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P06935

- POLG_WNV

UniProt

P06935 - POLG_WNV

Protein

Genome polyprotein

Gene
N/A
Organism
West Nile virus (WNV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (24 Oct 2003)
      Previous versions | rss
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    Functioni

    Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA By similarity.By similarity
    prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated By similarity.By similarity
    Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes By similarity.By similarity
    Non-structural protein 1 is involved in virus replication and regulation of the innate immune response.By similarity
    Non-structural protein 2A may be involved viral RNA replication and capsid assembly.Curated
    Non-structural protein 2B is a required cofactor for the serine protease function of NS3.PROSITE-ProRule annotation
    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 By similarity.PROSITE-ProRule annotation
    Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase By similarity.By similarity
    Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.By similarity
    Non-structural protein 4B inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway.By similarity
    RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) 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 genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host JAK1 and TYK2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway By similarity.PROSITE-ProRule annotation

    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.
    S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation
    S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-(mRNA) = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(mRNA).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei105 – 1062Cleavage; by viral protease NS3
    Sitei123 – 1242Cleavage; by host signal peptidaseBy similarity
    Sitei215 – 2162Cleavage; by host furinSequence Analysis
    Sitei290 – 2912Cleavage; by host signal peptidaseSequence Analysis
    Sitei787 – 7882Cleavage; by host signal peptidaseSequence Analysis
    Sitei1139 – 11402Cleavage; by hostSequence Analysis
    Sitei1370 – 13712Cleavage; by viral protease NS3
    Sitei1501 – 15022Cleavage; by autolysis
    Active sitei1552 – 15521Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
    Active sitei1576 – 15761Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
    Active sitei1636 – 16361Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
    Sitei2120 – 21212Cleavage; by autolysis
    Sitei2246 – 22472Cleavage; by viral protease NS3
    Sitei2269 – 22702Cleavage; by host signal peptidaseSequence Analysis
    Sitei2525 – 25262Cleavage; by viral protease NS3
    Binding sitei2538 – 25381mRNA capPROSITE-ProRule annotation
    Binding sitei2541 – 25411mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
    Binding sitei2542 – 25421mRNA capPROSITE-ProRule annotation
    Binding sitei2544 – 25441mRNA cap; via carbonyl oxygenPROSITE-ProRule annotation
    Sitei2549 – 25491mRNA cap bindingPROSITE-ProRule annotation
    Binding sitei2553 – 25531mRNA capPROSITE-ProRule annotation
    Binding sitei2581 – 25811S-adenosyl-L-methioninePROSITE-ProRule annotation
    Sitei2586 – 25861Essential for 2'-O-methyltransferase activity
    Binding sitei2611 – 26111S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
    Binding sitei2612 – 26121S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
    Binding sitei2629 – 26291S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei2630 – 26301S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
    Binding sitei2656 – 26561S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei2657 – 26571S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
    Sitei2671 – 26711Essential for 2'-O-methyltransferase and N-7 methyltransferase activity
    Sitei2672 – 26721S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
    Binding sitei2675 – 26751mRNA capPROSITE-ProRule annotation
    Sitei2707 – 27071Essential for 2'-O-methyltransferase activity
    Binding sitei2738 – 27381mRNA capPROSITE-ProRule annotation
    Binding sitei2740 – 27401mRNA capPROSITE-ProRule annotation
    Sitei2743 – 27431Essential for 2'-O-methyltransferase activity
    Binding sitei2745 – 27451S-adenosyl-L-methioninePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1695 – 17028ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. double-stranded RNA binding Source: InterPro
    4. metal ion binding Source: UniProtKB-KW
    5. mRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB-EC
    6. mRNA (nucleoside-2'-O-)-methyltransferase activity Source: UniProtKB-EC
    7. peptidase activity Source: CACAO
    8. protein binding Source: IntAct
    9. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    10. RNA helicase activity Source: InterPro
    11. serine-type endopeptidase activity Source: InterPro
    12. serine-type exopeptidase activity Source: InterPro
    13. structural molecule activity Source: InterPro

