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P06935 (POLG_WNV) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 13 chains:

  1. Peptide 2k
  2. Capsid protein C
    Alternative name(s):
    Core protein
  3. prM
  4. Peptide pr
  5. Small envelope protein M
    Alternative name(s):
    Matrix protein
  6. Envelope protein E
  7. Non-structural protein 1
    Short name=NS1
  8. Non-structural protein 2A
    Short name=NS2A
  9. Serine protease subunit NS2B
    Alternative name(s):
    Flavivirin protease NS2B regulatory subunit
    Non-structural protein 2B
  10. Serine protease NS3
    EC=3.4.21.91
    EC=3.6.1.15
    EC=3.6.4.13
    Alternative name(s):
    Flavivirin protease NS3 catalytic subunit
    Non-structural protein 3
  11. Non-structural protein 4A
    Short name=NS4A
  12. Non-structural protein 4B
    Short name=NS4B
  13. RNA-directed RNA polymerase NS5
    EC=2.1.1.56
    EC=2.1.1.57
    EC=2.7.7.48
    Alternative name(s):
    NS5
OrganismWest Nile virus (WNV) [Complete proteome]
Taxonomic identifier11082 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusJapanese encephalitis virus group
Virus hostAedes [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]

Protein attributes

Sequence length3430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA By similarity. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

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. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

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. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

Non-structural protein 1 is involved in virus replication and regulation of the innate immune response By similarity. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

Non-structural protein 2A may be involved viral RNA replication and capsid assembly Potential. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

Non-structural protein 2B is a required cofactor for the serine protease function of NS3 By similarity. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

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. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

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. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter By similarity. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

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. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

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. Ref.6 Ref.7 Ref.9 Ref.11 Ref.12

Catalytic activity

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).

NTP + H2O = NDP + phosphate.

ATP + H2O = ADP + phosphate.

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.

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).

Subunit structure

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.

Subcellular location

Capsid protein C: Virion Potential. Host membrane; Single-pass membrane protein Potential Ref.8.

Small envelope protein M: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.8.

Envelope protein E: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.8.

Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity Ref.8.

Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential Ref.8.

Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential Ref.8.

Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Remains non-covalently associated to NS3 protease By similarity. Ref.8

Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Located in RE-associated vesicles hosting the replication complex. Ref.8

Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.8.

RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Host nucleus. Note: Located in RE-associated vesicles hosting the replication complex. Ref.8

Post-translational modification

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. Ref.10

RNA-directed RNA polymerase NS5 is phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization By similarity.

Sequence similarities

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

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 mRNA cap 0-1 NS5-type MT domain.

Contains 1 peptidase S7 domain.

Contains 1 RdRp catalytic domain.

Ontologies

Keywords
   Biological processActivation of host autophagy by virus
Clathrin-mediated endocytosis of virus by host
Fusion of virus membrane with host endosomal membrane
Fusion of virus membrane with host membrane
Host-virus interaction
Inhibition of host innate immune response by virus
Inhibition of host interferon signaling pathway by virus
Inhibition of host 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
   Cellular componentCapsid protein
Host endoplasmic reticulum
Host membrane
Host nucleus
Membrane
Secreted
Viral envelope protein
Virion
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
S-adenosyl-L-methionine
   Molecular functionHelicase
Hydrolase
Methyltransferase
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Serine protease
Transferase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processclathrin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host endosome membrane

Inferred from electronic annotation. Source: UniProtKB-KW

induction by virus of host autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of viral genome replication

Inferred from mutant phenotype PubMed 22553322. Source: CACAO

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host JAK1 activity

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host TYK2 activity

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host apoptotic process

Inferred from direct assay PubMed 23115297. Source: CACAO

suppression by virus of host type I interferon-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

double-stranded RNA binding

Inferred from electronic annotation. Source: InterPro

mRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

mRNA (nucleoside-2'-O-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidase activity

Inferred from direct assay PubMed 23291011. Source: CACAO

protein binding

Inferred from physical interaction PubMed 16275649PubMed 20797779. Source: IntAct

