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 R1A_CVHNL               Reviewed;        4060 AA.
P0C6U6; Q6Q1S3;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
28-MAR-2018, entry version 64.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a 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=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Human coronavirus NL63 (HCoV-NL63).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Alphacoronavirus.
NCBI_TaxID=277944;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Amsterdam I;
PubMed=15034574; DOI=10.1038/nm1024;
Van Der Hoek L., Pyrc K., Jebbink M.F., Vermeulen-Oost W.,
Berkhout R.J., Wolthers K.C., Wertheim-Van Dillen P.M., Kaandorp J.,
Spaargaren J., Berkhout B.;
"Identification of a new human coronavirus.";
Nat. Med. 10:368-373(2004).
[2]
FUNCTION.
PubMed=20181693; DOI=10.1128/JVI.02406-09;
Clementz M.A., Chen Z., Banach B.S., Wang Y., Sun L., Ratia K.,
Baez-Santos Y.M., Wang J., Takayama J., Ghosh A.K., Li K.,
Mesecar A.D., Baker S.C.;
"Deubiquitinating and interferon antagonism activities of coronavirus
papain-like proteases.";
J. Virol. 84:4619-4629(2010).
-!- 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. {ECO:0000269|PubMed:20181693}.
-!- 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: 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}.
-!- 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).
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6U6-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6X5-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
-!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
association of the replication complex and thereby alter the
architecture of the host cell membrane.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases
yield mature proteins. 3CL-PRO and PL-PRO proteinases are
autocatalytically processed.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; AY567487; -; NOT_ANNOTATED_CDS; Genomic_RNA.
PDB; 2VRI; X-ray; 1.80 A; A=1258-1421.
PDB; 3TLO; X-ray; 1.60 A; A/B=2940-3242.
PDB; 5GWY; X-ray; 2.85 A; A/B=2940-3242.
PDBsum; 2VRI; -.
PDBsum; 3TLO; -.
PDBsum; 5GWY; -.
ProteinModelPortal; P0C6U6; -.
SMR; P0C6U6; -.
BindingDB; P0C6U6; -.
ChEMBL; CHEMBL3232683; -.
OrthoDB; VOG09000000; -.
EvolutionaryTrace; P0C6U6; -.
Proteomes; UP000008573; Genome.
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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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:InterPro.
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:0019079; P:viral genome replication; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
Gene3D; 1.10.150.420; -; 1.
Gene3D; 1.10.8.370; -; 1.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR038123; NSP4_C_sf.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF09401; NSP10; 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; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF51126; SSF51126; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 2.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus;
Complete proteome; 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;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Protease;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
Thiol protease; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
CHAIN 1 4060 Replicase polyprotein 1a.
/FTId=PRO_0000338230.
CHAIN 1 110 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338231.
CHAIN 111 898 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338232.
CHAIN 899 2462 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338233.
CHAIN 2463 2939 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338234.
CHAIN 2940 3242 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338235.
CHAIN 3243 3521 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338236.
CHAIN 3522 3604 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338237.
CHAIN 3605 3799 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338238.
CHAIN 3800 3908 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338239.
CHAIN 3909 4043 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338240.
CHAIN 4044 4060 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338241.
TRANSMEM 1903 1923 Helical. {ECO:0000255}.
TRANSMEM 1968 1988 Helical. {ECO:0000255}.
TRANSMEM 2050 2070 Helical. {ECO:0000255}.
TRANSMEM 2073 2093 Helical. {ECO:0000255}.
TRANSMEM 2111 2131 Helical. {ECO:0000255}.
TRANSMEM 2468 2488 Helical. {ECO:0000255}.
TRANSMEM 2727 2747 Helical. {ECO:0000255}.
TRANSMEM 2752 2769 Helical. {ECO:0000255}.
TRANSMEM 2772 2792 Helical. {ECO:0000255}.
TRANSMEM 2800 2820 Helical. {ECO:0000255}.
TRANSMEM 3254 3274 Helical. {ECO:0000255}.
TRANSMEM 3279 3299 Helical. {ECO:0000255}.
TRANSMEM 3303 3323 Helical. {ECO:0000255}.
TRANSMEM 3342 3362 Helical. {ECO:0000255}.
TRANSMEM 3376 3396 Helical. {ECO:0000255}.
TRANSMEM 3397 3417 Helical. {ECO:0000255}.
TRANSMEM 3442 3462 Helical. {ECO:0000255}.
DOMAIN 1021 1262 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1263 1421 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1640 1886 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 2940 3242 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1134 1165 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1757 1788 C4-type 2; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ZN_FING 3982 3998 {ECO:0000250}.
ZN_FING 4024 4037 {ECO:0000250}.
REGION 1903 2131 HD1. {ECO:0000250}.