    GO - Biological processi

    1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
    2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
    3. induction by virus of host autophagy Source: UniProtKB-KW
    4. positive regulation of viral genome replication Source: CACAO
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. suppression by virus of host apoptotic process Source: CACAO
    7. suppression by virus of host JAK1 activity Source: UniProtKB-KW
    8. suppression by virus of host TYK2 activity Source: UniProtKB-KW
    9. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
    10. transcription, DNA-templated Source: UniProtKB-KW
    11. viral RNA genome replication Source: InterPro
    12. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase, Methyltransferase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Transferase

    Keywords - Biological processi

    Activation 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 JAK1 by virus, Inhibition of host TYK2 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

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, S-adenosyl-L-methionine

    Protein family/group databases

    MEROPSiS07.001.

    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
    Alternative name(s):
    Flavivirin protease NS3 catalytic subunit
    Non-structural protein 3
    Alternative name(s):
    NS5
    OrganismiWest Nile virus (WNV)
    Taxonomic identifieri11082 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus group
    Virus hostiAedes [TaxID: 7158]
    Amblyomma variegatum (Tropical bont tick) [TaxID: 34610]
    Aves [TaxID: 8782]
    Culex [TaxID: 53527]
    Homo sapiens (Human) [TaxID: 9606]
    Hyalomma marginatum [TaxID: 34627]
    Mansonia uniformis [TaxID: 308735]
    Mimomyia [TaxID: 308737]
    Rhipicephalus [TaxID: 34630]
    ProteomesiUP000008600: Genome

    Subcellular locationi

    Chain Small envelope protein M : Virion membrane By similarity; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Chain Envelope protein E : Virion membrane By similarity; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Chain Non-structural protein 1 : Secreted. Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Lumenal side By similarity
    Chain Non-structural protein 2A : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein Curated
    Chain Serine protease subunit NS2B : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein Curated
    Chain 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 NS3 protease.PROSITE-ProRule annotation
    Chain Non-structural protein 4A : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Note: Located in RE-associated vesicles hosting the replication complex.
    Chain Non-structural protein 4B : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Multi-pass membrane protein By similarity
    Chain RNA-directed RNA polymerase NS5 : Host endoplasmic reticulum membrane PROSITE-ProRule annotation; Peripheral membrane protein PROSITE-ProRule annotation; Cytoplasmic side PROSITE-ProRule annotation. Host nucleus 1 Publication
    Note: Located in RE-associated vesicles hosting the replication complex.

    GO - Cellular componenti

    1. host cell endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. host cell nucleus Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. viral capsid Source: UniProtKB-KW
    5. viral envelope Source: UniProtKB-KW
    6. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2586 – 25861K → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. 1 Publication
    Mutagenesisi2671 – 26711D → A: Lethal for the virus. Complete loss of 2'-O and N-7 methyltransferase activies. 1 Publication
    Mutagenesisi2707 – 27071K → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. 1 Publication
    Mutagenesisi2743 – 27431E → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostSequence Analysis
    Chaini2 – 105104Capsid protein CPRO_0000037743Add
    BLAST
    Propeptidei106 – 12318ER anchor for the protein C, removed in mature form by serine protease NS3By similarityPRO_0000037744Add
    BLAST
    Chaini124 – 290167prMPRO_0000405150Add
    BLAST
    Chaini124 – 21592Peptide prPRO_0000405151Add
    BLAST
    Chaini216 – 29075Small envelope protein MPRO_0000037745Add
    BLAST
    Chaini291 – 787497Envelope protein EPRO_0000037746Add
    BLAST
    Chaini788 – 1139352Non-structural protein 1PRO_0000037747Add
    BLAST
    Chaini1140 – 1370231Non-structural protein 2APRO_0000037748Add
    BLAST
    Chaini1371 – 1501131Serine protease subunit NS2BPRO_0000037749Add
    BLAST
    Chaini1502 – 2120619Serine protease NS3PRO_0000037750Add
    BLAST
    Chaini2121 – 2246126Non-structural protein 4APRO_0000037751Add
    BLAST
    Peptidei2247 – 226923Peptide 2kBy similarityPRO_0000405152Add
    BLAST
    Chaini2270 – 2525256Non-structural protein 4BPRO_0000037752Add
    BLAST
    Chaini2526 – 3430905RNA-directed RNA polymerase NS5PRO_0000037753Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi138 – 1381N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi293 ↔ 3201 Publication
    Disulfide bondi350 ↔ 4061 Publication
    Disulfide bondi364 ↔ 3951 Publication
    Disulfide bondi382 ↔ 4111 Publication
    Disulfide bondi476 ↔ 5741 Publication
    Disulfide bondi591 ↔ 6221 Publication
    Glycosylationi917 – 9171N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi962 – 9621N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi994 – 9941N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi2336 – 23361N-linked (GlcNAc...); by hostSequence Analysis

