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 POLG_WNV                Reviewed;        3430 AA.
P06935;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
24-OCT-2003, sequence version 2.
10-MAY-2017, entry version 172.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Peptide 2k;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=prM;
Contains:
RecName: Full=Peptide pr;
Contains:
RecName: Full=Small envelope protein M;
AltName: Full=Matrix protein;
Contains:
RecName: Full=Envelope protein E;
Contains:
RecName: Full=Non-structural protein 1;
Short=NS1;
Contains:
RecName: Full=Non-structural protein 2A;
Short=NS2A;
Contains:
RecName: Full=Serine protease subunit NS2B;
AltName: Full=Flavivirin protease NS2B regulatory subunit;
AltName: Full=Non-structural protein 2B;
Contains:
RecName: Full=Serine protease NS3;
EC=3.4.21.91;
EC=3.6.1.15;
EC=3.6.4.13;
AltName: Full=Flavivirin protease NS3 catalytic subunit;
AltName: Full=Non-structural protein 3;
Contains:
RecName: Full=Non-structural protein 4A;
Short=NS4A;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=RNA-directed RNA polymerase NS5;
EC=2.1.1.56;
EC=2.1.1.57;
EC=2.7.7.48;
AltName: Full=NS5;
West Nile virus (WNV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Japanese encephalitis virus group.
NCBI_TaxID=11082;
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=34610; Amblyomma variegatum (Tropical bont tick).
NCBI_TaxID=8782; Aves.
NCBI_TaxID=53527; Culex.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=34627; Hyalomma marginatum.
NCBI_TaxID=308735; Mansonia uniformis.
NCBI_TaxID=308737; Mimomyia.
NCBI_TaxID=34630; Rhipicephalus.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3753811; DOI=10.1016/0042-6822(86)90082-6;
Castle E., Leidner U., Nowak T., Wengler G., Wengler G.;
"Primary structure of the West Nile flavivirus genome region coding
for all nonstructural proteins.";
Virology 149:10-26(1986).
[2]
SEQUENCE REVISION TO 1908; 2018-2036; 2242 AND 2859-2860.
PubMed=11277701; DOI=10.1006/viro.2000.0795;
Yamshchikov V.F., Wengler G., Perelygin A.A., Brinton M.A.,
Compans R.W.;
"An infectious clone of the West Nile flavivirus.";
Virology 281:294-304(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-291.
PubMed=2992152; DOI=10.1016/0042-6822(85)90156-4;
Castle E., Nowak T., Leidner U., Wengler G., Wengler G.;
"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.";
Virology 145:227-236(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 255-854.
PubMed=3855247; DOI=10.1016/0042-6822(85)90129-1;
Wengler G., Castle E., Leidner U., Nowak T., Wengler G.;
"Sequence analysis of the membrane protein V3 of the flavivirus West
Nile virus and of its gene.";
Virology 147:264-274(1985).
[5]
DISULFIDE BONDS IN ENVELOPE PROTEIN E.
PubMed=3811228; DOI=10.1016/0042-6822(87)90443-0;
Nowak T., Wengler G.;
"Analysis of disulfides present in the membrane proteins of the West
Nile flavivirus.";
Virology 156:127-137(1987).
[6]
FUNCTION OF ENVELOPE PROTEIN E.
PubMed=15367621; DOI=10.1128/JVI.78.19.10543-10555.2004;
Chu J.J., Ng M.L.;
"Infectious entry of West Nile virus occurs through a clathrin-
mediated endocytic pathway.";
J. Virol. 78:10543-10555(2004).
[7]
FUNCTION OF NON-STRUCTURAL PROTEIN 4B.
PubMed=15956546; DOI=10.1128/JVI.79.13.8004-8013.2005;
Munoz-Jordan J.L., Laurent-Rolle M., Ashour J., Martinez-Sobrido L.,
Ashok M., Lipkin W.I., Garcia-Sastre A.;
"Inhibition of alpha/beta interferon signaling by the NS4B protein of
flaviviruses.";
J. Virol. 79:8004-8013(2005).
[8]
SUBCELLULAR LOCATION OF SERINE PROTEASE NS3, AND SUBCELLULAR LOCATION
OF RNA-DIRECTED RNA POLYMERASE NS5.
