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 RPOA_LDVP               Reviewed;        3616 AA.
Q83017; Q83018; Q83024; Q83025; Q86716;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 2.
25-OCT-2017, entry version 109.
RecName: Full=Replicase polyprotein 1ab;
AltName: Full=ORF1ab polyprotein;
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=3.4.22.-;
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;
Lactate dehydrogenase elevating virus (strain Plagemann) (LDV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Arteriviridae.
NCBI_TaxID=300016;
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7778295; DOI=10.1006/viro.1995.1296;
Palmer G.A., Kuo L.L., Chen Z., Faaberg K.S., Plagemann P.G.W.;
"Sequence of the genome of lactate dehydrogenase-elevating virus:
heterogenicity between strains P and C.";
Virology 209:637-642(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-57.
PubMed=7512122; DOI=10.1099/0022-1317-75-4-925;
Chen Z., Faaberg K.S., Plagemann P.G.W.;
"Determination of the 5' end of the lactate dehydrogenase-elevating
virus genome by two independent approaches.";
J. Gen. Virol. 75:925-930(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 769-1187 AND 2307-2846.
PubMed=1870216;
Kuo L.L., Harty J.T., Erickson L., Palmer G.A., Plagemann P.G.W.;
"A nested set of eight RNAs is formed in macrophages infected with
lactate dehydrogenase-elevating virus.";
J. Virol. 65:5118-5123(1991).
[4]
ACTIVE SITES OF PCP1-ALPHA AND PCP1-BETA, AND MUTAGENESIS OF CYS-76
AND CYS-269.
PubMed=7769711;
den Boon J.A., Faaberg K.S., Meulenberg J.J.M., Wassenaar A.L.M.,
Plagemann P.G.W., Gorbalenya A.E., Snijder E.J.;
"Processing and evolution of the N-terminal region of the arterivirus
replicase ORF1a protein: identification of two papainlike cysteine
proteases.";
J. Virol. 69:4500-4505(1995).
-!- 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: The Nsp1 chain is essential for viral subgenomic mRNA
synthesis. {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.
-!- 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=Q83017-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=Q83017-2; Sequence=VSP_032889;
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}.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases
yield mature proteins. 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=AAA85664.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; U15146; AAA85663.1; -; Genomic_RNA.
EMBL; U15146; AAA85664.1; ALT_INIT; Genomic_RNA.
EMBL; S69379; AAB30448.1; -; Genomic_RNA.
EMBL; S50064; AAB19478.1; -; mRNA.
EMBL; S50068; AAB19479.1; -; mRNA.
PIR; B40901; B40901.
PIR; C40901; C40901.
PIR; JQ1998; JQ1998.
PIR; PQ0618; PQ0618.
ProteinModelPortal; Q83017; -.
SMR; Q83017; -.
MEROPS; C31.001; -.
GO; GO:0033644; C:host cell membrane; 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:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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.
Gene3D; 3.30.40.20; -; 1.
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; IPR023183; Chymotrypsin-like_domain3.
InterPro; IPR022230; DUF3756.
InterPro; IPR008760; EAV_peptidase_S32.
InterPro; IPR037227; EndoU-like.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF16749; Arteri_nsp7a; 1.
Pfam; PF12581; DUF3756; 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; 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;
ATP-binding; Helicase; Host cytoplasm; Host membrane; Hydrolase;
Membrane; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
Protease; Ribosomal frameshifting; RNA-directed RNA polymerase;
Serine protease; Thiol protease; Transferase; Transmembrane;
Transmembrane helix; Viral RNA replication; Zinc; Zinc-finger.
CHAIN 1 3616 Replicase polyprotein 1ab.
/FTId=PRO_0000036644.
CHAIN 1 ? Nsp1-alpha papain-like cysteine
proteinase. {ECO:0000250}.
/FTId=PRO_0000036646.
CHAIN ? 380 Nsp1-beta papain-like cysteine
proteinase. {ECO:0000250}.
/FTId=PRO_0000036647.
CHAIN 381 1286 Nsp2 cysteine proteinase. {ECO:0000250}.
/FTId=PRO_0000036648.
CHAIN 1287 1512 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000036649.
CHAIN 1513 1714 3C-like serine proteinase. {ECO:0000250}.
/FTId=PRO_0000036650.
CHAIN 1715 2161 Non-structural protein 5-6-7.
{ECO:0000250}.
/FTId=PRO_0000036651.
CHAIN 1715 1878 Non-structural protein 5. {ECO:0000250}.
/FTId=PRO_0000423114.
CHAIN 1879 1894 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000423115.
CHAIN 1895 2026 Non-structural protein 7-alpha.