    Post-translational modificationi

    Specific enzymatic cleavages in vivo by the viral protease NS3 and host cell enzymes yield mature proteins. The nascent 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 soluble protein C is released after cleavage by NS3 protease at a site upstream of this hydrophobic domain. prM is cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. 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 By similarity.By similarity
    RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization By similarity.By similarity

    Keywords - PTMi

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

    Interactioni

    Subunit structurei

    Capsid protein C forms homodimers. prM and envelope protein E form heterodimers in the endoplasmic reticulum and Golgi. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive. NS3 interacts with unphosphorylated NS5; this interaction stimulates NS5 guanylyltransferase activity By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTLMA15Q17NZ65EBI-2912469,EBI-2912457From a different organism.
    ITGB3P051064EBI-981051,EBI-702847From a different organism.

    Protein-protein interaction databases

    IntActiP06935. 3 interactions.

    Structurei

    Secondary structure

    1
    3430
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi595 – 6039
    Beta strandi605 – 6073
    Beta strandi609 – 6157
    Beta strandi621 – 6233
    Beta strandi626 – 6316
    Beta strandi634 – 6374
    Beta strandi639 – 6435
    Beta strandi657 – 6626
    Beta strandi665 – 6739
    Beta strandi679 – 6857
    Beta strandi1423 – 14286
    Helixi1434 – 14396
    Beta strandi1440 – 14434
    Beta strandi1444 – 14496
    Beta strandi1451 – 14533
    Beta strandi1455 – 14573
    Beta strandi1522 – 15276
    Beta strandi1536 – 15438
    Beta strandi1546 – 15505
    Helixi1551 – 15544
    Beta strandi1559 – 15613
    Beta strandi1564 – 15663
    Beta strandi1568 – 15725
    Turni1573 – 15764
    Beta strandi1577 – 15837
    Beta strandi1592 – 15943
    Beta strandi1596 – 16005
    Beta strandi1608 – 16125
    Beta strandi1615 – 16195
    Beta strandi1622 – 16276
    Helixi1633 – 16353
    Beta strandi1639 – 16413
    Beta strandi1647 – 16515
    Beta strandi1654 – 16563
    Beta strandi1662 – 16654
    Beta strandi1672 – 16743