STRAIN=E101;
PubMed=16699025; DOI=10.1128/JVI.01982-05;
Uchil P.D., Kumar A.V., Satchidanandam V.;
"Nuclear localization of flavivirus RNA synthesis in infected cells.";
J. Virol. 80:5451-5464(2006).
[9]
FUNCTION AS METHYLTRANSFERASE, AND MUTAGENESIS OF LYS-2586; ASP-2671;
LYS-2707 AND GLU-2743.
PubMed=17267492; DOI=10.1128/JVI.02704-06;
Zhou Y., Ray D., Zhao Y., Dong H., Ren S., Li Z., Guo Y.,
Bernard K.A., Shi P.-Y., Li H.;
"Structure and function of flavivirus NS5 methyltransferase.";
J. Virol. 81:3891-3903(2007).
[10]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=17067286; DOI=10.1042/BJ20061136;
Shiryaev S.A., Kozlov I.A., Ratnikov B.I., Smith J.W., Lebl M.,
Strongin A.Y.;
"Cleavage preference distinguishes the two-component NS2B-NS3 serine
proteinases of Dengue and West Nile viruses.";
Biochem. J. 401:743-752(2007).
[11]
FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5.
STRAIN=NY1999;
PubMed=20106931; DOI=10.1128/JVI.01161-09;
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.;
"The NS5 protein of the virulent West Nile virus NY99 strain is a
potent antagonist of type I interferon-mediated JAK-STAT signaling.";
J. Virol. 84:3503-3515(2010).
[12]
FUNCTION OF RNA-DIRECTED RNA POLYMERASE NS5.
STRAIN=NY1999;
PubMed=19850911; DOI=10.1261/rna.1609709;
Issur M., Geiss B.J., Bougie I., Picard-Jean F., Despins S.,
Mayette J., Hobdey S.E., Bisaillon M.;
"The flavivirus NS5 protein is a true RNA guanylyltransferase that
catalyzes a two-step reaction to form the RNA cap structure.";
RNA 15:2340-2350(2009).
[13]
X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1420-1688.
PubMed=16532006; DOI=10.1038/nsmb1073;
Erbel P., Schiering N., D'Arcy A., Renatus M., Kroemer M., Lim S.P.,
Yin Z., Keller T.H., Vasudevan S.G., Hommel U.;
"Structural basis for the activation of flaviviral NS3 proteases from
dengue and West Nile virus.";
Nat. Struct. Mol. Biol. 13:372-373(2006).
[14]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1419-1679.
PubMed=17400917; DOI=10.1110/ps.072753207;
Aleshin A.E., Shiryaev S.A., Strongin A.Y., Liddington R.C.;
"Structural evidence for regulation and specificity of flaviviral
proteases and evolution of the Flaviviridae fold.";
Protein Sci. 16:795-806(2007).
[15]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 291-688.
PubMed=19713934; DOI=10.1038/emboj.2009.245;
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.;
"Structural basis for the preferential recognition of immature
flaviviruses by a fusion-loop antibody.";
EMBO J. 28:3269-3276(2009).
-!- FUNCTION: Capsid protein C self-assembles to form an icosahedral
capsid about 30 nm in diameter. The capsid encapsulates the
genomic RNA. {ECO:0000250}.
-!- FUNCTION: 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. {ECO:0000250}.
-!- FUNCTION: 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.
{ECO:0000250}.
-!- FUNCTION: Non-structural protein 1 is involved in virus
replication and regulation of the innate immune response.
{ECO:0000250}.
-!- FUNCTION: Non-structural protein 2A may be involved viral RNA
replication and capsid assembly. {ECO:0000305}.