REGION 2468 2820 HD2. {ECO:0000250}.
REGION 3254 3462 HD3. {ECO:0000250}.
COMPBIAS 625 628 Poly-Leu.
COMPBIAS 1975 1978 Poly-Leu.
ACT_SITE 1062 1062 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1212 1212 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1678 1678 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1836 1836 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 2980 2980 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3083 3083 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 110 111 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 898 899 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2462 2463 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 2939 2940 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3242 3243 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3521 3522 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3604 3605 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3799 3800 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3908 3909 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4043 4044 Cleavage; by 3CL-PRO. {ECO:0000250}.
STRAND 1260 1263 {ECO:0000244|PDB:2VRI}.
STRAND 1266 1271 {ECO:0000244|PDB:2VRI}.
HELIX 1273 1276 {ECO:0000244|PDB:2VRI}.
TURN 1277 1279 {ECO:0000244|PDB:2VRI}.
STRAND 1283 1289 {ECO:0000244|PDB:2VRI}.
HELIX 1298 1306 {ECO:0000244|PDB:2VRI}.
TURN 1307 1309 {ECO:0000244|PDB:2VRI}.
HELIX 1310 1322 {ECO:0000244|PDB:2VRI}.
STRAND 1330 1334 {ECO:0000244|PDB:2VRI}.
STRAND 1339 1344 {ECO:0000244|PDB:2VRI}.
HELIX 1352 1365 {ECO:0000244|PDB:2VRI}.
STRAND 1366 1368 {ECO:0000244|PDB:2VRI}.
STRAND 1370 1373 {ECO:0000244|PDB:2VRI}.
HELIX 1378 1380 {ECO:0000244|PDB:2VRI}.
HELIX 1384 1392 {ECO:0000244|PDB:2VRI}.
STRAND 1400 1404 {ECO:0000244|PDB:2VRI}.
HELIX 1407 1418 {ECO:0000244|PDB:2VRI}.
HELIX 2950 2953 {ECO:0000244|PDB:3TLO}.
STRAND 2956 2961 {ECO:0000244|PDB:3TLO}.
STRAND 2964 2971 {ECO:0000244|PDB:3TLO}.
STRAND 2974 2978 {ECO:0000244|PDB:3TLO}.
HELIX 2979 2982 {ECO:0000244|PDB:3TLO}.
STRAND 2986 2988 {ECO:0000244|PDB:5GWY}.
HELIX 2992 2998 {ECO:0000244|PDB:3TLO}.
HELIX 3001 3003 {ECO:0000244|PDB:3TLO}.
STRAND 3004 3008 {ECO:0000244|PDB:3TLO}.
STRAND 3011 3013 {ECO:0000244|PDB:3TLO}.
STRAND 3015 3021 {ECO:0000244|PDB:3TLO}.
STRAND 3024 3031 {ECO:0000244|PDB:3TLO}.
STRAND 3038 3041 {ECO:0000244|PDB:3TLO}.
STRAND 3049 3056 {ECO:0000244|PDB:3TLO}.
STRAND 3059 3067 {ECO:0000244|PDB:3TLO}.
STRAND 3086 3090 {ECO:0000244|PDB:3TLO}.
STRAND 3096 3105 {ECO:0000244|PDB:3TLO}.
STRAND 3111 3114 {ECO:0000244|PDB:3TLO}.
HELIX 3121 3123 {ECO:0000244|PDB:3TLO}.
STRAND 3126 3128 {ECO:0000244|PDB:3TLO}.
HELIX 3140 3152 {ECO:0000244|PDB:3TLO}.
HELIX 3166 3175 {ECO:0000244|PDB:3TLO}.
HELIX 3185 3187 {ECO:0000244|PDB:3TLO}.
HELIX 3188 3194 {ECO:0000244|PDB:3TLO}.
HELIX 3198 3208 {ECO:0000244|PDB:3TLO}.
STRAND 3220 3222 {ECO:0000244|PDB:3TLO}.
HELIX 3229 3237 {ECO:0000244|PDB:3TLO}.
