Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 115 (26 Feb 2020)
Sequence version 1 (06 Dec 2005)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Genome polyprotein

Gene
N/A
Organism
Rocio virus (ROCV)
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.PROSITE-ProRule annotation
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%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1548Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1572Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1632Charge 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>Sitei1955Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1958Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei2534mRNA cap bindingPROSITE-ProRule annotation1
Sitei2537mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2538mRNA cap bindingPROSITE-ProRule annotation1
Sitei2540mRNA cap binding; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2545mRNA cap bindingPROSITE-ProRule annotation1
Sitei2549mRNA cap bindingPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei2577S-adenosyl-L-methioninePROSITE-ProRule annotation1
Active sitei2582For 2'-O-MTase activityBy similarity1
Sitei2582Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2607S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2608S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2625S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2626S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2652S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2653S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2667For 2'-O-MTase activityBy similarity1
Sitei2667Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2668S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei2671mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2702For 2'-O-MTase activityBy similarity1
Sitei2702Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Sitei2733mRNA cap bindingPROSITE-ProRule annotation1
Sitei2735mRNA cap bindingPROSITE-ProRule annotation1
Active sitei2738For 2'-O-MTase activityBy similarity1
Sitei2738Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2740S-adenosyl-L-methioninePROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi2960Zinc 1By similarity1
Metal bindingi2964Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2969Zinc 1By similarity1
Metal bindingi2972Zinc 1By similarity1
Metal bindingi3237Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3253Zinc 2By similarity1
Metal bindingi3372Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1691 – 1698ATPPROSITE-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, 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 STAT1 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, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S07.001

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
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:3.6.1.15, EC:3.6.4.13)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation, EC:2.1.1.57PROSITE-ProRule annotation, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
Non-structural protein 5
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRocio virus (ROCV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri64315 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesRiboviriaFlaviviridaeFlavivirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiCulex [TaxID: 7174]
Homo sapiens (Human) [TaxID: 9606]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000133235 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 103CytoplasmicSequence analysisAdd BLAST103
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei104 – 124HelicalSequence analysisAdd BLAST21
Topological domaini125 – 244ExtracellularSequence analysisAdd BLAST120
Transmembranei245 – 265HelicalSequence analysisAdd BLAST21
Topological domaini266 – 270CytoplasmicSequence analysis5
Transmembranei271 – 285HelicalCuratedAdd BLAST15
Topological domaini286 – 738ExtracellularSequence analysisAdd BLAST453
Transmembranei739 – 759HelicalSequence analysisAdd BLAST21
Topological domaini760 – 765CytoplasmicSequence analysis6
Transmembranei766 – 786HelicalSequence analysisAdd BLAST21
Topological domaini787 – 1170ExtracellularSequence analysisAdd BLAST384
Transmembranei1171 – 1191HelicalSequence analysisAdd BLAST21
Topological domaini1192 – 1213CytoplasmicSequence analysisAdd BLAST22
Transmembranei1214 – 1234HelicalSequence analysisAdd BLAST21
Topological domaini1235 – 1263LumenalSequence analysisAdd BLAST29
Transmembranei1264 – 1284HelicalSequence analysisAdd BLAST21
Topological domaini1285 – 1301CytoplasmicSequence analysisAdd BLAST17
Transmembranei1302 – 1322HelicalSequence analysisAdd BLAST21
Topological domaini1323 – 1333LumenalSequence analysisAdd BLAST11
Transmembranei1334 – 1354HelicalSequence analysisAdd BLAST21
Topological domaini1355 – 1367CytoplasmicSequence analysisAdd BLAST13
Transmembranei1368 – 1388HelicalSequence analysisAdd BLAST21
Topological domaini1389 – 1392LumenalSequence analysis4
Transmembranei1393 – 1413HelicalSequence analysisAdd BLAST21
Topological domaini1414 – 1469CytoplasmicSequence analysisAdd BLAST56
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1470 – 1490HelicalSequence analysisAdd BLAST21
Topological domaini1491 – 2166CytoplasmicSequence analysisAdd BLAST676
Transmembranei2167 – 2187HelicalSequence analysisAdd BLAST21
Topological domaini2188 – 2192LumenalSequence analysis5
Intramembranei2193 – 2212HelicalSequence analysisAdd BLAST20
Topological domaini2213 – 2214LumenalSequence analysis2
Transmembranei2215 – 2235HelicalSequence analysisAdd BLAST21
Topological domaini2236 – 2250CytoplasmicSequence analysisAdd BLAST15
Transmembranei2251 – 2265Helical; Note=Signal for NS4BCuratedAdd BLAST15
Topological domaini2266 – 2297LumenalSequence analysisAdd BLAST32
Intramembranei2298 – 2318HelicalSequence analysisAdd BLAST21
Topological domaini2319 – 2345LumenalSequence analysisAdd BLAST27
Transmembranei2346 – 2366HelicalSequence analysisAdd BLAST21
Topological domaini2367 – 2373CytoplasmicSequence analysis7
Transmembranei2374 – 2394HelicalSequence analysisAdd BLAST21
Topological domaini2395 – 2441LumenalSequence analysisAdd BLAST47
Transmembranei2442 – 2462HelicalSequence analysisAdd BLAST21
Topological domaini2463 – 3425CytoplasmicSequence analysisAdd BLAST963

