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Genome polyprotein

 A0A024B7W1_ZIKV         Unreviewed;      3423 AA.
A0A024B7W1;
09-JUL-2014, integrated into UniProtKB/TrEMBL.
09-JUL-2014, sequence version 1.
20-DEC-2017, entry version 31.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684};
Zika virus (strain Mr 766) (ZIKV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=64320 {ECO:0000313|EMBL:AHZ13508.1, ECO:0000313|Proteomes:UP000151151};
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).
NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
[1] {ECO:0000313|EMBL:AHZ13508.1, ECO:0000313|Proteomes:UP000151151}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=H/PF/2013 {ECO:0000313|EMBL:AHZ13508.1};
PubMed=24903869;
Baronti C., Piorkowski G., Charrel R.N., Boubis L., Leparc-Goffart I.,
de Lamballerie X.;
"Complete coding sequence of zika virus from a French polynesia
outbreak in 2013.";
Genome Announc. 2:e00500-14(2014).
[2] {ECO:0000213|PDB:5KVE}
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 589-697, AND DISULFIDE
BONDS.
PubMed=27475895; DOI=10.1016/j.cell.2016.07.020;
Zhao H., Fernandez E., Dowd K.A., Speer S.D., Platt D.J., Gorman M.J.,
Govero J., Nelson C.A., Pierson T.C., Diamond M.S., Fremont D.H.;
"Structural Basis of Zika Virus-Specific Antibody Protection.";
Cell 166:1016-1027(2016).
[3] {ECO:0000213|PDB:5KQR, ECO:0000213|PDB:5KQS}
X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 2521-2786 IN COMPLEX WITH
IRON-SULFUR (4FE-4S-S-ADOMET).
PubMed=27633330; DOI=10.1016/j.celrep.2016.08.091;
Coloma J., Jain R., Rajashankar K.R., Garcia-Sastre A., Aggarwal A.K.;
"Structures of NS5 Methyltransferase from Zika Virus.";
Cell Rep. 16:3097-3102(2016).
[4] {ECO:0000213|PDB:5H30, ECO:0000213|PDB:5H32, ECO:0000213|PDB:5H37}
STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) OF 291-794 AND
216-290, AND DISULFIDE BONDS.
PubMed=27882950; DOI=10.1038/ncomms13679;
Zhang S., Kostyuchenko V.A., Ng T.S., Lim X.N., Ooi J.S., Lambert S.,
Tan T.Y., Widman D.G., Shi J., Baric R.S., Lok S.M.;
"Neutralization mechanism of a highly potent antibody against Zika
virus.";
Nat. Commun. 7:13679-13679(2016).
[5] {ECO:0000213|PDB:5IZ7}
STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) OF 291-794 AND
216-290, AND DISULFIDE BONDS.
PubMed=27093288; DOI=10.1038/nature17994;
Kostyuchenko V.A., Lim E.X., Zhang S., Fibriansah G., Ng T.S.,
Ooi J.S., Shi J., Lok S.M.;
"Structure of the thermally stable Zika virus.";
Nature 533:425-428(2016).
[6] {ECO:0000213|PDB:5LBS, ECO:0000213|PDB:5LBV, ECO:0000213|PDB:5LCV}
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 291-698, AND DISULFIDE
BONDS.
PubMed=27338953; DOI=10.1038/nature18938;
Barba-Spaeth G., Dejnirattisai W., Rouvinski A., Vaney M.C.,
Medits I., Sharma A., Simon-Loriere E., Sakuntabhai A.,
Cao-Lormeau V.M., Haouz A., England P., Stiasny K., Mongkolsapaya J.,
Heinz F.X., Screaton G.R., Rey F.A.;
"Structural basis of potent Zika-dengue virus antibody cross-
neutralization.";
Nature 536:48-53(2016).
[7] {ECO:0000213|PDB:5JMT}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1674-2119.
PubMed=27172988; DOI=10.1007/s13238-016-0275-4;
Tian H., Ji X., Yang X., Xie W., Yang K., Chen C., Wu C., Chi H.,
Mu Z., Wang Z., Yang H.;
"The crystal structure of Zika virus helicase: basis for antiviral
drug design.";
Protein Cell 7:450-454(2016).
[8] {ECO:0000213|PDB:5IRE}
STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 291-794 AND
216-290, AND DISULFIDE BONDS.
