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Genome polyprotein

 Q8B454_9FLAV            Unreviewed;      3413 AA.
Q8B454;
01-MAR-2003, integrated into UniProtKB/TrEMBL.
10-FEB-2009, sequence version 2.
05-DEC-2018, entry version 105.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684};
Tick-borne encephalitis virus.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=11084 {ECO:0000313|EMBL:AAN87009.2, ECO:0000313|Proteomes:UP000157254};
[1] {ECO:0000313|EMBL:AAN87009.2, ECO:0000313|Proteomes:UP000157254}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Primorye-332 {ECO:0000313|EMBL:AAN87009.2};
PubMed=15164719;
Leonova G.N., Belikov S.I., Kulakova N.V., Pavlenko E.V.,
Borisevich V.G.;
"[Molecular typing of the tick-borne encephalitis virus isolated from
patients with different-infection severities in the south of Russia's
Far East].";
Mol. Genet. Mikrobiol. Virusol. 2:32-37(2004).
[2] {ECO:0000313|EMBL:AAN87009.2, ECO:0000313|Proteomes:UP000157254}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Primorye-332 {ECO:0000313|EMBL:AAN87009.2};
Belikov S.I., Leonova G.N., Kondratov I.G., Romanova E.V.,
Pavlenko E.V.;
"Coding Nucleotide Sequences of Tick-Borne Encephalitis Virus Strains
Isolated from Human Blood without Clinical Symptoms of Infection.";
Russ. J. Genet. 46:315-322(2010).
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
Evidence={ECO:0000256|SAAS:SAAS00368577};
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
Evidence={ECO:0000256|SAAS:SAAS00368620};
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
ChEBI:CHEBI:83400; Evidence={ECO:0000256|SAAS:SAAS00383097};
-!- SUBCELLULAR LOCATION: Host cytoplasm
{ECO:0000256|SAAS:SAAS00937464}. Host endoplasmic reticulum
{ECO:0000256|SAAS:SAAS00941764}. Virion membrane
{ECO:0000256|SAAS:SAAS00980400}; Multi-pass membrane protein
{ECO:0000256|SAAS:SAAS00980400}.
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EMBL; AY169390; AAN87009.2; -; Genomic_RNA.
Proteomes; UP000157254; Genome.
GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
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: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: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: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:0039503; P:suppression by virus of host innate immune response; 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; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_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; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
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; IPR038688; Flavi_propep_sf.
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; IPR038055; Glycoprot_E_dimer_dom.
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; 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.
4: Predicted;
Activation of host autophagy by virus {ECO:0000256|SAAS:SAAS00445756};
ATP-binding {ECO:0000256|SAAS:SAAS00058020};
Capsid protein {ECO:0000256|SAAS:SAAS00969288};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000157254};
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};
Helicase {ECO:0000256|SAAS:SAAS00058020};
Host cytoplasm {ECO:0000256|SAAS:SAAS00936979};
Host membrane {ECO:0000256|SAAS:SAAS00445977};
Host-virus interaction {ECO:0000256|SAAS:SAAS00445756,
ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00941647};
Hydrolase {ECO:0000256|SAAS:SAAS00058020};
Inhibition of host innate immune response by virus
{ECO:0000256|SAAS:SAAS00941647};
Membrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAAS:SAAS00445977, ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000256|PIRSR:PIRSR003817-4,
ECO:0000256|SAAS:SAAS00940329};
Methyltransferase {ECO:0000256|SAAS:SAAS00817755};
Nucleotide-binding {ECO:0000256|SAAS:SAAS00058020};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00510600};
RNA-binding {ECO:0000256|SAAS:SAAS00076745};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00510600};
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:SAAS00941647};
Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00489633};
Viral RNA replication {ECO:0000256|SAAS:SAAS01108918};
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 101 118 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 727 748 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 755 775 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1164 1182 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1236 1256 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1295 1313 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1325 1347 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1384 1402 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1452 1479 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2159 2183 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2195 2221 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2242 2258 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2296 2314 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2343 2362 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2368 2386 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 1356 1487 FLAVIVIRUS_NS2B.
{ECO:0000259|PROSITE:PS51527}.
DOMAIN 1489 1668 Peptidase S7.
{ECO:0000259|PROSITE:PS51528}.
DOMAIN 1674 1830 Helicase ATP-binding.
{ECO:0000259|PROSITE:PS51192}.
DOMAIN 1840 1999 Helicase C-terminal.
{ECO:0000259|PROSITE:PS51194}.
DOMAIN 2511 2775 MRNA cap 0-1 NS5-type MT.