{ECO:0000250}.
/FTId=PRO_0000423116.
CHAIN 2027 2161 Non-structural protein 7-beta.
{ECO:0000250}.
/FTId=PRO_0000423117.
CHAIN 2162 2843 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000036652.
CHAIN 2162 2206 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000036653.
CHAIN 2844 3272 Helicase. {ECO:0000250}.
/FTId=PRO_0000036654.
CHAIN 3273 3494 Non-structural protein 11. {ECO:0000250}.
/FTId=PRO_0000036655.
CHAIN 3495 3616 Non-structural protein 12. {ECO:0000250}.
/FTId=PRO_0000036656.
TRANSMEM 942 962 Helical. {ECO:0000255}.
TRANSMEM 977 997 Helical. {ECO:0000255}.
TRANSMEM 1010 1030 Helical. {ECO:0000255}.
TRANSMEM 1060 1080 Helical. {ECO:0000255}.
TRANSMEM 1085 1105 Helical. {ECO:0000255}.
TRANSMEM 1289 1309 Helical. {ECO:0000255}.
TRANSMEM 1364 1384 Helical. {ECO:0000255}.
TRANSMEM 1386 1406 Helical. {ECO:0000255}.
TRANSMEM 1425 1445 Helical. {ECO:0000255}.
TRANSMEM 1715 1735 Helical. {ECO:0000255}.
TRANSMEM 1737 1757 Helical. {ECO:0000255}.
TRANSMEM 1761 1781 Helical. {ECO:0000255}.
TRANSMEM 1832 1852 Helical. {ECO:0000255}.
DOMAIN 69 181 Peptidase C31. {ECO:0000255|PROSITE-
ProRule:PRU00872}.
DOMAIN 262 381 Peptidase C32. {ECO:0000255|PROSITE-
ProRule:PRU00873}.
DOMAIN 381 486 Peptidase C33. {ECO:0000255|PROSITE-
ProRule:PRU00871}.
DOMAIN 1513 1714 Peptidase S32. {ECO:0000255|PROSITE-
ProRule:PRU00826}.
DOMAIN 2590 2724 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 2844 2907 AV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
DOMAIN 2964 3116 (+)RNA virus helicase ATP-binding.
DOMAIN 3117 3248 (+)RNA virus helicase C-terminal.
ZN_FING 8 28 C4-type; atypical.
NP_BIND 2992 2999 ATP. {ECO:0000250}.
REGION 981 1105 HD1.
REGION 1289 1448 HD2.
REGION 1737 1852 HD3.
ACT_SITE 76 76 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00872,
ECO:0000269|PubMed:7769711}.
ACT_SITE 147 147 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00872,
ECO:0000269|PubMed:7769711}.
ACT_SITE 269 269 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873,
ECO:0000269|PubMed:7769711}.
ACT_SITE 340 340 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00873,
ECO:0000269|PubMed:7769711}.
ACT_SITE 390 390 For Nsp2 cysteine proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00871}.
ACT_SITE 456 456 For Nsp2 cysteine proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00871}.
ACT_SITE 1551 1551 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
ACT_SITE 1576 1576 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
ACT_SITE 1628 1628 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
METAL 2850 2850 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 2853 2853 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 2863 2863 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 2868 2868 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 2871 2871 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 2873 2873 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 2875 2875 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 2877 2877 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 2884 2884 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 2886 2886 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 2893 2893 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
METAL 2896 2896 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
SITE 181 182 Cleavage; by autolysis. {ECO:0000255}.
SITE 381 382 Cleavage; by autolysis. {ECO:0000255}.
SITE 1286 1287 Cleavage; by CP2. {ECO:0000250}.
SITE 1512 1513 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 1714 1715 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 1878 1879 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 1894 1895 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2026 2027 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2161 2162 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 2843 2844 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3272 3273 Cleavage; by 3CLSP. {ECO:0000250}.
SITE 3494 3495 Cleavage; by 3CLSP. {ECO:0000250}.
VAR_SEQ 2207 3616 Missing (in isoform Replicase polyprotein
1a). {ECO:0000305}.
/FTId=VSP_032889.
MUTAGEN 76 76 C->S: Complete loss of cleavage between
nsp1-alpha and nsp1-beta.
{ECO:0000269|PubMed:7769711}.
MUTAGEN 269 269 C->A: Complete loss of cleavage between
nsp1-beta and nsp2.
{ECO:0000269|PubMed:7769711}.
CONFLICT 1185 1185 E -> K (in Ref. 3). {ECO:0000305}.
CONFLICT 2748 2753 SEPKLP -> QNPNFL (in Ref. 3).
{ECO:0000305}.
