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 RPOA_PRRSB              Reviewed;        3961 AA.
Q8B912; Q8B911;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 3.
25-OCT-2017, entry version 99.
RecName: Full=Replicase polyprotein 1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Nsp1;
EC=3.4.22.-;
Contains:
RecName: Full=Nsp1-alpha papain-like cysteine proteinase;
EC=3.4.22.-;
AltName: Full=PCP1-alpha;
Contains:
RecName: Full=Nsp1-beta papain-like cysteine proteinase;
EC=3.4.22.-;
AltName: Full=PCP1-beta;
Contains:
RecName: Full=Nsp2 cysteine proteinase;
EC=3.4.19.12;
EC=3.4.22.-;
AltName: Full=CP2;
Short=CP;
Contains:
RecName: Full=Non-structural protein 3;
Short=Nsp3;
Contains:
RecName: Full=3C-like serine proteinase;
Short=3CLSP;
EC=3.4.21.-;
AltName: Full=Nsp4;
Contains:
RecName: Full=Non-structural protein 5-6-7;
Short=Nsp5-6-7;
Contains:
RecName: Full=Non-structural protein 5;
Short=Nsp5;
Contains:
RecName: Full=Non-structural protein 6;
Short=Nsp6;
Contains:
RecName: Full=Non-structural protein 7-alpha;
Short=Nsp7-alpha;
Contains:
RecName: Full=Non-structural protein 7-beta;
Short=Nsp7-beta;
Contains:
RecName: Full=Non-structural protein 8;
Short=Nsp8;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=Nsp9;
Contains:
RecName: Full=Helicase;
Short=Hel;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=Nsp10;
Contains:
RecName: Full=Non-structural protein 11;
Short=Nsp11;
Contains:
RecName: Full=Non-structural protein 12;
Short=Nsp12;
Name=rep; ORFNames=1a-1b;
Porcine reproductive and respiratory syndrome virus (strain HB-1)
(PRRSV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Arteriviridae; unclassified Arteriviridae.
NCBI_TaxID=300563;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15221535; DOI=10.1007/s00705-004-0292-0;
Gao Z.Q., Guo X., Yang H.C.;
"Genomic characterization of two Chinese isolates of porcine
respiratory and reproductive syndrome virus.";
Arch. Virol. 149:1341-1351(2004).
-!- FUNCTION: The replicase polyprotein 1ab is a multifunctional
protein: it contains the activities necessary for the
transcription of negative stranded RNA, leader RNA, subgenomic
mRNAs and progeny virion RNA as well as proteinases responsible
for the cleavage of the polyprotein into functional products.
-!- FUNCTION: Nsp1 is essential for viral subgenomic mRNA synthesis.
{ECO:0000250}.
-!- FUNCTION: Nsp1-alpha inhibits IFN-beta production. Counteracts the
action of NF-kappaB by decreasing the phosphorylation of IkappaB-
alpha, such that the degradation of IkappaB-alpha is suppressed.
This leads to the blockage of NF-kappaB nuclear translocation and
thus interference of NF-kappaB activation. Also seems to inhibit
IRF3-dependent pathways (By similarity). {ECO:0000250}.
-!- FUNCTION: Nsp2 cysteine proteinase which cleaves the nsp2/nsp3
site in the polyprotein. Also displays deubiquitinating and
deISGylase activities. The deubiquitinating activity cleaves both
ubiquitinated and ISGylated products and may therefore regulate
ubiquitin and ISG15 dependent host innate immunity.
Deubiquitinates host NFKBIA, thereby interfering with NFKBIA
degradation and impairing subsequent NF-kappa-B activation (By
similarity). {ECO:0000250}.
-!- FUNCTION: The 3C-like serine proteinase chain is responsible for
the majority of cleavages as it cleaves the C-terminus of the
polyprotein. {ECO:0000250}.
-!- FUNCTION: The helicase chain, which contains a zinc finger
structure, displays RNA and DNA duplex-unwinding activities with
5' to 3' polarity. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
-!- SUBCELLULAR LOCATION: Nsp1: Host nucleus {ECO:0000250}. Host
cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nsp1-alpha papain-like cysteine proteinase:
Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nsp1-beta papain-like cysteine proteinase:
Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nsp2 cysteine proteinase: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 5-6-7: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: 3C-like serine proteinase: Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase: Host cytoplasm,
host perinuclear region {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Helicase: Host cytoplasm, host perinuclear
region {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=Q8B912-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=Q8B912-2; Sequence=VSP_032891;
Note=Produced by conventional translation.;
-!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
association of the replication complex and thereby alter the
architecture of the host cell membrane. {ECO:0000250}.