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 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_00004415461 – 3425Genome polyproteinAdd BLAST3425
ChainiPRO_00004415471 – 101Capsid protein CBy similarityAdd BLAST101
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000441548102 – 118ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST17
ChainiPRO_0000441549119 – 285Protein prMBy similarityAdd BLAST167
ChainiPRO_0000441550119 – 210Peptide prBy similarityAdd BLAST92
ChainiPRO_0000441551211 – 285Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000441552286 – 786Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000441553787 – 1139Non-structural protein 1By similarityAdd BLAST353
ChainiPRO_00004415541140 – 1366Non-structural protein 2ABy similarityAdd BLAST227
ChainiPRO_00004415551367 – 1497Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00004415561498 – 2116Serine protease NS3By similarityAdd BLAST619
ChainiPRO_00004415572117 – 2242Non-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_00004415582243 – 2265Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004415592266 – 2521Non-structural protein 4BBy similarityAdd BLAST256
ChainiPRO_00004415602522 – 3425RNA-directed RNA polymerase NS5By similarityAdd BLAST904

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi133N-linked (GlcNAc...) asparagine; by hostBy similarity1
<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 bondi475 ↔ 573By similarity
Disulfide bondi590 ↔ 621By similarity
Disulfide bondi790 ↔ 801By similarity
Disulfide bondi841 ↔ 929By similarity
Glycosylationi916N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi965 ↔ 1009By similarity
Glycosylationi993N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi1067 ↔ 1116By similarity
Disulfide bondi1078 ↔ 1100By similarity
Disulfide bondi1078 ↔ 1099By similarity
Disulfide bondi1099 ↔ 1103By similarity
Disulfide bondi1100 ↔ 1103By 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 residuei2577PhosphoserineBy similarity1

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

Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.By similarity
N-glycosylated.1 Publication
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
Sitei101 – 102Cleavage; by viral protease NS3By similarity2
Sitei118 – 119Cleavage; by host signal peptidaseBy similarity2
Sitei210 – 211Cleavage; by host furinBy similarity2
Sitei285 – 286Cleavage; by host signal peptidaseBy similarity2
Sitei786 – 787Cleavage; by host signal peptidaseBy similarity2
Sitei1139 – 1140Cleavage; by hostBy similarity2
Sitei1366 – 1367Cleavage; by viral protease NS3By similarity2
Sitei1497 – 1498Cleavage; by autolysisBy similarity2
Sitei2116 – 2117Cleavage; by autolysisBy similarity2
Sitei2242 – 2243Cleavage; by viral protease NS3By similarity2
Sitei2265 – 2266Cleavage; by host signal peptidaseBy similarity2
Sitei2521 – 2522Cleavage; 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%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (By similarity).

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

By similarity

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

By similarity

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

Interacts with protein prM (By similarity).

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

By similarity

Homodimer; Homohexamer when secreted (By similarity).

