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 R1A_IBVM                Reviewed;        3953 AA.
P0C6V5; Q0GNB9;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 55.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a polyprotein;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p87;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.22.-;
AltName: Full=Papain-like proteinase;
Short=PL-PRO;
AltName: Full=p195;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
AltName: Full=Peptide HD2;
AltName: Full=p41;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=M-PRO;
AltName: Full=nsp5;
AltName: Full=p33;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
AltName: Full=p34;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
AltName: Full=p9;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
AltName: Full=p24;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
AltName: Full=p10;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
AltName: Full=p16;
Contains:
RecName: Full=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Avian infectious bronchitis virus (strain M41) (IBV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Gammacoronavirus.
NCBI_TaxID=11127;
NCBI_TaxID=9031; Gallus gallus (Chicken).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Mondal S.P., Buckles E.L.;
"Avian infectious bronchitis virus strain M41.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16934878; DOI=10.1016/j.jviromet.2006.07.018;
Callison S.A., Hilt D.A., Boynton T.O., Sample B.F., Robison R.,
Swayne D.E., Jackwood M.W.;
"Development and evaluation of a real-time Taqman RT-PCR assay for the
detection of infectious bronchitis virus from infected chickens.";
J. Virol. Methods 138:60-65(2006).
-!- FUNCTION: The papain-like proteinase (PL-PRO) is responsible for
the cleavages located at the N-terminus of replicase polyprotein.
Activity of PL-PRO is dependent on zinc (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 peptide p16 might be involved in the EGF signaling
pathway. {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}.
-!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. The three
peptides nsp2, nsp3 and nsp4 may form a complex. Nsp9 is a dimer.
Eight copies of nsp7 and eight copies of nsp8 assemble to form a
heterohexadecamer. 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=P0C6V5-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6Y3-1; 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 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; DQ834384; ABI26421.1; -; Genomic_RNA.
EMBL; AY851295; AAW33784.1; -; Genomic_RNA.
PDB; 3EWO; X-ray; 1.80 A; A/B=1005-1178.
PDB; 3EWP; X-ray; 2.00 A; A/B=1005-1178.
PDB; 3LD1; X-ray; 2.50 A; A=13-371.
PDBsum; 3EWO; -.
PDBsum; 3EWP; -.
PDBsum; 3LD1; -.
ProteinModelPortal; P0C6V5; -.
SMR; P0C6V5; -.
PRIDE; P0C6V5; -.
OrthoDB; VOG09000000; -.
EvolutionaryTrace; P0C6V5; -.
Proteomes; UP000007642; Genome.
Proteomes; UP000096468; 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:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0019079; P:viral genome replication; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
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; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus;
Complete proteome; Host cytoplasm; Host membrane;
Host-virus interaction; Hydrolase; Membrane; Metal-binding; Protease;
Repeat; Ribosomal frameshifting; RNA-binding; Thiol protease;
Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
CHAIN 1 3953 Replicase polyprotein 1a.
/FTId=PRO_0000338336.
CHAIN 1 673 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338337.
CHAIN 674 2267 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338338.
CHAIN 2268 2781 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338339.
CHAIN 2782 3088 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338340.
CHAIN 3089 3381 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338341.
CHAIN 3382 3464 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338342.
CHAIN 3465 3674 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338343.
CHAIN 3675 3785 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338344.
CHAIN 3786 3930 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338345.
CHAIN 3931 3953 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338346.
TRANSMEM 1723 1743 Helical. {ECO:0000255}.
TRANSMEM 1753 1773 Helical. {ECO:0000255}.
TRANSMEM 1846 1866 Helical. {ECO:0000255}.
TRANSMEM 1889 1909 Helical. {ECO:0000255}.
TRANSMEM 2283 2303 Helical. {ECO:0000255}.
TRANSMEM 2373 2393 Helical. {ECO:0000255}.
TRANSMEM 2562 2582 Helical. {ECO:0000255}.
TRANSMEM 2591 2611 Helical. {ECO:0000255}.
TRANSMEM 2614 2634 Helical. {ECO:0000255}.
TRANSMEM 2646 2666 Helical. {ECO:0000255}.
TRANSMEM 3103 3123 Helical. {ECO:0000255}.
TRANSMEM 3124 3144 Helical. {ECO:0000255}.
TRANSMEM 3154 3174 Helical. {ECO:0000255}.
TRANSMEM 3191 3211 Helical. {ECO:0000255}.
TRANSMEM 3222 3242 Helical. {ECO:0000255}.
TRANSMEM 3260 3280 Helical. {ECO:0000255}.
TRANSMEM 3299 3319 Helical. {ECO:0000255}.
DOMAIN 1005 1181 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1238 1499 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 2782 3088 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1355 1392 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 3860 3880 {ECO:0000250}.