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type exopeptidase activity

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTLMA15Q17NZ65EBI-2912469,EBI-2912457From a different organism.
ITGB3P051064EBI-981051,EBI-702847From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host Potential
Chain2 – 105104Capsid protein C
PRO_0000037743
Propeptide106 – 12318ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity
PRO_0000037744
Chain124 – 290167prM
PRO_0000405150
Chain124 – 21592Peptide pr
PRO_0000405151
Chain216 – 29075Small envelope protein M
PRO_0000037745
Chain291 – 787497Envelope protein E
PRO_0000037746
Chain788 – 1139352Non-structural protein 1
PRO_0000037747
Chain1140 – 1370231Non-structural protein 2A
PRO_0000037748
Chain1371 – 1501131Serine protease subunit NS2B
PRO_0000037749
Chain1502 – 2120619Serine protease NS3
PRO_0000037750
Chain2121 – 2246126Non-structural protein 4A
PRO_0000037751
Peptide2247 – 226923Peptide 2k By similarity
PRO_0000405152
Chain2270 – 2525256Non-structural protein 4B
PRO_0000037752
Chain2526 – 3430905RNA-directed RNA polymerase NS5
PRO_0000037753

Regions

Topological domain2 – 105104Cytoplasmic Potential
Transmembrane106 – 12621Helical; Potential
Topological domain127 – 248122Extracellular Potential
Transmembrane249 – 26921Helical; Potential
Topological domain270 – 2756Cytoplasmic Potential
Transmembrane276 – 29217Helical; Potential
Topological domain293 – 739447Extracellular Potential
Intramembrane740 – 76021Helical; Potential
Topological domain761 – 7666Extracellular Potential
Intramembrane767 – 78721Helical; Potential
Topological domain788 – 1138351Extracellular Potential
Transmembrane1139 – 115921Helical; Potential
Topological domain1160 – 121253Cytoplasmic Potential
Transmembrane1213 – 123321Helical; Potential
Topological domain1234 – 124310Lumenal Potential
Transmembrane1244 – 126421Helical; Potential
Topological domain1265 – 129228Cytoplasmic Potential
Transmembrane1293 – 131321Helical; Potential
Topological domain1314 – 134027Lumenal Potential
Transmembrane1341 – 136121Helical; Potential
Topological domain1362 – 137110Cytoplasmic Potential
Transmembrane1372 – 139221Helical; Potential
Topological domain1393 – 13953Lumenal Potential
Transmembrane1396 – 141621Helical; Potential
Topological domain1417 – 147357Cytoplasmic Potential
Intramembrane1474 – 149421Helical; Potential
Topological domain1495 – 2170676Cytoplasmic Potential
Transmembrane2171 – 219121Helical; Potential
Topological domain2192 – 21965Lumenal Potential
Intramembrane2197 – 221721Helical; Potential
Topological domain22181Lumenal Potential
Transmembrane2219 – 223921Helical; Potential
Topological domain2240 – 225415Cytoplasmic Potential
Transmembrane2255 – 227521Helical; Note=Signal for NS4B; Potential
Topological domain2276 – 230934Lumenal Potential
Intramembrane2310 – 233021Helical; Potential
Topological domain2331 – 235525Lumenal Potential
Intramembrane2356 – 237621Helical; Potential
Topological domain23771Lumenal Potential
Transmembrane2378 – 239821Helical; Potential
Topological domain2399 – 244143Cytoplasmic Potential
Transmembrane2442 – 246221Helical; Potential
Topological domain2463 – 24675Lumenal Potential
Transmembrane2468 – 248821Helical; Potential
Topological domain2489 – 3430942Cytoplasmic Potential
Domain1502 – 1679178Peptidase S7
Domain1682 – 1838157Helicase ATP-binding
Domain1849 – 2014166Helicase C-terminal
Domain2526 – 2791266mRNA cap 0-1 NS5-type MT
Domain3055 – 3207153RdRp catalytic
Nucleotide binding1695 – 17028ATP Potential
Region33 – 7442Hydrophobic; homodimerization of capsid protein C By similarity
Region388 – 40114Involved in fusion
Region1424 – 146340Interacts with and activates NS3 protease By similarity
Motif1786 – 17894DEAH box
Compositional bias281 – 2844Poly-Leu
Compositional bias2675 – 26784Poly-Ser