PubMed=27033547; DOI=10.1126/science.aaf5316;
Sirohi D., Chen Z., Sun L., Klose T., Pierson T.C., Rossmann M.G.,
Kuhn R.J.;
"The 3.8 A resolution cryo-EM structure of Zika virus.";
Science 352:467-470(2016).
[9] {ECO:0000313|Proteomes:UP000112691, ECO:0000313|Proteomes:UP000137079, ECO:0000313|Proteomes:UP000168269}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1_0049_PF {ECO:0000313|EMBL:ANO46302.1},
1_0087_PF {ECO:0000313|EMBL:ANO46301.1}, and
1_0181_PF {ECO:0000313|EMBL:ANO46304.1};
Nougairede A., Bouazza N., Piorkowski G., Baronti C., Musso D.,
De Lamballerie X.;
"Zika virus outbreak in French Polynesia, 2013-2014.";
Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
[10] {ECO:0000313|EMBL:AHZ13508.1}
NUCLEOTIDE SEQUENCE.
STRAIN=H/PF/2013 {ECO:0000313|EMBL:AHZ13508.1};
Seilhamer J.J.;
Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
[11] {ECO:0000213|PDB:5MRK}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2521-2784, AND DISULFIDE
BONDS.
PubMed=28357511; DOI=10.1007/s00705-017-3345-x;
Hercik K., Brynda J., Nencka R., Boura E.;
"Structural basis of Zika virus methyltransferase inhibition by
sinefungin.";
Arch. Virol. 162:2091-2096(2017).
[12] {ECO:0000213|PDB:5GOZ, ECO:0000213|PDB:5GP1}
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2524-2785 IN COMPLEX WITH
GTP; S-ADENOSYL-L-HOMOCYSTEINE AND SUCCINATE.
PubMed=27866982; DOI=10.1016/j.bbrc.2016.11.098;
Zhang C., Feng T., Cheng J., Li Y., Yin X., Zeng W., Jin X., Li Y.,
Guo F., Jin T.;
"Structure of the NS5 methyltransferase from Zika virus and
implications in inhibitor design.";
Biochem. Biophys. Res. Commun. 492:624-630(2017).
[13] {ECO:0000213|PDB:5M5B}
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 2525-2786 IN COMPLEX WITH
IRON-SULFUR (4FE-4S-S-ADOMET).
PubMed=28031359; DOI=10.1128/JVI.02202-16;
Coutard B., Barral K., Lichiere J., Selisko B., Martin B., Aouadi W.,
Lombardia M.O., Debart F., Vasseur J.J., Guillemot J.C., Canard B.,
Decroly E.;
"Zika Virus Methyltransferase: Structure and Functions for Drug Design
Perspectives.";
J. Virol. 91:0-0(2017).
[14] {ECO:0000213|PDB:5UHY}
STRUCTURE BY ELECTRON MICROSCOPY (6.20 ANGSTROMS) OF 291-686, AND
DISULFIDE BONDS.
PubMed=28300075; DOI=10.1038/ncomms14722;
Hasan S.S., Miller A., Sapparapu G., Fernandez E., Klose T., Long F.,
Fokine A., Porta J.C., Jiang W., Diamond M.S., Crowe J.E., Kuhn R.J.,
Rossmann M.G.;
"A human antibody against Zika virus crosslinks the E protein to
prevent infection.";
Nat. Commun. 8:14722-14722(2017).
[15] {ECO:0000213|PDB:5U4W}
STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS) OF 726-791 AND
238-290.
PubMed=28067914; DOI=10.1038/nsmb.3352;
Prasad V.M., Miller A.S., Klose T., Sirohi D., Buda G., Jiang W.,
Kuhn R.J., Rossmann M.G.;
"Structure of the immature Zika virus at 9 A resolution.";
Nat. Struct. Mol. Biol. 24:184-186(2017).
[16] {ECO:0000213|PDB:5ULP}
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2521-2788, AND DISULFIDE
BONDS.
PubMed=28487506; DOI=10.1038/s41598-017-01756-7;
Jain R., Butler K.V., Coloma J., Jin J., Aggarwal A.K.;
"Development of a S-adenosylmethionine analog that intrudes the RNA-
cap binding site of Zika methyltransferase.";
Sci. Rep. 7:1632-1632(2017).
-!- FUNCTION: Peptide 2k: Functions as a signal peptide for NS4B and
is required for the interferon antagonism activity of the latter.