ZN_FING 3906 3919 {ECO:0000250}.
REGION 1723 1909 HD1. {ECO:0000250}.
REGION 2283 2666 HD2. {ECO:0000250}.
REGION 2887 3319 HD3. {ECO:0000250}.
COMPBIAS 1729 1734 Poly-Phe.
ACT_SITE 1276 1276 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1439 1439 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 2822 2822 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 2924 2924 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 673 674 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 2267 2268 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 2781 2782 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3088 3089 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3381 3382 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3464 3465 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3674 3675 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3785 3786 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3930 3931 Cleavage; by 3CL-PRO. {ECO:0000250}.
VARIANT 807 807 L -> S.
VARIANT 1618 1618 S -> F.
VARIANT 1739 1739 S -> A.
VARIANT 2631 2631 M -> L.
VARIANT 2774 2774 S -> P.
STRAND 16 20 {ECO:0000244|PDB:3LD1}.
HELIX 25 32 {ECO:0000244|PDB:3LD1}.
HELIX 42 58 {ECO:0000244|PDB:3LD1}.
STRAND 62 66 {ECO:0000244|PDB:3LD1}.
STRAND 69 78 {ECO:0000244|PDB:3LD1}.
STRAND 81 83 {ECO:0000244|PDB:3LD1}.
STRAND 86 88 {ECO:0000244|PDB:3LD1}.
HELIX 94 101 {ECO:0000244|PDB:3LD1}.
HELIX 105 115 {ECO:0000244|PDB:3LD1}.
HELIX 117 120 {ECO:0000244|PDB:3LD1}.
HELIX 124 133 {ECO:0000244|PDB:3LD1}.
HELIX 134 136 {ECO:0000244|PDB:3LD1}.
HELIX 140 146 {ECO:0000244|PDB:3LD1}.
HELIX 152 174 {ECO:0000244|PDB:3LD1}.
HELIX 176 178 {ECO:0000244|PDB:3LD1}.
HELIX 179 182 {ECO:0000244|PDB:3LD1}.
TURN 186 188 {ECO:0000244|PDB:3LD1}.
HELIX 189 197 {ECO:0000244|PDB:3LD1}.
STRAND 199 202 {ECO:0000244|PDB:3LD1}.
HELIX 206 219 {ECO:0000244|PDB:3LD1}.
STRAND 226 229 {ECO:0000244|PDB:3LD1}.
STRAND 232 235 {ECO:0000244|PDB:3LD1}.
HELIX 236 238 {ECO:0000244|PDB:3LD1}.
HELIX 244 255 {ECO:0000244|PDB:3LD1}.
HELIX 261 263 {ECO:0000244|PDB:3LD1}.
STRAND 265 267 {ECO:0000244|PDB:3LD1}.
STRAND 270 272 {ECO:0000244|PDB:3LD1}.
STRAND 277 283 {ECO:0000244|PDB:3LD1}.
STRAND 292 299 {ECO:0000244|PDB:3LD1}.
STRAND 306 310 {ECO:0000244|PDB:3LD1}.
STRAND 314 320 {ECO:0000244|PDB:3LD1}.
STRAND 327 334 {ECO:0000244|PDB:3LD1}.
STRAND 337 344 {ECO:0000244|PDB:3LD1}.
STRAND 347 354 {ECO:0000244|PDB:3LD1}.
STRAND 363 367 {ECO:0000244|PDB:3LD1}.
STRAND 1017 1023 {ECO:0000244|PDB:3EWO}.
HELIX 1025 1035 {ECO:0000244|PDB:3EWO}.
STRAND 1037 1044 {ECO:0000244|PDB:3EWO}.
HELIX 1054 1063 {ECO:0000244|PDB:3EWO}.
HELIX 1065 1078 {ECO:0000244|PDB:3EWO}.
STRAND 1082 1086 {ECO:0000244|PDB:3EWO}.
STRAND 1093 1099 {ECO:0000244|PDB:3EWO}.
HELIX 1109 1120 {ECO:0000244|PDB:3EWO}.
STRAND 1127 1131 {ECO:0000244|PDB:3EWO}.
HELIX 1142 1153 {ECO:0000244|PDB:3EWO}.
STRAND 1159 1165 {ECO:0000244|PDB:3EWO}.
HELIX 1167 1176 {ECO:0000244|PDB:3EWO}.