-!- DOMAIN: The OTU-like region is responsible for the
deubiquitinating and deISGylation activities of Nsp2.
{ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases
yield mature proteins. Nsp1 is autocleaved into two subunits,
Nsp1-alpha and Nsp1-beta. There are two alternative pathways for
processing. Either nsp4-5 is cleaved, which represents the major
pathway or the nsp5-6 and nsp6-7 are processed, which represents
the minor pathway. The major pathway occurs when nsp2 acts as
cofactor for nsp4 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the arteriviridae polyprotein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAN73221.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY150312; AAN73220.1; -; mRNA.
EMBL; AY150312; AAN73221.1; ALT_INIT; mRNA.
SMR; Q8B912; -.
Proteomes; UP000124990; Genome.
GO; GO:0033644; C:host cell 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; 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:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IEA:UniProtKB-KW.
GO; GO:0039644; P:suppression by virus of host NF-kappaB transcription factor activity; IEA:UniProtKB-KW.
GO; GO:0039563; P:suppression by virus of host STAT1 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:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR031932; Arteri_nsp7a.
InterPro; IPR008743; Arterivirus_Nsp2_C33.
InterPro; IPR023338; Arterivirus_NSP4_peptidase.
InterPro; IPR008741; AV_PCPalpha.
InterPro; IPR025773; AV_PCPbeta.
InterPro; IPR027355; AV_ZBD.
InterPro; IPR008760; EAV_peptidase_S32.
InterPro; IPR037227; EndoU-like.
InterPro; IPR032855; NSP2-B_epitope.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR032785; Pdase_C33_assoc.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF16749; Arteri_nsp7a; 1.
Pfam; PF14757; NSP2-B_epitope; 1.
Pfam; PF14756; Pdase_C33_assoc; 1.
Pfam; PF05410; Peptidase_C31; 1.
Pfam; PF05411; Peptidase_C32; 1.
Pfam; PF05412; Peptidase_C33; 1.
Pfam; PF05579; Peptidase_S32; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF01443; Viral_helicase1; 1.
SUPFAM; SSF142877; SSF142877; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51538; AV_CP; 1.
PROSITE; PS51493; AV_NSP4_PRO; 1.
PROSITE; PS51539; AV_PCP_ALPHA; 1.
PROSITE; PS51540; AV_PCP_BETA; 1.
PROSITE; PS51652; AV_ZBD; 1.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Helicase; Host cytoplasm;
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 ISG15 by virus;
Inhibition of host NF-kappa-B by virus;
Inhibition of host STAT1 by virus; Membrane; Metal-binding;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase; Protease;
Reference proteome; Ribosomal frameshifting;
RNA-directed RNA polymerase; Serine protease; Thiol protease;
Transferase; Transmembrane; Transmembrane helix; Viral immunoevasion;
Viral RNA replication; Zinc; Zinc-finger.
CHAIN 1 3961 Replicase polyprotein 1ab.
/FTId=PRO_0000036670.
CHAIN 1 382 Nsp1. {ECO:0000250}.
/FTId=PRO_0000410827.
CHAIN 1 180 Nsp1-alpha papain-like cysteine
proteinase. {ECO:0000255}.
/FTId=PRO_0000036672.
CHAIN 181 383 Nsp1-beta papain-like cysteine
proteinase. {ECO:0000250}.
/FTId=PRO_0000036673.
CHAIN 384 1579 Nsp2 cysteine proteinase. {ECO:0000250}.
/FTId=PRO_0000036674.
CHAIN 1580 1809 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000036675.
CHAIN 1810 2013 3C-like serine proteinase. {ECO:0000250}.
/FTId=PRO_0000036676.
CHAIN 2014 2458 Non-structural protein 5-6-7.
{ECO:0000250}.
/FTId=PRO_0000036677.
CHAIN 2014 2183 Non-structural protein 5. {ECO:0000250}.
/FTId=PRO_0000423122.
CHAIN 2184 2199 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000423123.
CHAIN 2200 2348 Non-structural protein 7-alpha.
{ECO:0000250}.
/FTId=PRO_0000423124.
CHAIN 2349 2458 Non-structural protein 7-beta.
{ECO:0000250}.
/FTId=PRO_0000423125.
CHAIN 2459 3144 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000036678.
CHAIN 2459 2503 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000036679.
CHAIN 3145 3585 Helicase. {ECO:0000250}.