{ECO:0000256|SAAS:SAAS00892720}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000256|SAAS:SAAS00368577}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
{ECO:0000256|SAAS:SAAS00368620}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000256|SAAS:SAAS00383097}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
{ECO:0000256|SAAS:SAAS00232292}.
-!- 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:0000256|SAAS:SAAS00445805}.
-!- 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. {ECO:0000256|SAAS:SAAS00232385}.
-!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
{ECO:0000256|SAAS:SAAS00944756}; Peripheral membrane protein
{ECO:0000256|SAAS:SAAS00944756}; Lumenal side
{ECO:0000256|SAAS:SAAS00944756}. Host nucleus
{ECO:0000256|SAAS:SAAS00892522}. Secreted
{ECO:0000256|SAAS:SAAS00944768}. Virion membrane
{ECO:0000256|SAAS:SAAS00944678}; Multi-pass membrane protein
{ECO:0000256|SAAS:SAAS00944678}.
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EMBL; KJ776791; AHZ13508.1; -; Genomic_RNA.
EMBL; KX447509; ANO46301.1; -; Genomic_RNA.
EMBL; KX447510; ANO46302.1; -; Genomic_RNA.
EMBL; KX447512; ANO46304.1; -; Genomic_RNA.
PDB; 5GOZ; X-ray; 2.05 A; A/B/C=2524-2785.
PDB; 5GP1; X-ray; 2.44 A; A/B/C=2524-2785.
PDB; 5H30; EM; 4.40 A; A/B/C=291-794, D/E/F=216-290.
PDB; 5H32; EM; 12.00 A; A/B/C=291-693.
PDB; 5H37; EM; 4.00 A; A/B/C=291-794, D/E/F=216-290.
PDB; 5IRE; EM; 3.80 A; A/C/E=291-794, B/D/F=216-290.
PDB; 5IZ7; EM; 3.70 A; A/B/C=291-794, D/E/F=216-290.
PDB; 5JMT; X-ray; 1.80 A; A=1674-2119.
PDB; 5KQR; X-ray; 1.33 A; A=2521-2786.
PDB; 5KQS; X-ray; 1.50 A; A=2521-2786.
PDB; 5KVE; X-ray; 1.70 A; E=588-697.
PDB; 5LBS; X-ray; 2.41 A; A/B=291-698.
PDB; 5LBV; X-ray; 2.20 A; A/B=291-698.
PDB; 5LCV; X-ray; 2.64 A; A/B=291-698.
PDB; 5M5B; X-ray; 2.01 A; A/B=2525-2786.
PDB; 5MRK; X-ray; 1.90 A; A/B=2521-2784.
PDB; 5U4W; EM; 9.10 A; G/I/K=726-791, H/J/L=238-290.
PDB; 5UHY; EM; 6.20 A; A/C/E=291-686.
PDB; 5ULP; X-ray; 1.55 A; A/B=2521-2788.
PDBsum; 5GOZ; -.
PDBsum; 5GP1; -.
PDBsum; 5H30; -.
PDBsum; 5H32; -.
PDBsum; 5H37; -.
PDBsum; 5IRE; -.
PDBsum; 5IZ7; -.
PDBsum; 5JMT; -.
PDBsum; 5KQR; -.
PDBsum; 5KQS; -.
PDBsum; 5KVE; -.
PDBsum; 5LBS; -.
PDBsum; 5LBV; -.
PDBsum; 5LCV; -.
PDBsum; 5M5B; -.
PDBsum; 5MRK; -.
PDBsum; 5U4W; -.
PDBsum; 5UHY; -.
PDBsum; 5ULP; -.
Proteomes; UP000112691; Genome.
Proteomes; UP000137079; Genome.
Proteomes; UP000151151; Genome.
Proteomes; UP000168269; 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:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:InterPro.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
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: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: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: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.