Sites

Active site15521Charge relay system; for serine protease NS3 activity By similarity
Active site15761Charge relay system; for serine protease NS3 activity By similarity
Active site16361Charge relay system; for serine protease NS3 activity By similarity
Binding site25381mRNA cap By similarity
Binding site25411mRNA cap; via carbonyl oxygen By similarity
Binding site25421mRNA cap By similarity
Binding site25441mRNA cap; via carbonyl oxygen By similarity
Binding site25531mRNA cap By similarity
Binding site25811S-adenosyl-L-methionine By similarity
Binding site26111S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site26121S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site26291S-adenosyl-L-methionine By similarity
Binding site26301S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site26561S-adenosyl-L-methionine By similarity
Binding site26571S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site26751mRNA cap By similarity
Binding site27381mRNA cap By similarity
Binding site27401mRNA cap By similarity
Binding site27451S-adenosyl-L-methionine By similarity
Site105 – 1062Cleavage; by viral protease NS3
Site123 – 1242Cleavage; by host signal peptidase By similarity
Site215 – 2162Cleavage; by host furin Potential
Site290 – 2912Cleavage; by host signal peptidase Potential
Site787 – 7882Cleavage; by host signal peptidase Potential
Site1139 – 11402Cleavage; by host Potential
Site1370 – 13712Cleavage; by viral protease NS3
Site1501 – 15022Cleavage; by autolysis
Site2120 – 21212Cleavage; by autolysis
Site2246 – 22472Cleavage; by viral protease NS3
Site2269 – 22702Cleavage; by host signal peptidase Potential
Site2525 – 25262Cleavage; by viral protease NS3
Site25491mRNA cap binding By similarity
Site25861Essential for 2'-O-methyltransferase activity
Site26711Essential for 2'-O-methyltransferase and N-7 methyltransferase activity
Site26721S-adenosyl-L-methionine binding By similarity
Site27071Essential for 2'-O-methyltransferase activity
Site27431Essential for 2'-O-methyltransferase activity

Amino acid modifications

Glycosylation1381N-linked (GlcNAc...); by host Potential
Glycosylation9171N-linked (GlcNAc...); by host Potential
Glycosylation9621N-linked (GlcNAc...); by host Potential
Glycosylation9941N-linked (GlcNAc...); by host Potential
Glycosylation23361N-linked (GlcNAc...); by host Potential
Disulfide bond293 ↔ 320 Ref.5
Disulfide bond350 ↔ 406 Ref.5
Disulfide bond364 ↔ 395 Ref.5
Disulfide bond382 ↔ 411 Ref.5
Disulfide bond476 ↔ 574 Ref.5
Disulfide bond591 ↔ 622 Ref.5

Experimental info

Mutagenesis25861K → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. Ref.9
Mutagenesis26711D → A: Lethal for the virus. Complete loss of 2'-O and N-7 methyltransferase activies. Ref.9
Mutagenesis27071K → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. Ref.9
Mutagenesis27431E → A: Complete loss of 2'-O-methyltransferase activity. No effect on N-7 methyltransferase activity. Ref.9

Secondary structure

.................................................................... 3430
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06935 [UniParc].

