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Protein

Genome polyprotein

Gene

GP1

Organism
West Nile virus (strain NY-99) (WNV) (West Nile virus (strain NY-1999))
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway.By similarity
Capsid protein C: Inhibits RNA silencing by interfering with host Dicer.By similarity
Peptide pr: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.By similarity
Protein prM: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.By similarity
Small envelope protein M: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.By similarity
Envelope protein E: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particule 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).5 Publications
Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host alpha/beta interferon antiviral response.By similarity
Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).PROSITE-ProRule annotationBy similarity
Serine protease NS3: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.PROSITE-ProRule annotation1 Publication
Non-structural protein 4A: Regulates the ATPase activity of the NS3 helicase activity. NS4A allows NS3 helicase to conserve energy during unwinding.1 Publication
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 (PubMed:24465392). 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). Inhibits STAT2 translocation in the nucleus after IFN-alpha treatment (PubMed:15956546).2 Publications
RNA-directed RNA polymerase NS5: Replicates the viral (+) and (-) 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, PubMed:20685660). Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway (PubMed:20106931). Inhibits host JAK1 and TYK2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (PubMed:15650160).4 Publications

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.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
NTP + H2O = NDP + phosphate.
ATP + H2O = ADP + phosphate.1 Publication
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation2 Publications
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].PROSITE-ProRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1556Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1580Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1640Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Sitei1963Involved in NS3 ATPase and RTPase activitiesBy similarity1
Sitei1966Involved in NS3 ATPase and RTPase activitiesBy similarity1
Binding sitei2541mRNA capPROSITE-ProRule annotation1
Binding sitei2544mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2545mRNA capPROSITE-ProRule annotation1
Binding sitei2547mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei2552mRNA cap bindingPROSITE-ProRule annotation1 Publication1
Binding sitei2556mRNA capPROSITE-ProRule annotation1
Binding sitei2584S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1
Active sitei2589For 2'-O-MTase activity1 Publication1
Sitei2589Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2614S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2615S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2632S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2633S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei2639S-adenosyl-L-homocysteine1 Publication1
Binding sitei2659S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei2660S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei2674For 2'-O-MTase activity1 Publication1
Binding sitei2674S-adenosyl-L-homocysteine1 Publication1
Sitei2674Essential for 2'-O-methyltransferase and N-7 methyltransferase activityPROSITE-ProRule annotation1
Sitei2675S-adenosyl-L-methionine bindingPROSITE-ProRule annotation1
Binding sitei2678mRNA capPROSITE-ProRule annotation1
Active sitei2710For 2'-O-MTase activity1 Publication1
Sitei2710Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2741mRNA capPROSITE-ProRule annotation1
Binding sitei2743mRNA capPROSITE-ProRule annotation1
Active sitei2746For 2'-O-MTase activity1 Publication1
Sitei2746Essential for 2'-O-methyltransferase activityPROSITE-ProRule annotation1
Binding sitei2748S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi2968Zinc 1By similarity1
Metal bindingi2972Zinc 1; via tele nitrogenBy similarity1
Metal bindingi2977Zinc 1By similarity1
Metal bindingi2980Zinc 1By similarity1
Metal bindingi3245Zinc 2; via tele nitrogenBy similarity1
Metal bindingi3261Zinc 2By similarity1
Metal bindingi3380Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1699 – 1706ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
Core protein
Alternative name(s):
Matrix protein
Alternative name(s):
Flavivirin protease NS2B regulatory subunit
Non-structural protein 2B
Serine protease NS3 (EC:3.4.21.91, EC:3.6.1.151 Publication, EC:3.6.4.131 Publication)
Alternative name(s):
Flavivirin protease NS3 catalytic subunit
Non-structural protein 3
RNA-directed RNA polymerase NS5 (EC:2.1.1.56PROSITE-ProRule annotation2 Publications, EC:2.1.1.57PROSITE-ProRule annotation2 Publications, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
NS5
Gene namesi
Name:GP1Imported
ORF Names:MZ11_60484gpGP1Imported, MZ11_60553gpGP1Imported
OrganismiWest Nile virus (strain NY-99) (WNV) (West Nile virus (strain NY-1999))
Taxonomic identifieri1968826 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus group
Proteomesi
  • UP000123900 Componenti: Genome
  • UP000146770 Componenti: Genome
  • UP000107647 Componenti: Genome
  • UP000169485 Componenti: Genome
  • UP000139973 Componenti: Genome
  • UP000096925 Componenti: Genome
  • UP000163596 Componenti: Genome
  • UP000138291 Componenti: Genome

