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 R1A_PEDV7               Reviewed;        4117 AA.
P0C6V6; Q91AV2;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 57.
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;
Porcine epidemic diarrhea virus (strain CV777) (PEDV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Alphacoronavirus.
NCBI_TaxID=229032;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=9782358;
Bridgen A., Kocherhans R., Tobler K., Carvajal A., Ackermann M.;
"Further analysis of the genome of porcine epidemic diarrhea virus.";
Adv. Exp. Med. Biol. 440:781-786(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11724265; DOI=10.1023/A:1011831902219;
Kocherhans R., Bridgen A., Ackermann M., Tobler K.;
"Completion of the porcine epidemic diarrhoea coronavirus (PEDV)
genome sequence.";
Virus Genes 23:137-144(2001).
-!- 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: 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. The 3 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=P0C6V6-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6Y4-1; 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; AF353511; -; NOT_ANNOTATED_CDS; Genomic_RNA.
PDB; 5GWZ; X-ray; 2.44 A; A/B=2998-3299.
PDBsum; 5GWZ; -.
ProteinModelPortal; P0C6V6; -.
SMR; P0C6V6; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000008159; 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; 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; 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 4117 Replicase polyprotein 1a.
/FTId=PRO_0000338347.
CHAIN 1 110 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338348.
CHAIN 111 895 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338349.
CHAIN 896 2516 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338350.
CHAIN 2517 2997 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338351.
CHAIN 2998 3299 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338352.
CHAIN 3300 3579 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338353.
CHAIN 3580 3662 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338354.
CHAIN 3663 3857 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338355.
CHAIN 3858 3965 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338356.
CHAIN 3966 4100 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338357.
CHAIN 4111 4117 Non-structural protein 11. {ECO:0000250}.
/FTId=PRO_0000338358.
TRANSMEM 1959 1979 Helical. {ECO:0000255}.
TRANSMEM 2022 2042 Helical. {ECO:0000255}.
TRANSMEM 2105 2125 Helical. {ECO:0000255}.
TRANSMEM 2127 2147 Helical. {ECO:0000255}.
TRANSMEM 2150 2170 Helical. {ECO:0000255}.
TRANSMEM 2528 2548 Helical. {ECO:0000255}.
TRANSMEM 2619 2639 Helical. {ECO:0000255}.
TRANSMEM 2654 2674 Helical. {ECO:0000255}.
TRANSMEM 2754 2774 Helical. {ECO:0000255}.
TRANSMEM 2787 2807 Helical. {ECO:0000255}.
TRANSMEM 2814 2834 Helical. {ECO:0000255}.
TRANSMEM 2863 2883 Helical. {ECO:0000255}.
TRANSMEM 3336 3356 Helical. {ECO:0000255}.
TRANSMEM 3361 3381 Helical. {ECO:0000255}.
TRANSMEM 3399 3419 Helical. {ECO:0000255}.
TRANSMEM 3431 3451 Helical. {ECO:0000255}.
TRANSMEM 3454 3474 Helical. {ECO:0000255}.
TRANSMEM 3476 3496 Helical. {ECO:0000255}.
TRANSMEM 3500 3520 Helical. {ECO:0000255}.
DOMAIN 1057 1296 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1297 1465 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1691 1951 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 2998 3299 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1162 1193 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4039 4055 {ECO:0000250}.
ZN_FING 4081 4094 {ECO:0000250}.
REGION 1959 2170 HD1.
REGION 2528 2883 HD2.
REGION 3336 3520 HD3.
COMPBIAS 1816 1932 Val-rich.
ACT_SITE 1091 1091 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1239 1239 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1729 1729 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1888 1888 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3038 3038 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3141 3141 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 110 111 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 895 896 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2516 2517 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 2997 2998 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3299 3300 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3579 3580 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3662 3663 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3857 3858 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3965 3966 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4100 4101 Cleavage; by 3CL-PRO. {ECO:0000250}.
HELIX 3008 3011 {ECO:0000244|PDB:5GWZ}.
STRAND 3014 3019 {ECO:0000244|PDB:5GWZ}.
STRAND 3022 3029 {ECO:0000244|PDB:5GWZ}.
STRAND 3032 3036 {ECO:0000244|PDB:5GWZ}.