-!- FUNCTION: Non-structural protein 2B is a required cofactor for the
serine protease function of NS3. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
-!- FUNCTION: 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).
{ECO:0000255|PROSITE-ProRule:PRU00860}.
-!- FUNCTION: 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. {ECO:0000250}.
-!- FUNCTION: Peptide 2k functions as a signal peptide for NS4B and is
required for the interferon antagonism activity of the latter.
{ECO:0000250}.
-!- FUNCTION: 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. {ECO:0000250}.
-!- FUNCTION: 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).
{ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- 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.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
-!- CATALYTIC ACTIVITY: 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: 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. {ECO:0000250}.
-!- INTERACTION:
Q17NZ6:CTLMA15 (xeno); NbExp=5; IntAct=EBI-2912469, EBI-2912457;
P05106:ITGB3 (xeno); NbExp=4; IntAct=EBI-981051, EBI-702847;
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion {ECO:0000305}. Host
membrane {ECO:0000305}; Single-pass membrane protein
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted. Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Peripheral membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00860}; Lumenal side
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860};
Peripheral membrane protein {ECO:0000255|PROSITE-
ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-
ProRule:PRU00860}. Note=Remains non-covalently associated to NS3
protease. {ECO:0000255|PROSITE-ProRule:PRU00860}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
pass membrane protein {ECO:0000250}. Note=Located in RE-associated
vesicles hosting the replication complex.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
pass membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Peripheral membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
{ECO:0000255|PROSITE-ProRule:PRU00860}. Host nucleus
{ECO:0000269|PubMed:16699025}. Note=Located in RE-associated
vesicles hosting the replication complex.
-!- PTM: 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. {ECO:0000250}.
-!- PTM: RNA-directed RNA polymerase NS5 is phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear
localization. {ECO:0000250}.
-!- SIMILARITY: In the N-terminal section; belongs to the class I-like
SAM-binding methyltransferase superfamily. mRNA cap 0-1 NS5-type
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00924}.
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EMBL; M12294; AAA48498.2; -; Genomic_RNA.
PIR; A25256; GNWVWV.
RefSeq; NP_041724.2; NC_001563.2.
PDB; 2FP7; X-ray; 1.68 A; A=1420-1466, B=1517-1688.
PDB; 2G05; Model; -; D=1675-2120.
PDB; 2G2G; Model; -; D=1675-2120.
PDB; 2GGV; X-ray; 1.80 A; A=1419-1525, B=1503-1679.
PDB; 2IJO; X-ray; 2.30 A; A=1419-1482, B=1502-1685.
PDB; 2P5P; X-ray; 2.80 A; A/B/C=585-701.
PDB; 2YOL; X-ray; 3.20 A; A=1420-1465, A=1502-1671.
PDB; 3E90; X-ray; 2.45 A; A/C=1420-1463, B/D=1502-1685.
PDB; 3I50; X-ray; 3.00 A; E=291-688.
PDB; 5IDK; X-ray; 1.50 A; A/B/C=1420-1465.
PDBsum; 2FP7; -.
PDBsum; 2G05; -.
PDBsum; 2G2G; -.
PDBsum; 2GGV; -.
PDBsum; 2IJO; -.
PDBsum; 2P5P; -.
PDBsum; 2YOL; -.
PDBsum; 3E90; -.
PDBsum; 3I50; -.
PDBsum; 5IDK; -.
DisProt; DP00673; -.
ProteinModelPortal; P06935; -.
SMR; P06935; -.
IntAct; P06935; 4.
BindingDB; P06935; -.
ChEMBL; CHEMBL5419; -.
MEROPS; S07.003; -.
GeneID; 912267; -.
KEGG; vg:912267; -.
OrthoDB; VOG09000016; -.
BRENDA; 2.7.7.48; 6687.
BRENDA; 3.4.21.91; 6687.
EvolutionaryTrace; P06935; -.
PRO; PR:P06935; -.
Proteomes; UP000008600; Genome.
