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P06935

- POLG_WNV

UniProt

P06935 - POLG_WNV

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Protein

Genome polyprotein

Gene
N/A
Organism
West Nile virus (WNV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  9. RNA helicase activity Source: InterPro
  10. serine-type endopeptidase activity Source: InterPro
  11. serine-type exopeptidase activity Source: InterPro
  12. 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
Complete GO annotation...

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

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 Source: UniProtKB-KW
  2. host cell membrane Source: UniProtKB-KW
  3. host cell nucleus Source: UniProtKB-KW
  4. integral component of membrane Source: UniProtKB-KW
  5. viral capsid Source: UniProtKB-KW
  6. viral envelope Source: UniProtKB-KW
Complete GO annotation...

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

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        10         20         30         40         50
MSKKPGGPGK NRAVNMLKRG MPRGLSLIGL KRAMLSLIDG KGPIRFVLAL
60 70 80 90 100
LAFFRFTAIA PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRST
110 120 130 140 150
KQKKRGGTAG FTILLGLIAC AGAVTLSNFQ GKVMMTVNAT DVTDVITIPT
160 170 180 190 200
AAGKNLCIVR AMDVGYLCED TITYECPVLA AGNDPEDIDC WCTKSSVYVR
210 220 230 240 250
YGRCTKTRHS RRSRRSLTVQ THGESTLANK KGAWLDSTKA TRYLVKTESW
260 270 280 290 300
ILRNPGYALV AAVIGWMLGS NTMQRVVFAI LLLLVAPAYS FNCLGMSNRD
310 320 330 340 350
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLADVRSYC
360 370 380 390 400
YLASVSDLST RAACPTMGEA HNEKRADPAF VCKQGVVDRG WGNGCGLFGK
410 420 430 440 450
GSIDTCAKFA CTTKATGWII QKENIKYEVA IFVHGPTTVE SHGKIGATQA
460 470 480 490 500
GRFSITPSAP SYTLKLGEYG EVTVDCEPRS GIDTSAYYVM SVGEKSFLVH
510 520 530 540 550
REWFMDLNLP WSSAGSTTWR NRETLMEFEE PHATKQSVVA LGSQEGALHQ
560 570 580 590 600
ALAGAIPVEF SSNTVKLTSG HLKCRVKMEK LQLKGTTYGV CSKAFKFART
610 620 630 640 650
PADTGHGTVV LELQYTGTDG PCKVPISSVA SLNDLTPVGR LVTVNPFVSV
660 670 680 690 700
ATANSKVLIE LEPPFGDSYI VVGRGEQQIN HHWHKSGSSI GKAFTTTLRG
710 720 730 740 750
AQRLAALGDT AWDFGSVGGV FTSVGKAIHQ VFGGAFRSLF GGMSWITQGL
760 770 780 790 800
LGALLLWMGI NARDRSIAMT FLAVGGVLLF LSVNVHADTG CAIDIGRQEL
810 820 830 840 850
RCGSGVFIHN DVEAWMDRYK FYPETPQGLA KIIQKAHAEG VCGLRSVSRL
860 870 880 890 900
EHQMWEAIKD ELNTLLKENG VDLSVVVEKQ NGMYKAAPKR LAATTEKLEM
910 920 930 940 950
GWKAWGKSII FAPELANNTF VIDGPETEEC PTANRAWNSM EVEDFGFGLT
960 970 980 990 1000
STRMFLRIRE TNTTECDSKI IGTAVKNNMA VHSDLSYWIE SGLNDTWKLE
1010 1020 1030 1040 1050
RAVLGEVKSC TWPETHTLWG DGVLESDLII PITLAGPRSN HNRRPGYKTQ
1060 1070 1080 1090 1100
NQGPWDEGRV EIDFDYCPGT TVTISDSCEH RGPAARTTTE SGKLITDWCC
1110 1120 1130 1140 1150
RSCTLPPLRF QTENGCWYGM EIRPTRHDEK TLVQSRVNAY NADMIDPFQL
1160 1170 1180 1190 1200
GLMVVFLATQ EVLRKRWTAK ISIPAIMLAL LVLVFGGITY TDVLRYVILV
1210 1220 1230 1240 1250
GAAFAEANSG GDVVHLALMA TFKIQPVFLV ASFLKARWTN QESILLMLAA
1260 1270 1280 1290 1300
AFFQMAYYDA KNVLSWEVPD VLNSLSVAWM ILRAISFTNT SNVVVPLLAL
1310 1320 1330 1340 1350
LTPGLKCLNL DVYRILLLMV GVGSLIKEKR SSAAKKKGAC LICLALASTG
1360 1370 1380 1390 1400
VFNPMILAAG LMACDPNRKR GWPATEVMTA VGLMFAIVGG LAELDIDSMA
1410 1420 1430 1440 1450
IPMTIAGLMF AAFVISGKST DMWIERTADI TWESDAEITG SSERVDVRLD
1460 1470 1480 1490 1500