CONFLICT 2771 2777 VAALAYQ -> RRGASVS (in Ref. 3).
{ECO:0000305}.
CONFLICT 2820 2823 GSPW -> RKEG (in Ref. 3). {ECO:0000305}.
CONFLICT 2843 2843 E -> K (in Ref. 3). {ECO:0000305}.
SEQUENCE 3616 AA; 396434 MW; 6167A231CDE7B611 CRC64;
MQSGFDRCLC TPNARVFWEH GQVYCTRCLA ARPLLPLSQQ NPRLGALGLF YRPATPLTWE
APITYPTKEC RPGGLCWLSG IYPIARMTSG NHNFQARLNF VASVVYRDGK LTSKHLEEEF
EVYSRGCRWY PITGPVPGIA LYANAVHVSD EPFPGCTHVL SNLPLPQQPL RKGLCPFSDA
RAEVWRYKGN TIFVSEQGYL WTTGSNDSVP EPWGEARRLC EKIIASLPAD HLVKIEFSNY
PFDYSFTGGD GAGYVLFPCK KNDTKFSKCW EKVFEDHSSW KVACEEADLA DRMGYRTPAG
VAGPYLARRL QYRGLRAVVK PEQNDYVVWA LGVPESYIRH ISRAGEPVEN FFVRVGEFSI
VSNCVATPYP KFRFQTRKYY GYSPPGDGAC GLHCISAIIN DIFGDALCTK LTNCSRDSSE
WLSDQDMYQL VMTARLPATL GHCPSATYKL DCVNQHWTVT KRKGDRALGG LSPECVRGVC
GGECKFVPTY PREINLELAA KSPISALAFS LGVEPYCDCW NFTNSVLVND SLAVETARAG
EAYRSAMGIP KDDWVLLAEL MTENCLTRRE VLDKLQRGLR LHATSKPGSP ASVSPASSID
FSAAGLLLDG TESDKEAVVA VNNDCYTVLG FDKNSATKSE QELATGLFSE LVEPMETSTS
KHESRKILEA ASRALKSAKP KRKRNKKKKT SSPTPTPPET PTREVPGAIE VVSGDEEAGA
CESATIVPDK AQARPPPRPK RQALKKAEQG FILKDIIWNP TESGVKCLTI VEDVRAFLKS
ITPPGGALGT RARITAHIVE QFHVIRESTP ELVLAHAEHQ AKNMHELLLS EKAKLILGIG
EDTLKKLVSS QRSLPRSIGF GAWLSDQQKT ADSCGEREFV EVPLKSGAEP TPSKRDLGVS
LGDQLSQDGA PRLSSSTACE IKERVPPIKD SGGGLGQKFM AWLNHQVFLL SSHLLAMWSV
VLGSRQKLNW ADYVYTLFCL CCVLLCFHFP AIGFIPLAGC VFGSPWRVRL SVFSVWLCVA
VVVFQEVLPE PGSVCSSASA ECAAALERYS GNGVHRPVNH IGVGLVGTVA GFVARVVGGP
RHYWFYFLRL MVVLDLGLVF LAVALRGRCK KCFCKCVRVA PHEVHLRVFP LTKVARPTLE
AVCDMYSAPR VDPILVATGI KGCWQGKVSP HQVTDKPVSY SNLEEKKISN KTVVPPPTDP
QQAVKCLKVL QCGGSIQDVG VPEVKKVSKV PYKAPFFPNV SIDPECYIVV DPVTYSAAMR
GGYGVSHLIV GTGDFAEVNG LRFVSGGHVA DFVCLGLYVM LNFLISAWLS SPVSCGRGTN
DPWCKNPFSY PVVGQGVMCN SHLCISEDGL TSPMVLSYSL IDWALMIAVI ATVAIFIAKV
SLLVDVICVF LCLLMYVFPP LSVIAFAFPF ALCKVHLHPV TLVWVQFFLL AVNFWAGVAV
AVILISSWFL ARATSSTGLV TPYDVHLVTS TPRGASSLAS APEGTYLAAV RRSALTGRCC
MFVPTNFGSV LEGSLRTRGC AKNVVSVFGS ASGSGGVFTI HGNPVVVTAT HLLSDGKARV
SCVGFSQCLT FKSVGDYAFA RVAEWKGDAP KVELSDRRGR AYCSPQVEWS LVLLGPNTAF
CFTKCGDSGS PVVDEDGNLI GVHTGSNKRG SGMITTHNGK TLGMSNVKLS EMCQHYGGSG
VPVSTVRLPK HLIVDVEAVA SDLVAVVESL PTPEGALSSV QLLCVFFFLW RLIHVPFVPV