SEQUENCE 4060 AA; 451388 MW; 0F6313C474B7ED9C CRC64;
MFYNQVTLAV ASDSEISGFG FAIPSVAVRT YSEAAAQGFQ ACRFVAFGLQ DCVTGINDDD
YVIALTGTNQ LCAKILPFSD RPLNLRGWLI FSNSNYVLQD FDVVFGHGAG SVVFVDKYMC
GFDGKPVLPK NMWEFRDYFN NNTDSIVIGG VTYQLAWDVI RKDLSYEQQN VLAIESIHYL
GTTGHTLKSG CKLTNAKPPK YSSKVVLSGE WNAVYRAFGS PFITNGMSLL DIIVKPVFFN
AFVKCNCGSE SWSVGAWDGY LSSCCGTPAK KLCVVPGNVV PGDVIITSTS AGCGVKYYAG
LVVKHITNIT GVSLWRVTAV HSDGMFVASS SYDALLHRNS LDPFCFDVNT LLSNQLRLAF
LGASVTEDVK FAASTGVIDI SAGMFGLYDD ILTNNKPWFV RKASGLFDAI WDAFVAAIKL
VPTTTGVLVR FVKSIASTVL TVSNGVIIMC ADVPDAFQSV YRTFTQAICA AFDFSLDVFK
IGDVKFKRLG DYVLTENALV RLTTEVVRGV RDARIKKAMF TKVVVGPTTE VKFSVIELAT
VNLRLVDCAP VVCPKGKIVV IAGQAFFYSG GFYRFMVDPT TVLNDPVFTG DLFYTIKFSG
FKLDGFNHQF VTASSATDAI IAVELLLLDF KTAVFVYTCV VDGCSVIVRR DATFATHVCF
KDCYNVWEQF CIDNCGEPWF LTDYNAILQS NNPQCAIVQA SESKVLLERF LPKCPEILLS
IDDGHLWNLF VEKFNFVTDW LKTLKLTLTS NGLLGNCAKR FRRVLVKLLD VYNGFLETVC
SVAYTAGVCI KYYAVNVPYV VISGFVSRVI RRERCDMTFP CVSCVTFFYE FLDTCFGVSK
PNAIDVEHLE LKETVFVEPK DGGQFFVSGD YLWYVVDDIY YPASCNGVLP VAFTKLAGGK
ISFSDDVIVH DVEPTHKVKL IFEFEDDVVT SLCKKSFGKS IIYTGDWEGL HEVLTSAMNV
IGQHIKLPQF YIYDEEGGYD VSKPVMISQW PISNDSNGCV VEASTDFHQL ECIVDDSVRE
EVDIIEQPFE EVEHVLSIKQ PFSFSFRDEL GVRVLDQSDN NCWISTTLVQ LQLTKLLDDS
IEMQLFKVGK VDSIVQKCYE LSHLISGSLG DSGKLLSELL KEKYTCSITF EMSCDCGKKF
DDQVGCLFWI MPYTKLFQKG ECCICHKMQT YKLVSMKGTG VFVQDPAPID IDAFPVKPIC
SSVYLGVKGS GHYQTNLYSF NKAIDGFGVF DIKNSSVNTV CFVDVDFHSV EIEAGEVKPF
AVYKNVKFYL GDISHLVNCV SFDFVVNAAN ENLLHGGGVA RAIDILTEGQ LQSLSKDYIS
SNGPLKVGAG VMLECEKFNV FNVVGPRTGK HEHSLLVEAY NSILFENGIP LMPLLSCGIF
GVRIENSLKA LFSCDINKPL QVFVYSSNEE QAVLKFLDGL DLTPVIDDVD VVKPFRVEGN
FSFFDCGVNA LDGDIYLLFT NSILMLDKQG QLLDTKLNGI LQQAALDYLA TVKTVPAGNL
VKLFVESCTI YMCVVPSIND LSFDKNLGRC VRKLNRLKTC VIANVPAIDV LKKLLSSLTL
TVKFVVESNV MDVNDCFKND NVVLKITEDG INVKDVVVES SKSLGKQLGV VSDGVDSFEG
VLPINTDTVL SVAPEVDWVA FYGFEKAALF ASLDVKPYGY PNDFVGGFRV LGTTDNNCWV
NATCIILQYL KPTFKSKGLN VLWNKFVTGD VGPFVSFIYF ITMSSKGQKG DAEEALSKLS
EYLISDSIVT LEQYSTCDIC KSTVVEVKSA IVCASVLKDG CDVGFCPHRH KLRSRVKFVN
GRVVITNVGE PIISQPSKLL NGIAYTTFSG SFDNGHYVVY DAANNAVYDG ARLFSSDLST
LAVTAIVVVG GCVTSNVPTI VSEKISVMDK LDTGAQKFFQ FGDFVMNNIV LFLTWLLSMF
SLLRTSIMKH DIKVIAKAPK RTGVILTRSF KYNIRSALFV IKQKWCVIVT LFKFLLLLYA
IYALVFMIVQ FSPFNSLLCG DIVSGYEKST FNKDIYCGNS MVCKMCLFSY QEFNDLDHTS
