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 POLG_DEN28              Reviewed;        3391 AA.
P14337; Q20II6;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
10-MAY-2017, entry version 141.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=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=Non-structural protein 2A-alpha;
Short=NS2A-alpha;
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=Peptide 2k;
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=Non-structural protein 5;
Dengue virus type 2 (isolate Thailand/0168/1979) (DENV-2).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; Dengue virus group.
NCBI_TaxID=413041;
NCBI_TaxID=53540; Aedimorphus.
NCBI_TaxID=53539; Diceromyia.
NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=53541; Stegomyia.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 281-775.
STRAIN=Isolate Malaysia M1;
PubMed=2587234; DOI=10.1093/nar/17.21.8875;
Samuel S., Koh C.L., Blok J., Pang T., Lam S.K.;
"Nucleotide sequence of the envelope protein gene of a Malaysian
dengue-2 virus isolated from a patient with dengue haemorrhagic
fever.";
Nucleic Acids Res. 17:8875-8875(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16528037; DOI=10.1099/vir.0.81486-0;
Zhang C., Mammen M.P. Jr., Chinnawirotpisan P., Klungthong C.,
Rodpradit P., Nisalak A., Vaughn D.W., Nimmannitya S.,
Kalayanarooj S., Holmes E.C.;
"Structure and age of genetic diversity of dengue virus type 2 in
Thailand.";
J. Gen. Virol. 87:873-883(2006).
[3]
X-RAY CRYSTALLOGRAPHY (9.5 ANGSTROMS) OF 281-775, TOPOLOGY (ENVELOPE
PROTEIN E), AND TOPOLOGY (SMALL ENVELOPE PROTEIN M).
PubMed=14528291; DOI=10.1038/nsb990;
Zhang W., Chipman P.R., Corver J., Johnson P.R., Zhang Y.,
Mukhopadhyay S., Baker T.S., Strauss J.H., Rossmann M.G., Kuhn R.J.;
"Visualization of membrane protein domains by cryo-electron microscopy
of dengue virus.";
Nat. Struct. Biol. 10:907-912(2003).
[4]
X-RAY CRYSTALLOGRAPHY (12.5 ANGSTROMS) OF 115-195.
PubMed=18369147; DOI=10.1126/science.1153263;
Li L., Lok S.M., Yu I.M., Zhang Y., Kuhn R.J., Chen J., Rossmann M.G.;
"The flavivirus precursor membrane-envelope protein complex: structure
and maturation.";
Science 319:1830-1834(2008).
-!- FUNCTION: Protein C: Plays a role in virus budding by binding to
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 in host cytoplasm after hemifusion
induced by surface proteins. Can migrate tot cell nucleus where it
modulates host functions. {ECO:0000250|UniProtKB:P17763}.
-!- 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. Presumably to
avoid catastrophic activation of the viral fusion activity in
acidic GolGi compartment prior to virion release. prM-E cleavage
is ineficient, 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 extodomain. 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 particule 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
ineficient, 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. May play a role in viral genome replication. Assist
membrane bending and envelopment of genomic RNA at the endoplasmic
reticulum. Excreted as a hexameric lipoparticle that plays a role
against host immune responce. {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: Non-structural protein 2B: Required cofactor for the
serine protease function of NS3 (By similarity). 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 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.
{ECO:0000255|PROSITE-ProRule:PRU00860}.
-!- FUNCTION: Non-structural protein 4A: Induces host endoplasmic
regulate the ATPase activity of the NS3 helicase.
{ECO:0000250|UniProtKB:P17763}.
-!- 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: 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:P17763}.
-!- 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 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].
-!- SUBUNIT: Protein C: Homodimerizes. Protein prM: Forms homodimers
with envelope protein E in the endoplasmic reticulum and Golgi.
Envelope protein E: Forms homodimers with envelope protein E in
the endoplasmic reticulum and Golgi. Non-structural protein 1:
Forms homodimers as well as homohexamers. NS1 may interact with
NS4A. Non-structural protein 2B: Forms a heterodimer with Non-
structural protein 3. May form homooligomers. Non-structural
protein 3: Forms a heterodimer with Non-structural protein 2B.
