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 POLG_POWVL              Reviewed;        3415 AA.
Q04538;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
22-NOV-2017, entry version 144.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Peptide 2k;
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;
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 {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=NS5;
Tick-borne powassan virus (strain LB) (POWV) (Powassan virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus; tick-borne encephalitis virus group.
NCBI_TaxID=39008;
NCBI_TaxID=34620; Dermacentor andersoni (Rocky mountain wood tick).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=35565; Ixodes cookei.
NCBI_TaxID=6945; Ixodes scapularis (Black-legged tick) (Deer tick).
NCBI_TaxID=34614; Ixodes spinipalpis.
NCBI_TaxID=48086; Lepus americanus (Snowshoe hare).
NCBI_TaxID=9995; Marmota monax (Woodchuck).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8097605; DOI=10.1006/viro.1993.1247;
Mandl C.W., Holzmann H., Kunz C., Heinz F.X.;
"Complete genomic sequence of Powassan virus: evaluation of genetic
elements in tick-borne versus mosquito-borne flaviviruses.";
Virology 194:173-184(1993).
-!- 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.
{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 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 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: Regulates the ATPase activity
of the NS3 helicase activity. NS4A allows NS3 helicase to conserve
energy during unwinding. {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.
Inhibits STAT2 translocation in the nucleus after IFN-alpha
treatment. {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 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. Interacts with host SCRIB;
this interaction targets NS5 to the cell membrane periphery and
nucleus, thereby allowing efficient host nuclear STAT1 inhibition.
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Capsid protein C: Virion
{ECO:0000250|UniProtKB:P17763}. Host nucleus
{ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear
region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Peptide pr: Secreted
{ECO:0000250|UniProtKB:P17763}.
-!- SUBCELLULAR LOCATION: Small envelope protein M: Virion membrane
{ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- SUBCELLULAR LOCATION: Envelope protein E: Virion membrane
{ECO:0000305}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum
membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane
protein {ECO:0000255}. Note=ER membrane retention is mediated by
the transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
-!- 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:P14335}; 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:P14335}; 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: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:P06935}.
Note=Located in RE-associated vesicles hosting the replication
complex. NS5 protein is mainly localized in the nucleus rather
than in ER vesicles. {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: 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}.
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EMBL; L06436; AAA02739.1; -; Genomic_RNA.
PIR; A46105; A46105.
RefSeq; NP_620099.1; NC_003687.1.
ProteinModelPortal; Q04538; -.
SMR; Q04538; -.
GeneID; 940442; -.
KEGG; vg:940442; -.
OrthoDB; VOG090000KT; -.
Proteomes; UP000006848; 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:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; 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: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:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 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; 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_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; 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; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 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.
3: Inferred from homology;
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 nucleus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host STAT1 by virus; Inhibition of host STAT2 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; Suppressor of RNA silencing; 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; Zinc.
CHAIN 1 3415 Genome polyprotein.
/FTId=PRO_0000037724.
CHAIN 1 94 Capsid protein C.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000405239.
PROPEP 95 115 ER anchor for the capsid protein C,
removed in mature form by serine protease
NS3. {ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000405140.
CHAIN 116 278 Protein prM.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000405141.
CHAIN 116 203 Peptide pr.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037725.
CHAIN 204 278 Small envelope protein M.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037726.
CHAIN 279 775 Envelope protein E.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037727.
CHAIN 776 1128 Non-structural protein 1.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037728.
CHAIN 1129 1358 Non-structural protein 2A.
{ECO:0000250|UniProtKB:P06935}.
/FTId=PRO_0000037729.
CHAIN 1359 1489 Serine protease subunit NS2B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037730.
CHAIN 1490 2111 Serine protease NS3.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037731.
CHAIN 2112 2237 Non-structural protein 4A.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037732.
PEPTIDE 2238 2260 Peptide 2k.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000405142.
CHAIN 2261 2512 Non-structural protein 4B.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037733.
CHAIN 2513 3415 RNA-directed RNA polymerase NS5.
{ECO:0000250|UniProtKB:P03314}.
/FTId=PRO_0000037734.