GO; GO:0039714; C:cytoplasmic viral factory; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
GO; GO:1990904; C:ribonucleoprotein complex; IMP:CAFA.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IMP:CAFA.
GO; GO:1990814; F:DNA/DNA annealing activity; IMP:CAFA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0008233; F:peptidase activity; IDA:CACAO.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IMP:CAFA.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0033592; F:RNA strand annealing activity; IMP:CAFA.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:CACAO.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0043489; P:RNA stabilization; IMP:CAFA.
GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:CACAO.
GO; GO:0039576; P:suppression by virus of host JAK1 activity; IEA:UniProtKB-KW.
GO; GO:0039574; P:suppression by virus of host TYK2 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Capsid protein; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein; Helicase;
Host endoplasmic reticulum; Host membrane; Host nucleus;
Host-virus interaction; Hydrolase;
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;
Membrane; Metal-binding; Methyltransferase; mRNA capping;
mRNA processing; Multifunctional enzyme; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
RNA-directed RNA polymerase; S-adenosyl-L-methionine; Secreted;
Serine protease; Transcription; Transcription regulation; Transferase;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral immunoevasion;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell.
INIT_MET 1 1 Removed; by host. {ECO:0000255}.
CHAIN 2 105 Capsid protein C.
/FTId=PRO_0000037743.
PROPEP 106 123 ER anchor for the protein C, removed in
mature form by serine protease NS3.
{ECO:0000250}.
/FTId=PRO_0000037744.
CHAIN 124 290 prM.
/FTId=PRO_0000405150.
CHAIN 124 215 Peptide pr.
/FTId=PRO_0000405151.
CHAIN 216 290 Small envelope protein M.
/FTId=PRO_0000037745.
CHAIN 291 787 Envelope protein E.
/FTId=PRO_0000037746.
CHAIN 788 1139 Non-structural protein 1.
/FTId=PRO_0000037747.
CHAIN 1140 1370 Non-structural protein 2A.
/FTId=PRO_0000037748.
CHAIN 1371 1501 Serine protease subunit NS2B.
/FTId=PRO_0000037749.
CHAIN 1502 2120 Serine protease NS3.
/FTId=PRO_0000037750.
CHAIN 2121 2246 Non-structural protein 4A.
/FTId=PRO_0000037751.
PEPTIDE 2247 2269 Peptide 2k. {ECO:0000250}.
/FTId=PRO_0000405152.
CHAIN 2270 2525 Non-structural protein 4B.
/FTId=PRO_0000037752.
CHAIN 2526 3430 RNA-directed RNA polymerase NS5.
/FTId=PRO_0000037753.
TOPO_DOM 2 105 Cytoplasmic. {ECO:0000255}.
TRANSMEM 106 126 Helical. {ECO:0000255}.
TOPO_DOM 127 248 Extracellular. {ECO:0000255}.
TRANSMEM 249 269 Helical. {ECO:0000255}.
TOPO_DOM 270 275 Cytoplasmic. {ECO:0000255}.
TRANSMEM 276 292 Helical. {ECO:0000255}.
TOPO_DOM 293 739 Extracellular. {ECO:0000255}.
INTRAMEM 740 760 Helical. {ECO:0000255}.
TOPO_DOM 761 766 Extracellular. {ECO:0000255}.
INTRAMEM 767 787 Helical. {ECO:0000255}.
TOPO_DOM 788 1138 Extracellular. {ECO:0000255}.
TRANSMEM 1139 1159 Helical. {ECO:0000255}.
TOPO_DOM 1160 1212 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1213 1233 Helical. {ECO:0000255}.
TOPO_DOM 1234 1243 Lumenal. {ECO:0000255}.
TRANSMEM 1244 1264 Helical. {ECO:0000255}.
TOPO_DOM 1265 1292 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1293 1313 Helical. {ECO:0000255}.
TOPO_DOM 1314 1340 Lumenal. {ECO:0000255}.
