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 POLG_DEN1S              Reviewed;        3391 AA.
P33478;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
27-SEP-2017, sequence version 2.
20-DEC-2017, entry version 155.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Capsid protein C;
AltName: Full=Core protein;
Contains:
RecName: Full=Protein 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 {ECO:0000250|UniProtKB:Q9Q6P4};
EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9Q6P4};
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=Peptide 2k;
Contains:
RecName: Full=Non-structural protein 4B;
Short=NS4B;
Contains:
RecName: Full=RNA-directed RNA polymerase NS5;
EC=2.1.1.56 {ECO:0000255|PROSITE-ProRule:PRU00924};
EC=2.1.1.57 {ECO:0000255|PROSITE-ProRule:PRU00924};
EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
AltName: Full=Non-structural protein 5;
Dengue virus type 1 (strain Singapore/S275/1990) (DENV-1).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Dengue virus group.
NCBI_TaxID=33741;
NCBI_TaxID=7159; Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1585663; DOI=10.1016/0042-6822(92)90560-C;
Fu J., Tan B.H., Yap E.H., Chan Y.C., Tan Y.H.;
"Full-length cDNA sequence of dengue type 1 virus (Singapore strain
S275/90).";
Virology 188:953-958(1992).
-!- FUNCTION: Capsid protein C: Plays a role in virus budding by
binding to the cell membrane and gathering the viral RNA into a
nucleocapsid that forms the core of a mature virus particle.
During virus entry, may induce genome penetration into the host
cytoplasm after hemifusion induced by the surface proteins. Can
migrate to the cell nucleus where it modulates host functions.
Overcomes the anti-viral effects of host EXOC1 by sequestering and
degrading the latter through the proteasome degradation pathway.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Capsid protein C: Inhibits RNA silencing by interfering
with host Dicer. {ECO:0000250|UniProtKB:P03314}.
-!- FUNCTION: Peptide pr: Prevents premature fusion activity of
envelope proteins in trans-Golgi by binding to envelope protein E
at pH6.0. After virion release in extracellular space, gets
dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Protein prM: Acts as a chaperone for envelope protein E
during intracellular virion assembly by masking and inactivating
envelope protein E fusion peptide. prM is the only viral peptide
matured by host furin in the trans-Golgi network probably to avoid
catastrophic activation of the viral fusion activity in acidic
Golgi compartment prior to virion release. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Small envelope protein M: May play a role in virus
budding. Exerts cytotoxic effects by activating a mitochondrial
apoptotic pathway through M ectodomain. May display a viroporin
activity. {ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Envelope protein E: Binds to host cell surface receptor
and mediates fusion between viral and cellular membranes. Envelope
protein is synthesized in the endoplasmic reticulum in the form of
heterodimer with protein prM. They play a role in virion budding
in the ER, and the newly formed immature particle is covered with
60 spikes composed of heterodimer between precursor prM and
envelope protein E. The virion is transported to the Golgi
apparatus where the low pH causes dissociation of PrM-E
heterodimers and formation of E homodimers. prM-E cleavage is
inefficient, and many virions are only partially matured. These
uncleaved prM would play a role in immune evasion.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 1: Involved in immune evasion,
pathogenesis and viral replication. Once cleaved off the
polyprotein, is targeted to three destinations: the viral
replication cycle, the plasma membrane and the extracellular
compartment. Essential for viral replication. Required for
formation of the replication complex and recruitment of other non-
structural proteins to the ER-derived membrane structures.
Excreted as a hexameric lipoparticle that plays a role against
host immune response. Antagonizing the complement function. Binds
to the host macrophages and dendritic cells. Inhibits signal
transduction originating from Toll-like receptor 3 (TLR3).
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Non-structural protein 1: Disrupts the host endothelial
glycocalyx layer of host pulmonary microvascular endothelial
cells, inducing degradation of sialic acid and shedding of heparan
sulfate proteoglycans. NS1 induces expression of sialidases,
heparanase, and activates cathepsin L, which activates heparanase
via enzymatic cleavage. These effects are probably linked to the
endothelial hyperpermeability observed in severe dengue disease.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 2A: Component of the viral RNA
replication complex that functions in virion assembly and
antagonizes the host immune response.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the
serine protease function of NS3. May have membrane-destabilizing
activity and form viroporins (By similarity).
{ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00859}.
-!- FUNCTION: Serine protease NS3: Displays three enzymatic
activities: serine protease, NTPase and RNA c. 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.
{ECO:0000255|PROSITE-ProRule:PRU00860}.
-!- FUNCTION: Non-structural protein 4A: Regulates the ATPase activity
of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
energy during unwinding. Plays a role in the inhibition of the
host innate immune response. Interacts with host MAVS and thereby
prevents the interaction between DDX58 and MAVS. In turn, IFN-beta
production is impaired. {ECO:0000250|UniProtKB:P17763,
ECO:0000250|UniProtKB:Q9Q6P4}.
-!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
is required for the interferon antagonism activity of the latter.
{ECO:0000250|UniProtKB:P17763}.
-!- FUNCTION: Non-structural protein 4B: Induces the formation of ER-
derived membrane vesicles where the viral replication takes place.
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|UniProtKB:Q9Q6P4}.
-!- FUNCTION: RNA-directed RNA polymerase NS5: Replicates the viral
(+) and (-) RNA 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 RNA genome replication, also
prevents the establishment of cellular antiviral state by blocking
the interferon-alpha/beta (IFN-alpha/beta) signaling pathway.
Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing
activation of JAK-STAT signaling pathway.
{ECO:0000250|UniProtKB:P17763}.
-!- 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].
{ECO:0000255|PROSITE-ProRule:PRU00924}.
-!- SUBUNIT: Capsid protein C: Homodimer. Interacts (via N-terminus)
with host EXOC1 (via C-terminus); this interaction results in
EXOC1 degradation through the proteasome degradation pathway.
Protein prM: Forms heterodimers with envelope protein E in the
endoplasmic reticulum and Golgi. Envelope protein E: Homodimer; in
the endoplasmic reticulum and Golgi. Interacts with protein prM.
Interacts with non-structural protein 1. Non-structural protein 1:
Homodimer; Homohexamer when secreted. Interacts with envelope
protein E. Non-structural protein 2A: Interacts (via N-terminus)
with serine protease NS3. Non-structural protein 2B: Forms a
heterodimer with serine protease NS3. May form homooligomers.
Serine protease NS3: Forms a heterodimer with NS2B. Interacts with
NS4B. Interacts with unphosphorylated RNA-directed RNA polymerase
NS5; this interaction stimulates RNA-directed RNA polymerase NS5
guanylyltransferase activity. Non-structural protein 4A: Interacts
with host MAVS; this interaction inhibits the synthesis of IFN-
beta. Non-structural protein 4B: Interacts with serine protease
NS3. RNA-directed RNA polymerase NS5: Homodimer. Interacts with
host STAT2; this interaction inhibits the phosphorylation of the
latter, and, when all viral proteins are present (polyprotein),
targets STAT2 for degradation. Interacts with serine protease NS3.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear
region {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Peptide pr: Secreted
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}. Host endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane; Peripheral membrane protein; Lumenal side
{ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived
vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
endoplasmic reticulum membrane; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- 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
serine protease subunit NS2B. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4A: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Host
mitochondrion {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-
associated vesicles hosting the replication complex. Interacts
with host MAVS in the mitochondrion-associated endoplasmic
reticulum membranes. {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in
RE-derived vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:Q9Q6P4}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase NS5: Host
endoplasmic reticulum membrane; Peripheral membrane protein;
Cytoplasmic side. Host nucleus {ECO:0000250|UniProtKB:P17763}.
Note=Located in RE-associated vesicles hosting the replication
complex. NS5 protein is mainly localized in the nucleus rather
than in ER vesicles, especially in the DENV 2, 3, 4 serotypes.
{ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: The transmembrane domains of the small envelope protein M
and envelope protein E contain an endoplasmic reticulum retention
signal. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Cleavages in the lumen of endoplasmic
reticulum are performed by host signal peptidase, whereas
cleavages in the cytoplasmic side are performed by serine protease
NS3. Signal cleavage at the 2K-4B site requires a prior NS3
protease-mediated cleavage at the 4A-2K site.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Protein prM: Cleaved in post-Golgi vesicles by a host furin,
releasing the mature small envelope protein M, and peptide pr.
