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

 R1AB_BC512              Reviewed;        6793 AA.
P0C6W0; Q0Q467;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 72.
RecName: Full=Replicase polyprotein 1ab;
Short=pp1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Non-structural protein 1;
Short=nsp1;
AltName: Full=p9;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p87;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.19.12;
EC=3.4.22.-;
AltName: Full=PL1-PRO/PL2-PRO;
AltName: Full=PLP1/PLP2;
AltName: Full=Papain-like proteinases 1/2;
AltName: Full=p195;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
AltName: Full=Peptide HD2;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=M-PRO;
AltName: Full=nsp5;
AltName: Full=p34;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
AltName: Full=p5;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
AltName: Full=p23;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
AltName: Full=p12;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
AltName: Full=p14;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=nsp12;
AltName: Full=p100;
Contains:
RecName: Full=Helicase;
Short=Hel;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=nsp13;
AltName: Full=p66;
AltName: Full=p66-HEL;
Contains:
RecName: Full=Exoribonuclease;
Short=ExoN;
EC=3.1.13.-;
AltName: Full=nsp14;
Contains:
RecName: Full=Uridylate-specific endoribonuclease;
EC=3.1.-.-;
AltName: Full=NendoU;
AltName: Full=nsp15;
Contains:
RecName: Full=Putative 2'-O-methyl transferase;
EC=2.1.1.-;
AltName: Full=nsp16;
Name=rep; ORFNames=1a-1b;
Bat coronavirus 512/2005 (BtCoV) (BtCoV/512/2005).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Alphacoronavirus.
NCBI_TaxID=693999;
NCBI_TaxID=153297; Scotophilus kuhlii (Lesser asiatic yellow bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16840328; DOI=10.1128/JVI.00697-06;
Tang X.C., Zhang J.X., Zhang S.Y., Wang P., Fan X.H., Li L.F., Li G.,
Dong B.Q., Liu W., Cheung C.L., Xu K.M., Song W.J., Vijaykrishna D.,
Poon L.L.M., Peiris J.S.M., Smith G.J., Chen H., Guan Y.;
"Prevalence and genetic diversity of coronaviruses in bats from
China.";
J. Virol. 80:7481-7490(2006).
-!- FUNCTION: The replicase polyprotein of coronaviruses 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 papain-like proteinase 1 (PLP1) and papain-like
proteinase 2 (PLP2) are responsible for the cleavages located at
the N-terminus of the replicase polyprotein. In addition, PLP2
possesses a deubiquitinating/deISGylating activity and processes
both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from
cellular substrates. PLP2 also antagonizes innate immune induction
of type I interferon by blocking the nuclear translocation of host
IRF-3 (By similarity). {ECO:0000250}.
-!- FUNCTION: The main proteinase 3CL-PRO is responsible for the
majority of cleavages as it cleaves the C-terminus of replicase
polyprotein at 11 sites. Recognizes substrates containing the core
sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog
Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-
phosphate (ADRP)-binding function (By similarity).
{ECO:0000255|PROSITE-ProRule:PRU00772}.
-!- FUNCTION: The helicase which contains a zinc finger structure
displays RNA and DNA duplex-unwinding activities with 5' to 3'
polarity. ATPase activity is strongly stimulated by poly(U),
poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity).
{ECO:0000250}.
-!- FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3'
to 5' direction. {ECO:0000250}.
-!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity
to the polymerase, maybe by binding to dsRNA or by producing
primers utilized by the latter. {ECO:0000250}.
-!- FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
-!- FUNCTION: NendoU is a Mn(2+)-dependent, uridylate-specific enzyme,
which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.
{ECO:0000250}.
-!- 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).
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. Eight copies of
nsp7 and eight copies of nsp8 assemble to form a
heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 6: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 7: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 8: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 9: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 10: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Helicase: Host endoplasmic reticulum-Golgi
intermediate compartment {ECO:0000305}. Note=The helicase
interacts with the N protein in membranous complexes and
colocalizes with sites of synthesis of new viral RNA.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Uridylate-specific endoribonuclease: Host
cytoplasm, host perinuclear region {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6W0-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6F6-1; Sequence=External;
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. 3CL-PRO and PL-PRO proteinases are
autocatalytically processed (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: Bat coronavirus 512/2005 is highly similar to
porcine epidemic diarrhea virus (PEDV).
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DQ648858; ABG47077.1; -; Genomic_RNA.