Subcellular locationi

Capsid protein C :
  • Virion By similarity
  • Host nucleus By similarity
  • Host cytoplasm By similarity
  • host perinuclear region By similarity
Peptide pr :
  • Secreted By similarity
Small envelope protein M :
  • Virion membrane By similarity; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence analysis
  • Note: ER membrane retention is mediated by the transmembrane domains.By similarity
Envelope protein E :
  • Virion membrane Curated; Multi-pass membrane protein By similarity
  • Host endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Sequence analysis
  • Note: ER membrane retention is mediated by the transmembrane domains.By similarity
Non-structural protein 1 :
  • Secreted 1 Publication
  • Host endoplasmic reticulum membrane 1 Publication; Peripheral membrane protein ; Lumenal side By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.1 Publication
Non-structural protein 2A :
Serine protease subunit NS2B :
Serine protease NS3 :
  • Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation
  • Note: Remains non-covalently associated to serine protease subunit NS2B.PROSITE-ProRule annotation
Non-structural protein 4A :
  • Host endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.1 Publication
Non-structural protein 4B :
  • Host endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein By similarity
  • Note: Located in RE-derived vesicles hosting the replication complex.1 Publication
RNA-directed RNA polymerase NS5 :
  • Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Host nucleus By similarity
  • Note: Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 108CytoplasmicSequence analysisAdd BLAST107
Transmembranei109 – 129HelicalSequence analysisAdd BLAST21
Topological domaini130 – 248ExtracellularSequence analysisAdd BLAST119
Transmembranei249 – 269HelicalSequence analysisAdd BLAST21
Topological domaini270 – 275CytoplasmicSequence analysis6
Transmembranei276 – 290HelicalCuratedAdd BLAST15
Topological domaini291 – 743ExtracellularSequence analysisAdd BLAST453
Transmembranei744 – 764HelicalSequence analysisAdd BLAST21
Topological domaini765 – 770CytoplasmicSequence analysis6
Transmembranei771 – 791HelicalSequence analysisAdd BLAST21
Topological domaini792 – 1216ExtracellularSequence analysisAdd BLAST425
Transmembranei1217 – 1237HelicalSequence analysisAdd BLAST21
Topological domaini1238 – 1245CytoplasmicSequence analysis8
Transmembranei1246 – 1268HelicalSequence analysisAdd BLAST23
Topological domaini1269 – 1288LumenalSequence analysisAdd BLAST20
Transmembranei1289 – 1309HelicalSequence analysisAdd BLAST21
Topological domaini1310 – 1313CytoplasmicSequence analysis4
Transmembranei1314 – 1331HelicalSequence analysisAdd BLAST18
Topological domaini1332 – 1345LumenalSequence analysisAdd BLAST14
Transmembranei1346 – 1366HelicalSequence analysisAdd BLAST21
Topological domaini1367 – 1375CytoplasmicSequence analysis9
Transmembranei1376 – 1396HelicalSequence analysisAdd BLAST21
Topological domaini1397 – 1399LumenalSequence analysis3
Transmembranei1400 – 1420HelicalSequence analysisAdd BLAST21
Topological domaini1421 – 1477CytoplasmicSequence analysisAdd BLAST57
Intramembranei1478 – 1498HelicalSequence analysisAdd BLAST21
Topological domaini1499 – 2174CytoplasmicSequence analysisAdd BLAST676
Transmembranei2175 – 2195HelicalSequence analysisAdd BLAST21
Topological domaini2196 – 2200LumenalSequence analysis5
Intramembranei2201 – 2221HelicalSequence analysisAdd BLAST21
Topological domaini2222LumenalSequence analysis1
Transmembranei2223 – 2243HelicalSequence analysisAdd BLAST21
Topological domaini2244 – 2258CytoplasmicSequence analysisAdd BLAST15
Transmembranei2259 – 2279Helical; Note=Signal for NS4BSequence analysisAdd BLAST21
Topological domaini2280 – 2312LumenalSequence analysisAdd BLAST33
Intramembranei2313 – 2333HelicalSequence analysisAdd BLAST21
Topological domaini2334 – 2380LumenalSequence analysisAdd BLAST47
Transmembranei2381 – 2401HelicalSequence analysisAdd BLAST21
Topological domaini2402 – 2444CytoplasmicSequence analysisAdd BLAST43
Transmembranei2445 – 2465HelicalSequence analysisAdd BLAST21
Topological domaini2466 – 2470LumenalSequence analysis5
Transmembranei2471 – 2491HelicalSequence analysisAdd BLAST21
Topological domaini2492 – 3433CytoplasmicSequence analysisAdd BLAST942