Last modified October 24, 2003. Version 2.
Checksum: 42D71B7CB12DC45B

FASTA3,430380,110
        10         20         30         40         50         60 
MSKKPGGPGK NRAVNMLKRG MPRGLSLIGL KRAMLSLIDG KGPIRFVLAL LAFFRFTAIA 

        70         80         90        100        110        120 
PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRST KQKKRGGTAG FTILLGLIAC 

       130        140        150        160        170        180 
AGAVTLSNFQ GKVMMTVNAT DVTDVITIPT AAGKNLCIVR AMDVGYLCED TITYECPVLA 

       190        200        210        220        230        240 
AGNDPEDIDC WCTKSSVYVR YGRCTKTRHS RRSRRSLTVQ THGESTLANK KGAWLDSTKA 

       250        260        270        280        290        300 
TRYLVKTESW ILRNPGYALV AAVIGWMLGS NTMQRVVFAI LLLLVAPAYS FNCLGMSNRD 

       310        320        330        340        350        360 
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLADVRSYC YLASVSDLST 

       370        380        390        400        410        420 
RAACPTMGEA HNEKRADPAF VCKQGVVDRG WGNGCGLFGK GSIDTCAKFA CTTKATGWII 

       430        440        450        460        470        480 
QKENIKYEVA IFVHGPTTVE SHGKIGATQA GRFSITPSAP SYTLKLGEYG EVTVDCEPRS 

       490        500        510        520        530        540 
GIDTSAYYVM SVGEKSFLVH REWFMDLNLP WSSAGSTTWR NRETLMEFEE PHATKQSVVA 

       550        560        570        580        590        600 
LGSQEGALHQ ALAGAIPVEF SSNTVKLTSG HLKCRVKMEK LQLKGTTYGV CSKAFKFART 

       610        620        630        640        650        660 
PADTGHGTVV LELQYTGTDG PCKVPISSVA SLNDLTPVGR LVTVNPFVSV ATANSKVLIE 

       670        680        690        700        710        720 
LEPPFGDSYI VVGRGEQQIN HHWHKSGSSI GKAFTTTLRG AQRLAALGDT AWDFGSVGGV 

       730        740        750        760        770        780 
FTSVGKAIHQ VFGGAFRSLF GGMSWITQGL LGALLLWMGI NARDRSIAMT FLAVGGVLLF 

       790        800        810        820        830        840 
LSVNVHADTG CAIDIGRQEL RCGSGVFIHN DVEAWMDRYK FYPETPQGLA KIIQKAHAEG 

       850        860        870        880        890        900 
VCGLRSVSRL EHQMWEAIKD ELNTLLKENG VDLSVVVEKQ NGMYKAAPKR LAATTEKLEM 

       910        920        930        940        950        960 
GWKAWGKSII FAPELANNTF VIDGPETEEC PTANRAWNSM EVEDFGFGLT STRMFLRIRE 

       970        980        990       1000       1010       1020 
TNTTECDSKI IGTAVKNNMA VHSDLSYWIE SGLNDTWKLE RAVLGEVKSC TWPETHTLWG 

      1030       1040       1050       1060       1070       1080 
DGVLESDLII PITLAGPRSN HNRRPGYKTQ NQGPWDEGRV EIDFDYCPGT TVTISDSCEH 

      1090       1100       1110       1120       1130       1140 
RGPAARTTTE SGKLITDWCC RSCTLPPLRF QTENGCWYGM EIRPTRHDEK TLVQSRVNAY 

      1150       1160       1170       1180       1190       1200 
NADMIDPFQL GLMVVFLATQ EVLRKRWTAK ISIPAIMLAL LVLVFGGITY TDVLRYVILV 

      1210       1220       1230       1240       1250       1260 
GAAFAEANSG GDVVHLALMA TFKIQPVFLV ASFLKARWTN QESILLMLAA AFFQMAYYDA 

      1270       1280       1290       1300       1310       1320 
KNVLSWEVPD VLNSLSVAWM ILRAISFTNT SNVVVPLLAL LTPGLKCLNL DVYRILLLMV 

      1330       1340       1350       1360       1370       1380 
GVGSLIKEKR SSAAKKKGAC LICLALASTG VFNPMILAAG LMACDPNRKR GWPATEVMTA 

      1390       1400       1410       1420       1430       1440 
VGLMFAIVGG LAELDIDSMA IPMTIAGLMF AAFVISGKST DMWIERTADI TWESDAEITG 

      1450       1460       1470       1480       1490       1500 
SSERVDVRLD DDGNFQLMND PGAPWKIWML RMACLAISAY TPWAILPSVI GFWITLQYTK 