HELIX 3037 3040 {ECO:0000244|PDB:5GWZ}.
STRAND 3044 3046 {ECO:0000244|PDB:5GWZ}.
HELIX 3050 3056 {ECO:0000244|PDB:5GWZ}.
HELIX 3059 3061 {ECO:0000244|PDB:5GWZ}.
STRAND 3062 3066 {ECO:0000244|PDB:5GWZ}.
STRAND 3069 3071 {ECO:0000244|PDB:5GWZ}.
STRAND 3073 3079 {ECO:0000244|PDB:5GWZ}.
STRAND 3082 3089 {ECO:0000244|PDB:5GWZ}.
STRAND 3096 3099 {ECO:0000244|PDB:5GWZ}.
STRAND 3107 3114 {ECO:0000244|PDB:5GWZ}.
STRAND 3117 3125 {ECO:0000244|PDB:5GWZ}.
STRAND 3144 3149 {ECO:0000244|PDB:5GWZ}.
STRAND 3152 3162 {ECO:0000244|PDB:5GWZ}.
STRAND 3168 3171 {ECO:0000244|PDB:5GWZ}.
HELIX 3178 3180 {ECO:0000244|PDB:5GWZ}.
STRAND 3183 3186 {ECO:0000244|PDB:5GWZ}.
HELIX 3197 3209 {ECO:0000244|PDB:5GWZ}.
HELIX 3223 3230 {ECO:0000244|PDB:5GWZ}.
TURN 3231 3234 {ECO:0000244|PDB:5GWZ}.
HELIX 3242 3244 {ECO:0000244|PDB:5GWZ}.
HELIX 3245 3251 {ECO:0000244|PDB:5GWZ}.
HELIX 3255 3265 {ECO:0000244|PDB:5GWZ}.
STRAND 3277 3279 {ECO:0000244|PDB:5GWZ}.
HELIX 3286 3294 {ECO:0000244|PDB:5GWZ}.
SEQUENCE 4117 AA; 452818 MW; 4409589DAF0AA869 CRC64;
MASNHVTLAF ANDAEISAFG FCTASEAVSY YSEAAASGFM QCRFVSLDLA DTVEGLLPED
YVMVVIGTTK LSAYVDTFGS RPRNICGWLL FSNCNYFLEE LELTFGRRGG NIVPVDQYMC
GADGKPVLQE SEWEYTDFFA DSEDGQLNIA GITYVKAWIV ERSDVSYASQ NLTSIKSITY
CSTYEHTFLD GTAMKVARTP KIKKNVVLSE PLATIYREIG SPFVDNGSDA RSIIRRPVFL
HAFVKCKCGS YHWTVGDWTS YVSTCCGFKC KPVLVASCSA MPGSVVVTRA GAGTGVKYYN
NMFLRHVADI DGLAFWRILK VQSKDDLACS GKFLEHHEEG FTDPCYFLND SSLATKLKFD
ILSGKFSDEV KQAIIAGHVV VGSALVDIVD DALGQPWFIR KLGDLASAPW EQLKAVVRGL
GLLSDEVVLF GKRLSCATLS IVNGVFEFLA DVPEKLAAAV TVFVNFLNEF FESACDCLKV
GGKTFNKVGS YVLFDNALVK LVKAKARGPR QAGICEVRYT SLVVGSTTKV VSKRVENANV
NLVVVDEDVT LNTTGRTVVV DGLAFFESDG FYRHLADADV VIEHPVYKSA CELKPVFECD
PIPDFPLPVA ASVAELCVQT DLLLKNYNTP YKTYSCVVRG DKCCITCTLQ FKAPSYVEDA
VNFVDLCTKN IGTAGFHEFY ITAHEQQDLQ GFLTTCCTMS GFECFMPTIP QCPAVLEEID
GGSIWRSFIT GLNTMWDFCK RLKVSFGLDG IVVTVARKFK RLGALLAEMY NTYLSTVVEN
LVLAGVSFKY YATSVPKIVL GGCFHSVKSV FASVFQIPVQ AGIEKFKVFL NCVHPVVPRV
IETSFVELEE TTFKPPALNG GIAIVDGFAF YYDGTLYYPT DGNSVVPICF KKKGGGDVKF
SDEVSVKTID PVYKVSLEFE FESETIMAVL NKAVGNRIKV TGGWDDVVEY INVAIEVLKD
HVEVPKYYIY DEEGGTDPNL PVMVSQWPLN DDTISQDLLD VEVVTDAPID SEGDEVDSSA
PEKVADVANS EPGDDGLPVA PETNVESEVE EVAATLSFIK DTPSTVTKDP FAFDFVSYGG