GO - Cellular componenti

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi968T → N: No effect on TL3 signaling inhibition by NS1. 1 Publication1
Mutagenesisi982N → I: No effect on TL3 signaling inhibition by NS1. 1 Publication1
Mutagenesisi1029E → V: No effect on TL3 signaling inhibition by NS1. 1 Publication1
Mutagenesisi1046N → D: Complete loss of TL3 signaling inhibition by NS1. 1 Publication1
Mutagenesisi1086G → R: Almost no effect on TL3 signaling inhibition by NS1. 1 Publication1
Mutagenesisi1108T → I: Complete loss of TL3 signaling inhibition by NS1. 1 Publication1
Mutagenesisi1111P → S: About 50% loss of TL3 signaling inhibition by NS1. 1 Publication1
Mutagenesisi1124M → V: About 50% loss of TL3 signaling inhibition by NS1. 1 Publication1
Mutagenesisi2169 – 2173EELPD → KKLPK: Complete loss of regulation of the ATPase activity of NS3 helicase by NS4A. 1 Publication5
Mutagenesisi2557K → A: 85% loss of NS5-GMP formation. 1 Publication1
Mutagenesisi2589K → A, E or R: Complete loss of 2'-O-methyltranferase activity. 1 Publication1
Mutagenesisi2674D → A, N or K: Complete loss of 2'-O-methyltranferase activity. 1 Publication1
Mutagenesisi2676G → A: 86% loss of N7 guanine methyltransferase activity; 60% loss of 2'-O-methyltranferase activity. 1 Publication1
Mutagenesisi2688R → A: 78% loss of N7 guanine methyltransferase activity; no effect 2'-O-methyltranferase activity. 1 Publication1
Mutagenesisi2691R → A: 50% loss of N7 guanine methyltransferase activity; no effect 2'-O-methyltranferase activity. 1 Publication1
Mutagenesisi2692V → A: 10% loss of N7 guanine methyltransferase activity; 50% loss of 2'-O-methyltranferase activity. 1 Publication1
Mutagenesisi2710K → A, E or N: Complete loss of 2'-O-methyltranferase activity. 1 Publication1
Mutagenesisi2712L → A: 20% loss of N7 guanine methyltransferase activity7; 74% loss of 2'-O-methyltranferase activity. 1 Publication1
Mutagenesisi2746E → A, D or K: Complete loss of 2'-O-methyltranferase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004415761 – 3433Genome polyproteinAdd BLAST3433
ChainiPRO_00004415771 – 105Capsid protein CBy similarityAdd BLAST105
PropeptideiPRO_0000441578106 – 123ER anchor for the capsid protein C, removed in mature form by serine protease NS3By similarityAdd BLAST18
ChainiPRO_0000441579124 – 290prMBy similarityAdd BLAST167
ChainiPRO_0000441580124 – 215Peptide prBy similarityAdd BLAST92
ChainiPRO_0000441581216 – 290Small envelope protein MBy similarityAdd BLAST75
ChainiPRO_0000441582291 – 791Envelope protein EBy similarityAdd BLAST501
ChainiPRO_0000441583792 – 1143Non-structural protein 1By similarityAdd BLAST352
ChainiPRO_00004415841144 – 1374Non-structural protein 2ABy similarityAdd BLAST231
ChainiPRO_00004415851375 – 1505Serine protease subunit NS2BBy similarityAdd BLAST131
ChainiPRO_00004415861506 – 2124Serine protease NS3By similarityAdd BLAST619
ChainiPRO_00004415872125 – 2250Non-structural protein 4ABy similarityAdd BLAST126
PeptideiPRO_00004415882251 – 2273Peptide 2kBy similarityAdd BLAST23
ChainiPRO_00004415892274 – 2528Non-structural protein 4BBy similarityAdd BLAST255
ChainiPRO_00004415902529 – 3433RNA-directed RNA polymerase NS5By similarityAdd BLAST905