TOPO_DOM 1 96 Cytoplasmic. {ECO:0000255}.
TRANSMEM 97 117 Helical. {ECO:0000255}.
TOPO_DOM 118 243 Extracellular. {ECO:0000255}.
TRANSMEM 244 260 Helical. {ECO:0000255}.
TOPO_DOM 261 261 Cytoplasmic. {ECO:0000255}.
TRANSMEM 262 278 Helical. {ECO:0000255}.
TOPO_DOM 279 726 Extracellular. {ECO:0000255}.
TRANSMEM 727 747 Helical. {ECO:0000255}.
TOPO_DOM 748 754 Cytoplasmic. {ECO:0000255}.
TRANSMEM 755 775 Helical. {ECO:0000255}.
TOPO_DOM 776 1187 Extracellular. {ECO:0000255}.
TRANSMEM 1188 1208 Helical. {ECO:0000250|UniProtKB:P17763,
ECO:0000255}.
TOPO_DOM 1209 1233 Cytoplasmic.
{ECO:0000250|UniProtKB:P17763,
ECO:0000255}.
TRANSMEM 1234 1253 Helical. {ECO:0000250|UniProtKB:P17763,
ECO:0000255}.
TOPO_DOM 1254 1254 Lumenal. {ECO:0000250|UniProtKB:P17763,
ECO:0000255}.
TRANSMEM 1255 1275 Helical. {ECO:0000250|UniProtKB:P17763,
ECO:0000255}.
TOPO_DOM 1276 1292 Cytoplasmic.
{ECO:0000250|UniProtKB:P17763,
ECO:0000255}.
TRANSMEM 1293 1313 Helical. {ECO:0000250|UniProtKB:P17763,
ECO:0000255}.
TOPO_DOM 1314 1327 Lumenal. {ECO:0000250|UniProtKB:P17763,
ECO:0000255}.
TRANSMEM 1328 1348 Helical. {ECO:0000250|UniProtKB:P17763,
ECO:0000255}.
TOPO_DOM 1349 1359 Cytoplasmic.
{ECO:0000250|UniProtKB:P17763,
ECO:0000255}.
TRANSMEM 1360 1378 Helical. {ECO:0000255}.
TOPO_DOM 1379 1382 Lumenal. {ECO:0000255}.
TRANSMEM 1383 1403 Helical. {ECO:0000255}.
TOPO_DOM 1404 1452 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1453 1473 Helical. {ECO:0000255}.
TOPO_DOM 1474 2163 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2164 2184 Helical. {ECO:0000255}.
TOPO_DOM 2185 2190 Lumenal. {ECO:0000255}.
INTRAMEM 2191 2210 Helical. {ECO:0000255}.
TOPO_DOM 2211 2211 Lumenal. {ECO:0000255}.
TRANSMEM 2212 2232 Helical. {ECO:0000255}.
TOPO_DOM 2233 2243 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2244 2264 Helical; Note=Signal for NS4B.
{ECO:0000255}.
TOPO_DOM 2265 2300 Lumenal. {ECO:0000255}.
INTRAMEM 2301 2321 Helical. {ECO:0000255}.
TOPO_DOM 2322 2344 Lumenal. {ECO:0000255}.
INTRAMEM 2345 2365 Helical. {ECO:0000255}.
TOPO_DOM 2366 2369 Lumenal. {ECO:0000255}.
TRANSMEM 2370 2390 Helical. {ECO:0000255}.
TOPO_DOM 2391 2433 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2434 2454 Helical. {ECO:0000255}.
TOPO_DOM 2455 2479 Lumenal. {ECO:0000255}.
TRANSMEM 2480 2500 Helical. {ECO:0000255}.
TOPO_DOM 2501 3415 Cytoplasmic. {ECO:0000255}.
DOMAIN 1490 1669 Peptidase S7. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
DOMAIN 1675 1832 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1842 2001 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2513 2777 mRNA cap 0-1 NS5-type MT.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
DOMAIN 3041 3190 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1688 1695 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 376 389 Fusion peptide.
{ECO:0000250|UniProtKB:P14336}.