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FP7X-ray1.68A1420-1466[»]
    B1517-1688[»]
    2G05model-D1675-2120[»]
    2G2Gmodel-D1675-2120[»]
    2GGVX-ray1.80A1419-1525[»]
    B1503-1679[»]
    2IJOX-ray2.30A1419-1482[»]
    B1502-1685[»]
    2P5PX-ray2.80A/B/C585-701[»]
    2YOLX-ray3.20A1420-1465[»]
    A1502-1671[»]
    3E90X-ray2.45A/C1420-1463[»]
    B/D1502-1685[»]
    3I50X-ray3.00E291-688[»]
    DisProtiDP00673.
    ProteinModelPortaliP06935.
    SMRiP06935. Positions 25-97, 291-689, 1420-1458, 1502-2120, 2531-2792, 2799-3424.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06935.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 105104CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini127 – 248122ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini270 – 2756CytoplasmicSequence Analysis
    Topological domaini293 – 739447ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini761 – 7666ExtracellularSequence Analysis
    Topological domaini788 – 1138351ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1160 – 121253CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1234 – 124310LumenalSequence Analysis
    Topological domaini1265 – 129228CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1314 – 134027LumenalSequence AnalysisAdd
    BLAST
    Topological domaini1362 – 137110CytoplasmicSequence Analysis
    Topological domaini1393 – 13953LumenalSequence Analysis
    Topological domaini1417 – 147357CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1495 – 2170676CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2192 – 21965LumenalSequence Analysis
    Topological domaini2218 – 22181LumenalSequence Analysis
    Topological domaini2240 – 225415CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2276 – 230934LumenalSequence AnalysisAdd
    BLAST
    Topological domaini2331 – 235525LumenalSequence AnalysisAdd
    BLAST
    Topological domaini2377 – 23771LumenalSequence Analysis
    Topological domaini2399 – 244143CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2463 – 24675LumenalSequence Analysis
    Topological domaini2489 – 3430942CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei740 – 76021HelicalSequence AnalysisAdd
    BLAST
    Intramembranei767 – 78721HelicalSequence AnalysisAdd
    BLAST
    Intramembranei1474 – 149421HelicalSequence AnalysisAdd
    BLAST
    Intramembranei2197 – 221721HelicalSequence AnalysisAdd
    BLAST
    Intramembranei2310 – 233021HelicalSequence AnalysisAdd
    BLAST
    Intramembranei2356 – 237621HelicalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei106 – 12621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei249 – 26921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei276 – 29217HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1139 – 115921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1213 – 123321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1244 – 126421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1293 – 131321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1341 – 136121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1372 – 139221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1396 – 141621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2171 – 219121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2219 – 223921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2255 – 227521Helical; Note=Signal for NS4BSequence AnalysisAdd
    BLAST
    Transmembranei2378 – 239821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2442 – 246221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2468 – 248821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1502 – 1679178Peptidase S7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1682 – 1838157Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1849 – 2014166Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini2526 – 2791266mRNA cap 0-1 NS5-type MTPROSITE-ProRule annotationAdd
    BLAST
    Domaini3055 – 3207153RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni33 – 7442Hydrophobic; homodimerization of capsid protein CBy similarityAdd
    BLAST
    Regioni388 – 40114Involved in fusionAdd
    BLAST
    Regioni1424 – 146340Interacts with and activates NS3 proteasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1786 – 17894DEAH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi281 – 2844Poly-Leu
    Compositional biasi2675 – 26784Poly-Ser