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; 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 {ECO:0000213|PDB:5GOZ, ECO:0000213|PDB:5GP1,
ECO:0000213|PDB:5H30, ECO:0000213|PDB:5H32};
4Fe-4S {ECO:0000213|PDB:5KQR, ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B};
Activation of host autophagy by virus {ECO:0000256|SAAS:SAAS00445756};
ATP-binding {ECO:0000256|SAAS:SAAS00058020};
Capsid protein {ECO:0000256|SAAS:SAAS00969288};
Complete proteome {ECO:0000313|Proteomes:UP000112691,
ECO:0000313|Proteomes:UP000137079, ECO:0000313|Proteomes:UP000151151,
ECO:0000313|Proteomes:UP000168269};
Disulfide bond {ECO:0000256|PIRSR:PIRSR003817-3,
ECO:0000256|SAAS:SAAS00139753};
Fusion of virus membrane with host endosomal membrane
{ECO:0000256|SAAS:SAAS00489633};
Fusion of virus membrane with host membrane
{ECO:0000256|SAAS:SAAS00489633}; GTP-binding {ECO:0000213|PDB:5GOZ};
Helicase {ECO:0000256|SAAS:SAAS00058020};
Host endoplasmic reticulum {ECO:0000256|SAAS:SAAS00944771};
Host membrane {ECO:0000256|SAAS:SAAS00445977};
Host nucleus {ECO:0000256|SAAS:SAAS00892445};
Host-virus interaction {ECO:0000256|SAAS:SAAS00445756,
ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00892696};
Hydrolase {ECO:0000256|SAAS:SAAS00058020,
ECO:0000256|SAAS:SAAS00462397};
Inhibition of host innate immune response by virus
{ECO:0000256|SAAS:SAAS00892696};
Inhibition of host interferon signaling pathway by virus
{ECO:0000256|SAAS:SAAS00892696};
Inhibition of host STAT2 by virus {ECO:0000256|SAAS:SAAS00892696};
Iron {ECO:0000213|PDB:5KQR, ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B};
Iron-sulfur {ECO:0000213|PDB:5KQR, ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B};
Membrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAAS:SAAS00445977, ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000213|PDB:5KQR, ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B};
Methyltransferase {ECO:0000256|SAAS:SAAS00817755};
Nucleotide-binding {ECO:0000213|PDB:5GOZ,
ECO:0000256|SAAS:SAAS00058020};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510600};
Protease {ECO:0000256|SAAS:SAAS00462397};
RNA-binding {ECO:0000256|SAAS:SAAS00076745};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600};
Secreted {ECO:0000256|SAAS:SAAS00944674};
Serine protease {ECO:0000256|SAAS:SAAS00462397};
Transferase {ECO:0000256|SAAS:SAAS00510600,
ECO:0000256|SAAS:SAAS00817755};
Transmembrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Viral attachment to host cell {ECO:0000256|SAAS:SAAS00445995};
Viral immunoevasion {ECO:0000256|SAAS:SAAS00892696};
Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00489633};
Viral RNA replication {ECO:0000256|SAAS:SAAS00664279};
Virion {ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00969288};
Virus entry into host cell {ECO:0000256|SAAS:SAAS00445995,
ECO:0000256|SAAS:SAAS00489633};
Zinc {ECO:0000256|PIRSR:PIRSR003817-4}.
TRANSMEM 746 767 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 773 798 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1178 1197 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1273 1290 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1343 1366 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1378 1394 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1400 1417 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1473 1496 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2174 2192 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2199 2216 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2222 2241 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2253 2275 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2306 2327 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2334 2353 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2373 2392 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2442 2462 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 1373 1502 FLAVIVIRUS_NS2B.
{ECO:0000259|PROSITE:PS51527}.
DOMAIN 1503 1680 Peptidase S7.
{ECO:0000259|PROSITE:PS51528}.
DOMAIN 1683 1839 Helicase ATP-binding.
{ECO:0000259|PROSITE:PS51192}.
DOMAIN 1834 2013 Helicase C-terminal.
{ECO:0000259|PROSITE:PS51194}.
DOMAIN 2521 2785 MRNA cap 0-1 NS5-type MT.
{ECO:0000259|PROSITE:PS51591}.
DOMAIN 3049 3199 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
NP_BIND 2533 2539 GTP. {ECO:0000213|PDB:5GOZ}.
NP_BIND 2669 2675 GTP. {ECO:0000213|PDB:5GOZ}.
NP_BIND 2733 2735 GTP. {ECO:0000213|PDB:5GOZ}.
REGION 605 606 Mannose binding. {ECO:0000213|PDB:5LBV}.
REGION 2592 2594 Succinate 1 binding.
{ECO:0000213|PDB:5GOZ}.
REGION 2601 2607 S-adenosyl-L-homocysteine binding.
{ECO:0000213|PDB:5GOZ,
ECO:0000213|PDB:5GP1}.
REGION 2624 2625 S-adenosyl-L-homocysteine binding.
