Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]

 POLG_EBHSG              Reviewed;        2334 AA.
Q96725;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
23-MAY-2018, entry version 103.
RecName: Full=Genome polyprotein;
AltName: Full=p254;
Contains:
RecName: Full=Protein p16;
Contains:
RecName: Full=Protein p23;
Contains:
RecName: Full=NTPase;
EC=3.6.1.15;
AltName: Full=2C-like protein;
AltName: Full=P2C;
AltName: Full=p37;
Contains:
RecName: Full=Precursor p41;
Contains:
RecName: Full=Protein p29;
Contains:
RecName: Full=Protein p23/2;
Contains:
RecName: Full=Protein p18;
Contains:
RecName: Full=Viral genome-linked protein;
AltName: Full=VPg;
AltName: Full=p13;
Contains:
RecName: Full=3C-like protease;
Short=3CLpro;
EC=3.4.22.66;
AltName: Full=Calicivirin;
AltName: Full=Thiol protease P3C;
AltName: Full=p15;
Contains:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48;
AltName: Full=3Dpol;
AltName: Full=p58;
Contains:
RecName: Full=Capsid protein VP60;
ORFNames=ORF1;
European brown hare syndrome virus (strain GD)
(Ha/LV/EBHSV/GD/1989/FR) (EBHSV-GD).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Caliciviridae; Lagovirus.
NCBI_TaxID=316979;
NCBI_TaxID=9983; Lepus europaeus (European hare).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8760416;
Le Gall G., Huguet S., Vende P., Vautherot J.-F., Rasschaert D.;
"European brown hare syndrome virus: molecular cloning and sequencing
of the genome.";
J. Gen. Virol. 77:1693-1697(1996).
-!- FUNCTION: NTPase presumably plays a role in replication.
{ECO:0000250}.
-!- FUNCTION: Viral genome-linked protein is covalently linked to the
5'-end of the positive-strand, negative-strand genomic RNAs and
subgenomic RNA. Acts as a genome-linked replication primer. May
recruit ribosome to viral RNA thereby promoting viral proteins
translation (By similarity). {ECO:0000250}.
-!- FUNCTION: 3C-like protease processes the polyprotein: 3CLpro-RdRp
(p72) is first released by autocleavage, then all other proteins
are cleaved. {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase replicates genomic and
antigenomic RNA by recognizing replications specific signals.
Transcribes also a subgenomic mRNA by initiating RNA synthesis
internally on antigenomic RNA. This sgRNA codes for structural
proteins. Catalyzes the covalent attachment VPg with viral RNAs
(By similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- FUNCTION: Capsid protein VP60 self assembles to form an
icosahedral capsid with a T=3 symmetry, about 35 nm in diameter,
and consisting of 180 capsid proteins. A smaller form of capsid
with a diameter of 23 nm might be capsid proteins assembled as
icosahedron with T=1 symmetry. The capsid encapsulate VP2 proteins
and genomic or subgenomic RNA. Attaches virion to target cells by
binding histo-blood group antigens, inducing endocytosis of the
viral particle. Acidification of the endosome induces
conformational change of capsid protein thereby injecting virus
genomic RNA into host cytoplasm (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: Endopeptidase with a preference for cleavage
when the P1 position is occupied by Glu-|-Xaa and the P1' position
is occupied by Gly-|-Yaa.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBUNIT: Binds to histo-blood group antigens at surface of target
cells. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP60: Virion. Host cytoplasm
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=Genome polyprotein;
IsoId=Q96725-1; Sequence=Displayed;
Note=Produced from the genomic RNA.;
Name=Subgenomic capsid protein VP60; Synonyms=VP1;
IsoId=Q96725-2; Sequence=VSP_034377;
Note=Produced from the subgenomic RNA.;
-!- PTM: Specific enzymatic cleavages by its own cysteine protease
yield mature proteins. The protease cleaves itself from the
nascent polyprotein autocatalytically. Precursor p41 can be
cleaved by viral 3CLpro into protein p19 and VPg, or cleaved by
host protease into protein p23/2 and protein p18 (By similarity).