{ECO:0000259|PROSITE:PS51591}.
DOMAIN 3039 3188 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
COILED 2778 2798 {ECO:0000256|SAM:Coils}.
ACT_SITE 1542 1542 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1566 1566 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1626 1626 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
METAL 2949 2949 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2953 2953 Zinc 1; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 2958 2958 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2961 2961 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3223 3223 Zinc 2; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 3239 3239 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3358 3358 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
DISULFID 282 309 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 339 395 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 353 384 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 371 400 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 465 569 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 586 617 {ECO:0000256|PIRSR:PIRSR003817-3}.
SEQUENCE 3413 AA; 377871 MW; 708FF53A072D9304 CRC64;
MAGKAILKGK GGGPPRRVSK ETAKKTRQSR VRMPNGLVLM RMMGILWHAV AGTARSPVLK
SFWNSVPLRQ ATAALRKIKK AVSTLMVGLQ RRGKRRSAVN WTGWLLVVVL GVTLAATVRK
ERDGTTVIRA EGKDAATQVR VENGTCVILV TDMGSWCDDS LTYECVTIDQ GEEPVDVDCF
CRNVDGVYLE YGRCGKQEGS RTRRSVLIPS HAQGDLTGRG HKWLEGDSLR THLTRVEGWV
WKNKVLTLAV IAVVWLTVES VVTRVVVVVV LLCLAPVYAS RCTHLENRDF VTGTQGTTRV
TLVLELGGCV TITAEGKPSM DVWLDSIYQE NPAKTREYCL HAKLSDTKVA ARCPTMGPAT
LAEEHQSGTV CKRDQSDRGW GNHCGLFGKG SIVTCVKASC EAKKKATGHV YDANKIVYTV
KVEPHTGDYV AANETHSGRK TASFTVSSEK TILTMGDYGD VSLLCRVASG VDLAQTVILE
LDKTSEHLPT AWQVHRDWFN DLALPWKHEG AQNWNNAERL VEFGAPHAVK MDVYNLGDQT
GVLLKSLAGV PVAHIDGTKY HLKSGHVTCE VGLEKLKMKG LTYTMCDKTK FTWKRIPTDS
GHDTVVMEVA FSGTKPCRIP VRAVAHGSPD VNVAMLITPN PTIENNGGGF IEMQLPPGDN
IIYVGELSHQ WFQKGSSIGR VFQKTRKGIE RLTVIGEHAW DFGSTGGLLT SVGKALHTVL
GGAFNSLFGG VGFLPKILVG VALAWLGLNM RNPTMSMSFL LAGGLVLAMT LGVGADVGCA
VDTERMELRC GEGLVVWREV SEWYDNYAFY PETPGALASA IKETFEEGTC GIVPQNRLEM
AMWRSSATEL NLALAEGDAN LTVVVDKLDP TDYRGGIPGL LKKGKDIKVS WKSWGHSMIW
SVPEAPRRFM VGTEGGSECP LERRKTGVFT VAEFGVGLRT KVFLDFRQES THECDTGVMG
AAVKNGMAVH TDQSLWMKSV RNDTGTYIVE LLVTDLRNCS WPASHTIDNA EVVDSELFLP
ASLAGPRSWY NRIPGYSEQV KGPWKYSPIR VTREECPGTR VTINADCDKR GASVRSTTES
GKVIPEWCCR TCTLPPVTFR TGTDCWYAME IRPVHDQGGL VRSMVVADNG ELLSEGGIPG
IVALFVVLEY VIRRRPATGT TAMWGGIVVL ALLVTGLVRI ESLVRYVVAV GITFHLELGP
EIVALTLLQA VFELRVGLLS AFALRSNLTV REMVTIYFLL LVLELGLPSE GLGALWKWGD
ALAMGALIFR ACTAEEKTGV GLLLMALMTQ QDLAIAHYGL MLFLGVASCC SIWKLIRGHR
EQKGLTWIVP LAGLLGGEGS GVRLLAFWEL AIHGRRRSFS EPLTVVGVML TLASGMMRHT
SQEALCALAV ASFLLLMLVL GTRKMQLVAE WSGCVEWHPE LMNEGGEVSL RVRQDSMGNF
HLTELEKEER VMAFWLLAGL AASAVHWSGI LGVMGLWTLS EMLRTARRSD LVFSGQGGRE