Interacts with envelope protein E (By similarity). 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.

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

Interacts with serine protease NS3.

By similarity

GO - Molecular functioni

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1498 – 1675Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1678 – 1834Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1845 – 2010Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini2522 – 2786mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST265
Domaini3050 – 3202RdRp 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>Regioni2 – 15Interaction with host EXOC1By similarityAdd BLAST14
Regioni36 – 71Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni383 – 396Fusion peptideBy similarityAdd BLAST14
Regioni1420 – 1459Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1682 – 1685Important for RNA-bindingBy similarity4
Regioni2161 – 2165Regulates 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>Motifi1782 – 1785DEAH 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

Transmembrane, Transmembrane helix

Family and domain databases

Conserved Domains Database

More...
CDDi
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

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
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
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
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR04240 flavi_E_stem, 1 hit

PROSITE; a protein domain and family database

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

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

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

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

Q32ZD4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKKPGGPAG RRVVNMLKRP ASVSPIKGIK RLIGNLTDGR GPLRVVLAFI
60 70 80 90 100
AFFRFAAIMP TQGLLRRWRV MNKSEALKHL TSFKKEISNM LNIINRRKAK
110 120 130 140 150
RGNGSVLLWI ALVTGSMALR LGTYQGKVLM SINKTDVAEI IPIPTTKGDN
160 170 180 190 200
LCTVRAMDVG YMCQNDITYE CPRLEPGMDP EDIDCWCDRE AIYVHYGLCT
210 220 230 240 250
KNHRERRGRR SVNIPSHGES QLENRGTPWL DTAKTTKYLT KVENWMIRNP
260 270 280 290 300
GYAIVAVAAA WMLGSNTSQK VIFTIMLLLI APAYSINCLG VTNRDFVEGM
310 320 330 340 350
SGGTWVDIVL EGDGCVTIMA KDKPTLDIRL LKMEAKDLAT VRSYCYHATV
360 370 380 390 400
TSVSSEARCP TMGEAHNPKA LDSNYLCKST YVDRGWGNGC GLFGKGSLQT
410 420 430 440 450
CVKFGCTQKA MGMTIQRENL DYELAIYVHG PTSVAAHGNY TTQLGAKHAA
460 470 480 490 500
KFSITPSSPS FTANLGEYGE ATVDCEPRAA LDIDNYYVMS MNNKHWLVNR
510 520 530 540 550
DWFHDLDLPW TGPATDVWKY RESLVEFEEA HVTRQTVVAL AAQEGELHIV
560 570 580 590 600
LAGAIPVTVA GTTLTLTSGH LKCRMKLDKL KIKGSTYLMC KDKFAFAKNP
610 620 630 640 650
VDTGHGTIVT EVQYAGSDGP CRIPITMTEN LHDLTPIGRL VTVNPFVPSS
660 670 680 690 700