{ECO:0000250}.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
attached to the 5'-end of the polyadenylated genomic and
subgenomic RNAs. This uridylylated form acts as a nucleotide-
peptide primer for the polymerase (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: Two different RNAs lead the expression of the
capsid protein. One arises from the cleavage of the polyprotein
translated from the genomic RNA and the other from the translation
of a subgenomic RNA derived from the (-)RNA template. Capsid
protein expressed from the subgenomic mRNA is produced in much
larger amounts than the cleaved one (By similarity).
{ECO:0000250}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; Z69620; CAA93445.1; -; Genomic_RNA.
EMBL; Z32526; -; NOT_ANNOTATED_CDS; Genomic_RNA.
RefSeq; NP_068828.1; NC_002615.1.
ProteinModelPortal; Q96725; -.
SMR; Q96725; -.
MEROPS; C24.001; -.
PRIDE; Q96725; -.
GeneID; 912265; -.
KEGG; vg:912265; -.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; 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:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
CDD; cd00205; rhv_like; 1.
Gene3D; 2.60.120.20; -; 1.
InterPro; IPR004005; Calicivirus_coat.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000317; Peptidase_C24.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR029053; Viral_coat.
Pfam; PF00915; Calici_coat; 1.
Pfam; PF03510; Peptidase_C24; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00910; RNA_helicase; 1.
PRINTS; PR00916; 2CENDOPTASE.
PRINTS; PR00918; CALICVIRUSNS.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
3: Inferred from homology;
Alternative promoter usage; ATP-binding; Capsid protein;
Covalent protein-RNA linkage; Disulfide bond; Helicase;
Host cytoplasm; Hydrolase; Nucleotide-binding; Nucleotidyltransferase;
Phosphoprotein; Protease; RNA-directed RNA polymerase; Thiol protease;
Transferase; Viral RNA replication; Virion.
CHAIN 1 2334 Genome polyprotein.
/FTId=PRO_0000341986.
CHAIN 1 138 Protein p16. {ECO:0000250}.
/FTId=PRO_0000036986.
CHAIN 139 334 Protein p23. {ECO:0000250}.
/FTId=PRO_0000036987.
CHAIN 335 711 NTPase. {ECO:0000250}.
/FTId=PRO_0000036988.
CHAIN 712 1108 Precursor p41.
/FTId=PRO_0000341987.
CHAIN 712 986 Protein p29. {ECO:0000250}.
/FTId=PRO_0000036989.
CHAIN 712 929 Protein p23/2.
/FTId=PRO_0000341988.
CHAIN 930 1101 Protein p18.
/FTId=PRO_0000341989.
CHAIN 987 1101 Viral genome-linked protein.
{ECO:0000250}.
/FTId=PRO_0000036990.
CHAIN 1102 1244 3C-like protease. {ECO:0000250}.
/FTId=PRO_0000036991.
CHAIN 1245 1760 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000036992.
CHAIN 1761 2334 Capsid protein VP60. {ECO:0000250}.
/FTId=PRO_0000036994.
DOMAIN 487 647 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1113 1211 Peptidase C24.
DOMAIN 1488 1612 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
ACT_SITE 1128 1128 For 3CLpro activity. {ECO:0000250}.
ACT_SITE 1152 1152 For 3CLpro activity. {ECO:0000250}.
ACT_SITE 1205 1205 For 3CLpro activity. {ECO:0000255}.
SITE 138 139 Cleavage; by 3CLpro. {ECO:0000250}.
SITE 334 335 Cleavage; by 3CLpro. {ECO:0000250}.
SITE 711 712 Cleavage; by 3CLpro. {ECO:0000250}.
SITE 929 930 Cleavage; by host. {ECO:0000250}.
SITE 986 987 Cleavage; by 3CLpro. {ECO:0000250}.
SITE 1101 1102 Cleavage; by 3CLpro. {ECO:0000250}.
SITE 1244 1245 Cleavage; by 3CLpro. {ECO:0000250}.
SITE 1760 1761 Cleavage; by 3CLpro. {ECO:0000250}.
MOD_RES 1007 1007 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
DISULFID 1577 1584 {ECO:0000250}.
VAR_SEQ 1 1758 Missing (in isoform Subgenomic capsid
protein VP60). {ECO:0000305}.
/FTId=VSP_034377.