RefSeq; YP_001351683.1; NC_009657.1. [P0C6W0-1]
ProteinModelPortal; P0C6W0; -.
SMR; P0C6W0; -.
PRIDE; P0C6W0; -.
GeneID; 11266518; -.
KEGG; vg:11266518; -.
Proteomes; UP000113079; Genome.
GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0016896; F:exoribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0039548; P:suppression by virus of host IRF3 activity; 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.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR009461; Coronavirus_NSP16.
InterPro; IPR027352; CV_ZBD.
InterPro; IPR037227; EndoU-like.
InterPro; IPR002589; Macro_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR009466; NSP11.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR009469; RNA_pol_N_coronovir.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF06478; Corona_RPol_N; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF06471; NSP11; 1.
Pfam; PF06460; NSP13; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF08715; Viral_protease; 2.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF142877; SSF142877; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51653; CV_ZBD; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 2.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
3: Inferred from homology;
Activation of host autophagy by virus; ATP-binding; Complete proteome;
Endonuclease; Exonuclease; Helicase; Host cytoplasm; Host membrane;
Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host IRF3 by virus;
Inhibition of host RLR pathway by virus; Membrane; Metal-binding;
Methyltransferase;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Nuclease;
Nucleotide-binding; Nucleotidyltransferase; Protease;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
RNA-directed RNA polymerase; Thiol protease; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation pathway;
Viral immunoevasion; Viral RNA replication; Zinc; Zinc-finger.
CHAIN 1 110 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000289911.
CHAIN 111 897 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000289912.
CHAIN 898 2530 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000289913.
CHAIN 2531 3012 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000289914.
CHAIN 3013 3314 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000289915.
CHAIN 3315 3590 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000289916.
CHAIN 3591 3673 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000289917.
CHAIN 3674 3868 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000289918.
CHAIN 3869 3976 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000289919.
CHAIN 3977 4111 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000289920.
CHAIN 4112 5038 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000289921.
CHAIN 5039 5557 Helicase. {ECO:0000250}.
/FTId=PRO_0000289922.
CHAIN 5558 6153 Exoribonuclease. {ECO:0000250}.
/FTId=PRO_0000289923.
CHAIN 6154 6492 Uridylate-specific endoribonuclease.
{ECO:0000250}.
/FTId=PRO_0000289924.
CHAIN 6493 6793 Putative 2'-O-methyl transferase.
{ECO:0000250}.
/FTId=PRO_0000289925.
TRANSMEM 1973 1993 Helical. {ECO:0000255}.
TRANSMEM 2036 2056 Helical. {ECO:0000255}.
TRANSMEM 2119 2139 Helical. {ECO:0000255}.
TRANSMEM 2141 2161 Helical. {ECO:0000255}.
TRANSMEM 2164 2184 Helical. {ECO:0000255}.
TRANSMEM 2543 2563 Helical. {ECO:0000255}.
TRANSMEM 2634 2654 Helical. {ECO:0000255}.
TRANSMEM 2669 2689 Helical. {ECO:0000255}.
TRANSMEM 2769 2789 Helical. {ECO:0000255}.
TRANSMEM 2802 2822 Helical. {ECO:0000255}.
TRANSMEM 2829 2849 Helical. {ECO:0000255}.
TRANSMEM 2878 2898 Helical. {ECO:0000255}.
TRANSMEM 3351 3371 Helical. {ECO:0000255}.
TRANSMEM 3376 3396 Helical. {ECO:0000255}.
TRANSMEM 3414 3434 Helical. {ECO:0000255}.
TRANSMEM 3443 3463 Helical. {ECO:0000255}.
TRANSMEM 3466 3486 Helical. {ECO:0000255}.
TRANSMEM 3488 3507 Helical. {ECO:0000255}.
TRANSMEM 3511 3531 Helical. {ECO:0000255}.
DOMAIN 1069 1302 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1303 1467 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1699 1965 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3013 3314 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 5039 5122 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5296 5477 (+)RNA virus helicase ATP-binding.
DOMAIN 5478 5647 (+)RNA virus helicase C-terminal.
ZN_FING 1174 1205 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4050 4066 {ECO:0000250}.
ZN_FING 4092 4105 {ECO:0000250}.
NP_BIND 5321 5328 ATP. {ECO:0000250}.
REGION 1973 2184 HD1. {ECO:0000250}.
REGION 2543 2898 HD2. {ECO:0000250}.
REGION 3351 3531 HD3. {ECO:0000250}.