IAVAFFFLNE ILPVVLARLM FSFALSLFSV FTGFSVQVLL LRLVIAALNR SAVSFGSFLL
GQLFHCCLMP SHLETLGPVP GYFYPSTTEV ASKEIFVTLL AIHVLALLLS LFKRPMLADV
LVGNGSFDAA FFLKYFAEGN LRDGVSDSCN MTPEGLTAAL AITLSDDDLE FLQRHSEFKC
FVSASNMRNG AKEFIESAYA RALRAQLAAT DKIKASKSIL AKLESFAGGV VTKVEPGDVV
VVLGKKIVGD LVEITINDVK HVIRVIETRV MAGTQFSVGT ICGDLENACE DPSGLVKTSK
KQRRRQKRTG LGTEVVGTVE IDGVSYNKVW HKATGDVTYE GFLVSENSRL RTLGTSAIGR
FQEFIRKHGS KVKTSVEKYP VGKNKHIEFA VTTYNLDGEE FDVPDHEPLE WTITIGDSDL
EAERLTVDQA LRHMGHDSLL TPKEKEKLAR IIESLNGLQQ SSALNCLTTS GLERCSRGGV
TVSKDAVKIV KYHSRTFSIG DVNLKVMSFD EYRRTMGKPG HLLVAKLTDG VVVMRKHEPS
LVDVILTGED AEFFPRTHGP GNTGIHRFVW DFESPPVDLE LELSEQIITA CSMRRGDAPA
LDLPYKLHPV RGDPYRHRGV LFNTRFGDIT YLIPEKTKEP LHAAACYNKG VPVSDSETLV
ATTLPHGFEL YVPTLPPSVL EYLDSRPDTP RMLTKHGCAS AAEKDLQKFD LSRQGFVLPG
VLYMVRRYLS RLIGVRRRLF MPSTYPAKNS MAGINGGRFP LTWLQSHPDI DALCKRACEE
HWQTVTPCTL KKQYCSKSKT RTILGTNNFV ALGLRSALSG VTQGFMRKGI GTPICLGKNK
FTPLPVRIGG RCLEADLASC DRSTPAIIRW FTTNLLFELA GAEEWIPSYV LNCCHDVVST
MSGCFDKRGG LSSGDPVTSI SNTVYSLIIY AQHMVLSAFR CGHKIGGLFL QDSLEMEQLF
ELQPLLVYSD DVVFYNESDE LPNYHFFVDH LDLMLGFKTD RSKTVITSEP KLPGCRISGG
RVLVPQRDRI VAALAYQMKA SCVGEYFASA AAILMDACAC CDHDESWYFD LVCGIAECAG
SPWFRFPGPS FFLDMWNRLS AEEKKKCRTC AHCGAPATLV SSCGLNLCDY HGHGHPHCPV
VLPCGHAVGS GVCEQCSSSA MNLNTELDIL LMCVPYHPPK VELLSVNDKV SSLPPGAYQA
RGGVVSVRRD ILGNVVDLPD GDYQVMKVAQ TCADISMVSV NSNILRSQFV TGAPGTGKTT
YLLSVVRDDD VIYTPTHRTM LDVVKALKVC RFDPPKDTPL EFPVPGRTGP TVRLIGAGFV
PGRVSYLDEA AYCNPLDVLK VLSKTPLVCV GDLNQLPPVG FNGPCFAFSL MPGRQLIEVF
RFGPAVVNSI KKFYKEELVP RGPDTGVKFL KQYQPYGQVL TPYHRDRVDG AITIDSSQGC
TYDVVTVYLP TPKSLNSARA LVALTRARHY VFIYDPYDQL QQYLQVFEHE PADAWAFWCG
DQPKMIVGGV VKQLAGHSRT TDLKLQQLMG LEGTASPLPQ VGHNLGFYYS PDLIQFAKIP
PELCKHWPVV TAQNRTEWPD RLVCGMNKMD KNSRAVFCAG YYVGPSIFLG VPGVVSYYLT
KYLKGESVPL PDSIMSTGRI RLNVREYLDE NEIEFAKKCP QPFIGEVKGS NVGGCHHVTS
RFLPPVLVPG SVVKVGVSCP GKAAKGLCTV TDVYLPELDS YLHPPSKSMD YKLLVDFQPV
KLMVWKDATA YFHEGIRPME AMSRFLKVPE GEGVFFDLDE FVTNAKVSKL PCKYSVSAHQ
FLTEVVLSMT PTSEAPPDYE LLFARAYCVP GLDVGTLNAY IYKRGPSTYT TSNFARLVKD
TAVPVGCKGS GYMFPK


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