ETAQKILIEL EPPFGTSFIL VGTGPNQVKY QWHKSGSVIG SAFKTTIKGA
710 720 730 740 750
QRMAVLGETA WDFGSVGGVF NSIGKGIHGL FGGAFRTLFG GMSWVTQALM
760 770 780 790 800
GALLLWLGVS SRERTVSITL LATGGILLFL AMNVHADTGC AIDITRRELK
810 820 830 840 850
CGSGIFIHND VETWRDNYKY HPSTPKNFAK IIHKAYKEGI CGVRSASRLE
860 870 880 890 900
HEMWKHIAPE LNAILEDNEV DLSVVVEEHK GIYKKAPLRL ENTSDEMHFG
910 920 930 940 950
WKNWGKSFLF KTQMANSTFV VDGPETKECP TERRAWNSLE IEDFGVGIMS
960 970 980 990 1000
TKVFLKVNGD KTEVCDSMVM GTAIKGNRAV HSDLGYWIES GKNTSWRLER
1010 1020 1030 1040 1050
AVLGEVRSCT WPESHTLWNE GVEDSDLIIP PTLGGPRTHH NKREGYKTQL
1060 1070 1080 1090 1100
KGPWNEEGPI IIEFGECPGT KVTQEESCRN RAASARTTTA SGKVIRDWCC
1110 1120 1130 1140 1150
KNCTMPPLRF TTKNGCWYGM EIRPKHESEE TLIKSKVTAG TGNDICRFQL
1160 1170 1180 1190 1200
GLLMAFVFTQ EVLRKRWTAR LALPTAALLL ACFVLGAFTY SDMIRYFVLV
1210 1220 1230 1240 1250
GCAFAESNSG GDVIHLALIA VFNIQPAALV STFFRNRWTN RENLLLVIAA
1260 1270 1280 1290 1300
AMAQMAWSDV GIEIMPIMNA MALAWMILKA VSIGTVSTIA MPILSGLAPP
1310 1320 1330 1340 1350
MEWFGLDVLR CLLLIVGVAA LIKERKENLA KKKGALLISA GLALTGAFSP
1360 1370 1380 1390 1400
LVLQGALMLS ECATKRGWPA SEVLTAIGMT IALAGSVARL DSGTMAIPLA
1410 1420 1430 1440 1450
TTSILFVSYV LSGKSTDMWI ERCADVTWEE EAEITGTSPR LDVELDDNGD
1460 1470 1480 1490 1500
FKMINDPGVP MWMWASRMGL MCMAAYNPVL IPVSVAGYWM TRKIHKRGGV
1510 1520 1530 1540 1550
LWDLPAPKQM GRSDMKPGVY RVMTSGVLGS YQSGVGVMYD GVFHTMWHVT
1560 1570 1580 1590 1600
QGAALRNGEG RLNPTWGSVR DDLITYGGKW KLSATWDGTE EVQLIAAEPG
1610 1620 1630 1640 1650
KPVKNFQTRP GVFKTPAGEV GAITLDFPKG TSGSPIVNKA GAVIGLYGNG
1660 1670 1680 1690 1700
LVLSHGAYVS AISQGERQEE EAPEAFTPEM LRKRQLTILD LHPGAGKTRR
1710 1720 1730 1740 1750
VIPQIVREAV KQRLRTVILA PSRVVAAEIA EALRGLPVRF QTSAVKAEHS
1760 1770 1780 1790 1800
GTEIVDVMCH ATLTQRLMTP MRVPNYNVFV MDEAHFTDPA SIAARGYIST
1810 1820 1830 1840 1850
KVESGEAAAI FMTATPPGTI DPFPDSNSPI IDQEAEIPDR AWNSGFEWIT
1860 1870 1880 1890 1900
DYTGKTVWFV PSVRSGNEIA MCLTKAGKKV IQLNRKSYET EYQKCKGNDW
1910 1920 1930 1940 1950
DYVVTTDISE MGANFGAHRV IDSRKCVKPV IINDGEGRVQ LNGPLPITAS
1960 1970 1980 1990 2000
SAAQRRGRVG RDPTQSGDEY YYGGPITNDD TGHAHWIEAK MLLDNIQLQN
2010 2020 2030 2040 2050
GLVAQLYKPE RDKVFATDGE YRLRGEQKKH FVELMRTGEL PVWLSYKVAE
2060 2070 2080 2090 2100
AGINYTDRRW CFDGPHNNTI LEDNTEVEIW TRQGERKVLR PRWSDARVYS
2110 2120 2130 2140 2150
DNQALRAFKE FAAGKRSAGS MMDVMARMPD YFWTKTMNAA DNLYVLATTE
2160 2170 2180 2190 2200
KGGRAHRAAL EELPDTLETV LLIAMMSLAS CGMLALMMQR KGIGKTGMGT
2210 2220 2230 2240 2250
AVLTAVTILL WMADVPAPKI AGVLLISFLL MIVLIPEPEK QRSQTDNHLA
2260 2270 2280 2290 2300
VFLICALLLV SAVSANEMGW LDTTKRDLGK LFSGPSAVTT SRWEPLKLAL
2310 2320 2330 2340 2350
ALKPATAWAG YAGMTMLLTP LFRHLITTQY ISFSLTAITS QASALFGLNS
2360 2370 2380 2390 2400
GYPFVGVDLS VVFLLVGCYG QYNLPTTMAT IGLLVGHYAF MIPGWQAEAM
2410 2420 2430 2440 2450
RAAQRRTAAG VMKNAVVDGI VATDIPEMDT ATPIVEKKMG QVMLLIISAL