REGION 4649 4951 RNA-directed RNA polymerase.
{ECO:0000250}.
COMPBIAS 1827 1946 Val-rich.
ACT_SITE 1103 1103 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1252 1252 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1737 1737 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1902 1902 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3053 3053 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3156 3156 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
METAL 5043 5043 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5046 5046 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5054 5054 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5057 5057 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5064 5064 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5067 5067 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5071 5071 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5077 5077 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5088 5088 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5093 5093 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5110 5110 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5113 5113 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 110 111 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 897 898 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2530 2531 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 3012 3013 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3314 3315 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3590 3591 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3673 3674 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3868 3869 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3976 3977 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4111 4112 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5038 5039 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5557 5558 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6153 6154 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6492 6493 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 6793 AA; 757262 MW; 6C76171F3E67FE1D CRC64;
MASNHISLAF ANDEEISAIG FGSVEEAVSY YSDAAVNGFD QCRFVSLGLQ DAVVGVEDDD
VVMLITGVTQ LRAYLGTFGD RPLNLRGWLL FSNCNYFLEE LDLVFGRCGG TTIPVDQFMC
GADGAPVIQE GDWTFMDYFQ DSNQFTLNGI TYVKAWDVDR KPNDYAKQNV TCIRRITYIT
DHRHVLADGT TMKTARHPKV NKSVVLDSPF DQIYKEVGSP FMGNGSTFVE MLKDPAFFHA