/FTId=PRO_0000036680.
CHAIN 3586 3808 Non-structural protein 11. {ECO:0000250}.
/FTId=PRO_0000036681.
CHAIN 3809 3961 Non-structural protein 12. {ECO:0000250}.
/FTId=PRO_0000036682.
TRANSMEM 1266 1286 Helical. {ECO:0000255}.
TRANSMEM 1296 1316 Helical. {ECO:0000255}.
TRANSMEM 1368 1388 Helical. {ECO:0000255}.
TRANSMEM 1583 1603 Helical. {ECO:0000255}.
TRANSMEM 1648 1668 Helical. {ECO:0000255}.
TRANSMEM 1685 1705 Helical. {ECO:0000255}.
TRANSMEM 1719 1739 Helical. {ECO:0000255}.
TRANSMEM 2036 2056 Helical. {ECO:0000255}.
TRANSMEM 2060 2080 Helical. {ECO:0000255}.
TRANSMEM 2092 2112 Helical. {ECO:0000255}.
TRANSMEM 2137 2157 Helical. {ECO:0000255}.
TRANSMEM 2162 2182 Helical. {ECO:0000255}.
DOMAIN 69 180 Peptidase C31. {ECO:0000255|PROSITE-
ProRule:PRU00872}.
DOMAIN 263 383 Peptidase C32. {ECO:0000255|PROSITE-
ProRule:PRU00873}.
DOMAIN 428 535 Peptidase C33. {ECO:0000255|PROSITE-
ProRule:PRU00871}.
DOMAIN 1810 2013 Peptidase S32. {ECO:0000255|PROSITE-
ProRule:PRU00826}.
DOMAIN 2890 3024 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 3145 3208 AV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
DOMAIN 3265 3417 (+)RNA virus helicase ATP-binding.
DOMAIN 3418 3546 (+)RNA virus helicase C-terminal.
ZN_FING 8 28 C4-type; atypical.
NP_BIND 3293 3300 ATP. {ECO:0000250}.
REGION 69 182 PCP1-alpha.
REGION 263 382 PCP1-beta.
REGION 426 513 OTU-like.
REGION 1266 1388 HD1.
REGION 1583 1745 HD2.
REGION 2036 2157 HD3.
COMPBIAS 808 924 Pro-rich.
COMPBIAS 2329 2344 Pro-rich.
ACT_SITE 76 76 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00872}.
ACT_SITE 146 146 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00872}.
ACT_SITE 270 270 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873}.
ACT_SITE 339 339 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873}.
ACT_SITE 437 437 For Nsp2 cysteine proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00871}.
ACT_SITE 506 506 For Nsp2 cysteine proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00871}.
ACT_SITE 1848 1848 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
ACT_SITE 1873 1873 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
ACT_SITE 1927 1927 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
METAL 3151 3151 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3154 3154 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3164 3164 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3169 3169 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3172 3172 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3174 3174 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3176 3176 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3178 3178 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3185 3185 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3187 3187 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3194 3194 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 3197 3197 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
SITE 180 181 Cleavage; by autolysis. {ECO:0000250}.
SITE 383 384 Cleavage; by autolysis. {ECO:0000250}.
SITE 1579 1580 Cleavage; by CP2. {ECO:0000255}.
SITE 1809 1810 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2013 2014 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2183 2184 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2199 2200 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2348 2349 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2458 2459 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3144 3145 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3585 3586 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3808 3809 Cleavage; by 3CLSP. {ECO:0000250}.
VAR_SEQ 2504 3961 Missing (in isoform Replicase polyprotein
1a). {ECO:0000305}.
/FTId=VSP_032891.