Interacts with Non-structural protein 4B. Interacts with
unphosphorylated Non-structural protein 5; this interaction
stimulates Non-structural protein 5 guanylyltransferase activity.
Non-structural protein 4B: Interacts with non-structural protein
3. Non-structural protein 5: interacts with host STAT2; this
interaction inhibits the phosphorylation of the latter, and, when
all viral proteins are present (polyprotein), targets STAT2 for
degradation. {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{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:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 1: Secreted
{ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum
membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral
membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Lumenal
side {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A-alpha: Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 2A: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Serine protease subunit NS2B: Host
endoplasmic reticulum membrane {ECO:0000255|PROSITE-
ProRule:PRU00860}; Peripheral membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side
{ECO:0000250|UniProtKB:P17763, ECO:0000255|PROSITE-
ProRule:PRU00860}.
-!- 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|UniProtKB:P17763}. Note=Located
in RE-associated vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4B: Host endoplasmic
reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P17763}.
-!- 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:0000250|UniProtKB:P17763}. Note=Located in RE-associated
vesicles hosting the replication complex.
{ECO:0000250|UniProtKB:P17763}.
-!- DOMAIN: Transmembrane domains of the small envelope protein M and
envelope protein E contains an endoplasmic reticulum retention
signals. {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, wereas cleavages
in the cytoplasmic side are performed by the 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: Non-structural protein 2A-alpha: A C-terminally truncated
form of non-structural protein 2A, results from partial cleavage
by NS3. {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: Non-structural protein 1: 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: Phosphorylated on serines
residues. This phosphorylation may trigger NS5 nuclear
localization. {ECO:0000250|UniProtKB:P17763}.
-!- PTM: Envelope protein E: N-glycosylated.
{ECO:0000250|UniProtKB:P17763}.
-!- PTM: Non-structural protein 1: N-glycosylated.
{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; X15434; CAA33475.1; -; Genomic_RNA.
EMBL; DQ181805; ABA61184.1; -; Genomic_RNA.
PIR; S06747; S06747.
PDB; 1P58; EM; 9.50 A; A/B/C=281-775.
PDB; 2M9P; NMR; -; A=1391-1654.
PDB; 2M9Q; NMR; -; A=1391-1654.
PDB; 3C6D; EM; 12.50 A; D/E/F=115-195.
PDBsum; 1P58; -.
PDBsum; 2M9P; -.
PDBsum; 2M9Q; -.
PDBsum; 3C6D; -.
ProteinModelPortal; P14337; -.
SMR; P14337; -.
OrthoDB; VOG09000016; -.
EvolutionaryTrace; P14337; -.
PRO; PR:P14337; -.
Proteomes; UP000007195; Genome.
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: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: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.
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; 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 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; Transcription;
Transcription regulation; Transferase; Transmembrane;
Transmembrane helix; Transport; 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.
CHAIN 1 3391 Genome polyprotein.
/FTId=PRO_0000405210.
CHAIN 1 100 Protein C.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000267992.
PROPEP 101 114 ER anchor for the protein C, removed in
mature form by serine protease NS3.
/FTId=PRO_0000267993.
CHAIN 115 280 prM. {ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000267994.
CHAIN 115 205 Peptide pr.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000267995.
CHAIN 206 280 Small envelope protein M.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000267996.
CHAIN 281 775 Envelope protein E.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000037914.
CHAIN 776 1127 Non-structural protein 1.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000267997.
CHAIN 1128 1345 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000267999.
CHAIN 1128 1315 Non-structural protein 2A-alpha.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000267998.
CHAIN 1346 1475 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000268000.
CHAIN 1476 2093 Serine protease NS3.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000268001.
CHAIN 2094 2220 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000268002.
PEPTIDE 2221 2243 Peptide 2k.
/FTId=PRO_0000268003.
CHAIN 2244 2491 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000268004.
CHAIN 2492 3391 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P17763}.
/FTId=PRO_0000268005.
TOPO_DOM 1 101 Cytoplasmic. {ECO:0000255}.
TRANSMEM 102 122 Helical. {ECO:0000255}.
TOPO_DOM 123 238 Extracellular. {ECO:0000255}.
TRANSMEM 239 259 Helical. {ECO:0000255}.
TOPO_DOM 260 265 Cytoplasmic. {ECO:0000255}.