LITCECGRSE WTVGDWKGYN SLCCNIKCKP ITIVTPKAVP GAVVITKAGI GAGLKCYNNV
FLKHIIDLVV PGTNLGWGVW RIAKVQSKDD VATSGNVLVD DPEDRLDPCY FGNDGPFATK
FKFQLLANSF DDEVKGAIVQ GVVHVNTAIC DVVKDILGLP WFVKKLGSLV TVMWDQFVAG
VQSMKICTLK VVQLAKALSC ATMSVVKGVI TLVAEVPEIF KRLFYTLTSA LKSLCTSSCD
ALVVAGKSFA KIGDYVLLPS ALVRLVSSKV KGKAQSGIKQ LQFATVVLGD THKVESDRVE
FSSVNLKMVD EEFPLNPVGH TVAVGNQAFF CSDGLYRFMA DRDLVITSPI FKPELELEPI
FECDAIPGFP KVAASNVAEL CVKVDTLLFN YDKIYKKYST IIKGDRCYIQ CTHTFKAPSY
YFDDDEFVEL CTKYYKLPDF DAFYNAVHAA TDMDQFCALC TSGFEVFIPR VPDCPPILND
IDGGSIWTSF ILSVRSATDF IKTLKIDLGL NGVVVFVTKK FRKAGALLQK LYNAFLDTVT
SFIKVAGVAF KYCATCVPKI VINGCYHTVT RLFAKDLQIP TEDGVADFNT FNHCVFPVNP
TRIETDSLEL EEVDFVEPGV DGKLVILDDY SFYSDGTNYY PSDGKGVVAS CFKKKGGGVV
TISDEVQVRT IDPVYKVRLE YEFEDETLVK VCEKAIGTKL KVTGDWSNLL ETLEKAMDVV
RQHLDVPDYF VYDEEGGTDL NLTIMVSQWP LSSDSEDDFK AVDDEPNANT DETVDTFAED
VAETQNVQQD VTQDEVEAVC DLVVKATEEG PIEHEELSED QKEVQQALAF IEDKPVVVKP
DVFAFSYASY GGLKVLNQSS NNCWVSSALV QLQLTGLLDS DEMQLFNAGR VSPMVKRCYE
SQRAIFGSLG DVSACLESLL KDRDGMSITC TIDCGCGPGV RVYENAIFRF TPLKTAFPMG
RCLICSKTLM HTITQMKGTG IFCRDATALD VDTLVVKPLC AAVYVGAQDG GHYLTNMYDA
NMAVDGHGRH PIKFNTINTL CYKDVDWEVS NGSCDVKPFL TYKNIEFYQG ELSALLSVNH
DFVVNAANEQ LSHGGGIAKA LDDLTKGELQ VLSNQYVSRN GSIKVGSGVL IKCKEHSILN
VVGPRKGKHA AELLTKAYTF VFKQKGVPLM PLLSVGIFKV PITESLAAFL ACVGDRVCKC
FCYTDKERLA IQNFVTSFQT EQPVEPLPVI QEVKGVQLEK PVPDVKVENP CEPFRIEGDA
KFYDLTPSMV QSLQVTRLVS FTNSDLCLGS FVRDCDGYVQ GSLGGAIANY KKSNPVLPAG
NCVTLKCDGF ISFTFVILPK EGDTNYEKNF NRAIAKFLKL KGSLLVVVED SSVFNKISHA
SVAGYVAKPA LVDTLFEAKP VQVVVTQDQR SFHTVELSTS QTYGQQLGDC VVEDKKVTNL
KPVSKDKVVS VVPNVDWDKH YGFVDAGIFH TLDHTMFVFD NNVVNGKRVL RTSDNNCWIN
AVCLQLQFAN AKFKPKGLQQ LWESYCTGDV AMFVHWLYWI TGVEKGEPSD AENTLNIISR
FLKPQGSVEM LRATSTTCDG TCSTKRVVST PVVNASVLKV GLDDGNCVHG LPLVDRVVSV
NGTVIITNVG DTPGKPVVAT ENLLLDGVSY TVFQDSTTGV GHYTVFDKEA KLMFDGDVLK
PCDLNVSPVT SVVVCNNKKI VVQDPVKRVE LDASKFLDTM NVASEKFFTF GDFVSRNIIV
LIVYLFSLLA ICFRALKKRD MKVMAGVPER TGIILKRSVK YNYKALKFFF RLKFQYIKVF
LKFSLVLYTL YALMFMFIRF TPVGTPICKR YTDGYANSTF DKNDYCGNVL CKICLYGYEE
LSDFTHTRVI WQHLKDPLIG NILPLFYLVF LIIFGGFFVR IGITYFIMQY INAAGVALGY
QDNVWLLHLL PFNSMGNIIV VAFIVTRILL FLKHVLFGCD KPSCIACSKS AKLTRVPLQT
ILQGVTKSFY VNANGGKKFC KKHNFFCVDC DSYGYGCTFI NDVIAPELSN VTKLNVIPTG
PATIIIDKVE FSNGFYYLYS GSTFWKYNFD ITEAKYACKD VLKNCNILTD FVVFNNSGSN
VTQVKNACVY FSQLLCKPIK LVDSALLASL NVDFSANLHK AFVEVLSNSF GKDLSNCSNM
NECRESLGLS DVPEEEFSAA VSEAHRYDVL ISDVSFNNLI VSYAKPEEKL AVHDIANCMR
