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 RPOA_PRRS1              Reviewed;        3961 AA.
Q9YN02; Q9YN01;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 3.
10-MAY-2017, entry version 113.
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 16244B)
(PRRSV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Arteriviridae; unclassified Arteriviridae.
NCBI_TaxID=300561;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=10073689;
Allende R., Lewis T.L., Lu Z., Rock D.L., Kutish G.F., Ali A.,
Doster A.R., Osorio F.A.;
"North American and European porcine reproductive and respiratory
syndrome viruses differ in non-structural protein coding regions.";
J. Gen. Virol. 80:307-315(1999).
-!- 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=Q9YN02-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=Q9YN02-2; Sequence=VSP_032890;
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=AAC64692.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF046869; AAC64691.1; -; Genomic_RNA.
EMBL; AF046869; AAC64692.1; ALT_INIT; Genomic_RNA.
PDB; 5EYI; X-ray; 2.16 A; A/B=3586-3808.
PDBsum; 5EYI; -.
SMR; Q9YN02; -.
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; 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; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
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.
1: Evidence at protein level;
3D-structure; ATP-binding; 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;
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_0000036657.
CHAIN 1 382 Nsp1. {ECO:0000250}.
/FTId=PRO_0000410826.
CHAIN 1 180 Nsp1-alpha papain-like cysteine
proteinase. {ECO:0000250}.
/FTId=PRO_0000036659.
CHAIN 181 383 Nsp1-beta papain-like cysteine
proteinase. {ECO:0000250}.
/FTId=PRO_0000036660.
CHAIN 384 1579 Nsp2 cysteine proteinase. {ECO:0000255}.
/FTId=PRO_0000036661.
CHAIN 1580 1809 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000036662.
CHAIN 1810 2013 3C-like serine proteinase. {ECO:0000250}.
/FTId=PRO_0000036663.
CHAIN 2014 2458 Non-structural protein 5-6-7.
{ECO:0000250}.
/FTId=PRO_0000036664.
CHAIN 2014 2183 Non-structural protein 5. {ECO:0000250}.
/FTId=PRO_0000423118.
CHAIN 2184 2199 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000423119.
CHAIN 2200 2348 Non-structural protein 7-alpha.
{ECO:0000250}.
/FTId=PRO_0000423120.
CHAIN 2349 2458 Non-structural protein 7-beta.
{ECO:0000250}.
/FTId=PRO_0000423121.
CHAIN 2459 3144 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000036665.
CHAIN 2459 2503 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000036666.
CHAIN 3145 3585 Helicase. {ECO:0000250}.
/FTId=PRO_0000036667.
CHAIN 3586 3808 Non-structural protein 11. {ECO:0000250}.
/FTId=PRO_0000036668.
CHAIN 3809 3961 Non-structural protein 12. {ECO:0000250}.
/FTId=PRO_0000036669.
TRANSMEM 1266 1286 Helical. {ECO:0000255}.
TRANSMEM 1296 1316 Helical. {ECO:0000255}.
TRANSMEM 1345 1365 Helical. {ECO:0000255}.
TRANSMEM 1368 1388 Helical. {ECO:0000255}.
TRANSMEM 1583 1603 Helical. {ECO:0000255}.
TRANSMEM 1650 1670 Helical. {ECO:0000255}.
TRANSMEM 1685 1705 Helical. {ECO:0000255}.
TRANSMEM 1719 1739 Helical. {ECO:0000255}.
TRANSMEM 2012 2032 Helical. {ECO:0000255}.
TRANSMEM 2060 2080 Helical. {ECO:0000255}.
TRANSMEM 2092 2112 Helical. {ECO:0000255}.
TRANSMEM 2137 2157 Helical. {ECO:0000255}.
TRANSMEM 2164 2184 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 3298 3305 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 808 930 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 3195 3195 Involved in mRNA transcription process.
{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_032890.