TRANSMEM 1341 1361 Helical. {ECO:0000255}.
TOPO_DOM 1362 1371 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1372 1392 Helical. {ECO:0000255}.
TOPO_DOM 1393 1395 Lumenal. {ECO:0000255}.
TRANSMEM 1396 1416 Helical. {ECO:0000255}.
TOPO_DOM 1417 1473 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1474 1494 Helical. {ECO:0000255}.
TOPO_DOM 1495 2170 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2171 2191 Helical. {ECO:0000255}.
TOPO_DOM 2192 2196 Lumenal. {ECO:0000255}.
INTRAMEM 2197 2217 Helical. {ECO:0000255}.
TOPO_DOM 2218 2218 Lumenal. {ECO:0000255}.
TRANSMEM 2219 2239 Helical. {ECO:0000255}.
TOPO_DOM 2240 2254 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2255 2275 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2276 2309 Lumenal. {ECO:0000255}.
INTRAMEM 2310 2330 Helical. {ECO:0000255}.
TOPO_DOM 2331 2355 Lumenal. {ECO:0000255}.
INTRAMEM 2356 2376 Helical. {ECO:0000255}.
TOPO_DOM 2377 2377 Lumenal. {ECO:0000255}.
TRANSMEM 2378 2398 Helical. {ECO:0000255}.
TOPO_DOM 2399 2441 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2442 2462 Helical. {ECO:0000255}.
TOPO_DOM 2463 2467 Lumenal. {ECO:0000255}.
TRANSMEM 2468 2488 Helical. {ECO:0000255}.
TOPO_DOM 2489 3430 Cytoplasmic. {ECO:0000255}.
DOMAIN 1502 1679 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1682 1838 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1849 2014 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2526 2791 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3055 3207 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1695 1702 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 33 74 Hydrophobic; homodimerization of capsid
protein C. {ECO:0000250}.
REGION 388 401 Involved in fusion.
REGION 1424 1463 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
MOTIF 1786 1789 DEAH box.
COMPBIAS 281 284 Poly-Leu.
COMPBIAS 2675 2678 Poly-Ser.
ACT_SITE 1552 1552 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1576 1576 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1636 1636 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
BINDING 2538 2538 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2541 2541 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2542 2542 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2544 2544 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2553 2553 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2581 2581 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2611 2611 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2612 2612 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2629 2629 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2630 2630 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2656 2656 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2657 2657 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2675 2675 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2738 2738 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2740 2740 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2745 2745 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 105 106 Cleavage; by viral protease NS3.
SITE 123 124 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 215 216 Cleavage; by host furin. {ECO:0000255}.
SITE 290 291 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 787 788 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 1139 1140 Cleavage; by host. {ECO:0000255}.
SITE 1370 1371 Cleavage; by viral protease NS3.
SITE 1501 1502 Cleavage; by autolysis.
SITE 2120 2121 Cleavage; by autolysis.
SITE 2246 2247 Cleavage; by viral protease NS3.
SITE 2269 2270 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 2525 2526 Cleavage; by viral protease NS3.
SITE 2549 2549 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2586 2586 Essential for 2'-O-methyltransferase
activity.
SITE 2671 2671 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
SITE 2672 2672 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2707 2707 Essential for 2'-O-methyltransferase
activity.
SITE 2743 2743 Essential for 2'-O-methyltransferase
activity.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 917 917 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 962 962 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 994 994 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2336 2336 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 293 320 {ECO:0000269|PubMed:3811228}.
DISULFID 350 406 {ECO:0000269|PubMed:3811228}.
DISULFID 364 395 {ECO:0000269|PubMed:3811228}.
DISULFID 382 411 {ECO:0000269|PubMed:3811228}.
DISULFID 476 574 {ECO:0000269|PubMed:3811228}.
DISULFID 591 622 {ECO:0000269|PubMed:3811228}.
MUTAGEN 2586 2586 K->A: Complete loss of 2'-O-
methyltransferase activity. No effect on
N-7 methyltransferase activity.