      1510       1520       1530       1540       1550       1560 
RGGVLWDTPS PKEYKKGDTT TGVYRIMTRG LLGSYQAGAG VMVEGVFHTL WHTTKGAALM 

      1570       1580       1590       1600       1610       1620 
SGEGRLDPYW GSVKEDRLCY GGPWKLQHKW NGHDEVQMIV VEPGKNVKNV QTKPGVFKTP 

      1630       1640       1650       1660       1670       1680 
EGEIGAVTLD YPTGTSGSPI VDKNGDVIGL YGNGVIMPNG SYISAIVQGE RMEEPAPAGF 

      1690       1700       1710       1720       1730       1740 
EPEMLRKKQI TVLDLHPGAG KTRKILPQII KEAINKRLRT AVLAPTRVVA AEMSEALRGL 

      1750       1760       1770       1780       1790       1800 
PIRYQTSAVH REHSGNEIVD VMCHATLTHR LMSPHRVPNY NLFIMDEAHF TDPASIAARG 

      1810       1820       1830       1840       1850       1860 
YIATKVELGE AAAIFMTATP PGTSDPFPES NAPISDMQTE IPDRAWNTGY EWITEYVGKT 

      1870       1880       1890       1900       1910       1920 
VWFVPSVKMG NEIALCLQRA GKKVIQLNRK SYETEYPKCK NDDWDFVITT DISEMGANFK 

      1930       1940       1950       1960       1970       1980 
ASRVIDSRKS VKPTIIEEGD GRVILGEPSA ITAASAAQRR GRIGRNPSQV GDEYCYGGHT 

      1990       2000       2010       2020       2030       2040 
NEDDSNFAHW TEARIMLDNI NMPNGLVAQL YQPEREKVYT MDGEYRLRGE ERKNFLEFLR 

      2050       2060       2070       2080       2090       2100 
TADLPVWLAY KVAAAGISYH DRKWCFDGPR TNTILEDNNE VEVITKLGER KILRPRWADA 

      2110       2120       2130       2140       2150       2160 
RVYSDHQALK SFKDFASGKR SQIGLVEVLG RMPEHFMVKT WEALDTMYVV ATAEKGGRAH 

      2170       2180       2190       2200       2210       2220 
RMALEELPDA LQTIVLIALL SVMSLGVFFL LMQRKGIGKI GLGGVILGAA TFFCWMAEVP 

      2230       2240       2250       2260       2270       2280 
GTKIAGMLLL SLLLMIVLIP EPEKQRSQTD NQLAVFLICV LTLVGAVAAN EMGWLDKTKN 

      2290       2300       2310       2320       2330       2340 
DIGSLLGHRP EARETTLGVE SFLLDLRPAT AWSLYAVTTA VLTPLLKHLI TSDYINTSLT 

      2350       2360       2370       2380       2390       2400 
SINVQASALF TLARGFPFVD VGVSALLLAV GCWGQVTLTV TVTAAALLFC HYAYMVPGWQ 

      2410       2420       2430       2440       2450       2460 
AEAMRSAQRR TAAGIMKNVV VDGIVATDVP ELERTTPVMQ KKVGQIILIL VSMAAVVVNP 

      2470       2480       2490       2500       2510       2520 
SVRTVREAGI LTTAAAVTLW ENGASSVWNA TTAIGLCHIM RGGWLSCLSI MWTLIKNMEK 

      2530       2540       2550       2560       2570       2580 
PGLKRGGAKG RTLGEVWKER LNHMTKEEFT RYRKEAITEV DRSAAKHARR EGNITGGHPV 

      2590       2600       2610       2620       2630       2640 
SRGTAKLRWL VERRFLEPVG KVVDLGCGRG GWCYYMATQK RVQEVKGYTK GGPGHEEPQL 

      2650       2660       2670       2680       2690       2700 
VQSYGWNIVT MKSGVDVFYR PSEASDTLLC DIGESSSSAE VEEHRTVRVL EMVEDWLHRG 