    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
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 mRNA cap 0-1 NS5-type MT domain.PROSITE-ProRule annotation
    Contains 1 peptidase S7 domain.PROSITE-ProRule annotation
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di2.60.40.350. 1 hit.
    2.60.98.10. 2 hits.
    3.30.387.10. 1 hit.
    3.40.50.150. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR011492. DEAD_Flavivir.
    IPR000069. Env_glycoprot_M_flavivir.
    IPR013755. Flav_gly_cen_dom_subdom1.
    IPR001122. Flavi_capsidC.
    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.
    IPR027287. Flavovir_Ig-like.
    IPR014412. Gen_Poly_FLV.
    IPR011998. Glycoprot_cen/dimer.
    IPR013754. GlyE_dim.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR014756. Ig_E-set.
    IPR026490. mRNA_cap_0/1_MeTrfase.
    IPR027417. P-loop_NTPase.
    IPR000208. RNA-dir_pol_flavivirus.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF01003. 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.
    PF00271. Helicase_C. 1 hit.
    PF00949. Peptidase_S7. 1 hit.
    [Graphical view]
    PIRSFiPIRSF003817. Gen_Poly_FLV. 1 hit.
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    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.
    PROSITEiPS51527. 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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P06935-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKKPGGPGK NRAVNMLKRG MPRGLSLIGL KRAMLSLIDG KGPIRFVLAL     50
    LAFFRFTAIA PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRST 100
    KQKKRGGTAG FTILLGLIAC AGAVTLSNFQ GKVMMTVNAT DVTDVITIPT 150
    AAGKNLCIVR AMDVGYLCED TITYECPVLA AGNDPEDIDC WCTKSSVYVR 200
    YGRCTKTRHS RRSRRSLTVQ THGESTLANK KGAWLDSTKA TRYLVKTESW 250
    ILRNPGYALV AAVIGWMLGS NTMQRVVFAI LLLLVAPAYS FNCLGMSNRD 300
    FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLADVRSYC 350
    YLASVSDLST RAACPTMGEA HNEKRADPAF VCKQGVVDRG WGNGCGLFGK 400
    GSIDTCAKFA CTTKATGWII QKENIKYEVA IFVHGPTTVE SHGKIGATQA 450
    GRFSITPSAP SYTLKLGEYG EVTVDCEPRS GIDTSAYYVM SVGEKSFLVH 500
    REWFMDLNLP WSSAGSTTWR NRETLMEFEE PHATKQSVVA LGSQEGALHQ 550
    ALAGAIPVEF SSNTVKLTSG HLKCRVKMEK LQLKGTTYGV CSKAFKFART 600
    PADTGHGTVV LELQYTGTDG PCKVPISSVA SLNDLTPVGR LVTVNPFVSV 650
    ATANSKVLIE LEPPFGDSYI VVGRGEQQIN HHWHKSGSSI GKAFTTTLRG 700
    AQRLAALGDT AWDFGSVGGV FTSVGKAIHQ VFGGAFRSLF GGMSWITQGL 750
    LGALLLWMGI NARDRSIAMT FLAVGGVLLF LSVNVHADTG CAIDIGRQEL 800
    RCGSGVFIHN DVEAWMDRYK FYPETPQGLA KIIQKAHAEG VCGLRSVSRL 850
    EHQMWEAIKD ELNTLLKENG VDLSVVVEKQ NGMYKAAPKR LAATTEKLEM 900
    GWKAWGKSII FAPELANNTF VIDGPETEEC PTANRAWNSM EVEDFGFGLT 950
    STRMFLRIRE TNTTECDSKI IGTAVKNNMA VHSDLSYWIE SGLNDTWKLE 1000
    RAVLGEVKSC TWPETHTLWG DGVLESDLII PITLAGPRSN HNRRPGYKTQ 1050
    NQGPWDEGRV EIDFDYCPGT TVTISDSCEH RGPAARTTTE SGKLITDWCC 1100
    RSCTLPPLRF QTENGCWYGM EIRPTRHDEK TLVQSRVNAY NADMIDPFQL 1150
    GLMVVFLATQ EVLRKRWTAK ISIPAIMLAL LVLVFGGITY TDVLRYVILV 1200
    GAAFAEANSG GDVVHLALMA TFKIQPVFLV ASFLKARWTN QESILLMLAA 1250