REGION 1410 1449 Interacts with and activates NS3
protease. {ECO:0000255|PROSITE-
ProRule:PRU00859}.
REGION 2731 2735 Interaction with host SCRIB.
{ECO:0000250|UniProtKB:Q01299}.
MOTIF 1780 1783 DEAH box. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
COMPBIAS 1746 1749 Poly-Ser.
COMPBIAS 1971 1974 Poly-Asp.
ACT_SITE 1543 1543 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1567 1567 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 1627 1627 Charge relay system; for serine protease
NS3 activity. {ECO:0000255|PROSITE-
ProRule:PRU00860}.
ACT_SITE 2573 2573 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2658 2658 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2695 2695 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
ACT_SITE 2731 2731 For 2'-O-MTase activity.
{ECO:0000250|UniProtKB:Q6YMS4}.
METAL 2951 2951 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2955 2955 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 2960 2960 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 2963 2963 Zinc 1. {ECO:0000250|UniProtKB:P14335}.
METAL 3225 3225 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P14335}.
METAL 3241 3241 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
METAL 3360 3360 Zinc 2. {ECO:0000250|UniProtKB:P14335}.
BINDING 2525 2525 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2528 2528 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2529 2529 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2531 2531 mRNA cap; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2540 2540 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2568 2568 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2598 2598 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2599 2599 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2616 2616 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2617 2617 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2643 2643 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
BINDING 2644 2644 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2662 2662 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2726 2726 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2728 2728 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
BINDING 2733 2733 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 94 95 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 114 115 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 115 116 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 203 204 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P06935}.
SITE 278 279 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P06935}.
SITE 775 776 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 1128 1129 Cleavage; by host.
{ECO:0000250|UniProtKB:P06935}.
SITE 1358 1359 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P06935}.
SITE 1489 1490 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03314}.
SITE 1950 1950 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 1953 1953 Involved in NS3 ATPase and RTPase
activities.
{ECO:0000250|UniProtKB:P14335}.
SITE 2111 2112 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P03314}.
SITE 2237 2238 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 2260 2261 Cleavage; by host signal peptidase.
{ECO:0000250|UniProtKB:P03314}.
SITE 2512 2513 Cleavage; by viral protease NS3.
{ECO:0000250|UniProtKB:P03314}.
SITE 2536 2536 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2573 2573 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2658 2658 Essential for 2'-O-methyltransferase and
N-7 methyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2659 2659 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU00924}.
SITE 2695 2695 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
SITE 2731 2731 Essential for 2'-O-methyltransferase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00924}.
MOD_RES 2568 2568 Phosphoserine.
{ECO:0000250|UniProtKB:P03314}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 432 432 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250|UniProtKB:P14336,
ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 860 860 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 983 983 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 999 999 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 281 308 {ECO:0000250|UniProtKB:P14336}.
DISULFID 338 399 {ECO:0000250|UniProtKB:P17763}.
DISULFID 338 394 {ECO:0000250|UniProtKB:P14336}.
DISULFID 352 383 {ECO:0000250|UniProtKB:P14336}.
DISULFID 370 399 {ECO:0000250|UniProtKB:P14336}.
DISULFID 370 394 {ECO:0000250|UniProtKB:P17763}.
DISULFID 464 568 {ECO:0000250|UniProtKB:P14336}.
DISULFID 585 617 {ECO:0000250|UniProtKB:P14336}.
DISULFID 779 790 {ECO:0000250|UniProtKB:P17763}.
DISULFID 830 920 {ECO:0000250|UniProtKB:P17763}.
DISULFID 955 1000 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1057 1106 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1068 1090 {ECO:0000250|UniProtKB:P17763}.
DISULFID 1089 1093 {ECO:0000250|UniProtKB:P17763}.