      2710       2720       2730       2740       2750       2760 
PKEFCIKVLC PYMPKVIEKM ETLQRRYGGG LIRNPLSRNS THEMYWVSHA SGNIVHSVNM 

      2770       2780       2790       2800       2810       2820 
TSQVLLGRME KKTWKGPQFE EDVNLGSGTR AVGKPLLNSD TSKIKNRIER LKKEYSSTWH 

      2830       2840       2850       2860       2870       2880 
QDANHPYRTW NYHGSYEVKP TGSASSLVNG VVRLLSKPWD TITNVTTMAM TDTTPFGQQR 

      2890       2900       2910       2920       2930       2940 
VFKEKVDTKA PEPPEGVKYV LNETTNWLWA FLARDKKPRM CSREEFIGKV NSNAALGAMF 

      2950       2960       2970       2980       2990       3000 
EEQNQWKNAR EAVEDPKFWE MVDEEREAHL RGECNTCIYN MMGKREKKPG EFGKAKGSRA 

      3010       3020       3030       3040       3050       3060 
IWFMWLGARF LEFEALGFLN EDHWLGRKNS GGGVEGLGLQ KLGYILKEVG TKPGGKVYAD 

      3070       3080       3090       3100       3110       3120 
DTAGWDTRIT KADLENEAKV LELLDGEHRR LARSIIELTY RHKVVKVMRP AADGKTVMDV 

      3130       3140       3150       3160       3170       3180 
ISREDQRGSG QVVTYALNTF TNLAVQLVRM MEGEGVIGPD DVEKLGKGKG PKVRTWLFEN 

      3190       3200       3210       3220       3230       3240 
GEERLSRMAV SGDDCVVKPL DDRFATSLHF LNAMSKVRKD IQEWKPSTGW YDWQQVPFCS 

      3250       3260       3270       3280       3290       3300 
NHFTELIMKD GRTLVVPCRG QDELIGRARI SPGAGWNVRD TACLAKSYAQ MWLLLYFHRR 

      3310       3320       3330       3340       3350       3360 
DLRLMANAIC SAVPANWVPT GRTTWSIHAK GEWMTTEDML AVWNRVWIEE NEWMEDKTPV 

      3370       3380       3390       3400       3410       3420 
ERWSDVPYSG KREDIWCGSL IGTRTRATWA ENIHVAINQV RSVIGEEKYV DYMSSLRRYE 

      3430 
DTIVVEDTVL 

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References

[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]"An infectious clone of the West Nile flavivirus."
Yamshchikov V.F., Wengler G., Perelygin A.A., Brinton M.A., Compans R.W.
Virology 281:294-304(2001) [PubMed] [Europe PMC] [Abstract]
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]"Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody."
Cherrier M.V., Kaufmann B., Nybakken G.E., Lok S.M., Warren J.T., Chen B.R., Nelson C.A., Kostyuchenko V.A., Holdaway H.A., Chipman P.R., Kuhn R.J., Diamond M.S., Rossmann M.G., Fremont D.H.
EMBO J. 28:3269-3276(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 291-688.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12294 Genomic RNA. Translation: AAA48498.2.
PIRGNWVWV. A25256.
RefSeqNP_041724.2. NC_001563.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00673.
ProteinModelPortalP06935.
SMRP06935. Positions 25-97, 291-689, 1420-1458, 1502-2120, 2531-2792, 2799-3424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP06935. 3 interactions.

Chemistry

BindingDBP06935.
ChEMBLCHEMBL5419.

Protein family/group databases

MEROPSS07.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID912267.

Family and domain databases

Gene3D2.60.40.350. 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.
InterProIPR011492. 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]
PfamPF01003. 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]
PIRSFPIRSF003817. Gen_Poly_FLV. 1 hit.
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsTIGR04240. flavi_E_stem. 1 hit.
PROSITEPS51527. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP06935.
PROP06935.

Entry information

Entry namePOLG_WNV
AccessionPrimary (citable) accession number: P06935
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 24, 2003
Last modified: July 9, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references