    AFFQMAYYDA KNVLSWEVPD VLNSLSVAWM ILRAISFTNT SNVVVPLLAL 1300
    LTPGLKCLNL DVYRILLLMV GVGSLIKEKR SSAAKKKGAC LICLALASTG 1350
    VFNPMILAAG LMACDPNRKR GWPATEVMTA VGLMFAIVGG LAELDIDSMA 1400
    IPMTIAGLMF AAFVISGKST DMWIERTADI TWESDAEITG SSERVDVRLD 1450
    DDGNFQLMND PGAPWKIWML RMACLAISAY TPWAILPSVI GFWITLQYTK 1500
    RGGVLWDTPS PKEYKKGDTT TGVYRIMTRG LLGSYQAGAG VMVEGVFHTL 1550
    WHTTKGAALM SGEGRLDPYW GSVKEDRLCY GGPWKLQHKW NGHDEVQMIV 1600
    VEPGKNVKNV QTKPGVFKTP EGEIGAVTLD YPTGTSGSPI VDKNGDVIGL 1650
    YGNGVIMPNG SYISAIVQGE RMEEPAPAGF EPEMLRKKQI TVLDLHPGAG 1700
    KTRKILPQII KEAINKRLRT AVLAPTRVVA AEMSEALRGL PIRYQTSAVH 1750
    REHSGNEIVD VMCHATLTHR LMSPHRVPNY NLFIMDEAHF TDPASIAARG 1800
    YIATKVELGE AAAIFMTATP PGTSDPFPES NAPISDMQTE IPDRAWNTGY 1850
    EWITEYVGKT VWFVPSVKMG NEIALCLQRA GKKVIQLNRK SYETEYPKCK 1900
    NDDWDFVITT DISEMGANFK ASRVIDSRKS VKPTIIEEGD GRVILGEPSA 1950
    ITAASAAQRR GRIGRNPSQV GDEYCYGGHT NEDDSNFAHW TEARIMLDNI 2000
    NMPNGLVAQL YQPEREKVYT MDGEYRLRGE ERKNFLEFLR TADLPVWLAY 2050
    KVAAAGISYH DRKWCFDGPR TNTILEDNNE VEVITKLGER KILRPRWADA 2100
    RVYSDHQALK SFKDFASGKR SQIGLVEVLG RMPEHFMVKT WEALDTMYVV 2150
    ATAEKGGRAH RMALEELPDA LQTIVLIALL SVMSLGVFFL LMQRKGIGKI 2200
    GLGGVILGAA TFFCWMAEVP GTKIAGMLLL SLLLMIVLIP EPEKQRSQTD 2250
    NQLAVFLICV LTLVGAVAAN EMGWLDKTKN DIGSLLGHRP EARETTLGVE 2300
    SFLLDLRPAT AWSLYAVTTA VLTPLLKHLI TSDYINTSLT SINVQASALF 2350
    TLARGFPFVD VGVSALLLAV GCWGQVTLTV TVTAAALLFC HYAYMVPGWQ 2400
    AEAMRSAQRR TAAGIMKNVV VDGIVATDVP ELERTTPVMQ KKVGQIILIL 2450
    VSMAAVVVNP SVRTVREAGI LTTAAAVTLW ENGASSVWNA TTAIGLCHIM 2500
    RGGWLSCLSI MWTLIKNMEK PGLKRGGAKG RTLGEVWKER LNHMTKEEFT 2550
    RYRKEAITEV DRSAAKHARR EGNITGGHPV SRGTAKLRWL VERRFLEPVG 2600
    KVVDLGCGRG GWCYYMATQK RVQEVKGYTK GGPGHEEPQL VQSYGWNIVT 2650
    MKSGVDVFYR PSEASDTLLC DIGESSSSAE VEEHRTVRVL EMVEDWLHRG 2700
    PKEFCIKVLC PYMPKVIEKM ETLQRRYGGG LIRNPLSRNS THEMYWVSHA 2750
    SGNIVHSVNM TSQVLLGRME KKTWKGPQFE EDVNLGSGTR AVGKPLLNSD 2800
    TSKIKNRIER LKKEYSSTWH QDANHPYRTW NYHGSYEVKP TGSASSLVNG 2850
    VVRLLSKPWD TITNVTTMAM TDTTPFGQQR VFKEKVDTKA PEPPEGVKYV 2900
    LNETTNWLWA FLARDKKPRM CSREEFIGKV NSNAALGAMF EEQNQWKNAR 2950
    EAVEDPKFWE MVDEEREAHL RGECNTCIYN MMGKREKKPG EFGKAKGSRA 3000
    IWFMWLGARF LEFEALGFLN EDHWLGRKNS GGGVEGLGLQ KLGYILKEVG 3050
    TKPGGKVYAD DTAGWDTRIT KADLENEAKV LELLDGEHRR LARSIIELTY 3100
    RHKVVKVMRP AADGKTVMDV ISREDQRGSG QVVTYALNTF TNLAVQLVRM 3150
    MEGEGVIGPD DVEKLGKGKG PKVRTWLFEN GEERLSRMAV SGDDCVVKPL 3200
    DDRFATSLHF LNAMSKVRKD IQEWKPSTGW YDWQQVPFCS NHFTELIMKD 3250
    GRTLVVPCRG QDELIGRARI SPGAGWNVRD TACLAKSYAQ MWLLLYFHRR 3300
    DLRLMANAIC SAVPANWVPT GRTTWSIHAK GEWMTTEDML AVWNRVWIEE 3350
    NEWMEDKTPV ERWSDVPYSG KREDIWCGSL IGTRTRATWA ENIHVAINQV 3400
    RSVIGEEKYV DYMSSLRRYE DTIVVEDTVL 3430
    Length:3,430
    Mass (Da):380,110
    Last modified:October 24, 2003 - v2
    Checksum:i42D71B7CB12DC45B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12294 Genomic RNA. Translation: AAA48498.2.
    PIRiA25256. GNWVWV.
    RefSeqiNP_041724.2. NC_001563.2.