VGAKVVNHNV LTKDNVPVVW LAKDFIALSE EARKYIVRTT KTKGINFMLT FNDRRMHLTI
PTISVANKKG AGLPSLFTRL YSFFWHLCVL IVVLFVATSL LDFSAQVTSD TQYDFKYIEN
GVLKVFEKPL DCVHNAFVNF NEWHNAKFGS IPTNSRRCPI VVGTSDEVRY IPGVPAGVFL
YGKSLIFAMS TIFGTSGLCF DDRGLTDPDS CIFNSACTTL SGIGGRNVYC YREGVVDNAK
LYSSLLPHSY YRLMDGNHIV LPEIITRGFG IRTIKTQAMT YCRTGECIDS QAGVCVGLDR
FFVYSKTPGS DYVCGTGFFS LLFNVIGMFS NSIPVTVMSG QILLNCVVAF TAVMACFAFT
KFKRLFGDMS FGVLSVGLCT VVNNLSYVVT QNSIGMLAYA TLYFLCTKGV RYSWVWHVGF
AISYCFLAPW WVVLAYLICA LLEFLPNLFK LKVSTQLFEG DKFVGSFESA ASGTFVLDMH
SYQKLANSIS TEKLKQYCAS YNRYKYYSGS ASEADYRLAC FAHLAKAMSD FANDHMDKLY
TPPTVSYNST LQAGLRKMAQ PSGIVEGCIV RVSYGNLTLN GLWLGDTVIC PRHVIASNTT
NVIDYDHAMS LVRLHNFSIS SGNMFLGVIS ASMRGTLLHI KVNQSNVNTP NYTYKVLKPG
DSFNILACYD GSAAGVYGVN MRTNYTIRGS FISGACGSPG YNINNGVVEF CYMHHLELGS
GCHVGSDMDG TMYGKYEDQP TLQIEGASNL VTENVCSWLY GALINGDRWW LSSVSVGVDT
YNEWALRNGM TALKNVDCFS LLVAKTGVDV GRLLASIQKL HGNFGGKSIL GCTSLCDEFT
LSEVVKQMYG VTLQSGKVSR AFRNASIVCC LLFLFLSEML NHSKLFWINP GYITPVFLAI
IVASSALMLL VKHKLLFLQL YLLPSLCIVS GYNIFKDYHF YTYMLEEFDY KVPFGGFNVT
GVLNISLCCF VMGLHTFRFL QTPNKIFSYV VAVLTVLYTY YYSTDVLGLI LTSMSGFTNY
WFIGTATYKL ATYVLPHTSL LDSFDAIKAV VFLYLLLGYC NCVYYGSLYW INRFCKLTLG
CYEFKVSAAE FKYMVANGLR APTGVFDALI LSLKLIGVGG RKTIKISSVQ SKLTDLKCTN
VVLLGCLSNM NIAANSREWA YCVDLHNKIN LCNDAEAAQE MLLALLAFFL SKNSAFGVDE
LLDSYFNDSS VLQSVAATYV NLPSYLAYET ARQSYEDALA NGSPPQLVKQ LRHAMNVAKS
EFDREASTQR KLDRMAEQAA SQMYKEARAV NRKSKVVSAM HSLLFGMLRR LDMSSVDTIL
SLAKDGVVPL SIIPAVSATK LNIVVSDIES YSKIQREGCV HYAGVIWSVV DIKDNDGKPV
HAKEVVTSNV ESLAWPLFLN CERIIKLQNN EIIPSKIKQR PIKAEGEGVV ADGNALYSNE
GGRTFMYAFI SDKPDLKVVK WEFDGGSNAI ELEPPCKFLV EAPSGPVVKY LYFVRNLNNL
RRGAVLGFIG ATVRLQAGKQ TEQATNSSLL TLCAFAVDPP KTYLDAVKSG HRPVGNCVKM
LANGSGNGQA ITNGVEASTN QDSYGGASVC LYCRAHVEHP DMDGFCKLRG KYVQVPLGTL
DPIRFVLENT VCKVCGCWQA NGCTCDRAVI QSVDSGYLNR VRGSSAARLE PLNGSDTHHV
FRAFDVYNRD VACISKFLKV NCVRLKNLDK HDAFWIVKKC TKSVMEHEQS IYNLISDCGA
VAKHDFFTWK EGRSVYGNVC RQDLTEYTMM DLCYALRNFD ENNCETLKKI LVVVGACDES
YFDNKLWFDP VENEDVHRVY AKLGTIVARA MLKCVKYCDA MVEQGIVGVI TLDNQDLNGD
FYDFGDFVTS VKGMGVPICT SYYSYMMPVM GMTNCLASEC FIKSDIFGED FRTFDLLAYD
FTEHKVNLFN KYFKHWGQTY HPNCEDCHDE SCIVHCANFN TLFATTIPIT AFGPLCRKCW
IDGVPLVTTA GYHFKQLGIV WNKDLNLHSS RLTINELLQF CADPSLLIAS SPALVDKRTV
CFSVAALGTG MTNQTVKPGH FNREFYDFLR SQGFFEEGSE LTLKHFFFAQ KGDAAVRDFD
YYRYNRTTVL DICQARVVYQ IVQCYFGMYE GGCITAKEVI VNNLNKSAGY PFNKFGKAGL
YYDSLSYEEQ DDLYAYTKRN IIPTMTQLNL KYAISGKDRA RTVGGVSLLS TMTTRQYHQK