This cleavage is incomplete as up to 30% of viral particles still
carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: N-glycosylated. The excreted form
is glycosylated and this is required for efficient secretion of
the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: RNA-directed RNA polymerase NS5: Sumoylation of RNA-directed
RNA polymerase NS5 increases NS5 protein stability allowing proper
viral RNA replication. {ECO:0000250|UniProtKB:P29990}.
-!- PTM: RNA-directed RNA polymerase NS5: Phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear
localization. {ECO:0000250|UniProtKB:P17763}.
-!- 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}.
-!- WEB RESOURCE: Name=Virus Pathogen Resource;
URL="http://www.viprbrc.org/brc/home.do?decorator=flavi_dengue";
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EMBL; M87512; -; NOT_ANNOTATED_CDS; Genomic_RNA.
PIR; A42551; A42551.
PDB; 3L6P; X-ray; 2.20 A; A=1393-1439, A=1475-1499.
PDB; 3LKW; X-ray; 2.00 A; A=1393-1439, A=1475-1499.
PDBsum; 3L6P; -.
PDBsum; 3LKW; -.
ProteinModelPortal; P33478; -.
SMR; P33478; -.
MEROPS; S07.001; -.
PRIDE; P33478; -.
OrthoDB; VOG090001ER; -.
PRO; PR:P33478; -.
Proteomes; UP000007194; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
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:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
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:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
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:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 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.
CDD; cd00079; HELICc; 1.
CDD; cd06174; MFS; 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; IPR037172; Flavi_capsidC_sf.
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_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR020846; MFS_dom.
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; SSF101257; SSF101257; 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 cytoplasm; Host endoplasmic reticulum; Host membrane;
Host mitochondrion; 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 MAVS by virus;
Inhibition of host RLR pathway by virus;
Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
Ion channel; Ion transport; 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;
Suppressor of RNA silencing; Transcription; Transcription regulation;
Transferase; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation; Viral attachment to host cell;
Viral envelope protein; Viral immunoevasion; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
CHAIN 1 3391 Genome polyprotein.
/FTId=PRO_0000405206.
CHAIN 1 100 Capsid protein C.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037894.
PROPEP 101 114 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037895.
CHAIN 115 280 Protein prM.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264654.
CHAIN 115 205 Peptide pr.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264655.
CHAIN 206 280 Small envelope protein M.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037896.
CHAIN 281 774 Envelope protein E.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037897.
CHAIN 775 1126 Non-structural protein 1.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037898.
CHAIN 1127 1344 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037899.
CHAIN 1345 1474 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037900.
CHAIN 1475 2093 Serine protease NS3.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037901.
CHAIN 2094 2220 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037902.
PEPTIDE 2221 2243 Peptide 2k.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000264657.
CHAIN 2244 2492 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000037903.
CHAIN 2493 3391 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P29990}.
/FTId=PRO_0000437990.
TOPO_DOM 1 101 Cytoplasmic. {ECO:0000255}.
TRANSMEM 102 119 Helical. {ECO:0000255}.
TOPO_DOM 120 242 Extracellular. {ECO:0000255}.
TRANSMEM 243 260 Helical. {ECO:0000255}.
TOPO_DOM 261 261 Cytoplasmic. {ECO:0000255}.
TRANSMEM 262 280 Helical. {ECO:0000255}.
TOPO_DOM 281 725 Extracellular. {ECO:0000255}.
TRANSMEM 726 746 Helical. {ECO:0000255}.
TOPO_DOM 747 752 Cytoplasmic. {ECO:0000255}.
TRANSMEM 753 773 Helical. {ECO:0000255}.
TOPO_DOM 774 1198 Extracellular. {ECO:0000255}.
TRANSMEM 1199 1219 Helical. {ECO:0000255}.
TOPO_DOM 1220 1225 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1226 1244 Helical. {ECO:0000255}.
TOPO_DOM 1245 1268 Lumenal. {ECO:0000255}.
TRANSMEM 1269 1289 Helical. {ECO:0000255}.
TOPO_DOM 1290 1290 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1291 1309 Helical. {ECO:0000255}.
TOPO_DOM 1310 1314 Lumenal. {ECO:0000255}.
TRANSMEM 1315 1335 Helical. {ECO:0000255}.
TOPO_DOM 1336 1345 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1346 1366 Helical. {ECO:0000255}.