SEQUENCE 3415 AA; 378570 MW; E71092FE64049F46 CRC64;
MMTTSKGKGG GPPRRKLKVT ANKSRPATSP MPKGFVLSRM LGILWHAVTG TARPPVLKMF
WKTVPLRQAE AVLKKIKRVI GNLMQSLHMR GRRRSGVDWT WIFLTMALMT MAMATTIHRD
REGYMVMRAS GRDAASQVRV QNGTCVILAT DMGEWCEDSI TYSCVTIDQE EEPVDVDCFC
RGVDRVKLEY GRCGRQAGSR GKRSVVIPTH AQKDMVGRGH AWLKGDNIRD HVTRVEGWMW
KNKLLTAAIV ALAWLMVDSW MARVTVILLA LSLGPVYATR CTHLENRDFV TGTQGTTRVS
LVLELGGCVT ITAEGKPSID VWLEDIFQES PAETREYCLH AKLTNTKVEA RCPTTGPATL
PEEHQANMVC KRDQSDRGWG NHCGFFGKGS IVACAKFECE EAKKAVGHVY DSTKITYVVK
VEPHTGDYLA ANETNSNRKS AQFTVASEKV ILRLGDYGDV SLTCKVASGI DVAQTVVMSL
DSSKDHLPSA WQVHRDWFED LALPWKHKDN QDWNSVEKLV EFGPPHAVKM DVFNLGDQTA
VLLKSLAGVP LASVEGQKYH LKSGHVTCDV GLEKLKLKGT TYSMCDKAKF KWKRVPVDSG
HDTVVMEVSY TGSDKPCRIP VRAVAHGVPA VNVAMLITPN PTIETNGGGF IEMQLPPGDN
IIYVGDLSQQ WFQKGSTIGR MFEKTRRGLE RLSVVGEHAW DFGSVGGVLS SVGKAIHTVL
GGAFNTLFGG VGFIPKMLLG VALVWLGLNA RNPTMSMTFL AVGALTLMMT MGVGADYGCA
IDPERMEIRC GEGLVVWKEV SEWYDGYAYH PESPDTLAQA LREAFERGVC GVVPQNRLEM
AMWRSTAPEL NLVLSEGEAN LTIVVDKTDP ADYRGGTPMV LKKTGKESKV SWKSWGKSIL
WSVPDSPRRM MMGVDGVGEC PLYRRATGVF TVAEFGVGLR TKVFLDLRGE ASKECDTGVM
GAAVKNGKAI HTDQSMWMSS FRNDTGTYIH ELILTDLRNC TWPASHTIDN DGVLDSHLFL
PVTLAGPRSK YNRIPGYSEQ VRGPWDQTPL RVVRDHCPGT SVRIDSHCDK RGASVRSTTE
SGKIIPEWCC RACELPPVTF RSGTDCWYAM EIRPVHSQGG LVRSMVVADN GALLSEGGVP
GLVAVFVLME FLLRRRPGSV TSILWGGILM LGLLVTGLVR VEEIVRYVIA VGVTFHLELG
PETMVLVMLQ AVFNMRTCYL MGFLVKRVIT TREVVTVYFL LLVLEMGIPE MNFGHLWEWA
DALAMGLLII KASAMEDRRG LGFLLAGLMT QRHLVAVHHG LMVFLTVALA VVGRNIYNGQ
KERKGLCFTV PLASLLGGSG SGLRMLALWE CLGGRGRRSL SEPLTVVGVM LAMASGLLRH
SSQEALLALS AGSFLILMLI LGTRRLQLTA EWAGVVEWNP ELVNEGGEVS LKVRQDAMGN
LHLTEVEREE RRLALWLVFG LLASAYHWSG ILVTMGAWTV YELFSSTRRT DLVFSGQLPD
QGEKRSFDIK EGVYRIYAPG LFWGYRQIGV GYGTKGVLHT MWHVTRGAAL SVEGATSGPY
WADVREDVVC YGGAWGLDKK WGGEVVQVHA FPPDSGHKIH QCQPGKLNLE GGRVLGAIPI
DLPRGTSGSP IINAQGDVLG LYGNGLKSND VYISSIAQGN VEKSRPEMPL AVQGGKWTSK