{ECO:0000269|PubMed:17267492}.
MUTAGEN 2671 2671 D->A: Lethal for the virus. Complete loss
of 2'-O and N-7 methyltransferase
activies. {ECO:0000269|PubMed:17267492}.
MUTAGEN 2707 2707 K->A: Complete loss of 2'-O-
methyltransferase activity. No effect on
N-7 methyltransferase activity.
{ECO:0000269|PubMed:17267492}.
MUTAGEN 2743 2743 E->A: Complete loss of 2'-O-
methyltransferase activity. No effect on
N-7 methyltransferase activity.
{ECO:0000269|PubMed:17267492}.
STRAND 595 603 {ECO:0000244|PDB:2P5P}.
STRAND 605 607 {ECO:0000244|PDB:2P5P}.
STRAND 609 615 {ECO:0000244|PDB:2P5P}.
STRAND 621 623 {ECO:0000244|PDB:2P5P}.
STRAND 626 631 {ECO:0000244|PDB:2P5P}.
STRAND 634 637 {ECO:0000244|PDB:2P5P}.
STRAND 639 643 {ECO:0000244|PDB:2P5P}.
STRAND 657 662 {ECO:0000244|PDB:2P5P}.
STRAND 665 673 {ECO:0000244|PDB:2P5P}.
STRAND 679 685 {ECO:0000244|PDB:2P5P}.
STRAND 1422 1428 {ECO:0000244|PDB:5IDK}.
HELIX 1434 1439 {ECO:0000244|PDB:2GGV}.
STRAND 1440 1443 {ECO:0000244|PDB:2GGV}.
STRAND 1444 1449 {ECO:0000244|PDB:5IDK}.
STRAND 1451 1453 {ECO:0000244|PDB:2YOL}.
STRAND 1455 1457 {ECO:0000244|PDB:5IDK}.
STRAND 1503 1505 {ECO:0000244|PDB:5IDK}.
STRAND 1521 1532 {ECO:0000244|PDB:5IDK}.
STRAND 1534 1543 {ECO:0000244|PDB:5IDK}.
STRAND 1546 1549 {ECO:0000244|PDB:5IDK}.
HELIX 1551 1554 {ECO:0000244|PDB:5IDK}.
STRAND 1559 1561 {ECO:0000244|PDB:5IDK}.
STRAND 1564 1566 {ECO:0000244|PDB:5IDK}.
STRAND 1568 1572 {ECO:0000244|PDB:5IDK}.
TURN 1573 1576 {ECO:0000244|PDB:5IDK}.
STRAND 1577 1583 {ECO:0000244|PDB:5IDK}.
STRAND 1592 1594 {ECO:0000244|PDB:5IDK}.
STRAND 1596 1600 {ECO:0000244|PDB:5IDK}.
STRAND 1608 1612 {ECO:0000244|PDB:5IDK}.
STRAND 1615 1618 {ECO:0000244|PDB:5IDK}.
STRAND 1623 1627 {ECO:0000244|PDB:5IDK}.
HELIX 1633 1635 {ECO:0000244|PDB:2FP7}.
STRAND 1639 1641 {ECO:0000244|PDB:5IDK}.
STRAND 1647 1650 {ECO:0000244|PDB:5IDK}.
STRAND 1654 1656 {ECO:0000244|PDB:5IDK}.
STRAND 1662 1665 {ECO:0000244|PDB:5IDK}.
STRAND 1672 1674 {ECO:0000244|PDB:2IJO}.