HLKSIVNTRG ASVVIGTTKF YGGWDNMLKT LIKDVENPHL MGWDYPKCDR ALPNMIRMIS
AMILGSKHVN CCSSSDRYYR LCNELAQVLT EMVYSNGGFY VKPGGTTSGD ATTAYANSVF
NIFQATSANV NRLLSVDSNT CNNIEVKQLQ RKLYDCCYRS SSVDQSFVEE YFGYLRKHFS
MMILSDDGVV CYNSEYAALG YVADLNAFKA VLYYQNNVFM SASKCWIEPD INKGPHEFCS
QHTMQIVDKD GTYYLPYPDP SRILSAGVFV DDIVKTDPVI LLERYVSLAI DAYPLSKHDN
PEYRRVFTVM LDWVKHLYKT LNQGVLDSFS VTLLEDATAK FWDESFYASM YEQSSVLQSA
GLCVVCSSQT VLRCGDCIRR PMLCTKCAYD HVVSTSHKFI LAITPYVCCS SGCGVSDVTK
LYLGGLSYWC VDHKPRLSFP LCSSGNVFGL YKNSATGSPD VDDFNTLATS DWTDVKDYKL
ANDVKDSLRL FAAETIKAKE ESVKSSYACA TIHEVVGPKE LVLKWEVGKP RPPLSRNSVF
TCYHITKNTK FQVGEFTFEK LDYDNDAVSY KSTATTKLVP GMVFVLTSHN VQPLRAPTII
NQERYSTLHK LRPAFNIHED YSNLIPYYQL IGKQKLTTIQ GPPGSGKSHC VIGLGLYFPG
ARIVFTACSH AAVDSLCVKA ATAYSSDRCS RIIPQKARIE CYDGFKSNNT SAQYLFSTVN
ALPEVNADIC VVDEVSMCTN YDLSVINQRV NYRHIVYVGD PQQLPAPRVM ITRGVLVPED
YNVVTRRMCV LKPDIFLHKC YRCPAEIVNT VSEMVYENQF VPVKSESKEC FKIYCRGNVQ
VDNGSSINRR QLEVVRMFLA KNPKWAKAVF ISPYNSQNYV AGRVLGLQIQ TVDSSQGSEY
DYVIYTQTSD TAHASNVNRF NVAITRAKKG ILCIMCDREL FDILKFYELK LSDLQVGDGC
GLFKDCYKGE DNLPPSHAPT FMSLSDNFKT DKDLAVQIGV NGPVKYEHVI SFMGFRFDIN
VPNQHTLFCT RDFAMRNARG WLGFDVEGAH VIGSNVGTNV PLQLGFSNGV DFVVRPEGCV
STEVGDVIQP VRARAPPGDQ FTHLLPLLRK GQPWSVIRRR IVQMCSDYLA NLSDTLIFVL
WSGGLELTTM RYFVKLGPVQ TCDCGKRATC YNSTNHTFSC FRHALGSDYI YNCYCIDIQQ
WGYTGSLSMN HHEVCNIHRN EHVASGDAAM TRCLAIHDCF VKNVDWSITY PFIANEQAIN
KSGRLVQSHV MRAVLKLYNP KAIHDVGNPK GIRCVVTDAS WYCYDKNPTN TNVKMLEYDY
ITHGQLDGLC LFWNCNVDMY PEFSVVCRFD TRMRSTLNLE GCNGGSLYVN NHAFHTPAYD
KRAFAKLKAM PFFFYDDSEC EKLQDAVNYV PLRASNCITR CNVGGAVCSK HCALYHNYVM
AYNTFTTAGF TIWVPNSFDM FNLWQTFKNS NVQGLENIAY NVVKKGSFVG VEGELPVAVV
NDKVMVRDGV SDNVVFVNNT SLPTNVAFEL YAKRKVGLTP PLTILKNLGV VCTSKCVLWD
YEASRPLTTF TKDVCKYTDF DGDVCTLFDN SVPGAFERFT VTKNAVLISL TAVKKLTAIK
LTYGYLNGVP VFTHEDKPFT WYIYTRKDGA FVEYPDGYFT QGRVISDFQP RSNMEEDFLN
MDMGLFISKY GLEDYGFEHV VFGDVSKTTL GGLHLLISQI RLSKIGVLKV EDFVSSSDST
LKSCTVTYVD NPSSKMVCTY VDLLLDDFVN ILKSVDLSVV SKVHEVVIDC KVWRWMLWCK
DHKVQTFYPQ LQSAEWKCGY SMPSIYKIQR MCLEPCNLYN YGSGLKLPDG IMFNVVKYTQ
LCQYLNSTTM CVPHHMRVLH LGAGSDKGVA PGTAVLRRWL PLDAVIVDND VNDYVSDADF
SYTGDCASMY LTDKFDLVIS DMYDGRTKSC DGDNVSKEGF FPYINGVITE KLALGGTVAI
KITEFSWNKK LYELIQKFEY WTLFCTSVNT SSSEAFLIGV HFLGDFSTNA IIDGNIMHAN
YIFWRNSTIM TMSYNSVLDL SKFSCKHKAT VVVNLKDSSV TDLVLGLLKN GKLLIRNNGV
VCGFSNHLVN STK


Related products :

Catalog number Product name Quantity


 

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