GSITVLDMHP GSGKTHRVLP ELIRECIDKR LRTVVLAPTR VVLKEMERAL QGKRVKFHSA
AVDNASSSSG AIVDVMCHAT YVNRRLLPQG RQNWEVAIMD EAHWTDPHSI AARGHLYSLA
KENRCALVLM TATPPGKSEA FPESKGAIVS EEKPIPEGEW RDGFDWITEF EGRTAWFVPS
IAKGGAIART LRQKGKSVIC LNSKTFDKDY GRVHEEKPDF VVTTDISEMG ANLDVNRVID
GRTNIKPEEI DGKVELIGTR RVTTASAAQR RGRVGRHEGR TDLYVYSGQC DDDDSSLVQW
KEAQILLDNI TTVRGPVATF YGPEQGKMLE VAGHFRLTEE KRKHFRHLLT NCDFTPWLAW
HVAANTACVT DRKWTWEGPD ENAIDGPGGE LVTFRSPNGA ERKLKPIWKD SRMFREGRDV
ADFIQYASGR RSAVDILTGL GGVPDLLRLR CTAAWDVVYT LLNETPGSRA MKMAERDAPE
AMLTLLEVAV LGIATLGVVW CFIVRTSVSR MVLGTLVLAV ALILLWLGGM DYGTMAGVAL
IFYLLLTVLQ PEPGKQRSGE DNRLAFLLIG LGSVVGLVAA NELGYLEQTK TDISGLFRRE
DQGGMVWDAW TNIDIQPARS WGTYVLIVSL FTPYMLHQLQ TKIQRLVNSS VAAGTQAMRD
LGGGTPFFGV AGHVVALGVT SLVGATPTSL ALGVALAALH LAVVTSGLEA ELTQRAHRAF
FSAMVKNPMV DGEIINPIPD GDPKPALYER KMSLFLAIGL CIAAVALNRT AAAMTEAGAV
AVAALGQLLR PEEESWWTMP MACGMAGLVR GSLWGLLPVL HRIWLRTQGA RRGGAEGSTL
GDIWKQRLNS CTKEEFFAYR RTGVMETNRD QARELLRRGE TNMGLAVSRG CAKLAWLEER
GYATLKGEVV DLGCGRGGWS YYAASRPSVM AVRAYTIGGK GHEAPRLVTS LGWNLIKFRS
GMDVFSMATT RADTILCDIG ESSPDPEKEG ARSRRVILLM EQWKARNPDA AAVFKVLAPY
RPEVLEALHR FQLQWGGGLV RVPFSRNSTH EMYYSTAVTG NLVNSVNVLS RKLLARFGET
RGPIQVPEID LGTGTRCVTL AEDKVKPRDV AERIGALREQ YSESWHEDKE HPYRTWQYWG
SYRTPATGSA ASLINGVVKL LSWPWNARED VTRMAMTDTT AFGQQRVFKE KVDTKAQEPQ
PGTRVIMRAV SDWLLEHLSR RAKVRMCTKD EFIAKVRSNA ALGAWSDEQN KWSSAKEAVE
DPEFWKLVDE ERSRHLKGQC RHCVYNMMGK REKKLGEFGV AKGSRAIWYM WLGSRFLEFE
VLGFLNEEHW ASREVSGAGV EGTSLNYLGW LLRELGMKDG GKLYADDTAG WDTRITNADL
EDEEQILRYM EGEHHVLAKT ILEKAYHAKV VKVARPSPQG GCVMDVITRR DQRGSGQVVT
YALNTITNMK VQLIRMMEGE GVIGPADSQD PRLKRVETWL KEHGVERLGR MLVSGDDCVV
KPIDDRFGKA LYFLNDMAKV RKDVGEWEPS MGFTEWEEVP FCSHHFHELV MKDGRSLIVP
CRDQDELVGR ARVSPGCGWS VRETACLSKA YGQMWLLNYF HRRDLRTLGF AICSAVPVSW
VPMGRTTWSI HASGEWMTTE DMLRIWNKVW ILDNPHMEDK QTVDEWRDIP YLPKTQDLVC
SSLVGRKERA EWAKNIWGSV EKVRKLIGPE DYRDYLSSMD RHDLHWELKL ESSII


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