SEQUENCE 3430 AA; 380110 MW; 42D71B7CB12DC45B CRC64;
MSKKPGGPGK NRAVNMLKRG MPRGLSLIGL KRAMLSLIDG KGPIRFVLAL LAFFRFTAIA
PTRAVLDRWR GVNKQTAMKH LLSFKKELGT LTSAINRRST KQKKRGGTAG FTILLGLIAC
AGAVTLSNFQ GKVMMTVNAT DVTDVITIPT AAGKNLCIVR AMDVGYLCED TITYECPVLA
AGNDPEDIDC WCTKSSVYVR YGRCTKTRHS RRSRRSLTVQ THGESTLANK KGAWLDSTKA
TRYLVKTESW ILRNPGYALV AAVIGWMLGS NTMQRVVFAI LLLLVAPAYS FNCLGMSNRD
FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLADVRSYC YLASVSDLST
RAACPTMGEA HNEKRADPAF VCKQGVVDRG WGNGCGLFGK GSIDTCAKFA CTTKATGWII
QKENIKYEVA IFVHGPTTVE SHGKIGATQA GRFSITPSAP SYTLKLGEYG EVTVDCEPRS
GIDTSAYYVM SVGEKSFLVH REWFMDLNLP WSSAGSTTWR NRETLMEFEE PHATKQSVVA
LGSQEGALHQ ALAGAIPVEF SSNTVKLTSG HLKCRVKMEK LQLKGTTYGV CSKAFKFART
PADTGHGTVV LELQYTGTDG PCKVPISSVA SLNDLTPVGR LVTVNPFVSV ATANSKVLIE
LEPPFGDSYI VVGRGEQQIN HHWHKSGSSI GKAFTTTLRG AQRLAALGDT AWDFGSVGGV
FTSVGKAIHQ VFGGAFRSLF GGMSWITQGL LGALLLWMGI NARDRSIAMT FLAVGGVLLF
LSVNVHADTG CAIDIGRQEL RCGSGVFIHN DVEAWMDRYK FYPETPQGLA KIIQKAHAEG
VCGLRSVSRL EHQMWEAIKD ELNTLLKENG VDLSVVVEKQ NGMYKAAPKR LAATTEKLEM
GWKAWGKSII FAPELANNTF VIDGPETEEC PTANRAWNSM EVEDFGFGLT STRMFLRIRE
TNTTECDSKI IGTAVKNNMA VHSDLSYWIE SGLNDTWKLE RAVLGEVKSC TWPETHTLWG
DGVLESDLII PITLAGPRSN HNRRPGYKTQ NQGPWDEGRV EIDFDYCPGT TVTISDSCEH
RGPAARTTTE SGKLITDWCC RSCTLPPLRF QTENGCWYGM EIRPTRHDEK TLVQSRVNAY
NADMIDPFQL GLMVVFLATQ EVLRKRWTAK ISIPAIMLAL LVLVFGGITY TDVLRYVILV
GAAFAEANSG GDVVHLALMA TFKIQPVFLV ASFLKARWTN QESILLMLAA AFFQMAYYDA
KNVLSWEVPD VLNSLSVAWM ILRAISFTNT SNVVVPLLAL LTPGLKCLNL DVYRILLLMV
GVGSLIKEKR SSAAKKKGAC LICLALASTG VFNPMILAAG LMACDPNRKR GWPATEVMTA
VGLMFAIVGG LAELDIDSMA IPMTIAGLMF AAFVISGKST DMWIERTADI TWESDAEITG
SSERVDVRLD DDGNFQLMND PGAPWKIWML RMACLAISAY TPWAILPSVI GFWITLQYTK
RGGVLWDTPS PKEYKKGDTT TGVYRIMTRG LLGSYQAGAG VMVEGVFHTL WHTTKGAALM
SGEGRLDPYW GSVKEDRLCY GGPWKLQHKW NGHDEVQMIV VEPGKNVKNV QTKPGVFKTP
EGEIGAVTLD YPTGTSGSPI VDKNGDVIGL YGNGVIMPNG SYISAIVQGE RMEEPAPAGF
EPEMLRKKQI TVLDLHPGAG KTRKILPQII KEAINKRLRT AVLAPTRVVA AEMSEALRGL