SEQUENCE 3953 AA; 441177 MW; 70AB99DED32F2B89 CRC64;
MASSLKQGVS PKLRDVILVS KDIPEQLCDA LFFYTSHNPK DYADAFAVRQ KFDRNLQTGK
QFKFETVCGL FLLKGVDKIT PGVPAKVLKA TSKLADLEDI FGVSPFARKY RELLKTACQW
SLTVETLDAR AQTLDEIFDP TEILWLQVAA KIQVSAMAMR RLVGEVTAKV MDALGSNMSA
LFQIFKQQIV RIFQKALAIF ENVSELPQRI AALKMAFAKC AKSITVVVME RTLVVREFAG
TCLASINGAV AKFFEELPNG FMGAKIFTTL AFFREAAVKI VDNIPNAPRG TKGFEVVGNA
KGTQVVVRGM RNDLTLLDQK AEIPVESEGW SAILGGHLCY VFKSGDRFYA APLSGNFALH
DVHCCERVVC LSDGVTPEIN DGLILAAIYS SFSVAELVAA IKRGEPFKFL GHKFVYAKDA
AVSFTLAKAA TIADVLKLFQ SARVKVEDVW SSLTEKSFEF WRLAYGKVRN LEEFVKTCFC
KAQMAIVILA TVLGEGIWHL VSQVIYKVGG LFTKVVDFCE KYWKGFCAQL KRAKLIVTET
LCVLKGVAQH CFQLLLDAIQ FMYKSFKKCA LGRIHGDLLF WKGGVHKIIQ EGDEIWFDAI
DSIDVEDLGV VQEKLIDFDV CDNVTLPENQ PGHMVQIEDD GKNYMFFRFK KDENIYYTPM
SQLGAINVVC KAGGKTVTFG ETTVQEIPPP DVVFIKVSIE CCGEPWNTIF KKAYKEPIEV
ETDLTVEQLL SVVYEKMCDD LKLFPEAPEP PPFENVTLVD KNGKDLDCIK SCHLIYRDYE
SDDDIEEEDA EECDTDSGDA EECDTNLECE EEDEDTKVLA LIQDPASNKY PLPLDDDYSV
YNGCIVHKDA LDVVNLPSGE ETFVVNNCFE GAVKALPQKV IDVLGDWGEA VDAQEQLCQQ
ESTRVISEKS VEGFTGSCDA MAEQAIVEEQ EIVPVVEQSQ DVVVFTPADL EVVKETAEEV
DEFILISAVP KEEVVSQEKE EPQVEQEPTL VVKAQREKKA KKFKVKPATC EKPKFLEYKT
CVGDLAVVIA KALDEFKEFC IVNAANEHMS HGGGVAKAIA DFCGPDFVEY CADYVKKHGP
QQKLVTPSFV KGIQCVNNVV GPRHGDSNLR EKLVAAYKSV LVGGVVNYVV PVLSSGIFGV
DFKISIDAMR EAFKGCAIRV LLFSLSQEHI DYFDATCKQK TIYLTEDGVK YRSVVLKPGD
SLGQFGQVFA RNKVVFSADD VEDKEILFIP TTDKTILEYY GLDAQKYVTY LQTLAQKWDV
QYRDNFVILE WRDGNCWISS AIVLLQAAKI RFKGFLAEAW AKLLGGDPTD FVAWCYASCN
AKVGDFSDAN WLLANLAEHF DADYTNALLK KCVSCNCGVK SYELRGLEAC IQPVRAPNLL
HFKTQYSNCP TCGASSTDEV IEASLPYLLL FATDGPATVD CDENAVGTVV FIGSTNSGHC
YTQADGKAFD NLAKDRKFGR KSPYITAMYT RFSLRSENPL LVVEHSKGKA KVVKEDVSNL
ATSSKASFDD LTDFEQWYDS NIYESLKVQE TPDNLDEYVS FTTKEDSKLP LTLKVRGIKS
VVDFRSKDGF TYKLTPDTDE NSKTPVYYPV LDSISLRAIW VEGSANFVVG HPNYYSKSLR
IPTFWENAES FVKMGYKIDG VTMGLWRAEH LNKPNLERIF NIAKKAIVGS SVVTTQCGKI
LVKAATYVAD KVGDGVVRNI TDRIKGLCGF TRGHFEKKMS LQFLKTLVFF FFYFLKASSK
SLVSSYKIVL CKVVFATLLI VWFIYTSNPV VFTGIRVLDF LFEGSLCGPY NDYGKDSFDV
LRYCAGDFTC RVCLHDRDSL HLYKHAYSVE QIYKDAASGI NFNWNWLYLV FLILFVKPVA
GFVIICYCVK YLVLSSTVLQ TGVGFLDWFV KTVFTHFNFM GAGFYFWLFY KIYVQVHHIL
YCKDVTCEVC KRVARSNRQE VSVVVGGRKQ IVHVYTNSGY NFCKRHNWYC RNCDDYGHQN