HELIX 3592 3597 {ECO:0000244|PDB:5EYI}.
STRAND 3602 3605 {ECO:0000244|PDB:5EYI}.
STRAND 3609 3611 {ECO:0000244|PDB:5EYI}.
HELIX 3614 3619 {ECO:0000244|PDB:5EYI}.
STRAND 3622 3626 {ECO:0000244|PDB:5EYI}.
STRAND 3632 3640 {ECO:0000244|PDB:5EYI}.
STRAND 3647 3651 {ECO:0000244|PDB:5EYI}.
STRAND 3654 3656 {ECO:0000244|PDB:5EYI}.
STRAND 3659 3661 {ECO:0000244|PDB:5EYI}.
STRAND 3667 3676 {ECO:0000244|PDB:5EYI}.
STRAND 3679 3681 {ECO:0000244|PDB:5EYI}.
HELIX 3692 3695 {ECO:0000244|PDB:5EYI}.
HELIX 3703 3711 {ECO:0000244|PDB:5EYI}.
HELIX 3713 3716 {ECO:0000244|PDB:5EYI}.
STRAND 3719 3721 {ECO:0000244|PDB:5EYI}.
STRAND 3724 3726 {ECO:0000244|PDB:5EYI}.
STRAND 3742 3752 {ECO:0000244|PDB:5EYI}.
TURN 3753 3755 {ECO:0000244|PDB:5EYI}.
STRAND 3756 3764 {ECO:0000244|PDB:5EYI}.
HELIX 3768 3774 {ECO:0000244|PDB:5EYI}.
STRAND 3778 3788 {ECO:0000244|PDB:5EYI}.
STRAND 3791 3798 {ECO:0000244|PDB:5EYI}.
TURN 3799 3801 {ECO:0000244|PDB:5EYI}.
STRAND 3802 3806 {ECO:0000244|PDB:5EYI}.
SEQUENCE 3961 AA; 432802 MW; 111B73F5926C9DB0 CRC64;
MSGILDRCTC TPNARVFVAE GQVYCTRCLS ARSLLPLNLQ VSELGVLGLF YRPEEPLRWT
LPRAFPTVEC SPAGACWLSA IFPIARMTSG NLNFQQRMVR VAAEIYRAGQ LTPAVLKALQ
VYERGCRWYP IVGPVPGVAV FANSLHVSDK PFPGATHVLT NLPLPQRPKP EDFCPFECAM
ATVYDIGHDA VMYVAEGKIS WAPRGGDEVK FEAVPGELKL IANRLRTSFP PHHAVDMSKF
AFTAPGCGVS MRVERQHGCL PADTVPEGNC WWSLFDLLPL EVQDKEIRHA NQFGYQTKHG
VSGKYLQRRL QVNGLRAVTD SNGPIVVQYF SVKESWIRHL KLAGEPSYSG FEDLLRIRVE
PNTSPLANTE GKIFRFGSHK WYGAGKRARK ARSCATATVA GRALSVRETR QAKEHEVAGA
DKAEHLKHYS PPAEGNCGWH CISAIANRMV NSIFETTLPE RVRPPDDWAT DDDLANAIQI
LRLPAALDRN GACTSAKYVL KLEGEHWTVT VTPGMSPSLL PLECVQGCCE HKGGLGSPDA
IEVSGFDPAC LDWLAEVMHL PSSAIPAALA EMSGDSDRSA SPVTTVWTVS QFFARHSGGN
HPDQVRLGKI ISLCQVIEDC CCSQNKTNRV TPEEVAAKID LYLRGATNLE ECLARLEKAR
PPRVIDTSFD WDVVLPGVEA ATQTNKLPQV NQCRALVPVV TQKSLDNNSV PLTAFSLANY