TOPO_DOM 1367 1369 Lumenal. {ECO:0000255}.
TRANSMEM 1370 1390 Helical. {ECO:0000255}.
TOPO_DOM 1391 1446 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1447 1467 Helical. {ECO:0000255}.
TOPO_DOM 1468 2147 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2148 2168 Helical. {ECO:0000255}.
TOPO_DOM 2169 2170 Lumenal. {ECO:0000255}.
INTRAMEM 2171 2191 Helical. {ECO:0000255}.
TOPO_DOM 2192 2192 Lumenal. {ECO:0000255}.
TRANSMEM 2193 2213 Helical. {ECO:0000255}.
TOPO_DOM 2214 2228 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2229 2249 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2250 2275 Lumenal. {ECO:0000255}.
INTRAMEM 2276 2296 Helical. {ECO:0000255}.
TOPO_DOM 2297 2348 Lumenal. {ECO:0000255}.
TRANSMEM 2349 2369 Helical. {ECO:0000255}.
TOPO_DOM 2370 2414 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2415 2435 Helical. {ECO:0000255}.
TOPO_DOM 2436 2460 Lumenal. {ECO:0000255}.
TRANSMEM 2461 2481 Helical. {ECO:0000255}.
TOPO_DOM 2482 3391 Cytoplasmic. {ECO:0000255}.
DOMAIN 1475 1652 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1655 1811 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1821 1988 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2494 2755 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3019 3168 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1668 1675 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 1 15 Interaction with host EXOC1.
{ECO:0000250|UniProtKB:P17763}.
REGION 37 72 Hydrophobic; homodimerization of capsid
protein C.
{ECO:0000250|UniProtKB:P29990}.
REGION 378 391 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1397 1436 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 1659 1662 Important for RNA-binding.
{ECO:0000250|UniProtKB:P14340}.
MOTIF 1759 1762 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 2569 2572 SUMO-interacting motif.
{ECO:0000250|UniProtKB:P29990}.
ACT_SITE 1525 1525 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1549 1549 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1609 1609 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2553 2553 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2638 2638 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2672 2672 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2708 2708 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2929 2929 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2933 2933 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2938 2938 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2941 2941 Zinc 1. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3203 3203 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3219 3219 Zinc 2. {ECO:0000250|UniProtKB:Q6YMS4}.
METAL 3338 3338 Zinc 2. {ECO:0000250|UniProtKB:Q6YMS4}.
BINDING 2506 2506 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2509 2509 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2510 2510 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2512 2512 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2521 2521 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2548 2548 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2578 2578 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2579 2579 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2596 2596 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2597 2597 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2623 2623 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2624 2624 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2642 2642 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2703 2703 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2705 2705 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2710 2710 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 100 101 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 114 115 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 205 206 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P29990,
ECO:0000255}.
SITE 280 281 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 774 775 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 1126 1127 Cleavage; by host.
{ECO:0000250|UniProtKB:P29990}.
SITE 1344 1345 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 1474 1475 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P29990}.
SITE 1932 1932 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1935 1935 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2093 2094 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P29990}.
SITE 2220 2221 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 2243 2244 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P29990}.
SITE 2492 2493 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P29990}.
SITE 2517 2517 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2553 2553 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2638 2638 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2639 2639 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2672 2672 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2708 2708 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2548 2548 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 904 904 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 981 981 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1189 1189 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2302 2302 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2306 2306 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 2458 2458 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 283 310 {ECO:0000250|UniProtKB:P17763}.
DISULFID 340 401 {ECO:0000250|UniProtKB:P17763}.
DISULFID 354 385 {ECO:0000250|UniProtKB:P17763}.
DISULFID 372 396 {ECO:0000250|UniProtKB:P17763}.
DISULFID 465 565 {ECO:0000250|UniProtKB:P17763}.
DISULFID 582 613 {ECO:0000250|UniProtKB:P17763}.
DISULFID 778 789 {ECO:0000250|UniProtKB:P17763}.
DISULFID 829 917 {ECO:0000250|UniProtKB:P17763}.
DISULFID 953 997 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1054 1103 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1065 1087 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1086 1090 {ECO:0000250|UniProtKB:P17763}.
STRAND 1395 1401 {ECO:0000244|PDB:3LKW}.
