSAHCIG ITDRDFIEGV
310 320 330 340 350
HGGTWVSATL EQDKCVTVMA PDKPSLDISL ETVAIDRPAE VRKVCYNAVL
360 370 380 390 400
THVKINDKCP STGEAHLAEE NEGDNACKRT YSDRGWGNGC GLFGKGSIVA
410 420 430 440 450
CAKFTCAKSM SLFEVDQTKI QYVIRAQLHV GAKQENWNTD IKTLKFDALS
460 470 480 490 500
GSQEVEFIGY GKATLECQVQ TAVDFGNSYI AEMETESWIV DRQWAQDLTL
510 520 530 540 550
PWQSGSGGVW REMHHLVEFE PPHAATIRVL ALGNQEGSLK TALTGAMRVT
560 570 580 590 600
KDTNDNNLYK LHGGHVSCRV KLSALTLKGT SYKICTDKMF FVKNPTDTGH
610 620 630 640 650
GTVVMQVKVS KGAPCRIPVI VADDLTAAIN KGILVTVNPI ASTNDDEVLI
660 670 680 690 700
EVNPPFGDSY IIVGRGDSRL TYQWHKEGSS IGKLFTQTMK GVERLAVMGD
710 720 730 740 750
TAWDFSSAGG FFTSVGKGIH TVFGSAFQGL FGGLNWITKV IMGAVLIWVG
760 770 780 790 800
INTRNMTMSM SMILVGVIMM FLSLGVGADQ GCAINFGKRE LKCGDGIFIF
810 820 830 840 850
RDSDDWLNKY SYYPEDPVKL ASIVKASFEE GKCGLNSVDS LEHEMWRSRA
860 870 880 890 900
DEINAIFEEN EVDISVVVQD PKNVYQRGTH PFSRIRDGLQ YGWKTWGKNL
910 920 930 940 950
VFSPGRKNGS FIIDGKSRKE CPFSNRVWNS FQIEEFGTGV FTTRVYMDAV
960 970 980 990 1000
FEYTIDCDGS ILGAAVNGKK SAHGSPTFWM GSHEVNGTWM IHTLEALDYK
1010 1020 1030 1040 1050
ECEWPLTHTI GTSVEESEMF MPRSIGGPVS SHNHIPGYKV QTNGPWMQVP
1060 1070 1080 1090 1100
LEVKREACPG TSVIIDGNCD GRGKSTRSTT DSGKVIPEWC CRSCTMPPVS
1110 1120 1130 1140 1150
FHGSDGCWYP MEIRPRKTHE SHLVRSWVTA GEIHAVPFGL VSMMIAMEVV
1160 1170 1180 1190 1200
LRKRQGPKQM LVGGVVLLGA MLVGQVTLLD LLKLTVAVGL HFHEMNNGGD
1210 1220 1230 1240 1250
AMYMALIAAF SIRPGLLIGF GLRTLWSPRE RLVLTLGAAM VEIALGGVMG
1260 1270 1280 1290 1300
GLWKYLNAVS LCILTINAVA SRKASNTILP LMALLTPVTM AEVRLAAMFF
1310 1320 1330 1340 1350
CAVVIIGVLH QNFKDTSMQK TIPLVALTLT SYLGLTQPFL GLCAFLATRI
1360 1370 1380 1390 1400
FGRRSIPVNE ALAAAGLVGV LAGLAFQEME NFLGPIAVGG LLMMLVSVAG
1410 1420 1430 1440 1450
RVDGLELKKL GEVSWEEEAE ISGSSARYDV ALSEQGEFKL LSEEKVPWDQ
1460 1470 1480 1490 1500
VVMTSLALVG AALHPFALLL VLAGWLFHVR GARRSGDVLW DIPTPKIIEE
1510 1520 1530 1540 1550
CEHLEDGIYG IFQSTFLGAS QRGVGVAQGG VFHTMWHVTR GAFLVRNGKK
1560 1570 1580 1590 1600
LIPSWASVKE DLVAYGGSWK LEGRWDGEEE VQLIAAVPGK NVVNVQTKPS
1610 1620 1630 1640 1650
LFKVRNGGEI GAVALDYPSG TSGSPIVNRN GEVIGLYGNG ILVGDNSFVS
1660 1670 1680 1690 1700
AISQTEVKEE GKEELQEIPT MLKKGMTTVL DFHPGAGKTR RFLPQILAEC
1710 1720 1730 1740 1750
ARRRLRTLVL APTRVVLSEM KEAFHGLDVK FHTQAFSAHG SGREVIDAMC
1760 1770 1780 1790 1800
HATLTYRMLE PTRVVNWEVI IMDEAHFLDP ASIAARGWAA HRARANESAT
1810 1820 1830 1840 1850
ILMTATPPGT SDEFPHSNGE IEDVQTDIPS EPWNTGHDWI LADKRPTAWF
1860 1870 1880 1890 1900
LPSIRAANVM AASLRKAGKS VVVLNRKTFE REYPTIKQKK PDFILATDIA
1910 1920 1930 1940 1950
EMGANLCVER VLDCRTAFKP VLVDEGRKVA IKGPLRISAS SAAQRRGRIG
1960 1970 1980 1990 2000
RNPNRDGDSY YYSEPTSENN AHHVCWLEAS MLLDNMEVRG GMVAPLYGVE