YYRAQGDEVR HRERLTAVLS KLEEVVREEY GLMPTEPGPR PTLPRGLDEL KDQMEEDLLR
LANAQATSDM MAWAVEQVDL KTWVKNYPRW TPPPPPPKVQ PRKTKPVKSL PERKPVPAPR
RKVGPDCGSP VSLGGDVPNS WEDLAVSSPL DLPTPPEPAT LSSELVIVSS PQCIFRPATP
LSEPAPIPAP RGTVSRPVTP LSEPIPVPAP RRKFQQVKRL SSAAAVPLHQ NEPLDLSASS
QTEYEASPSA PPQSGGVLGV EGHEAEETLS EISDMSGNIK PASVSSSSSL SSVEITRPKY
SAQAIIDSGG PCSGHLQGVK ETCLSVMREA CDATKLDDPA TQEWLSRMWD RVDMLTWRNT
SVCQAIRTLD GRLKFLPKMI LETPPPYPCE FVMMPHTPAP SVGAESDLTI GSVATEDVPR
ILEKIENVGE MANQEPSAFS EDKPVDDQLV NDPRISSRRP DESTAAPSAG TGGAGSFTDL
PSSDGADADG GGPFRTAKRK AERLFDQLSR QVFDLVSHLP VFFSRLFHPG GGYSTGDWGF
AAFTLLCLFL CYSYPAFGIA PLLGVFSGTS RRVRMGVFGC WLAFAVGLFK PVSDPVGAAC
EFDSPECRNI LLSFELLKPW DPVRSLVVGP VGLGLAILGR LLGGARCIWH FLLRLGIVAD
CILAGAYVLS QGRCKKCWGS CIRTAPNEVA FNVFPFTRAT RSSLIDLCDR FCAPKGMDPI
FLATGWRGCW AGRSPIEQPS EKPIAFAQLD EKKITARTVV AQPYDPNQAV KCLRVLQAGG
AMVAEAVPKV VKVSAVPFRA PFFPTGVKVD PDCRVVVDPD TFTAALRSGY STTNLVLGVG
DFAQLNGLKI RQISKPSGGG PHLMAALHVA CSMALHMLTG IYVTAVGSCG TGTNDPWCAN
PFAVPGYGPG SLCTSRLCIS QHGLTLPLTA LVAGFGIQEI ALVVLIFVSI GGMAHRLSCK
ADMLCILLAI ASYVWVPLTW LLCVFPCWLR CFSLHPLTIL WLVFFLISVN MPSGILAMVL
LVSLWLLGRY TNVAGLVTPY DIHHYTSGPR GVAALATAPD GTYLAAVRRA ALTGRTMLFT
PSQLGSLLEG AFRTRKPSLN TVNVIGSSMG SGGVFTIDGK VKCVTAAHVL TGNSARVSGV
GFNQMLDFDV KGDFAIADCP NWQGAAPKAQ FCADGWTGRA YWLTSSGVEP GVIGKGFAFC
FTACGDSGSP VITEAGELVG VHTGSNKQGG GIVTRPSGQF CNVAPIKLSE LSEFFAGPKV
PLGDVKVGSH IIKDISEVPS DLCALLAAKP ELEGGLSTVQ LLCVFFLLWR MMGHAWTPLV
AVSFFILNEV LPAVLVRSVF SFGMFVLSWL TPWSAQILMI RLLTAALNRN RWSLAFFSLG
AVTGFVADLA ATQGHPLQAV MNLSTYAFLP RMMVVTSPVP VITCGVVHLL AIILYLFKYR
GLHQILVGDG VFSAAFFLRY FAEGKLREGV SQSCGMNHES LTGALAMRLN DEDLDFLMKW
TDFKCFVSAS NMRNAAGQFI EAAYAKALRV ELAQLVQVDK VRGVLAKLEA FADTVAPQLS
PGDIVVALGH TPVGSIFDLK VGSTKHTLQA IETRVLAGSK MTVARVVDPT PTPPPAPVPI