PIRYQTSAVH REHSGNEIVD VMCHATLTHR LMSPHRVPNY NLFIMDEAHF TDPASIAARG
YIATKVELGE AAAIFMTATP PGTSDPFPES NAPISDMQTE IPDRAWNTGY EWITEYVGKT
VWFVPSVKMG NEIALCLQRA GKKVIQLNRK SYETEYPKCK NDDWDFVITT DISEMGANFK
ASRVIDSRKS VKPTIIEEGD GRVILGEPSA ITAASAAQRR GRIGRNPSQV GDEYCYGGHT
NEDDSNFAHW TEARIMLDNI NMPNGLVAQL YQPEREKVYT MDGEYRLRGE ERKNFLEFLR
TADLPVWLAY KVAAAGISYH DRKWCFDGPR TNTILEDNNE VEVITKLGER KILRPRWADA
RVYSDHQALK SFKDFASGKR SQIGLVEVLG RMPEHFMVKT WEALDTMYVV ATAEKGGRAH
RMALEELPDA LQTIVLIALL SVMSLGVFFL LMQRKGIGKI GLGGVILGAA TFFCWMAEVP
GTKIAGMLLL SLLLMIVLIP EPEKQRSQTD NQLAVFLICV LTLVGAVAAN EMGWLDKTKN
DIGSLLGHRP EARETTLGVE SFLLDLRPAT AWSLYAVTTA VLTPLLKHLI TSDYINTSLT
SINVQASALF TLARGFPFVD VGVSALLLAV GCWGQVTLTV TVTAAALLFC HYAYMVPGWQ
AEAMRSAQRR TAAGIMKNVV VDGIVATDVP ELERTTPVMQ KKVGQIILIL VSMAAVVVNP
SVRTVREAGI LTTAAAVTLW ENGASSVWNA TTAIGLCHIM RGGWLSCLSI MWTLIKNMEK
PGLKRGGAKG RTLGEVWKER LNHMTKEEFT RYRKEAITEV DRSAAKHARR EGNITGGHPV
SRGTAKLRWL VERRFLEPVG KVVDLGCGRG GWCYYMATQK RVQEVKGYTK GGPGHEEPQL
VQSYGWNIVT MKSGVDVFYR PSEASDTLLC DIGESSSSAE VEEHRTVRVL EMVEDWLHRG
PKEFCIKVLC PYMPKVIEKM ETLQRRYGGG LIRNPLSRNS THEMYWVSHA SGNIVHSVNM
TSQVLLGRME KKTWKGPQFE EDVNLGSGTR AVGKPLLNSD TSKIKNRIER LKKEYSSTWH
QDANHPYRTW NYHGSYEVKP TGSASSLVNG VVRLLSKPWD TITNVTTMAM TDTTPFGQQR
VFKEKVDTKA PEPPEGVKYV LNETTNWLWA FLARDKKPRM CSREEFIGKV NSNAALGAMF
EEQNQWKNAR EAVEDPKFWE MVDEEREAHL RGECNTCIYN MMGKREKKPG EFGKAKGSRA
IWFMWLGARF LEFEALGFLN EDHWLGRKNS GGGVEGLGLQ KLGYILKEVG TKPGGKVYAD
DTAGWDTRIT KADLENEAKV LELLDGEHRR LARSIIELTY RHKVVKVMRP AADGKTVMDV
ISREDQRGSG QVVTYALNTF TNLAVQLVRM MEGEGVIGPD DVEKLGKGKG PKVRTWLFEN
GEERLSRMAV SGDDCVVKPL DDRFATSLHF LNAMSKVRKD IQEWKPSTGW YDWQQVPFCS
NHFTELIMKD GRTLVVPCRG QDELIGRARI SPGAGWNVRD TACLAKSYAQ MWLLLYFHRR
DLRLMANAIC SAVPANWVPT GRTTWSIHAK GEWMTTEDML AVWNRVWIEE NEWMEDKTPV
ERWSDVPYSG KREDIWCGSL IGTRTRATWA ENIHVAINQV RSVIGEEKYV DYMSSLRRYE
DTIVVEDTVL


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