STRAND 1420 1422 {ECO:0000244|PDB:3LKW}.
STRAND 1428 1430 {ECO:0000244|PDB:3LKW}.
STRAND 1495 1499 {ECO:0000244|PDB:3LKW}.
SEQUENCE 3391 AA; 379086 MW; 6F24E1E8FC56AE5E CRC64;
MNNQRKKTAR PSFNMLKRAR NRVSTGSQLA KRFSKGLLSG QGPMKLVMAF IAFLRFLAIP
PTAGILARWG SFKKNGAIKV LRGFKKEISN MLNIMNRRKR SVTMLLMLLP TALAFHLTTR
GGEPHMIVSK QEREKSLLFK TSVGVNMCTL IAMDLGELCE DTMTYKCPRI TEAEPDDVDC
WCNATDTWVT YGTCSQTGEH RRDKRSVALA PHVGLGLETR TETWMSSEGA WKQIQRVETW
ALRHPGFTVI ALFLAHAIGT SITQKGIIFI LLMLVTPSMA MRCVGIGSRD FVEGLSGATW
VDVVLEHGSC VTTMAKDKPT LDIELLKTEV TNPAVLRKLC IEAKISNTTT DSRCPTQGEA
TLVEEQDANF VCRRTFVDRG WGNGCGLFGK GSLLTCAKFK CVTKLEGKIV QYENLKYSVI
VTVHTGDQHQ VGNETTEHGT IATITPQAPT SEIQLTDYGA LTLDCSPRTG LDFNEMVLLT
MKEKSWLVHK QWFLDLPLPW TSGASTSQET WNRQDLLVTF KTAHAKKQEV VVLGSQEGAM
HTALTGATEI QTSGTTTIFA GHLKCRLKMD KLTLKGMSYV MCTGSFKLEK EVAETQHGTV
LVQVKYEGTD APCKIPFSTQ DEKGVTQNRL ITANPIVTDK EKPVNIETEP PFGESYIVVG
AGEKALKQCW FKKGSSIGKM FEATARGARR MAILGDTAWD FGSIGGVFTS VGKLVHQVFG
TAYGVLFSGV SWTMKIGIGI LLTWLGLNSR STSLSMTCIA VGMVTLYLGV MVQADSGCVI
NWKGRELKCG SGIFVTNEVH TWTEQYKFQA DSPKRLSAAI GKAWEEGVCG IRSATRLENI
MWKQISNELN HILLENDMKF TVVVGDVVGI LAQGKKMIRP QPMEHKYSWK SWGKAKIIGA
DIQNTTFIID GPDTPECPDD QRAWNIWEVE DYGFGIFTTN IWLKLRDSYT QMCDHRLMSA
AIKDSKAVHA DMGYWIESEK NETWKLARAS FIEVKTCVWP KSHTLWSNGV LESEMIIPKI
YGGPISQHNY RPGYFTQTAG PWHLGKLELD FDLCEGTTVV VDEHCGNRGP SLRTTTVTGK
IIHEWCCRSC TLPPLRFKGE DGCWYGMEIR PVKEKEENLV KSMVSAGSGE VDSFSLGLLC
ISIMIEEVMR SRWSRKMLMT GTLAVFLLLI MGQLTWNDLI RLCIMVGANA SDRMGMGTTY
LALMATFKMR PMFAVGLLFR RLTSREVLLL TIGLSLVASV ELPNSLEELG DGLAMGIMIL
KLLTDFQSHQ LWATLLSLTF VKTTFSLHYA WKTMAMVLSI VSLFPLCLST TSQKTTWLPV
LLGSLGCKPL TMFLIAENKI WGRKSWPLNE GIMAVGIVSI LLSSLLKNDV PLAGPLIAGG
MLIACYVISG SSADLSLEKA AEVSWEEEAE HSGASHNILV EVQDDGTMKI KDEERDDTLT
ILLKATLLAV SGVYPLSIPA TLFVWYFWQK KKQRSGVLWD TPSPPEVERA VLDDGIYRIM
QRGLLGRSQV GVGVFQDGVF HTMWHVTRGA VLMYQGKRLE PSWASVKKDL ISYGGGWRFQ
GSWNTGEEVQ VIAVEPGKNP KNVQTAPGTF KTPEGEVGAI ALDFKPGTSG SPIVNREGKI