TRANSMEM 266 280 Helical. {ECO:0000255}.
TOPO_DOM 281 725 Extracellular. {ECO:0000255}.
INTRAMEM 726 746 Helical. {ECO:0000255}.
TOPO_DOM 747 752 Extracellular. {ECO:0000255}.
INTRAMEM 753 773 Helical. {ECO:0000255}.
TOPO_DOM 774 1124 Extracellular. {ECO:0000255}.
TRANSMEM 1125 1145 Helical. {ECO:0000255}.
TOPO_DOM 1146 1156 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1157 1177 Helical. {ECO:0000255}.
TOPO_DOM 1178 1182 Lumenal. {ECO:0000255}.
TRANSMEM 1183 1203 Helical. {ECO:0000255}.
TOPO_DOM 1204 1271 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1272 1292 Helical. {ECO:0000255}.
TOPO_DOM 1293 1317 Lumenal. {ECO:0000255}.
TRANSMEM 1318 1338 Helical. {ECO:0000255}.
TOPO_DOM 1339 1346 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1347 1367 Helical. {ECO:0000255}.
TOPO_DOM 1368 1370 Lumenal. {ECO:0000255}.
TRANSMEM 1371 1391 Helical. {ECO:0000255}.
TOPO_DOM 1392 1447 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1448 1468 Helical. {ECO:0000255}.
TOPO_DOM 1469 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 2277 Lumenal. {ECO:0000255}.
INTRAMEM 2278 2295 Helical. {ECO:0000255}.
TOPO_DOM 2296 2316 Lumenal. {ECO:0000255}.
INTRAMEM 2317 2337 Helical. {ECO:0000255}.
TOPO_DOM 2338 2347 Lumenal. {ECO:0000255}.
TRANSMEM 2348 2368 Helical. {ECO:0000255}.
TOPO_DOM 2369 2413 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2414 2434 Helical. {ECO:0000255}.
TOPO_DOM 2435 2459 Lumenal. {ECO:0000255}.
TRANSMEM 2460 2480 Helical. {ECO:0000255}.
TOPO_DOM 2481 3391 Cytoplasmic. {ECO:0000255}.
DOMAIN 1476 1653 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1655 1811 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1821 1988 Helicase C-terminal.
DOMAIN 2493 2755 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3020 3169 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1668 1675 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 33 74 Hydrophobic; homodimerization of capsid
protein C. {ECO:0000250}.
REGION 1398 1437 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
MOTIF 1759 1762 DEAH box.
COMPBIAS 97 100 Poly-Arg.
COMPBIAS 1434 1437 Poly-Glu.
COMPBIAS 2148 2154 Poly-Leu.
COMPBIAS 2354 2357 Poly-Leu.
COMPBIAS 3383 3386 Poly-Glu.
ACT_SITE 1526 1526 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1550 1550 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1610 1610 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
BINDING 2505 2505 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2508 2508 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2509 2509 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2511 2511 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2520 2520 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2547 2547 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2577 2577 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2578 2578 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2595 2595 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2596 2596 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2622 2622 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2623 2623 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2641 2641 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:0000255}.
SITE 114 115 Cleavage; by host signal peptidase.
{ECO:0000250}.
SITE 205 206 Cleavage; by host furin. {ECO:0000255}.
SITE 280 281 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 775 776 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 1127 1128 Cleavage; by host. {ECO:0000250}.
SITE 1345 1346 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 1475 1476 Cleavage; by autolysis. {ECO:0000255}.
SITE 2093 2094 Cleavage; by autolysis. {ECO:0000255}.
SITE 2220 2221 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 2243 2244 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 2491 2492 Cleavage; by viral protease NS3.
{ECO:0000255}.
SITE 2516 2516 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2552 2552 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2637 2637 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2638 2638 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}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 433 433 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 982 982 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2301 2301 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2305 2305 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 2457 2457 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
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 779 790 {ECO:0000250|UniProtKB:P17763}.
DISULFID 830 918 {ECO:0000250|UniProtKB:P17763}.
DISULFID 954 998 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1055 1104 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1066 1088 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1087 1091 {ECO:0000250|UniProtKB:P17763}.
VARIANT 291 291 F -> L (in strain: Isolate Malaysia M1).