TFMSPEVAGE LSEKLKRHVK PTAYAYHVVY EACVVDDFVN LKYKAAIPGK DNASSAVKCF
SVTDFLKKAV FLKEALKCEQ ISNDGFIVCN TQSAHALEEA KNAAVYYAQY LCKPILILDQ
ALYEQLIVEP VSKSVIDKVC SILSNIISVD TAALNYKAGT LRDALLSITK DEEAVDMAIF
CHNHEVEYTG DGFTNVIPSY GMDTDKLTPR DRGFLINADA SIANLRVKNA PPVVWKFSDL
IKLSDSCLKY LISATVKSGG RFFITKSGAK QVISCHTQKL LVEKKAGGVI NNTFKWFMSC
FKWLFVFYIL FTACCLGYYY MEMNKSFVHP MYDVNSTLHV EGFKVIDKGV IREIVSEDNC
FSNKFVNFDA FWGKSYENNK NCPIVTVVID GDGTVAVGVP GFVSWVMDGV MFVHMTQTDR
RPWYIPTWFN REIVGYTQDS IITEGSFYTS IALFSARCLY LTASNTPQLY CFNGDNDAPG
ALPFGSIIPH RVYFQPNGVR LIVPQQILHT PYIVKFVSDS YCRGSVCEYT KPGYCVSLDS
QWVLFNDEYI SKPGVFCGST VRELMFNMVS TFFTGVNPNI YIQLATMFLI LVVIVLIFAM
VIKFQGVFKA YATIVFTIML VWVINAFVLC VHSYNSVLAV ILLVLYCYAS MVTSRNTAII
MHCWLVFTFG LIVPTWLACC YLGFILYMYT PLVFWCYGTT KNTRKLYDGN EFVGNYDLAA
KSTFVIRGTE FVKLTNEIGD KFEAYLSAYA RLKYYSGTGS EQDYLQACRA WLAYALDQYR
NSGVEVVYTP PRYSIGVSRL QAGFKKLVSP SSAVEKCIVS VSYRGNNLNG LWLGDSIYCP
RHVLGKFSGD QWGDVLNLAN NHEFEVVTQN GVTLNVVSRR LKGAVLILQT AVANAETPKY
KFVKANCGDS FTIACSYGGT VIGLYPVTMR SNGTIRASFL AGACGSVGFN IEKGVVNFFY
MHHLELPNAL HTGTDLMGEF YGGYVDEEVA QRVPPDNLVT NNIVAWLYAA IISVKESSFS
QPKWLESTTV SIEDYNRWAS DNGFTPFSTS TAITKLSAIT GVDVCKLLRT IMVKSAQWGS
DPILGQYNFE DELTPESVFN QVGGVRLQSS FVRKATSWFW SRCVLACFLF VLCAIVLFTA
VPLKFYVHAA VILLMAVLFI SFTVKHVMAY MDTFLLPTLI TVIIGVCAEV PFIYNTLISQ
VVIFLSQWYD PVVFDTMVPW MLLPLVLYTA FKCVQGCYMN SFNTSLLMLY QFMKLGFVIY
TSSNTLTAYT EGNWELFFEL VHTIVLANVS SNSLIGLIVF KCAKWMLYYC NATYFNNYVL
MAVMVNGIGW LCTCYFGLYW WVNKVFGLTL GKYNFKVSVD QYRYMCLHKV NPPKTVWEVF
TTNILIQGIG GDRVLPIATV QSKLSDVKCT TVVLMQLLTK LNVEANSKMH AYLVELHNKI
LASDDVGECM DNLLGMLITL FCIDSTIDLG EYCDDILKRS TVLQSVTQEF SHIPSYAEYE
RAKSIYEKVL ADSKNGGVTQ QELAAYRKAA NIAKSVFDRD LAVQKKLDSM AERAMTTMYK
EARVTDRRAK LVSSLHALLF SMLKKIDSEK LNVLFDQANS GVVPLATVPI VCSNKLTLVI
PDPETWVKCV EGVHVTYSTV VWNIDCVTDA DGTELHPTST GSGLTYCISG DNIAWPLKVN
LTRNGHNKVD VALQNNELMP HGVKTKACVA GVDQAHCSVE SKCYYTSISG SSVVAAITSS
NPNLKVASFL NEAGNQIYVD LDPPCKFGMK VGDKVEVVYL YFIKNTRSIV RGMVLGAISN
VVVLQSKGHE TEEVDAVGIL SLCSFAVDPA DTYCKYVAAG NQPLGNCVKM LTVHNGSGFA
ITSKPSPTPD QDSYGGASVC LYCRAHIAHP GGAGNLDGRC QFKGSFVQIP TTEKDPVGFC
LRNKVCTVCQ CWIGYGCQCD SLRQPKPSVQ SVAVASGFDK NYLNGYGVAV RLG


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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