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi138N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi293 ↔ 3201 Publication
Disulfide bondi350 ↔ 4112 Publications
Disulfide bondi350 ↔ 406By similarity
Disulfide bondi364 ↔ 3952 Publications
Disulfide bondi382 ↔ 411By similarity
Disulfide bondi382 ↔ 4062 Publications
Disulfide bondi480 ↔ 5782 Publications
Disulfide bondi595 ↔ 6261 Publication
Disulfide bondi795 ↔ 8061 Publication
Disulfide bondi846 ↔ 9341 Publication
Glycosylationi921N-linked (GlcNAc...) asparagine; by host1 Publication1
Glycosylationi966N-linked (GlcNAc...) asparagine; by host1 Publication1
Disulfide bondi970 ↔ 10142 Publications
Glycosylationi998N-linked (GlcNAc...) asparagine; by host1 Publication1
Disulfide bondi1071 ↔ 11202 Publications
Disulfide bondi1082 ↔ 11032 Publications
Disulfide bondi1104 ↔ 11072 Publications
Modified residuei2584PhosphoserineBy similarity1

Post-translational modificationi

Genome polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site.By similarity
Protein prM: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM.By similarity
Envelope protein E: N-glycosylated.By similarity
Non-structural protein 1: N-glycosylated (PubMed:24505133). The excreted form is glycosylated and this is required for efficient secretion of the protein from infected cells (By similarity).By similarity1 Publication
RNA-directed RNA polymerase NS5: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei105 – 106Cleavage; by viral protease NS3By similarity2
Sitei123 – 124Cleavage; by host signal peptidaseBy similarity2
Sitei215 – 216Cleavage; by host furinBy similarity2
Sitei290 – 291Cleavage; by host signal peptidaseBy similarity2
Sitei791 – 792Cleavage; by host signal peptidaseBy similarity2
Sitei1143 – 1144Cleavage; by hostBy similarity2
Sitei1374 – 1375Cleavage; by viral protease NS3By similarity2
Sitei1505 – 1506Cleavage; by autolysisBy similarity2
Sitei2124 – 2125Cleavage; by autolysisBy similarity2
Sitei2250 – 2251Cleavage; by viral protease NS3By similarity2
Sitei2273 – 2274Cleavage; by host signal peptidaseBy similarity2
Sitei2528 – 2529Cleavage; by viral protease NS3By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Interactioni

Subunit structurei

Capsid protein C: Homodimer. 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 (PubMed:20956322). Non-structural protein 1: Homodimer; Homohexamer when secreted (PubMed:24505133, PubMed:24594604). NS1 interacts with NS4B (PubMed:22553322). Interacts with host complement protein CFH; this interaction leads to the degradation of C3 (PubMed:17132743). Non-structural protein 2B: Forms a heterodimer with serine protease NS3. May form homooligomers (By similarity). Serine protease NS3: Forms a heterodimer with NS2B. Interacts with NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase NS5; this interaction stimulates RNA-directed RNA polymerase NS5 guanylyltransferase activity (By similarity). Non-structural protein 4B: Interacts with serine protease NS3 (By similarity). Interacts with NS1 (PubMed:22553322). RNA-directed RNA polymerase NS5: Homodimer (By similarity). Interacts with host STAT2; this interaction inhibits the phosphorylation of the latter, and, when all viral proteins are present (polyprotein), targets STAT2 for degradation (By similarity).By similarity5 Publications

GO - Molecular functioni

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OY0X-ray2.80A/B2534-2795[»]
3I50X-ray3.00E291-692[»]
3IYWelectron microscopy13.70A/B/C291-690[»]
3J0Belectron microscopy10.30A/B/C291-690[»]
3LKZX-ray2.00A/B2529-2828[»]
4O6CX-ray2.75A/B/C/D/E/F791-1143[»]
4O6DX-ray2.59A/B791-1143[»]
4OIEX-ray1.85A963-1143[»]
4OIIX-ray3.00A/B963-1143[»]
SMRiQ9Q6P4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1506 – 1683Peptidase S7PROSITE-ProRule annotationAdd BLAST178
Domaini1686 – 1842Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST157
Domaini1853 – 2018Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini2529 – 2794mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd BLAST266
Domaini3058 – 3210RdRp catalyticPROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 15Interaction with host EXOC1By similarityAdd BLAST14
Regioni37 – 72Hydrophobic; homodimerization of capsid protein CBy similarityAdd BLAST36
Regioni388 – 401Fusion peptideBy similarityAdd BLAST14
Regioni1428 – 1467Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd BLAST40
Regioni1690 – 1693Important for RNA-bindingBy similarity4
Regioni2169 – 2173Regulates the ATPase activity of NS3 helicase1 Publication5
Regioni2614 – 2615S-adenosyl-L-homocysteine bindingCombined sources2
Regioni2659 – 2660S-adenosyl-L-homocysteine bindingCombined sources2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1790 – 1793DEAH boxPROSITE-ProRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi281 – 284Poly-LeuSequence analysis4