LKVLRQSHNN CWVTSTLVQL QLLGIVDDPA MELFSAGRVG PMVRKCYESQ KAILGSLGDV
SACLESLTKD LHTLKITCSV VCGCGTGERI YEGCAFRMTP TLEPFPYGAC AQCAQVLMHT
FKSIVGTGIF CRDTTALSLD SLVVKPLCAA AFIGKDSGHY VTNFYDAAMA IDGYGRHQIK
YDTLNTICVK DVNWTAPLVP AVDSVVEPVV KPFYSYKNVD FYQGDFSDLV KLPCDFVVNA
ANEKLSHGGG IAKAIDVYTK GMLQKCSNDY IKAHGPIKVG RGVMLEALGL KVFNVVGPRK
GKHAPELLVK AYKSVFANSG VALTPLISVG IFSVPLEESL SAFLACVGDR HCKCFCYGDK
EREAIIKYMD GLVDAIFKEA LVDTTPVQED VQQVSQKPVL PNFEPFRIEG AHAFYECNPE
GLMSLGADKL VLFTNSNLDF CSVGKCLNDV TSGALLEAIN VFKKSNKTVP AGNCVTLDCA
NMISITMVVL PFDGDANYDK NYARAVVKVS KLKGKLVLAV DDATLYSKLS HLSVLGFVST
PDDVERFYAN KSVVIKVTED TRSVKAVKVE STATYGQQIG PCLVNDTVVT DNKPVVADVV
AKVVPNANWD SHYGFDKAGE FHMLDHTGFT FPSEVVNGRR VIKTTDNNCW VNVTCLQLQF
ARFRFKSAGL QAMWESYCTG DVAMFVHWLY WLTGVDKGQP SDSENALNML SKYIVPAGSV
TIERVTHDGC CCSKRVVTAP VVNASVLKLG VEDGLCPHGL NYIGKVVVVK GTTIVVNVGK
PVVAPSHLFL KGVSYTTFLD NGNGVVGHYT VFDHGTGMVH DGDAFVPGDL NVSPVTNVVV
SEQTAVVIKD PVKKAELDAT KLLDTMNYAS ERFFSFGDFM SRNLITVFLY ILSILGLCFR
AFRKRDVKVL AGVPQRTGII LRKSMRYNAK ALGVFFKLKL YWFKVLGKFS LGIYALYALL
FMTIRFTPIG SPVCDDVVAG YANSSFDKNE YCNSVICKVC LYGYQELSDF SHTQVVWQHL
RDPLIGNVMP FFYLAFLAIF GGVYVKAITL YFIFQYLNSL GVFLGLQQSI WFLQLVPFDV
FGDEIVVFFI VTRVLMFIKH VCLGCDKASC VACSKSARLK RVPVQTIFQG TSKSFYVHAN
GGSKFCKKHN FFCLNCDSYG PGCTFINDVI ATEVGNVVKL NVQPTGPATI LIDKVEFSNG
FYYLYSGDTF WKYNFDITDS KYTCKEALKN CSIITDFIVF NNNGSNVNQV KNACVYFSQM
LCKPVKLVDS ALLASLSVDF GASLHSAFVS VLSNSFGKDL SSCNDMQDCK STLGFDDVPL
DTFNAAVAEA HRYDVLLTDM SFNNFTTSYA KPEEKFPVHD IATCMRVGAK IVNHNVLVKD
SIPVVWLVRD FIALSEETRK YIIRTTKVKG ITFMLTFNDC RMHTTIPTVC IANKKGAGLP
SFSKVKKFFW FLCLFIVAAF FALSFLDFST QVSSDSDYDF KYIESGQLKT FDNPLSCVHN
VFINFDQWHD AKFGFTPVNN PSCPIVVGVS DEARTVPGIP AGVYLAGKTL VFAINTIFGT
SGLCFDASGV ADKGACIFNS ACTTLSGLGG TAVYCYKNGL VEGAKLYSEL APHSYYKMVD
GNAVSLPEII SRGFGIRTIR TKAMTYCRVG QCVQSAEGVC FGADRFFVYN AESGSDFVCG
TGLFTLLMNV ISVFSKTVPV TVLSGQILFN CIIAFVAVAV CFLFTKFKRM FGDMSVGVFT
VGACTLLNNV SYIVTQNTLG MLGYATLYFL CTKGVRYMWI WHLGFLISYI LIAPWWVLMV
YAFSAIFEFM PNLFKLKVST QLFEGDKFVG SFENAAAGTF VLDMHAYERL ANSISTEKLR
QYASTYNKYK YYSGSASEAD YRLACFAHLA KAMMDYASNH NDTLYTPPTV SYNSTLQAGL
RKMAQPSGVV EKCIVRVCYG NMALNGLWLG DIVMCPRHVI ASSTTSTIDY DYALSVLRLH
NFSISSGNVF LGVVSATMRG ALLQIKVNQN NVHTPKYTYR TVRPGESFNI LACYDGAAAG