2010 2020 2030 2040 2050
GTKTPVSPGE MRLRDDQRKV FRELVRNCDL PVWLSWQVAK AGLKTNDRKW
2060 2070 2080 2090 2100
CFEGPEEHEI LNDSGETVKC RAPGGAKKPL RPRWCDERVS SDQSALSEFI
2110 2120 2130 2140 2150
KFAEGRRGAA EVLVVLSELP DFLAKKGGEA MDTISVFLHS EEGSRAYRNA
2160 2170 2180 2190 2200
LSMMPEAMTI VMLFILAGLL TSGMVIFFMS PKGISRMSMA MGTMAGCGYL
2210 2220 2230 2240 2250
MFLGGVKPTH ISYVMLIFFV LMVVVIPEPG QQRSIQDNQV AYLIIGILTL
2260 2270 2280 2290 2300
VSAVAANELG MLEKTKEDLF GKKNLIPSSA SPWSWPDLDL KPGAAWTVYV
2310 2320 2330 2340 2350
GIVTMLSPML HHWIKVEYGN LSLSGIAQSA SVLSFMDKGI PFMKMNISVI
2360 2370 2380 2390 2400
MLLVSGWNSI TVMPLLCGIG CAMLHWSLIL PGIKAQQSKL AQRRVFHGVA
2410 2420 2430 2440 2450
ENPVVDGNPT VDIEEAPEMP ALYEKKLALY LLLALSLASV AMCRTPFSLA
2460 2470 2480 2490 2500
EGIVLASAAL GPLIEGNTSL LWNGPMAVSM TGVMRGNHYA FVGVMYNLWK
2510 2520 2530 2540 2550
MKTGRRGSAN GKTLGEVWKR ELNLLDKRQF ELYKRTDIVE VDRDTARRHL
2560 2570 2580 2590 2600
AEGKVDTGVA VSRGTAKLRW FHERGYVKLE GRVIDLGCGR GGWCYYAAAQ
2610 2620 2630 2640 2650
KEVSGVKGFT LGRDGHEKPM NVQSLGWNII TFKDKTDIHR LEPVKCDTLL
2660 2670 2680 2690 2700
CDIGESSSSS VTEGERTVRV LDTVEKWLAC GVDNFCVKVL APYMPDVLEK
2710 2720 2730 2740 2750
LELLQRRFGG TVIRNPLSRN STHEMYYVSG ARSNVTFTVN QTSRLLMRRM
2760 2770 2780 2790 2800
RRPTGKVTLE ADVILPIGTR SVETDKGPLD KEAIEERVER IKSEYMTSWF
2810 2820 2830 2840 2850
YDNDNPYRTW HYCGSYVTKT SGSAASMVNG VIKILTYPWD RIEEVTRMAM
2860 2870 2880 2890 2900
TDTTPFGQQR VFKEKVDTRA KDPPAGTRKI MKVVNRWLFR HLAREKNPRL
2910 2920 2930 2940 2950
CTKEEFIAKV RSHAAIGAYL EEQEQWKTAN EAVQDPKFWE LVDEERKLHQ
2960 2970 2980 2990 3000
QGRCRTCVYN MMGKREKKLS EFGKAKGSRA IWYMWLGARY LEFEALGFLN
3010 3020 3030 3040 3050
EDHWASRENS GGGVEGIGLQ YLGYVIRDLA AMDGGGFYAD DTAGWDTRIT
3060 3070 3080 3090 3100
EADLDDEQEI LNYMSPHHKK LAQAVMEMTY KNKVVKVLRP APGGKAYMDV
3110 3120 3130 3140 3150
ISRRDQRGSG QVVTYALNTI TNLKVQLIRM AEAEMVIHHQ HVQDCDESVL
3160 3170 3180 3190 3200
TRLEAWLTEH GCDRLKRMAV SGDDCVVRPI DDRFGLALSH LNAMSKVRKD
3210 3220 3230 3240 3250
ISEWQPSKGW NDWENVPFCS HHFHELQLKD GRRIVVPCRE QDELIGRGRV
3260 3270 3280 3290 3300
SPGNGWMIKE TACLSKAYAN MWSLMYFHKR DMRLLSLAVS SAVPTSWVPQ
3310 3320 3330 3340 3350
GRTTWSIHGK GEWMTTEDML EVWNRVWITN NPHMQDKTMV KKWRDVPYLT
3360 3370 3380 3390 3400
KRQDKLCGSL IGMTNRATWA SHIHLVIHRI RTLIGQEKYT DYLTVMDRYS
3410
VDADLQLGEL I
Length:3,411
Mass (Da):379,518
Last modified:July 21, 1986 - 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:i680E0FACD23DCFA6
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti341V → A in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti438N → T in strain: Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine and Isolate 17D-204-USA HONG3 vaccine. 1