Domaini

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

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

CDDicd12149. Flavi_E_C. 1 hit.
Gene3Di2.60.40.350. 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.
IPR013755. Flav_gly_cen_dom_subdom1.
IPR001122. Flavi_capsidC.
IPR027287. Flavi_E_Ig-like.
IPR026470. Flavi_E_Stem/Anchor_dom.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flavivir/Alphavir_Ig-like.
IPR001850. Flavivirus_NS3_S7.
IPR014412. Gen_Poly_FLV.
IPR011998. Glycoprot_cen/dimer.
IPR013756. GlyE_cen_dom_subdom2.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR026490. mRNA_cap_0/1_MeTrfase.
IPR027417. P-loop_NTPase.
IPR009003. Peptidase_S1_PA.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
PfamiView protein in Pfam
PF01003. Flavi_capsid. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00949. Peptidase_S7. 1 hit.
PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTiView protein in SMART
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
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.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Q6P4-1 [UniParc]FASTAAdd to basket

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        10         20         30         40         50
MSKKPGGPGK SRAVNMLKRG MPRVLSLIGL KRAMLSLIDG KGPIRFVLAL
60 70 80 90 100
LAFFRFTAIA PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRSS
110 120 130 140 150
KQKKRGGKTG IAVMIGLIAS VGAVTLSNFQ GKVMMTVNAT DVTDVITIPT
160 170 180 190 200
AAGKNLCIVR AMDVGYMCDD TITYECPVLS AGNDPEDIDC WCTKSAVYVR
210 220 230 240 250
YGRCTKTRHS RRSRRSLTVQ THGESTLANK KGAWMDSTKA TRYLVKTESW
260 270 280 290 300
ILRNPGYALV AAVIGWMLGS NTMQRVVFVV LLLLVAPAYS FNCLGMSNRD
310 320 330 340 350
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLAEVRSYC
360 370 380 390 400
YLATVSDLST KAACPTMGEA HNDKRADPAF VCRQGVVDRG WGNGCGLFGK
410 420 430 440 450
GSIDTCAKFA CSTKAIGRTI LKENIKYEVA IFVHGPTTVE SHGNYSTQVG
460 470 480 490 500
ATQAGRFSIT PAAPSYTLKL GEYGEVTVDC EPRSGIDTNA YYVMTVGTKT
510 520 530 540 550
FLVHREWFMD LNLPWSSAGS TVWRNRETLM EFEEPHATKQ SVIALGSQEG
560 570 580 590 600
ALHQALAGAI PVEFSSNTVK LTSGHLKCRV KMEKLQLKGT TYGVCSKAFK
610 620 630 640 650
FLGTPADTGH GTVVLELQYT GTDGPCKVPI SSVASLNDLT PVGRLVTVNP
660 670 680 690 700
FVSVATANAK VLIELEPPFG DSYIVVGRGE QQINHHWHKS GSSIGKAFTT
710 720 730 740 750
TLKGAQRLAA LGDTAWDFGS VGGVFTSVGK AVHQVFGGAF RSLFGGMSWI
760 770 780 790 800
TQGLLGALLL WMGINARDRS IALTFLAVGG VLLFLSVNVH ADTGCAIDIS
810 820 830 840 850
RQELRCGSGV FIHNDVEAWM DRYKYYPETP QGLAKIIQKA HKEGVCGLRS
860 870 880 890 900