VARIANT 357 357 Q -> L (in strain: Isolate Malaysia M1).
VARIANT 370 370 F -> L (in strain: Isolate Malaysia M1).
VARIANT 444 444 V -> I (in strain: Isolate Malaysia M1).
VARIANT 540 540 M -> I (in strain: Isolate Malaysia M1).
VARIANT 590 590 K -> E (in strain: Isolate Malaysia M1).
VARIANT 647 647 I -> V (in strain: Isolate Malaysia M1).
VARIANT 687 687 R -> I (in strain: Isolate Malaysia M1).
VARIANT 696 696 G -> R (in strain: Isolate Malaysia M1).
VARIANT 773 773 V -> C (in strain: Isolate Malaysia M1).
STRAND 1396 1402 {ECO:0000244|PDB:2M9P}.
STRAND 1411 1414 {ECO:0000244|PDB:2M9P}.
STRAND 1418 1420 {ECO:0000244|PDB:2M9Q}.
STRAND 1422 1424 {ECO:0000244|PDB:2M9P}.
TURN 1425 1427 {ECO:0000244|PDB:2M9P}.
STRAND 1428 1433 {ECO:0000244|PDB:2M9P}.
STRAND 1453 1455 {ECO:0000244|PDB:2M9P}.
STRAND 1483 1485 {ECO:0000244|PDB:2M9P}.
STRAND 1486 1488 {ECO:0000244|PDB:2M9Q}.
STRAND 1496 1504 {ECO:0000244|PDB:2M9P}.
STRAND 1507 1517 {ECO:0000244|PDB:2M9P}.
STRAND 1520 1525 {ECO:0000244|PDB:2M9P}.
TURN 1526 1529 {ECO:0000244|PDB:2M9P}.
STRAND 1533 1535 {ECO:0000244|PDB:2M9P}.
STRAND 1538 1540 {ECO:0000244|PDB:2M9P}.
STRAND 1543 1546 {ECO:0000244|PDB:2M9P}.
TURN 1547 1550 {ECO:0000244|PDB:2M9P}.
STRAND 1551 1558 {ECO:0000244|PDB:2M9P}.
STRAND 1570 1575 {ECO:0000244|PDB:2M9P}.
STRAND 1581 1587 {ECO:0000244|PDB:2M9P}.
STRAND 1589 1592 {ECO:0000244|PDB:2M9P}.
STRAND 1597 1602 {ECO:0000244|PDB:2M9P}.
STRAND 1612 1616 {ECO:0000244|PDB:2M9P}.
STRAND 1623 1631 {ECO:0000244|PDB:2M9P}.
TURN 1632 1634 {ECO:0000244|PDB:2M9P}.
STRAND 1635 1641 {ECO:0000244|PDB:2M9P}.
STRAND 1647 1650 {ECO:0000244|PDB:2M9P}.
SEQUENCE 3391 AA; 379394 MW; 5325B9EEB03F40F9 CRC64;
MNNQRKKAKN TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLFMAL VAFLRFLTIP
PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNRRRR SAGMIIMLIP TVMAFHLTTR
NGEPHMIVSR QEKGKSLLFK TEDGVNMCTL MAMDLGELCE DTITYKCPLL RQNEPEDIDC
WCNSTSTWVT YGTCTTTGEH RREKRSVALV PHVGMGLETR TETWMSSEGA WKHAQRIETW
ILRHPGFTIM AAILAYTIGT THFQRALIFI LLTAVAPSMT MRCIGISNRD FVEGVSGGSW
VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT ESRCPTQGEP
SLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT CKKNMEGKIV QPENLEYTIV
VTPHSGEEHA VGNDTGKHGK EIKVTPQSSI TEAELTGYGT VTMECSPRTG LDFNEMVLLQ
MENKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM
HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKVVK EIAETQHGTI
VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE KDSPVNIEAE PPFGDSYIII
GVEPGQLKLN WFKKGSSIGQ MFETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF
GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVSLV LVGIVTLYLG VMVQADSGCV
VSWKNKELKC GSGIFITDNV HTWTEQYKFQ PESPSKLASA IQKAQEEGIC GIRSVTRLEN
LMWKQITPEL NHILAENEVK LTIMTGDIKG IMQAGKRSLR PQPTELKYSW KTWGKAKMLS
TESHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLKEKQ DAFCDSKLMS
AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKNCHW PKSHTLWSNG VLESEMIIPK