Natural varianti440D → S in strain: Isolate 17DD vaccine. 1
Natural varianti610S → P in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti629I → V in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1
Natural varianti701T → V in strain: Isolate 17DD vaccine. 1
Natural varianti744A → V in strain: Isolate 17D-204-South Africa vaccine large plaque variant. 1
Natural varianti764L → M in strain: Isolate 17D-204-South Africa vaccine large plaque variant. 1
Natural varianti1299F → L in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti1666Q → R in strain: Isolate 17DD vaccine. 1
Natural varianti1669P → S in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1
Natural varianti1679V → I in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti2214V → I in strain: Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine, Isolate 17D-204-USA HONG3 vaccine, Isolate Spain/AVD2791-93F/04 vaccine, Isolate Brazil/YF-VAVD/75 vaccine, Isolate 17DD vaccine and Isolate Pasteur 17D-204 vaccine. 1
Natural varianti2277P → S in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1
Natural varianti2401E → K in strain: Isolate 17D-204-South Africa vaccine large plaque variant, Isolate 17D-204-South Africa vaccine medium plaque variant, Isolate 17D-204-South Africa vaccine, Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine, Isolate 17D-204-USA HONG3 vaccine, Isolate Brazil/YF-VAVD/75 vaccine, Isolate Spain/AVD2791-93F/04 vaccine, Isolate 17DD vaccine and Isolate Pasteur 17D-204 vaccine. 1
Natural varianti2460L → S in strain: Isolate 17D-204-USA HONG vaccine1, Isolate 17D-204-USA HONG2 vaccine and Isolate 17D-204-USA HONG3 vaccine. 1
Natural varianti2528R → Q in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti2643P → S in strain: Isolate 17D-204-South Africa vaccine medium plaque variant. 1
Natural varianti2661V → I in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1
Natural varianti2897N → S in strain: Isolate Brazil/YF-VAVD/75 vaccine and Isolate 17DD vaccine. 1
Natural varianti3110G → R in strain: Isolate 17D-204-USA HONG2 vaccine. 1
Natural varianti3135M → N in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1
Natural varianti3163D → N in strain: Isolate 17D-204-South Africa vaccine large plaque variant, Isolate 17D-204-South Africa vaccine medium plaque variant, Isolate 17D-204-South Africa vaccine, Isolate 17D-204-USA HONG1 vaccine, Isolate 17D-204-USA HONG2 vaccine, Isolate 17D-204-USA HONG3 vaccine, Isolate Brazil/YF-VAVD/75 vaccine, Isolate Spain/AVD2791-93F/04 vaccine, Isolate 17DD vaccine and Isolate Pasteur 17D-204 vaccine. 1
Natural varianti3222H → R in strain: Isolate Brazil/YF-VAVD/75 vaccine. 1