{ECO:0000213|PDB:5GP1}.
REGION 2630 2631 S-adenosyl-L-homocysteine binding.
{ECO:0000213|PDB:5GOZ,
ECO:0000213|PDB:5GP1}.
REGION 2651 2652 S-adenosyl-L-homocysteine binding.
{ECO:0000213|PDB:5GOZ,
ECO:0000213|PDB:5GP1}.
ACT_SITE 1553 1553 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1577 1577 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1637 1637 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
METAL 2576 2576 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000213|PDB:5KQR,
ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B}.
METAL 2578 2578 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000213|PDB:5KQR,
ECO:0000213|PDB:5M5B}.
METAL 2606 2606 Iron-sulfur (4Fe-4S-S-AdoMet); via amide
nitrogen. {ECO:0000213|PDB:5KQR,
ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B}.
METAL 2607 2607 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000213|PDB:5KQR,
ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B}.
METAL 2625 2625 Iron-sulfur (4Fe-4S-S-AdoMet); via amide
nitrogen. {ECO:0000213|PDB:5KQR,
ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B}.
METAL 2630 2630 Iron-sulfur (4Fe-4S-S-AdoMet); via pros
nitrogen. {ECO:0000213|PDB:5KQR}.
METAL 2650 2650 Iron-sulfur (4Fe-4S-S-AdoMet); via
carbonyl oxygen. {ECO:0000213|PDB:5KQR,
ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B}.
METAL 2651 2651 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000213|PDB:5KQR,
ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B}.
METAL 2652 2652 Iron-sulfur (4Fe-4S-S-AdoMet); via amide
nitrogen. {ECO:0000213|PDB:5KQR,
ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B}.
METAL 2653 2653 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000213|PDB:5KQR,
ECO:0000213|PDB:5M5B}.
METAL 2666 2666 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000213|PDB:5KQR,
ECO:0000213|PDB:5KQS,
ECO:0000213|PDB:5M5B}.
METAL 2959 2959 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2963 2963 Zinc 1; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 2968 2968 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2971 2971 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3234 3234 Zinc 2; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 3250 3250 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3369 3369 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
BINDING 396 396 Beta-D-mannose; via amide nitrogen.
{ECO:0000213|PDB:5LBV}.
BINDING 423 423 Mannose. {ECO:0000213|PDB:5LBV}.
BINDING 438 438 Fucose. {ECO:0000213|PDB:5LBV,
ECO:0000213|PDB:5LCV}.
BINDING 2544 2544 GTP. {ECO:0000213|PDB:5GOZ}.
BINDING 2548 2548 GTP. {ECO:0000213|PDB:5GOZ}.
BINDING 2576 2576 S-adenosyl-L-homocysteine.
{ECO:0000213|PDB:5GOZ,
ECO:0000213|PDB:5GP1}.
BINDING 2576 2576 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
BINDING 2606 2606 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2607 2607 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2616 2616 Succinate 1. {ECO:0000213|PDB:5GOZ}.
BINDING 2616 2616 Succinate 2. {ECO:0000213|PDB:5GOZ}.
BINDING 2624 2624 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
BINDING 2625 2625 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2651 2651 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
BINDING 2652 2652 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2666 2666 S-adenosyl-L-homocysteine.
{ECO:0000213|PDB:5GOZ,
ECO:0000213|PDB:5GP1}.
BINDING 2693 2693 Succinate 3. {ECO:0000213|PDB:5GOZ}.
BINDING 2717 2717 Succinate 4. {ECO:0000213|PDB:5GOZ}.
BINDING 2740 2740 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
CARBOHYD 444 444 N-linked (GlcNAc...).
{ECO:0000213|PDB:5H37,
ECO:0000213|PDB:5IZ7,
ECO:0000213|PDB:5LBV}.
DISULFID 293 320 {ECO:0000213|PDB:5H37,
ECO:0000213|PDB:5IZ7,
ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 350 411 {ECO:0000213|PDB:5H37,
ECO:0000213|PDB:5IZ7,
ECO:0000213|PDB:5LBS}.
DISULFID 350 406 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 364 395 {ECO:0000213|PDB:5H37,
ECO:0000213|PDB:5IRE,
ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 382 411 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 382 406 {ECO:0000213|PDB:5H37,
ECO:0000213|PDB:5IRE,
ECO:0000213|PDB:5IZ7}.