VSRLEHQMWE AVKDELNTLL KENGVDLSVV VEKQEGMYKS APKRLTATTE
910 920 930 940 950
KLEIGWKAWG KSILFAPELA NNTFVVDGPE TKECPTQNRA WNSLEVEDFG
960 970 980 990 1000
FGLTSTRMFL KVRESNTTEC DSKIIGTAVK NNLAIHSDLS YWIESRLNDT
1010 1020 1030 1040 1050
WKLERAVLGE VKSCTWPETH TLWGDGILES DLIIPVTLAG PRSNHNRRPG
1060 1070 1080 1090 1100
YKTQNQGPWD EGRVEIDFDY CPGTTVTLSE SCGHRGPATR TTTESGKLIT
1110 1120 1130 1140 1150
DWCCRSCTLP PLRYQTDSGC WYGMEIRPQR HDEKTLVQSQ VNAYNADMID
1160 1170 1180 1190 1200
PFQLGLLVVF LATQEVLRKR WTAKISMPAI LIALLVLVFG GITYTDVLRY
1210 1220 1230 1240 1250
VILVGAAFAE SNSGGDVVHL ALMATFKIQP VFMVASFLKA RWTNQENILL
1260 1270 1280 1290 1300
MLAAVFFQMA YHDARQILLW EIPDVLNSLA VAWMILRAIT FTTTSNVVVP
1310 1320 1330 1340 1350
LLALLTPGLR CLNLDVYRIL LLMVGIGSLI REKRSAAAKK KGASLLCLAL
1360 1370 1380 1390 1400
ASTGLFNPMI LAAGLIACDP NRKRGWPATE VMTAVGLMFA IVGGLAELDI
1410 1420 1430 1440 1450
DSMAIPMTIA GLMFAAFVIS GKSTDMWIER TADISWESDA EITGSSERVD
1460 1470 1480 1490 1500
VRLDDDGNFQ LMNDPGAPWK IWMLRMVCLA ISAYTPWAIL PSVVGFWITL
1510 1520 1530 1540 1550
QYTKRGGVLW DTPSPKEYKK GDTTTGVYRI MTRGLLGSYQ AGAGVMVEGV
1560 1570 1580 1590 1600
FHTLWHTTKG AALMSGEGRL DPYWGSVKED RLCYGGPWKL QHKWNGQDEV
1610 1620 1630 1640 1650
QMIVVEPGKN VKNVQTKPGV FKTPEGEIGA VTLDFPTGTS GSPIVDKNGD
1660 1670 1680 1690 1700
VIGLYGNGVI MPNGSYISAI VQGERMDEPI PAGFEPEMLR KKQITVLDLH
1710 1720 1730 1740 1750
PGAGKTRRIL PQIIKEAINR RLRTAVLAPT RVVAAEMAEA LRGLPIRYQT
1760 1770 1780 1790 1800
SAVPREHNGN EIVDVMCHAT LTHRLMSPHR VPNYNLFVMD EAHFTDPASI
1810 1820 1830 1840 1850
AARGYISTKV ELGEAAAIFM TATPPGTSDP FPESNSPISD LQTEIPDRAW
1860 1870 1880 1890 1900
NSGYEWITEY TGKTVWFVPS VKMGNEIALC LQRAGKKVVQ LNRKSYETEY
1910 1920 1930 1940 1950
PKCKNDDWDF VITTDISEMG ANFKASRVID SRKSVKPTII TEGEGRVILG
1960 1970 1980 1990 2000
EPSAVTAASA AQRRGRIGRN PSQVGDEYCY GGHTNEDDSN FAHWTEARIM
2010 2020 2030 2040 2050
LDNINMPNGL IAQFYQPERE KVYTMDGEYR LRGEERKNFL ELLRTADLPV
2060 2070 2080 2090 2100
WLAYKVAAAG VSYHDRRWCF DGPRTNTILE DNNEVEVITK LGERKILRPR
2110 2120 2130 2140 2150
WIDARVYSDH QALKAFKDFA SGKRSQIGLI EVLGKMPEHF MGKTWEALDT
2160 2170 2180 2190 2200
MYVVATAEKG GRAHRMALEE LPDALQTIAL IALLSVMTMG VFFLLMQRKG
2210 2220 2230 2240 2250
IGKIGLGGAV LGVATFFCWM AEVPGTKIAG MLLLSLLLMI VLIPEPEKQR
2260 2270 2280 2290 2300
SQTDNQLAVF LICVMTLVSA VAANEMGWLD KTKSDISSLF GQRIEVKENF
2310 2320 2330 2340 2350
SMGEFLLDLR PATAWSLYAV TTAVLTPLLK HLITSDYINT SLTSINVQAS
2360 2370 2380 2390 2400
ALFTLARGFP FVDVGVSALL LAAGCWGQVT LTVTVTAATL LFCHYAYMVP
2410 2420 2430 2440 2450
GWQAEAMRSA QRRTAAGIMK NAVVDGIVAT DVPELERTTP IMQKKVGQIM
2460 2470 2480 2490 2500