SEQUENCE 3961 AA; 433077 MW; 45D39828CC48EA77 CRC64;
MSGILDRCTC TPNARVFVAE GQVYCTRCLS ARSLLPLNLQ VPELGVLGLF YRPEEPLRWT
LPRAFPTVEC SPTGACWLSA IFPIARMTSG NLNFQQRMVR VAGEIYRAGQ LTPTVLKTIQ
VYERGCRWYP IVGPVPGVGV YANSLHVSDK PFPGATHVLT NLPLPQRPKP EDFCPFECAM
ADVYDIGRGA VMYVAGGKVS WAPRGGDEVK FEPVPKELKL VANRLHTSFP PHHVVDMSKF
TFMTPGSGVS MRVEYQYGCL PADTVPEGNC WWRLFDLLPP EVQNKEIRHA NQFGYQTKHG
VPGKYLQRRL QVNGLRAVTD THGPIVIQYF SVKESWIRHL KPVEEPSLPG FEDLLRIRVE
PNTSPLAGKN EKIFRFGSHK WYGAGKRARK ARSGATTMVA HRASSAHETR QATKHEGAGA
NKAEHLKLYS PPAEGNCGWH CISAIVNRMV NSNFETTLPE RVRPPDDWAT DEDLVNTIQI
LRLPAALDRN GACGGAKYVL KLEGEHWTVS VNPGMSPSLL PLECVQGCCE HKGGLGSPDA
VEVSGFDPAC LDRLLQVMHL PSSTIPAALA ELSDDSNRPV SPAAATWTVS QSYARHRGGN
HHDQVCLGKI ISLCQVIEDC CCHQNKTNRA TPEEVAAKID QYLRGATSLE ECLAKLERVS
PPGAADTSFD WNVVLPGVEA AHQTTEQLHV NPCRTLVPPV TQEPLGKDSV PLTAFSLSNC
YYPAQGNEVR HRERLNSVLS KLEEVVLEEY GLMSTGLGPR PVLPSGLDEL KDQMEEDLLK
LANTQATSEM MAWAAEQVDL KAWVKSYPRW TPPPPPPRVQ PRKTKSVKSL PEDKPVPAPR
RKVRSGCGSP VLMGDNVPNG SEDLTVGGPL NFPTPSEPMT PMSEPVLTPA LQRVPKLMTP
LDGSAPVPAP RRTVSRPMTP LSEPIFLSAP RHKFQQVEEA NPATTTLTHQ NEPLDLSASS
QTEYEASPLA SSQNMSILEA GGQEAEEVLS EISDILNDTS PAPVSSSSSL SSVKITRPKY
SAQAIIDSGG PCSGHLQKEK EACLSIMREA CDASKLSDPA TQEWLSRMWD RVDMLTWRNT
SAYQAFRTLN GRFEFLPKMI LETPPPHPCG FVMLPHTPAP SVSAESDLTI GSVATEDVPR
ILGKIGDTGE LLNQGPSAPF KGGPVCDQPA KNSRMSPRES DESIIAPPAD TGGAGSFTDL
PSSDSVDANG GGPLRTVKTK AGRLLDQLSC QVFSLVSHLP VFFSHLFKSD SGYSPGDWGF
AAFTLFCLFL CYSYPFFGFA PLLGVFSGSS RRVRMGVFGC WLAFAVGLFK PVSDPVGTAC
EFDSPECRNV LHSFELLKPW DPVRSLVVGP VGLGLAILGR LLGGARYVWH FLLRFGIVAD
CILAGAYVLS QGRCKKCWGS CVRTAPNEIA FNVFPFTRAT RSSLIDLCDR FCAPKGMDPI
FLATVWRGCW TGRSPIEQPS EKPIAFAQLD EKRITARTVV AQPYDPNQAV KCLRVLQAGG
AMVAEAVPKV VKVSAIPFRA PFFPAGVKVD PECRIVVDPD TFTTALRSGY STTNLVLGMG
DFAQLNGLKI RQISKPSGGG SHLVAALHVA CSMALHMLAG VYVTAVGSCG TGTNDPWCTN
PFAAPGYGPG SLCTSRLCIS QHGLTLPLTA LVAGFGLQEI ALVVLIFVSM GGMAHRLSCK
ADMLCILLAI ASYVWVPLTW LLCVFPCWLR WFSLHPLTIL WLVFFLISVN IPSGILAVVL
LVSLWLLGRY TNIAGLVTPY DIHHYTSGPR GVAALATAPD GTYLAAVRRA ALTGRTMLFT
PSQLGSLLEG AFRTQKPSLN TVNVVGSSMG SGGVFTIDGK IKCVTAAHVL TGNSARVSGV
GFNQMLDFDV KGDFAIADCP NWQGAAPKAQ FCEDGWTGRA YWLTSSGVEP GVIGNGFAFC
FTACGDSGSP VITEAGELVG VHTGSNKQGG GIVTRPSGQF CNVTPIKLSE LSEFFAGPKV