    Genome annotation databases

    GeneIDi912267.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12294 Genomic RNA. Translation: AAA48498.2 .
    PIRi A25256. GNWVWV.
    RefSeqi NP_041724.2. NC_001563.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FP7 X-ray 1.68 A 1420-1466 [» ]
    B 1517-1688 [» ]
    2G05 model - D 1675-2120 [» ]
    2G2G model - D 1675-2120 [» ]
    2GGV X-ray 1.80 A 1419-1525 [» ]
    B 1503-1679 [» ]
    2IJO X-ray 2.30 A 1419-1482 [» ]
    B 1502-1685 [» ]
    2P5P X-ray 2.80 A/B/C 585-701 [» ]
    2YOL X-ray 3.20 A 1420-1465 [» ]
    A 1502-1671 [» ]
    3E90 X-ray 2.45 A/C 1420-1463 [» ]
    B/D 1502-1685 [» ]
    3I50 X-ray 3.00 E 291-688 [» ]
    DisProti DP00673.
    ProteinModelPortali P06935.
    SMRi P06935. Positions 25-97, 291-689, 1420-1458, 1502-2120, 2531-2792, 2799-3424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P06935. 3 interactions.

    Chemistry

    BindingDBi P06935.
    ChEMBLi CHEMBL5419.

    Protein family/group databases

    MEROPSi S07.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 912267.

    Miscellaneous databases

    EvolutionaryTracei P06935.
    PROi P06935.