PLPPKVLENG PNAWGDEDRL NKKKRRRMEA LGIYVMGGKK YQKFWDKNSG DVFYEEVHNN
TDEWECLRVG DPADFDPEKG TLCGHVTIEN KAYHVYISPS GKKFLVPVNP ENGRVQWEAA
KLSMEQALGM MNVDGELTAK ELEKLKRIID KLQGLTKEQC LNCLLAASGL TRCGRGGLVV
TETAVKIVKF HNRTFTLGPV NLKVASEVEL KDAVEHNQHP VARPIDGGVV LLRSAVPSLI
DVLISGADAS PKLLAHHGPG NTGIDGTLWD FESEATKEEV ALSAQIIQAC DIRRGDAPKI
GLPYKLYPVR GNPERVKGVL QNTRFGDIPY KTPSDTGSPV HAAACLTPNA TPVTDGRSVL
ATTMPPGFEL YVPTIPASVL DYLDSRPDCP KQLTEHGCED AALKDLSKYD LSTQGFVLPG
VLRLVRKYLF AHVGKCPPVH RPSTYPAKNS MAGINGNRFP TKDIQSVPEI DVLCAQAVRE
NWQTVTPCTL KKQYCGKKKT RTILGTNNFI ALAHRAALSG VTQGFMKKAF NSPIALGKNK
FKELQTSVLG RCLEADLASC DRSTPAIVRW FAANLLYELA CAEEHLPSYV LNCCHDLLVT
QSGAVTKRGG LSSGDPITSV SNTIYSLVIY AQHMVLSYFK SGHPHGLLFL QDQLKFEDML
KVQPLIVYSD DLVLYAESPT MPNYHWWVEH LNLMLGFQTD PKKTAITDSP SFLGCRIING
RQLVPNRDRI LAALAYHMKA SNVSEYYASA AAILMDSCAC LEYDPEWFEE LVVGIAQCAR
KDGYSFPGTP FFMSMWEKLR SNYEGKKSRV CGYCGAPAPY ATACGLDVCI YHTHFHQHCP
VTIWCGHPAG SGSCSECKSP VGKGTSPLDE VLEQVPYKPP RTVIMHVEQG LTPLDPGRYQ
TRRGLVSVRR GIRGNEVELP DGDYASTALL PTCKEINMVA VASNVLRSRF IIGPPGAGKT
YWLLQQVQDG DVIYTPTHQT MLDMIRALGT CRFNVPAGTT LQFPVPSRTG PWVRILAGGW
CPGKNSFLDE AAYCNHLDVL RLLSKTTLTC LGDFKQLHPV GFDSHCYVFD IMPQTQLKTI
WRFGQNICDA IQPDYRDKLM SMVNTTRVTY VEKPVRYGQV LTPYHRDRED DAITIDSSQG
ATFDVVTLHL PTKDSLNRQR ALVAITRARH AIFVYDPHRQ LQGLFDLPAK GTPVNLAVHR
DGQLIVLDRN NKECTVAQAL GNGDKFRATD KRVVDSLRAI CADLEGSSSP LPKVAHNLGF
YFSPDLTQFA KLPVELAPHW PVVTTQNNEK WPDRLVASLR PIHKYSRACI GAGYMVGPSV
FLGTPGVVSY YLTKFVKGEA QLLPETVFST GRIEVDCREY LDDREREVAA SLPHAFIGDV
KGTTVGGCHH VTSRYLPRVL PKESVAVVGV SSPGKAAKAL CTLTDVYLPD LEAYLHPETQ
SKCWKMMLDF KEVRLMVWRD KTAYFQLEGR YFTWYQLASY ASYIRVPVNS TVYLDPCMGP
ALCNRRVVGS THWGADLAVT PYDYGAKIIL SSAYHGEMPP GYKILACAEF SLDDPVRYKH
TWGFESDTAY LYEFTGNGED WEDYNDAFRA RQEGKIYKAT ATSLKFHFPP GPVIEPTLGL
N


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