LILVSLAAVV VNPSVKTVRE AGILITAAAV TLWENGASSV WNATTAIGLC
2510 2520 2530 2540 2550
HIMRGGWLSC LSITWTLIKN MEKPGLKRGG AKGRTLGEVW KERLNQMTKE
2560 2570 2580 2590 2600
EFTRYRKEAI IEVDRSAAKH ARKEGNVTGG HPVSRGTAKL RWLVERRFLE
2610 2620 2630 2640 2650
PVGKVIDLGC GRGGWCYYMA TQKRVQEVRG YTKGGPGHEE PQLVQSYGWN
2660 2670 2680 2690 2700
IVTMKSGVDV FYRPSECCDT LLCDIGESSS SAEVEEHRTI RVLEMVEDWL
2710 2720 2730 2740 2750
HRGPREFCVK VLCPYMPKVI EKMELLQRRY GGGLVRNPLS RNSTHEMYWV
2760 2770 2780 2790 2800
SRASGNVVHS VNMTSQVLLG RMEKRTWKGP QYEEDVNLGS GTRAVGKPLL
2810 2820 2830 2840 2850
NSDTSKIKNR IERLRREYSS TWHHDENHPY RTWNYHGSYD VKPTGSASSL
2860 2870 2880 2890 2900
VNGVVRLLSK PWDTITNVTT MAMTDTTPFG QQRVFKEKVD TKAPEPPEGV
2910 2920 2930 2940 2950
KYVLNETTNW LWAFLAREKR PRMCSREEFI RKVNSNAALG AMFEEQNQWR
2960 2970 2980 2990 3000
SAREAVEDPK FWEMVDEERE AHLRGECHTC IYNMMGKREK KPGEFGKAKG
3010 3020 3030 3040 3050
SRAIWFMWLG ARFLEFEALG FLNEDHWLGR KNSGGGVEGL GLQKLGYILR
3060 3070 3080 3090 3100
EVGTRPGGKI YADDTAGWDT RITRADLENE AKVLELLDGE HRRLARAIIE
3110 3120 3130 3140 3150
LTYRHKVVKV MRPAADGRTV MDVISREDQR GSGQVVTYAL NTFTNLAVQL
3160 3170 3180 3190 3200
VRMMEGEGVI GPDDVEKLTK GKGPKVRTWL FENGEERLSR MAVSGDDCVV
3210 3220 3230 3240 3250
KPLDDRFATS LHFLNAMSKV RKDIQEWKPS TGWYDWQQVP FCSNHFTELI
3260 3270 3280 3290 3300
MKDGRTLVVP CRGQDELVGR ARISPGAGWN VRDTACLAKS YAQMWLLLYF
3310 3320 3330 3340 3350
HRRDLRLMAN AICSAVPVNW VPTGRTTWSI HAGGEWMTTE DMLEVWNRVW
3360 3370 3380 3390 3400
IEENEWMEDK TPVEKWSDVP YSGKREDIWC GSLIGTRARA TWAENIQVAI
3410 3420 3430
NQVRAIIGDE KYVDYMSSLK RYEDTTLVED TVL
Length:3,433
Mass (Da):381,176
Last modified:March 1, 2001 - v2
Checksum:iA742A68D0E55947E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF196835 Genomic RNA. Translation: AAF20092.2.
AF404755 Genomic RNA. Translation: AAM81751.1.
HM488125 Genomic RNA. Translation: ADL27936.1.
HM488126 Genomic RNA. Translation: ADL27937.1.
HM488127 Genomic RNA. Translation: ADL27938.1.
HM488128 Genomic RNA. Translation: ADL27939.1.
KC407666 Genomic RNA. Translation: AGI15883.1.
KM083619 Genomic RNA. Translation: AIO10814.1.
KX547386 Genomic RNA. Translation: ANW69091.1.
KX547393 Genomic RNA. Translation: ANW69112.1.
AB185914 Genomic RNA. Translation: BAD34488.1.

Similar proteinsi

Entry informationi

Entry nameiPOLG_WNV9
AccessioniPrimary (citable) accession number: Q9Q6P4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2017
Last sequence update: March 1, 2001
Last modified: September 27, 2017
This is version 158 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

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