DISULFID 480 581 {ECO:0000213|PDB:5H37,
ECO:0000213|PDB:5IZ7,
ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 598 629 {ECO:0000213|PDB:5H37,
ECO:0000213|PDB:5IZ7,
ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 2556 2556 Interchain. {ECO:0000213|PDB:5MRK,
ECO:0000213|PDB:5ULP}.
SEQUENCE 3423 AA; 379113 MW; 5F0E490EE43DE346 CRC64;
MKNPKKKSGG FRIVNMLKRG VARVSPFGGL KRLPAGLLLG HGPIRMVLAI LAFLRFTAIK
PSLGLINRWG SVGKKEAMEI IKKFKKDLAA MLRIINARKE KKRRGADTSV GIVGLLLTTA
MAAEVTRRGS AYYMYLDRND AGEAISFPTT LGMNKCYIQI MDLGHMCDAT MSYECPMLDE
GVEPDDVDCW CNTTSTWVVY GTCHHKKGEA RRSRRAVTLP SHSTRKLQTR SQTWLESREY
TKHLIRVENW IFRNPGFALA AAAIAWLLGS STSQKVIYLV MILLIAPAYS IRCIGVSNRD
FVEGMSGGTW VDVVLEHGGC VTVMAQDKPT VDIELVTTTV SNMAEVRSYC YEASISDMAS
DSRCPTQGEA YLDKQSDTQY VCKRTLVDRG WGNGCGLFGK GSLVTCAKFA CSKKMTGKSI
QPENLEYRIM LSVHGSQHSG MIVNDTGHET DENRAKVEIT PNSPRAEATL GGFGSLGLDC
EPRTGLDFSD LYYLTMNNKH WLVHKEWFHD IPLPWHAGAD TGTPHWNNKE ALVEFKDAHA
KRQTVVVLGS QEGAVHTALA GALEAEMDGA KGRLSSGHLK CRLKMDKLRL KGVSYSLCTA
AFTFTKIPAE TLHGTVTVEV QYAGTDGPCK VPAQMAVDMQ TLTPVGRLIT ANPVITESTE
NSKMMLELDP PFGDSYIVIG VGEKKITHHW HRSGSTIGKA FEATVRGAKR MAVLGDTAWD
FGSVGGALNS LGKGIHQIFG AAFKSLFGGM SWFSQILIGT LLMWLGLNTK NGSISLMCLA
LGGVLIFLST AVSADVGCSV DFSKKETRCG TGVFVYNDVE AWRDRYKYHP DSPRRLAAAV
KQAWEDGICG ISSVSRMENI MWRSVEGELN AILEENGVQL TVVVGSVKNP MWRGPQRLPV
PVNELPHGWK AWGKSYFVRA AKTNNSFVVD GDTLKECPLK HRAWNSFLVE DHGFGVFHTS
VWLKVREDYS LECDPAVIGT AVKGKEAVHS DLGYWIESEK NDTWRLKRAH LIEMKTCEWP
KSHTLWTDGI EESDLIIPKS LAGPLSHHNT REGYRTQMKG PWHSEELEIR FEECPGTKVH
VEETCGTRGP SLRSTTASGR VIEEWCCREC TMPPLSFRAK DGCWYGMEIR PRKEPESNLV
RSMVTAGSTD HMDHFSLGVL VILLMVQEGL KKRMTTKIII STSMAVLVAM ILGGFSMSDL
AKLAILMGAT FAEMNTGGDV AHLALIAAFK VRPALLVSFI FRANWTPRES MLLALASCLL
QTAISALEGD LMVLINGFAL AWLAIRAMVV PRTDNITLAI LAALTPLARG TLLVAWRAGL
ATCGGFMLLS LKGKGSVKKN LPFVMALGLT AVRLVDPINV VGLLLLTRSG KRSWPPSEVL
TAVGLICALA GGFAKADIEM AGPMAAVGLL IVSYVVSGKS VDMYIERAGD ITWEKDAEVT
GNSPRLDVAL DESGDFSLVE DDGPPMREII LKVVLMTICG MNPIAIPFAA GAWYVYVKTG
KRSGALWDVP APKEVKKGET TDGVYRVMTR RLLGSTQVGV GVMQEGVFHT MWHVTKGSAL