DDGNFQLMND PGAPWKIWML RMACLAISAY TPWAILPSVI GFWITLQYTK
1510 1520 1530 1540 1550
RGGVLWDTPS PKEYKKGDTT TGVYRIMTRG LLGSYQAGAG VMVEGVFHTL
1560 1570 1580 1590 1600
WHTTKGAALM SGEGRLDPYW GSVKEDRLCY GGPWKLQHKW NGHDEVQMIV
1610 1620 1630 1640 1650
VEPGKNVKNV QTKPGVFKTP EGEIGAVTLD YPTGTSGSPI VDKNGDVIGL
1660 1670 1680 1690 1700
YGNGVIMPNG SYISAIVQGE RMEEPAPAGF EPEMLRKKQI TVLDLHPGAG
1710 1720 1730 1740 1750
KTRKILPQII KEAINKRLRT AVLAPTRVVA AEMSEALRGL PIRYQTSAVH
1760 1770 1780 1790 1800
REHSGNEIVD VMCHATLTHR LMSPHRVPNY NLFIMDEAHF TDPASIAARG
1810 1820 1830 1840 1850
YIATKVELGE AAAIFMTATP PGTSDPFPES NAPISDMQTE IPDRAWNTGY
1860 1870 1880 1890 1900
EWITEYVGKT VWFVPSVKMG NEIALCLQRA GKKVIQLNRK SYETEYPKCK
1910 1920 1930 1940 1950
NDDWDFVITT DISEMGANFK ASRVIDSRKS VKPTIIEEGD GRVILGEPSA
1960 1970 1980 1990 2000
ITAASAAQRR GRIGRNPSQV GDEYCYGGHT NEDDSNFAHW TEARIMLDNI
2010 2020 2030 2040 2050
NMPNGLVAQL YQPEREKVYT MDGEYRLRGE ERKNFLEFLR TADLPVWLAY
2060 2070 2080 2090 2100
KVAAAGISYH DRKWCFDGPR TNTILEDNNE VEVITKLGER KILRPRWADA
2110 2120 2130 2140 2150
RVYSDHQALK SFKDFASGKR SQIGLVEVLG RMPEHFMVKT WEALDTMYVV
2160 2170 2180 2190 2200
ATAEKGGRAH RMALEELPDA LQTIVLIALL SVMSLGVFFL LMQRKGIGKI
2210 2220 2230 2240 2250
GLGGVILGAA TFFCWMAEVP GTKIAGMLLL SLLLMIVLIP EPEKQRSQTD
2260 2270 2280 2290 2300
NQLAVFLICV LTLVGAVAAN EMGWLDKTKN DIGSLLGHRP EARETTLGVE
2310 2320 2330 2340 2350
SFLLDLRPAT AWSLYAVTTA VLTPLLKHLI TSDYINTSLT SINVQASALF
2360 2370 2380 2390 2400
TLARGFPFVD VGVSALLLAV GCWGQVTLTV TVTAAALLFC HYAYMVPGWQ
2410 2420 2430 2440 2450
AEAMRSAQRR TAAGIMKNVV VDGIVATDVP ELERTTPVMQ KKVGQIILIL
2460 2470 2480 2490 2500
VSMAAVVVNP SVRTVREAGI LTTAAAVTLW ENGASSVWNA TTAIGLCHIM
2510 2520 2530 2540 2550
RGGWLSCLSI MWTLIKNMEK PGLKRGGAKG RTLGEVWKER LNHMTKEEFT
2560 2570 2580 2590 2600
RYRKEAITEV DRSAAKHARR EGNITGGHPV SRGTAKLRWL VERRFLEPVG
2610 2620 2630 2640 2650
KVVDLGCGRG GWCYYMATQK RVQEVKGYTK GGPGHEEPQL VQSYGWNIVT
2660 2670 2680 2690 2700
MKSGVDVFYR PSEASDTLLC DIGESSSSAE VEEHRTVRVL EMVEDWLHRG
2710 2720 2730 2740 2750
PKEFCIKVLC PYMPKVIEKM ETLQRRYGGG LIRNPLSRNS THEMYWVSHA
2760 2770 2780 2790 2800
SGNIVHSVNM TSQVLLGRME KKTWKGPQFE EDVNLGSGTR AVGKPLLNSD
2810 2820 2830 2840 2850
TSKIKNRIER LKKEYSSTWH QDANHPYRTW NYHGSYEVKP TGSASSLVNG
2860 2870 2880 2890 2900
VVRLLSKPWD TITNVTTMAM TDTTPFGQQR VFKEKVDTKA PEPPEGVKYV
2910 2920 2930 2940 2950
LNETTNWLWA FLARDKKPRM CSREEFIGKV NSNAALGAMF EEQNQWKNAR
2960 2970 2980 2990 3000
EAVEDPKFWE MVDEEREAHL RGECNTCIYN MMGKREKKPG EFGKAKGSRA
3010 3020 3030 3040 3050
IWFMWLGARF LEFEALGFLN EDHWLGRKNS GGGVEGLGLQ KLGYILKEVG
3060 3070 3080 3090 3100
TKPGGKVYAD DTAGWDTRIT KADLENEAKV LELLDGEHRR LARSIIELTY
3110 3120 3130 3140 3150
RHKVVKVMRP AADGKTVMDV ISREDQRGSG QVVTYALNTF TNLAVQLVRM
3160 3170 3180 3190 3200
MEGEGVIGPD DVEKLGKGKG PKVRTWLFEN GEERLSRMAV SGDDCVVKPL
3210 3220 3230 3240 3250
DDRFATSLHF LNAMSKVRKD IQEWKPSTGW YDWQQVPFCS NHFTELIMKD
3260 3270 3280 3290 3300
GRTLVVPCRG QDELIGRARI SPGAGWNVRD TACLAKSYAQ MWLLLYFHRR
3310 3320 3330 3340 3350
DLRLMANAIC SAVPANWVPT GRTTWSIHAK GEWMTTEDML AVWNRVWIEE
3360 3370 3380 3390 3400
NEWMEDKTPV ERWSDVPYSG KREDIWCGSL IGTRTRATWA ENIHVAINQV
3410 3420 3430
RSVIGEEKYV DYMSSLRRYE DTIVVEDTVL
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.

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 29, 2014
This is version 155 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