VGLYGNGVVT TSGTYVSAIA QAKASQEGPL PEIEDEVFRK RNLTIMDLHP GSGKTRRYLP
AIVREAIRRN VRTLILAPTR VVASEMAEAL KGMPIRYQTT AVKSEHTGKE IVDLMCHATF
TMRLLSPVRV PNYNMIIMDE AHFTDPASIA RRGYISTRVG MGEAAAIFMT ATPPGSVEAF
PQSNAVIQDE ERDIPERSWN SGYEWITDFP GKTVWFVPSI KSGNDIANCL RKNGKRVIQL
SRKTFDTEYQ KTKNNDWDYV VTTDISEMGA NFRADRVIDP RRCLKPVILK DGPERVILAG
PMPVTVASAA QRRGRIGRNQ NKEGDQYVYM GQPLNNDEDH AHWTEAKMLL DNINTPEGII
PALFEPEREK SAAIDGEYRL RGEARKTFVE LMRRGDLPVW LSYKVASEGF QYSDRRWCFD
GERNNQVLEE NMDVEMWTKE GERKKLRPRW LDARTYSDPL ALREFKEFAA GRRSVSGDLI
LEIGKLPQHL TQRAQNALDN LVMLHNSEQG GRAYRHAMEE LPDTIETLML LALIAVLTGG
VTLFFLSGKG LGKTSIGLLC VMASSVLLWM ASVEPHWIAA SIILEFFLMV LLIPEPDRQR
TPQDNQLAYV VIGLLFMILT VAANEMGLLE TTKKDLGIGH VAAENHHHAT MLDVDLRPAS
AWTLYAVATT VITPMMRHTI ENTTANISLT AIANQAAILM GLDKGWPISK MDIGVPLLAL
GCYSQVNPLT LTAAVLMLVA HYAIIGPGLQ AKATREAQKR TAAGIMKNPT VDGIVAIDLD
PVVYDAKFEK QLGQIMLLIL CTSQILLMRT TWALCESITL ATGPLTTLWE GSPGKFWNTT
IAVSMANIFR GSYLAGAGLA FSLMKSLGGG RRGTGAKGKH WERNGKDRLN QLSKSEFNTY
KRSGIMEVDR SEAKEGLKRG ETTKHAVSRG TAKLRWFVER NLVKPEGKVI DLGCGRGGWS
YYCAGLKKVT EVKGYTKGGP GHEEPIPMAT YGWNLVKLYS GKDVFFTPPE KCDTLLCDIG
ESSPNPTIEE GRTLRVLKMV EPWLRGNQFC IKILNPYMPS VVETLEQMQR KHGGMLVRNP
LSRNSTHEMY WVSCGTGNIV SAVNMTSRML LNRFTMAHRK PTYERDVDLG AGTRHVAVEP
EVANLDIIGQ RIENIKHEHK STWHYDEDNP YKTWAYHGSY EVKPSGSASS MVNGVVKLLT
KPWDAIPMVT QIAMTDTTPF GQQRVFKEKV DTRTPKAKRG TAQIMEVTAR WLWGFLSRNK
KPRICTREEF TRKVRSNAAI GAVFVDENQW NSAKEAVEDE RFWDLVHRER ELHKQGKCAT
CVYNMMGKRE KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFMNEDHWFS RENSLSGVEG
EGLHKLGYIL RDISKIPGGN MYADDTAGWD TRITEDDLQN EAKITDIMEP EHALLATSIF
KLTYQNKVVR VQRPAKNGTV MDVISRRDQR GSGQVGTYGL NTFTNMEAQL IRQMESEGIF
SPSELETPNL AERVLDWLEK YGVERLKRMA ISGDDCVVKP IDDRFATALT ALNDMGKVRK
DIPQWEPSKG WNDWQQVPFC SHHFHQLIMK DGREIVVPCR NQDELVGRAR VSQGAGWSLR
ETACLGKSYA QMWQLMYFHR RDLRLAANAI CSAVPVDWVP TSRTTWSIHA HHQWMTTEDM
LSVWNRVWIE ENPWMEDKTH VSSWEDVPYL GKREDQWCGS LIGLTARATW ATNIQVAINQ
VRRLIGNENY LDYMTSMKRF KNESDPEGAL W


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