LVWKHIRDPI LISLQPFVIL VILLIFGNMY LRFGLLYFVA QFISTFGSFL GFHQKQWFLH
FVPFDVLCNE FLATFIVCKI VLFVRHIIVG CNNADCVACS KSARLKRVPL QTIINGMHKS
FYVNANGGTC FCNKHNFFCV NCDSFGPGNT FINGDIAREL GNVVKTAVQP TAPAYVIIDK
VDFVNGFYRL YSGDTFWRYD FDITESKYSC KEVLKNCNVL ENFIVYNNSG SNITQIKNAC
VYFSQLLCEP IKLVNSELLS TLSVDFNGVL HKAYVDVLCN SFFKELTANM SMAECKATLG
LTVSDDDFVS AVANAHRYDV LLSDLSFNNF FISYAKPEDK LSVYDIACCM RAGSKVVNHN
VLIKESIPIV WGVKDFNTLS QEGKKYLVKT TKAKGLTFLL TFNDNQAITQ VPATSIVAKQ
GAGFKRTYNF LWYVCLFVVA LFIGVSFIDY TTTVTSFHGY DFKYIENGQL KVFEAPLHCV
RNVFDNFNQW HEAKFGVVTT NSDKCPIVVG VSERINVVPG VPTNVYLVGK TLVFTLQAAF
GNTGVCYDFD GVTTSDKCIF NSACTRLEGL GGDNVYCYNT DLIEGSKPYS TLQPNAYYKY
DAKNYVRFPE ILARGFGLRT IRTLATRYCR VGECRDSHKG VCFGFDKWYV NDGRVDDGYI
CGDGLIDLLV NVLSIFSSSF SVVAMSGHML FNFLFAAFIT FLCFLVTKFK RVFGDLSYGV
FTVVCATLIN NISYVVTQNL FFMLLYAILY FVFTRTVRYA WIWHIAYIVA YFLLIPWWLL
TWFSFAAFLE LLPNVFKLKI STQLFEGDKF IGTFESAAAG TFVLDMRSYE RLINTISPEK
LKNYAASYNK YKYYSGSASE ADYRCACYAH LAKAMLDYAK DHNDMLYSPP TISYNSTLQS
GLKKMAQPSG CVERCVVRVC YGSTVLNGVW LGDTVTCPRH VIAPSTTVLI DYDHAYSTMR
LHNFSVSHNG VFLGVVGVTM HGSVLRIKVS QSNVHTPKHV FKTLKPGDSF NILACYEGIA
SGVFGVNLRT NFTIKGSFIN GACGSPGYNV RNDGTVEFCY LHQIELGSGA HVGSDFTGSV
YGNFDDQPSL QVESANLMLS DNVVAFLYAA LLNGCRWWLC STRVNVDGFN EWAMANGYTS
VSSVECYSIL AAKTGVSVEQ LLASIQHLHE GFGGKNILGY SSLCDEFTLA EVVKQMYGVN
LQSGKVIFGL KTMFLFSVFF TMFWAELFIY TNTIWINPVI LTPIFCLLLF LSLVLTMFLK
HKFLFLQVFL LPTVIATALY NCVLDYYIVK FLADHFNYNV SVLQMDVQGL VNVLVCLFVV
FLHTWRFSKE RFTHWFTYVC SLIAVAYTYF YSGDFLSLLV MFLCAISSDW YIGAIVFRLS
RLIVFFSPES VFSVFGDVKL TLVVYLICGY LVCTYWGILY WFNRFFKCTM GVYDFKVSAA
EFKYMVANGL HAPHGPFDAL WLSFKLLGIG GDRCIKISTV QSKLTDLKCT NVVLLGCLSS
MNIAANSSEW AYCVDLHNKI NLCDDPEKAQ SMLLALLAFF LSKHSDFGLD GLIDSYFDNS
STLQSVASSF VSMPSYIAYE NARQAYEDAI ANGSSSQLIK QLKRAMNIAK SEFDHEISVQ
KKINRMAEQA ATQMYKEARS VNRKSKVISA MHSLLFGMLR RLDMSSVETV LNLARDGVVP
LSVIPATSAS KLTIVSPDLE SYSKIVCDGS VHYAGVVWTL NDVKDNDGRP VHVKEITKEN
VETLTWPLIL NCERVVKLQN NEIMPGKLKQ KPMKAEGDGG VLGDGNALYN TEGGKTFMYA
YISNKADLKF VKWEYEGGCN TIELDSPCRF MVETPNGPQV KYLYFVKNLN TLRRGAVLGF
IGATIRLQAG KQTELAVNSG LLTACAFSVD PATTYLEAVK HGAKPVSNCI KMLSNGAGNG
QAITTSVDAN TNQDSYGGAS ICLYCRAHVP HPSMDGYCKF KGKCVQVPIG CLDPIRFCLE
NNVCNVCGCW LGHGCACDRT TIQSVDISYL NEQGVLVQLD


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