RSGEGRLDPY WGDVKQDLVS YCGPWKLDAA WDGHSEVQLL AVPPGERARN IQTLPGIFKT
KDGDIGAVAL DYPAGTSGSP ILDKCGRVIG LYGNGVVIKN GSYVSAITQG RREEETPVEC
FEPSMLKKKQ LTVLDLHPGA GKTRRVLPEI VREAIKTRLR TVILAPTRVV AAEMEEALRG
LPVRYMTTAV NVTHSGTEIV DLMCHATFTS RLLQPIRVPN YNLYIMDEAH FTDPSSIAAR
GYISTRVEMG EAAAIFMTAT PPGTRDAFPD SNSPIMDTEV EVPERAWSSG FDWVTDHSGK
TVWFVPSVRN GNEIAACLTK AGKRVIQLSR KTFETEFQKT KHQEWDFVVT TDISEMGANF
KADRVIDSRR CLKPVILDGE RVILAGPMPV THASAAQRRG RIGRNPNKPG DEYLYGGGCA
ETDEDHAHWL EARMLLDNIY LQDGLIASLY RPEADKVAAI EGEFKLRTEQ RKTFVELMKR
GDLPVWLAYQ VASAGITYTD RRWCFDGTTN NTIMEDSVPA EVWTRHGEKR VLKPRWMDAR
VCSDHAALKS FKEFAAGKRG AAFGVMEALG TLPGHMTERF QEAIDNLAVL MRAETGSRPY
KAAAAQLPET LETIMLLGLL GTVSLGIFFV LMRNKGIGKM GFGMVTLGAS AWLMWLSEIE
PARIACVLIV VFLLLVVLIP EPEKQRSPQD NQMAIIIMVA VGLLGLITAN ELGWLERTKS
DLSHLMGRRE EGATIGFSMD IDLRPASAWA IYAALTTFIT PAVQHAVTTS YNNYSLMAMA
TQAGVLFGMG KGMPFYAWDF GVPLLMIGCY SQLTPLTLIV AIILLVAHYM YLIPGLQAAA
ARAAQKRTAA GIMKNPVVDG IVVTDIDTMT IDPQVEKKMG QVLLIAVAVS SAILSRTAWG
WGEAGALITA ATSTLWEGSP NKYWNSSTAT SLCNIFRGSY LAGASLIYTV TRNAGLVKRR
GGGTGETLGE KWKARLNQMS ALEFYSYKKS GITEVCREEA RRALKDGVAT GGHAVSRGSA
KLRWLVERGY LQPYGKVIDL GCGRGGWSYY AATIRKVQEV KGYTKGGPGH EEPMLVQSYG
WNIVRLKSGV DVFHMAAEPC DTLLCDIGES SSSPEVEEAR TLRVLSMVGD WLEKRPGAFC
IKVLCPYTST MMETLERLQR RYGGGLVRVP LSRNSTHEMY WVSGAKSNTI KSVSTTSQLL
LGRMDGPRRP VKYEEDVNLG SGTRAVVSCA EAPNMKIIGN RIERIRSEHA ETWFFDENHP
YRTWAYHGSY EAPTQGSASS LINGVVRLLS KPWDVVTGVT GIAMTDTTPY GQQRVFKEKV
DTRVPDPQEG TRQVMSMVSS WLWKELGKHK RPRVCTKEEF INKVRSNAAL GAIFEEEKEW
KTAVEAVNDP RFWALVDKER EHHLRGECQS CVYNMMGKRE KKQGEFGKAK GSRAIWYMWL
GARFLEFEAL GFLNEDHWMG RENSGGGVEG LGLQRLGYVL EEMSRIPGGR MYADDTAGWD
TRISRFDLEN EALITNQMEK GHRALALAII KYTYQNKVVK VLRPAEKGKT VMDIISRQDQ
RGSGQVVTYA LNTFTNLVVQ LIRNMEAEEV LEMQDLWLLR RSEKVTNWLQ SNGWDRLKRM
AVSGDDCVVK PIDDRFAHAL RFLNDMGKVR KDTQEWKPST GWDNWEEVPF CSHHFNKLHL
KDGRSIVVPC RHQDELIGRA RVSPGAGWSI RETACLAKSY AQMWQLLYFH RRDLRLMANA
ICSSVPVDWV PTGRTTWSIH GKGEWMTTED MLVVWNRVWI EENDHMEDKT PVTKWTDIPY
LGKREDLWCG SLIGHRPRTT WAENIKNTVN MVRRIIGDEE KYMDYLSTQV RYLGEEGSTP
GVL


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