SEQUENCE 2334 AA; 255925 MW; 3865CFA2457C0FB6 CRC64;
MAVASRPCGV ATSVLPAKKP LSFFTDLVGK TPPRCIRAPH TLAWPVFADL DNEEESPEIC
RKCGKYANGF GVFDLTDLGD VCLCSIRPQR HVGGPCCLCN KQYIRACGRY CARVLKHYKA
FNKVIPCLHS RQVKPVFEGE VEDLFVELGA PTRMNFTEAE LASQGASIMD RFVDLVEPCL
STEDSNFLDN ICSDASIRKR LEDEYDVDMI AAARARKDFA KTLKLALQDR ERKPDKWYSK
LGCITTKGRQ WAKKVVHGAK KLSDPLKTLA AILLVALHNC VAVDTTTMLS HFKPVNLLAI
LLDWTNDLPG FLTTLIRFME LYGVVQSTVN LVVDAIKSFW DRVMCATERC CDLLKRLFDK
FEDSVPTGPT AGCLIFMSFV FSVIVGYLPN NSVISTFMKG AGKLTTFAGV IGAIRTLWIT
INQHMVAKDI TSIQEKVMAV VKMANEAATL NQLEIVSVLC SELESTLTNR CTLPSYNQHM
GVLNAAQKVV ADIHTLVLGK INMTKQRPQP VAVVFKGAPG IGKTYLVHRL AKDLGCPHPS
NINFGLDHFD SYTGEDVAIA DEFNTSGDER WVELFIQMVN TNPCPLNCDK VENKNKVFSS
KYLLCTTNSS MVLNATHPRA TAFYRRVIIV DVRNKAVEGW QSTRHGSKPG KHCYTKDMSH
LTFQVYPHNM PAPGFVFVGE KLVKSQVAPR ELKYNELLDM IKNEHPDANF EGATKHEFVY
PDVQYEQALL MWKQYFLMYG CTARLAKVFV DDIPYNQVHV ARKSDPRSPG AVHHECELKY
IWRMVPHFAL GCVNMTNQLG TDLTQSQLDR ITCGVEGITV TTVDNILPFH SQNTLINPSF
LKLIWALRRH LRGLRGITQV ATFIWKVMCN PVCAYDTLIR TLTGAATFSE DPVTTTIVCP
NCTIQIHTCG GLLVRYSGDP APVASDNVDR GNQGIDCLTN PNLIAGFSWR QIADLFSTVM
TSLCNNHLVN LATMAAIGAV ATKALQGVKG KTKRGRGARI NLGNDEYDEW QQMRREFNNA
HDMTAEEFLE LRNRAAMGSD DADAIKFRSW WTNRQLRQDE AHVTVVGKGG VRNEVIRTRV
RNAPKGPRTL DDGGFYDNDY EGLPGYLRFN GSGWMIHIGN GMYLSNTHTA RSSCSEIVTC
SPTTDLCLVK AEPIRSVAQI AEGTPVRDWK RASITTYGLK KTFSDSTKID VLAYDGPTQT
THGDCGLPLF DEAGKVVAIH TGKLLGFSKM CTLIDCTITK GVYENTDLFC GDPIDYRGLV
AFRVAGVEPR PPVSGTRYAK VPGVPEEYHT GYRPANLGRG DPDSHCTLMN IAVKNLQVYQ
QEPKLTKVDT FIERAAADVL GFLRFLTKGE RQMNLNFSAA FNVLDLSTSC GPFVPGKKID
HVKDGKLDEV LSKHLYKCWS VANSGKALHH VYACGLKDEL RPLDKVKEGK KRLLWGCNVG
VALCAAAVFH NLCFKLKTVA RFGPIAVGID MTSRDVDVMI TQLTSKAGDF LCLDYSKWDS
TMSPCVVRLA IDILADCCEQ TELTKSVVLT LKSLPMTVLD AMIVPTKRGL PSGMPFTSVI
NSICHWLLWS AAVYKACDEI GLFCSNLYED APFFVYGDDG VYAMTPMMVS LLPAILDNLR
DYGLSPTAAD KTEFIDVCPL KDISFLKRKF VMSELGWLSQ LDRSSILRQL EWTKTAKRHM
CIEECSELDK DERGVQLEEL QIHAAAHGEE FFELVKKELR RQQAFTRFSV FDYQTARKTL
GDRKRIVSVV PDDSFVNVME GKPRADAPGT ATTASVPGTT TDGMDPGVVA STDVVTADNV
AASVATAGIG GPPQQASPQE SWRVNFFYND VFTWSVTDAP GSILYTVQHS PQNNPFTQVL
SQMYAGWAGG MQFRFIVAGS GIFGGRLVCA IIPPGIQIQP GLEVRQFPHV VIDARSLEPV
TITMPDLRPE MYHPTGNPGL VPTLVVSVYN NLINPFGGTT SAIQVTVETR PSEDFEFVLI
RAPSSKTVDS VNPSWLLTTP VLTGAGSDNR WGAPIVGLQP VPGGFSTSNR HWNMNGETYG
WSSPRFDDID HPSGNVSYPS GSATNTIETW YANAGTATTN PISNIAPDGF PDMGAIPFSG
TTIPTGAWVG FGQVWNASNG TPYVGTVQAY ELGFANGAPS SIRPVTTTTG AQLVAKSIYG
VAIAQNQTSA GIIFLSKGMV STPGVAATTY TPQPSAIVTT PGTPVAAPIG KNTPIMFSAV
VRRTGDVNAG PGSANGTQYG VGSQPLSVTL GLSLTNYSSA LQPGQFFVWQ LNFASGFMEV
GMNTDGYFYA GTGAYSGMID LTDLIDVRPV GVRPNTSTLV FNLAGVATTG YSYV


Related products :

Catalog number Product name Quantity
18-272-197027 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.1 mg
18-272-197028 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.1 mg