NLAGPVSQHN YRPGYHTQIA GPWHLGKLEM DFDFCDGTTV VVTEDCGNRG PSLRTTTASG
KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QVDNFSLGVL
GMALFLEEML RTRVGTKHAI LLVAVSFVTL ITGNMSFKDL GRVVVMVGAT MTDDIGMGVT
YLALLAAFKV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ STIPETILEL TDALALGMMV
LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA VVSVSPLLLT SSQQKTDWIP
LALTIKGLNP TAIFLTTLSR TSKKRSWPLN EAIMAVGMVS ILASSLLKND IPMTGPLVAG
GLLTVCYVLT GRSADLELER AADVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL
TILIRTGLLV ISGLFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPMGK AELEDGAYRI
KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD LISYGGGWKL
EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FKTNAGTIGA VSLDFSPGTS GSPIIDKKGK
VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RRLTIMDLHP GAGKTKRYLP
AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE IVDLMCHATF
TMRLLSPVRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
PQSNAPIIDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KAGNDIAACL RKNGKKVIQL
SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT DGEERVILAG
PMPVTHSSAA QRRGRIGRNP KNENDQYIYM GEPLENDEDC AHWKEAKMLL DNINTPEGII
PSMFEPEREK VDAIDGEYRL RGEARKTFVD LMRRGDLPVW LAYKVAAEGI NYADRRWCFD
GIKNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA GRKSLTLNLI
TEMGRLPTFM TQKTRDALDN LAVLHTAEAG GRAYNHALSE LPETLETLLL LTLLATVTGG
IFLFLMSGRG IGKMTLGMCC IITASVLLWY AQIQPHWIAA SIILEFFLIV LLIPEPEKQR
TPQDNQLTYV VIAILTVVAA TMANEMGFLE KTKKDLGLGS IATQQPESNI LDIDLRPASA
WTLYAVATTF VTPMLRHSIE NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG
CYSQVNPITL TAALLLLVAH YAIIGPGLQA KATREAQKRA AAGIMKNPTV DGITVIDLDP
IPYDPKFEKQ LGQVMLLVLC VTQVLMMRTT WALCEALTLA TGPISTLWEG NPGRFWNTTI
AVSMANIFRG SYLAGAGLLF SIMKNTTNTR RGTGNIGETL GEKWKSRLNA LGKSEFQIYK
KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS AKLRWFVERN MVTPEGKVVD LGCGRGGWSY
YCGGLKNVRE VKGLTKGGPG HEEPIPMSTY GWNLVRLQSG VDVFFIPPEK CDTLLCDIGE
SSPSPTVEAG RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMETLQR KYGGALVRNP
LSRNSTHEMY WVSNASGNIV SSVNMISRML INRFTMRHKK ATYEPDVDLG SGTRNIGIES
EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY ETKQTGSASS MVNGVVRLLT
KPWDVLPTVT QMAMTDTTPF GQQRVFKEKV DTRTQEPKEG TKKLMKITAE WLWKELGKKK
TPRMCTREEF TRKVRSNAAL GAIFTDENKW KSAREAVEDS RFWELVDKER NLHLEGKCET
CVYNMMGKRE KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RENSLSGVEG
EGLHKLGYIL RDVSKKEGGA MYADDTAGWD TRITLEDLKN EEMVTNHMEG EHKKLAEAIF
KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL NTFTNMEAQL IRQMEGEGVF
KNIQHLTVTE EIAVQNWLAR VGRERLSRMA ISGDDCVVKP LDDRFASALT ALNDMGKIRK
DIQQWEPSRG WNDWTQVPFC SHHFHELIMK DGRVLVVPCR NQDELIGRAR ISQGAGWSLR
ETACLGKSYA QMWSLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA KHEWMTTEDM
LTVWNRVWIQ ENPWMEDKTP VESWEEIPYL GKREDQWCGS LIGLTSRATW AKNIQAAINQ
VRSLIGNEEY TDYMPSMKRF RREEEEAGVL W


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