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X03700 Genomic RNA Translation: CAA27332.1
X15062 Genomic RNA Translation: CAB37419.1
U17066 Genomic RNA Translation: AAC54267.1
U17067 Genomic RNA Translation: AAC54268.1
AF052437 Genomic RNA Translation: AAC35899.1
AF052438 Genomic RNA Translation: AAC35900.1
AF052439 Genomic RNA Translation: AAC35901.1
AF052444 Genomic RNA Translation: AAC35906.1
AF052445 Genomic RNA Translation: AAC35907.1
AF052446 Genomic RNA Translation: AAC35908.1
DQ118157 Genomic RNA Translation: AAZ31436.1
DQ100292 Genomic RNA Translation: AAZ07885.1

Protein sequence database of the Protein Information Resource

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PIRi
A03914 GNWVY
S07757 GNWVYP

NCBI Reference Sequences

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RefSeqi
NP_041726.1, NC_002031.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
1502173

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
vg:1502173

<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
X03700 Genomic RNA Translation: CAA27332.1
X15062 Genomic RNA Translation: CAB37419.1
U17066 Genomic RNA Translation: AAC54267.1
U17067 Genomic RNA Translation: AAC54268.1
AF052437 Genomic RNA Translation: AAC35899.1
AF052438 Genomic RNA Translation: AAC35900.1
AF052439 Genomic RNA Translation: AAC35901.1
AF052444 Genomic RNA Translation: AAC35906.1
AF052445 Genomic RNA Translation: AAC35907.1
AF052446 Genomic RNA Translation: AAC35908.1
DQ118157 Genomic RNA Translation: AAZ31436.1
DQ100292 Genomic RNA Translation: AAZ07885.1
PIRiA03914 GNWVY
S07757 GNWVYP
RefSeqiNP_041726.1, NC_002031.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NA4electron microscopy-
1YKSX-ray1.80A1671-2107[»]
3EVAX-ray1.50A2507-2772[»]
3EVBX-ray1.85A2507-2772[»]
3EVCX-ray1.60A2507-2772[»]
3EVDX-ray1.50A2507-2772[»]
3EVEX-ray1.70A2507-2772[»]
3EVFX-ray1.45A2507-2772[»]
5FFMX-ray2.60A1671-2107[»]
5N6BX-ray1.71C/F2470-2478[»]
ProteinModelPortaliP03314
SMRiP03314
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP03314

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1502173
KEGGivg:1502173

Enzyme and pathway databases

BRENDAi2.7.7.50 6740
3.6.4.13 6740

Miscellaneous databases

EvolutionaryTraceiP03314

Family and domain databases

CDDicd12149 Flavi_E_C, 1 hit
cd00079 HELICc, 1 hit
cd06174 MFS, 1 hit
Gene3Di1.10.8.970, 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
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
IPR013755 Flav_gly_cen_dom_subdom1
IPR001122 Flavi_capsidC
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
IPR020846 MFS_dom
IPR026490 mRNA_cap_0/1_MeTrfase
IPR027417 P-loop_NTPase
IPR009003 Peptidase_S1_PA
IPR000208 RNA-dir_pol_flavivirus
IPR007094 RNA-dir_pol_PSvirus
IPR002877 rRNA_MeTrfase_FtsJ_dom
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF01003 Flavi_capsid, 1 hit
PF07652 Flavi_DEAD, 1 hit
PF02832 Flavi_glycop_C, 1 hit
PF00869 Flavi_glycoprot, 1 hit
PF01004 Flavi_M, 1 hit
PF00948 Flavi_NS1, 1 hit
PF01005 Flavi_NS2A, 1 hit
PF01002 Flavi_NS2B, 1 hit
PF01350 Flavi_NS4A, 1 hit
PF01349 Flavi_NS4B, 1 hit
PF00972 Flavi_NS5, 1 hit
PF01570 Flavi_propep, 1 hit
PF01728 FtsJ, 1 hit
PF00949 Peptidase_S7, 1 hit
PIRSFiPIRSF003817 Gen_Poly_FLV, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 2 hits
SSF53335 SSF53335, 1 hit
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
PS50507 RDRP_SSRNA_POS, 1 hit
PS51591 RNA_CAP01_NS5_MT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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_YEFV1
<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: P03314
Secondary accession number(s): O42028
, O91857, P19901, Q102J3, Q45RQ2, Q89275, Q89276, Q9W878, Q9YWN0, Q9YWN1, Q9YWN2
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 16, 2019
This is version 185 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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