2460 2470 2480 2490 2500
AILLNPDTMT VVEGGVLITA ALATLLEGNA NTVWNSTVAV GVCHLMRGGW
2510 2520 2530 2540 2550
AAGPSIGWTI IRNLEAPKVK RGGIAAPTLG EIWKSRLNQL TREQFMEYRK
2560 2570 2580 2590 2600
DGIIEVDRTA ARRARREGNR TGGHPVSRGT AKLRWLVERG FAKPLGKVVD
2610 2620 2630 2640 2650
LGCGRGGWSY YCATLRHVQE VRGYTKGGPG HEEPMLMQSY GWNIVSMKSG
2660 2670 2680 2690 2700
IDVFYRPTEA CDTVLCDIGE SSPSPGVEEA RTLRVLEMIE PWLRTANQYC
2710 2720 2730 2740 2750
VKVLCPYTPK VIERLEKLQR KYGGGLVRVP LSRNSNHEMY WVSEASSNLI
2760 2770 2780 2790 2800
NAVNATSQVL LQRLEKDHRK GPRYEEDVDL GSGTRSVARR SPFMDTRKIH
2810 2820 2830 2840 2850
HRIERLKSEF STTWHYDCEH PYRTWNYHGS YEVKPTGSAS SMVNGVVKLM
2860 2870 2880 2890 2900
SKPWDSIQSV LTMAMTDTTP FGQQRVFKEK VDTKAPEPAP GVKAVLDLTT
2910 2920 2930 2940 2950
DWLWAVLCRR KKPRMCTKEE FIAKVNSHAA LGAIFEEQNQ WASAREAVED
2960 2970 2980 2990 3000
PGFWNFVDKE RQAHLEGRCE TCIYNMMGKR EKKLGEFGKA KGSRAIWYMW
3010 3020 3030 3040 3050
LGARFLEFEA LGFLNEDHWM SRENSYGGVE GKGLQKLGYI LQEISRKEGG
3060 3070 3080 3090 3100
HMFADDTAGW DTRVTLTDLE NEAKITRWME PEHRKLAEAM IELTYKNKVV
3110 3120 3130 3140 3150
KVTRPGKEGK TVMDIISRND QRGSGQVVTY ALNTYTNLAV QLIRCMEGEG
3160 3170 3180 3190 3200
LLEEEETMRI SDAKRRAVQA WLDTNGTERL TPMAVSGDDC VVKPIDNRFA
3210 3220 3230 3240 3250
TALHFLNGMS KVRKDIQEWK PSTGWTNWQE VPFCSHHFNE LVMRDGRKIV
3260 3270 3280 3290 3300
VPCRAQDELI GRARVSPGSG WSLRETACLG KAYAQMWLLM YFHRRDLRLM
3310 3320 3330 3340 3350
ANAICSAVPI DWVPTGRTTW SIHGKGEWMT TEDMLAVWNR VWIFENEHME
3360 3370 3380 3390 3400
DKTPVYSWTD VPYIGKREDQ WCGSLIGHRS RATWAENIYT PIMQVRNLIG
3410 3420
AERYVDYMPA QTRFAHEAEL QGGVL
Length:3,425
Mass (Da):380,351
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:iBECDB3B4317051FA
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
AY632542 Genomic RNA Translation: AAV34158.1

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY632542 Genomic RNA Translation: AAV34158.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein family/group databases

MEROPSiS07.001

Family and domain databases

CDDicd12149 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
InterProiView protein in InterPro
IPR011492 DEAD_Flavivir
IPR000069 Env_glycoprot_M_flavivir
IPR038302 Env_glycoprot_M_sf_flavivir
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
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
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLG_ROCV
<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: Q32ZD4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2017
Last sequence update: December 6, 2005
Last modified: February 26, 2020
This is version 115 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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

Documents

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

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

Do not show this banner again