RGDKPFEVKD GVYRIFSPGL LWGQRQVGVG YGFKGVLHTM WHVTRGAALS IDDAVAGPYW
ADVKEDVVCY GGAWSLEEKW KGETVQVHAF PPGRAHEVHQ CQPGELLLDT GRRIGAVPID
LAKGTSGSPI LNSQGVVVGL YGNGLKTNET YVSSIAQGEA EKSRPNLPPA VIGTGWTAKG
QITVLDMHPG SGKTHRVLPE LIRQCIDRRL RTLVLAPTRV VLKEMERALN GKRVRFHSPA
VGDQQVGGAI VDVMCHATYV NRRLLPQGRQ NWEVAIMDEA HWTDPHSIAA RGHLYTLAKE
NKCALVLMTA TPPGKSEPFP ESNGAISSEE KQIPDGEWRD GFDWITEYEG RTAWFVPSIA
KGGIIARTLR QKGKSVICLN SKTFEKDYSR VRDEKPDFVV TTDISEMGAN LDVSRVIDGR
TNIKPEEVDG RVELTGTRRV TTASAAQRRG RVGRQEGRTD EYIYSGQCDD DDSGLVQWKE
AQILLDNITT LRGPVATFYG PEQDKMPEVA GHFRLTEEKR KHFRHLLTHC DFTPWLAWHV
AANVSSVTSR NWTWEGPEEN TVDEANGDLV TFRSPNGAER TLKPVWRDAR MFREGRDIRE
FVAYASGRRS FGDVLSGMSG VPELLRHRCV SAMDVFYTLM HEEPGSRAMR MAERDAPEAF
LTVVEMMVLG LATLGVVWCF VVRTSISRMM LGTLVLLASL ALLWAGGVSY GNMAGVALIF
YTLLTVLQPE AGKQRSSDDN KLAYFLLTLC SLAGLVAANE MGFLEKTKAD LSTVLWSEHE
ELRSWEEWTN IDIQPARSWG TYVLVVSLFT PYIIHQLQTK IQQLVNSAVA TGAQAMRDLG
GGAPFFGVAG HVVALGVVSL VGATPTSLVV GVGLAAFHLA IVVSGLEAEL TQRAHKVFFS
AMVRNPMVDG DVINPFGEGE AKPALYERKM SLVLAIALCL MSVVMNRTVP SITEASAVGL
AAAGQLLRPE VDTLWTMPVA CGLSGVVRGS LWGFLPLGHR LWLRASGSRR GGSEGDTLGD
LWKRKLNGCT KEEFFAYRRT GILETERDKA RELLRRGETN MGLAVSRGTA KLAWLEERGY
ATLKGEVVDL GCGRGGWSYY AASRPAVMSV KAYTIGGKGH ETPKMVTSLG WNLIKFRAGM
DVFSMQPHRA DTIMCDIGES NPDAVVEGER TRKVILLMEQ WKNRNPTATC VFKVLAPYRP
EVIEALHRFQ LQWGGGLVRT PFSRNSTHEM YYSTAVTGNI VNSVNIQSRK LLARFGDQRG
PTRVPELDLG VGTRCVVLAE DKVKEKDVQE RISALREQYG ETWHMDREHP YRTWQYWGSY
RTAPTGSAAS LINGVVKLLS WPWNAREDVV RMAMTDTTAF GQQRVFKEKV DTKAQEPQPG
TKVIMRAVND WILERLARKS KPRMCSREEF IAKVKSNAAL GAWSDEQNRW SSAKEAVEDP
AFWQLVDEER ERHLAGRCAH CVYNMMGKRE KKLGEFGVAK GSRAIWYMWL GSRFLEFEAL
GFLNEDHWAS RGSSGSGVEG ISLNYLGWYL KGLSILEGGL FYADDTAGWD TKVTNADLED
EEQLLRYMEG EHRQLAATIM QKAYHAKVVK VARPSRDGGC IMDVITRRDQ RGSGQVVTYA
LNTLTNIKVQ LIRMMEGEGV IEATDAHNPR LLRVERWLRD HGEERLGRML VSGDDCVVRP
VDDRFSKALY FLNDMAKTRK DVGEWEHSVG FSNWEEVPFC SHHFHELVMK DGRSLIVPCR
DQDELVGRAR VSPGCGWSVR ETACLSKAYG QMWLLSYFHR RDLRTLGLAI CSAVPVDWVP
TGRTTWSIHA SGAWITTEDM LDVWNRVWIL DNPFMHSKEK IAEWRDVPYL PKSHDMLCSS
LVGRKERAEW AKNIWGAVEK VRKMIGQEKC KDYPSCMDRH DLHWELKLES SII


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Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
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Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
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IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
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BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
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TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

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GENTAUR Italy
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Piazza Giacomo Matteotti, 6
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Fax 02 36 00 65 94
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