VYGVNMRSNY TIRGSFINGA CGSPGYNINN GTVEFCYLHQ LELGSGCHVG SDLDGVMYGG
YEDQPTLQVE GASSLFTENV LAFLYAALIN GSTWWLSSSR IAVDRFNEWA VHNGMTTVGN
TDCFSILAAK TGVDVQRLLA SIQSLHKNFG GKQILGHTSL TDEFTTGEVV RQMYGVNLQG
GYVSRACRNV LLVGSFLTFF WSELVSYTKF FWVNPGYVTP MFACLSLLSS LLMFTLKHKT
LFFQVFLIPA LIVTSCINLA FDVEVYNYLA EHFDYHVSLM GFNAQGLVNI FVCFVVTILH
GTYTWRFFNT PASSVTYVVA LLTAAYNYFY ASDILSCAMT LFASVTGNWF VGAVCYKVAV
YMALRFPTFV AIFGDIKSVM FCYLVLGYFT CCFYGILYWF NRFFKVSVGV YDYTVSAAEF
KYMVANGLRA PTGTLDSLLL SAKLIGIGGE RNIKISSVQS KLTDIKCSNV VLLGCLSSMN
VSANSTEWAY CVDLHNKINL CNDPEKAQEM LLALLAFFLS KNSAFGLDDL LESYFNDNSM
LQSVASTYVG LPSYVIYENA RQQYEDAVNN GSPPQLVKQL RHAMNVAKSE FDREASTQRK
LDRMAEQAAA QMYKEARAVN RKSKVVSAMH SLLFGMLRRL DMSSVDTILN LAKDGVVPLS
VIPAVSATKL NIVTSDIDSY NRIQREGCVH YAGTIWNIID IKDNDGKVVH VKEVTAQNAE
SLSWPLVLGC ERIVKLQNNE IIPGKLKQRS IKAEGDGIVG EGKALYNNEG GRTFMYAFIS
DKPDLRVVKW EFDGGCNTIE LEPPRKFLVD SPNGAQIKYL YFVRNLNTLR RGAVLGYIGA
TVRLQAGKQT EQAINSSLLT LCAFAVDPAK TYIDAVKSGH KPVGNCVKML ANGSGNGQAV
TNGVEASTNQ DSYGGASVCL YCRAHVEHPS MDGFCRLKGK YVQVPLGTVD PIRFVLENDV
CKVCGCWLSN GCTCDRSIMQ STDMAYLNEY GALVQLD


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Fax 0032 16 50 90 45
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GENTAUR Ltd.
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Whetstone London N20 9BH
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GENTAUR France SARL
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Tel 01 43 25 01 50

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RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
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52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
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IBAN lautet DE8839050000107569353
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Tel (408) 780-0908,
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Kuiper 1
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nl@gentaur.com | Gentaur
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ГЕНТАУЪР БЪЛГАРИЯ
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GENTAUR Poland Sp. z o.o.


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poland@gentaur.com | Gentaur

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