PLGDVKIGSH IIKDTCEVPS DLCALLAAKP ELEGGLSTVQ LLCVFFLLWR MMGHAWTPLV
AVGFFILNEI LPAVLVRSVF SFGMFVLSWL TPWSAQVLMI RLLTAALNRN RLSLGFYSLG
AVTSFVADLA VTQGHPLQVV MNLSTYAFLP RMMVVTSPVP VIACGVVHLL AIILYLFKYR
CLHYVLVGDG VFSSAFFLRY FAEGKLREGV SQSCGMSHES LTGALAMRLT DEDLDFLTKW
TDFKCFVSAS NMRNAAGQFI EAAYAKALRI ELAQLVQVDK VRGTLAKLEA FADTVAPQLS
PGDIVVALGH TPVGSIFDLK VGSTKHTLQA IETRVLAGSK MTVARVVDPT PAPPPVPVPI
PLPPKVLENG PNAWGDEDRL NKKKRRRMEA VGIFVMDGKK YQKFWDKNSG DVFYEEVHNS
TDEWECLRAG DPADFDPETG VQCGHITIED RVYNVFTSPS GRKFLVPANP ENRRAQWEAA
KLSVEQALGM MNVDGELTAK ELEKLKGIID KLQGLTKEQC LNCLLAASGL TRCGRGGLVV
TETAVKIVKF HNRTFTLGPV NLKVASEVEL KDAVEHNQHP VARPVDGGVV LLRSAVPSLI
DVLISGADAS PKLLARHGPG NTGIDGTLWD FEAEATKEEV ALSAQIIQAC DIRRGDAPEI
GLPYKLYPVR GNPERVKGVL QNTRFGDIPY KTPSDTGSPV HAAACLTPNA TPVTDGRSVL
ATTMPSGFEL YVPTIPASVL DYLDSRPDCP KQLTEHGCED AALRDLSKYD LVTQGFVLPG
VLRLVRKYLF AHVGKCPPVH RPSTYPAKNS MAGINGNRFP TKDIQSVPEI DVLCAQAVRE
NWQTVTPCTL KKQYCGKKKT RTILGTNNFI ALAHRAALSG VTQGFMKKAF NSPIALGKNK
FKELQTPVLG RCLEADLASC DRSTPAIVRW FAANLLYELA CAEEHLPSYV LNCCHDLLVT
QSGAVTKRGG LSSGDPITSV SNTIYSLVIY AQHMVLSYFK SGHPHGLLFL QDQLKFEDML
KVQPLIVYSD DLVLYAESPS MPNYHWWVEH LNLMLGFQTD PKKTAITDSP TFLGCRIING
RQLVPNRDRI LAALAYHMKA SNVSEYYASA AAILMDSCAC LEYDPEWFEE LVVGIAQCAR
KDGYSFPGPP FFLSMWEKLR SNHEGKKSRM CGYCMAPAPY ATACGLDVCV YHTHFHQHCP
VIIWCGHPAG SGSCGECEPP LGKGTSPLDE VLEQVPYKPP RTVIMHVEQG LTPLDPGRYQ
TRRGLVSVRR GIRGNEVDLP DGDYASTALL PTCKEINMVA VAPNVLRSRF IIGPPGAGKT
HWLLQQVQDG DVIYTPTHQT MLDMIRALGT CRFNVPAGTT LQFPAPSRTG PWVRILAGGW
CPGKNSFLDE AAYCNHLDVL RLLSKTTLTC LGDFKQLHPV GFDSHCYVFD IMPQTQLKTI
WRFGQNICDA IQPDYRDKLV SMVNTTRVTY VEKPVRYGQV LTPYHRDRED GAITIDSSQG
ATFDVVTLHL PTKDSLNRQR ALVAITRARH AIFVYDPHRQ LQSMFDLPAK GTPVNLAVHR
DEQLIVLDRN NKEITVAQAL GNGDKFRATD KRVVDSLRAI CADLEGSSSP LPKVAHNLGF
YFSPDLTQFA KLPAELAPHW PVVTTQNNER WPDRLVASLR PIHKYSRACI GAGYMVGPSV
FLGTPGVVSY YLTKFVRGEA QVLPETVFST GRIEVDCREY LDDREREVAE SLPHAFIGDV
KGTTVGGCHH VTSKYLPRFL PKESVAVVGV SSPGEAAKAF CTLTDVYLPD LEAYLHPETQ
SKCWKVMLDF KEVRLMVWKG KTAYFQLEGR HFTWYQLASY TSYIRVPVNS TVYLDPCMGP
ALCNRRVVGS THWGADLAVT PYDYGAKIIL SSAYHGEMPP GYKILACAEF SLDDPVRYKH
TWGFESDTAY LYEFTGNGED WEDYNGAFRA RQKGKIYKAT ATSMKFHFPP GPVIEPTLGL
N


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