    Family and domain databases

    Gene3Di 2.60.40.350. 1 hit.
    2.60.98.10. 2 hits.
    3.30.387.10. 1 hit.
    3.40.50.150. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR011492. DEAD_Flavivir.
    IPR000069. Env_glycoprot_M_flavivir.
    IPR013755. Flav_gly_cen_dom_subdom1.
    IPR001122. Flavi_capsidC.
    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.
    IPR027287. Flavovir_Ig-like.
    IPR014412. Gen_Poly_FLV.
    IPR011998. Glycoprot_cen/dimer.
    IPR013754. GlyE_dim.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR014756. Ig_E-set.
    IPR026490. mRNA_cap_0/1_MeTrfase.
    IPR027417. P-loop_NTPase.
    IPR000208. RNA-dir_pol_flavivirus.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami 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.
    PF00271. Helicase_C. 1 hit.
    PF00949. Peptidase_S7. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF003817. Gen_Poly_FLV. 1 hit.
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF53335. SSF53335. 1 hit.
    SSF56983. SSF56983. 1 hit.
    SSF81296. SSF81296. 1 hit.
    TIGRFAMsi TIGR04240. flavi_E_stem. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the West Nile flavivirus genome region coding for all nonstructural proteins."
      Castle E., Leidner U., Nowak T., Wengler G., Wengler G.
      Virology 149:10-26(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: SEQUENCE REVISION TO 1908; 2018-2036; 2242 AND 2859-2860.
    3. "Sequence analysis of the viral core protein and the membrane-associated proteins V1 and NV2 of the flavivirus West Nile virus and of the genome sequence for these proteins."
      Castle E., Nowak T., Leidner U., Wengler G., Wengler G.
      Virology 145:227-236(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-291.
    4. "Sequence analysis of the membrane protein V3 of the flavivirus West Nile virus and of its gene."
      Wengler G., Castle E., Leidner U., Nowak T., Wengler G.
      Virology 147:264-274(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 255-854.
    5. "Analysis of disulfides present in the membrane proteins of the West Nile flavivirus."
      Nowak T., Wengler G.
      Virology 156:127-137(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS IN ENVELOPE PROTEIN E.
    6. "Infectious entry of West Nile virus occurs through a clathrin-mediated endocytic pathway."
      Chu J.J., Ng M.L.
      J. Virol. 78:10543-10555(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ENVELOPE PROTEIN E.
    7. "Inhibition of alpha/beta interferon signaling by the NS4B protein of flaviviruses."
      Munoz-Jordan J.L., Laurent-Rolle M., Ashour J., Martinez-Sobrido L., Ashok M., Lipkin W.I., Garcia-Sastre A.
      J. Virol. 79:8004-8013(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF NON-STRUCTURAL PROTEIN 4B.
    8. "Nuclear localization of flavivirus RNA synthesis in infected cells."
      Uchil P.D., Kumar A.V., Satchidanandam V.
      J. Virol. 80:5451-5464(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION OF SERINE PROTEASE NS3, SUBCELLULAR LOCATION OF RNA-DIRECTED RNA POLYMERASE NS5.
      Strain: E101.
    9. "Structure and function of flavivirus NS5 methyltransferase."
      Zhou Y., Ray D., Zhao Y., Dong H., Ren S., Li Z., Guo Y., Bernard K.A., Shi P.-Y., Li H.
      J. Virol. 81:3891-3903(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS METHYLTRANSFERASE, MUTAGENESIS OF LYS-2586; ASP-2671; LYS-2707 AND GLU-2743.
    10. "Cleavage preference distinguishes the two-component NS2B-NS3 serine proteinases of Dengue and West Nile viruses."
      Shiryaev S.A., Kozlov I.A., Ratnikov B.I., Smith J.W., Lebl M., Strongin A.Y.
      Biochem. J. 401:743-752(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    11. "The NS5 protein of the virulent West Nile virus NY99 strain is a potent antagonist of type I interferon-mediated JAK-STAT signaling."
      Laurent-Rolle M., Boer E.F., Lubick K.J., Wolfinbarger J.B., Carmody A.B., Rockx B., Liu W., Ashour J., Shupert W.L., Holbrook M.R., Barrett A.D., Mason P.W., Bloom M.E., Garcia-Sastre A., Khromykh A.A., Best S.M.
      J. Virol. 84:3503-3515(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5.
      Strain: NY1999.
    12. "The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form the RNA cap structure."
      Issur M., Geiss B.J., Bougie I., Picard-Jean F., Despins S., Mayette J., Hobdey S.E., Bisaillon M.
      RNA 15:2340-2350(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5.
      Strain: NY1999.
    13. "Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus."
      Erbel P., Schiering N., D'Arcy A., Renatus M., Kroemer M., Lim S.P., Yin Z., Keller T.H., Vasudevan S.G., Hommel U.
      Nat. Struct. Mol. Biol. 13:372-373(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1420-1688.
    14. "Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold."
      Aleshin A.E., Shiryaev S.A., Strongin A.Y., Liddington R.C.
      Protein Sci. 16:795-806(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1419-1679.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 291-688.

    Entry informationi

    Entry nameiPOLG_WNV
    AccessioniPrimary (citable) accession number: P06935
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: October 24, 2003
    Last modified: October 1, 2014
    This is version 154 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3