18-272-197033 Amyloid Precursor Protein - Goat polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 P 0.05 ml
18-272-197032 Amyloid Precursor Protein - Goat polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 P 0.05 ml
18-272-195345 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.05 ml
18-272-195346 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.05 ml
18-272-196327 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.5 ml
20-272-190769 Amyloid Precursor Protein - Mouse monoclonal [3E9] to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; 0.05 mg
18-272-196328 Amyloid Precursor Protein prediluted - Rabbit polyclonal to Amyloid Precursor Protein prediluted; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin- 7 ml
EIAAB35745 A34.5,Anti-sense to ERCC-1 protein,Ase1,ASE-1,Cd3eap,CD3E-associated protein,CD3-epsilon-associated protein,DNA-directed RNA polymerase I subunit RPA34,Mouse,Mus musculus,Paf49,RNA polymerase I-associ
EIAAB35359 BLAP75,BLM-associated protein of 75 kDa,C9orf76,FAAP75,Homo sapiens,Human,RecQ-mediated genome instability protein 1,RMI1
EIAAB35365 BLAP18,BLM-associated protein of 18 kDa,C16orf75,Homo sapiens,hRMI2,Human,RecQ-mediated genome instability protein 2,RMI2
18-661-15141 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.1 mg
18-001-30061 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.1 mg
18-003-42864 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.05 mg Aff Pur
EIAAB35746 A34.5,Antisense to ERCC-1 protein,ASE1,ASE-1,CAST,CAST,CD3EAP,CD3E-associated protein,CD3-epsilon-associated protein,DNA-directed RNA polymerase I subunit RPA34,Homo sapiens,Human,PAF49,RNA polymerase
25-375 This protein is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by t 0.05 mg
EIAAB45903 ERVK6,HERV-K(C7) Pro protein,HERV-K(HML-2.HOM) Pro protein,HERV-K_7p22.1 provirus ancestral Pro protein,HERV-K108 Pro protein,Homo sapiens,Human,PR,Protease,Proteinase
28-544 MCM7 encodes a protein that is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-533 MCM3 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein complex formed by MCM protein 0.05 mg
28-534 MCM3 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein complex formed by MCM protein 0.05 mg
28-535 The protein encoded by MCM2 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein comple 0.1 mg
28-536 The protein encoded by MCM4 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-539 MCM7 encodes a protein that is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-540 MCM7 encodes a protein that is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
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
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






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
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur