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 R1A_BCRP3               Reviewed;        4380 AA.
P0C6T7; Q3I5J6;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 61.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a polyprotein;
Contains:
RecName: Full=Non-structural protein 1;
Short=nsp1;
AltName: Full=Leader protein;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65 homolog;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.19.12;
EC=3.4.22.69;
AltName: Full=PL2-PRO;
AltName: Full=Papain-like proteinase;
Short=PL-PRO;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=nsp5;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
Contains:
RecName: Full=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Bat coronavirus Rp3/2004 (BtCoV/Rp3/2004) (SARS-like coronavirus Rp3).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=349344;
NCBI_TaxID=59479; Rhinolophus ferrumequinum (Greater horseshoe bat).
NCBI_TaxID=196889; Rhinolophus macrotis (Big-eared horseshoe bat).
NCBI_TaxID=188571; Rhinolophus pearsonii.
NCBI_TaxID=89399; Rhinolophus sinicus (Chinese rufous horseshoe bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16195424; DOI=10.1126/science.1118391;
Li W., Shi Z., Yu M., Ren W., Smith C., Epstein J.H., Wang H.,
Crameri G., Hu Z., Zhang H., Zhang J., McEachern J., Field H.,
Daszak P., Eaton B.T., Zhang S., Wang L.F.;
"Bats are natural reservoirs of SARS-like coronaviruses.";
Science 310:676-679(2005).
-!- FUNCTION: The papain-like proteinase (PL-PRO) is responsible for
the cleavages located at the N-terminus of replicase polyprotein.
In addition, PL-PRO possesses a deubiquitinating/deISGylating
activity and processes both 'Lys-48'- and 'Lys-63'-linked
polyubiquitin chains from cellular substrates. Antagonizes innate
immune induction of type I interferon by blocking the
phosphorylation, dimerization and subsequent 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}.
-!- FUNCTION: Non-structural protein 1: binds to the 40S ribosomal
subunit and inhibits host translation. The nsp1-40S ribosome
complex further induces an endonucleolytic cleavage near the 5'UTR
of host mRNAs, targeting them for degradation. By suppressing host
gene expression, nsp1 facilitates efficient viral gene expression
in infected cells and evasion from host immune response (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the
two peptides corresponding to the two self-cleavage sites of the
SARS 3C-like proteinase are the two most reactive peptide
substrates. The enzyme exhibits a strong preference for substrates
containing Gln at P1 position and Leu at P2 position.
-!- 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=P0C6T7-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6W6-1; 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. {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 rp3 is highly similar to SARS-CoV
(SARS-like).
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DQ071615; AAZ67050.1; -; Genomic_RNA.
ProteinModelPortal; P0C6T7; -.
SMR; P0C6T7; -.
MEROPS; C16.009; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000006570; 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:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
GO; GO:0016788; F:hydrolase activity, acting on ester bonds; 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:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
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:0039579; P:suppression by virus of host ISG15 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; 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; IPR032592; NAR_dom.
InterPro; IPR021590; NSP1.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR024375; Nsp3_coronavir.
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; IPR024358; SARS-CoV_Nsp3_N.
InterPro; IPR022733; SARS_polyprot_cleavage.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF12379; DUF3655; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF11501; Nsp1; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF12124; Nsp3_PL2pro; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF11633; SUD-M; 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.
3: Inferred from homology;
Activation of host autophagy by virus; Complete proteome;
Decay of host mRNAs by virus;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Host cytoplasm;
Host gene expression shutoff by virus; Host membrane;
Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host IRF3 by virus; Inhibition of host ISG15 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; Repeat;
Ribosomal frameshifting; RNA-binding; Thiol protease; Transmembrane;
Transmembrane helix; Ubl conjugation pathway; Viral immunoevasion;
Zinc; Zinc-finger.
CHAIN 1 4380 Replicase polyprotein 1a.
/FTId=PRO_0000338122.
CHAIN 1 179 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338123.
CHAIN 180 818 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338124.
CHAIN 819 2738 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338125.
CHAIN 2739 3238 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338126.
CHAIN 3239 3544 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338127.
CHAIN 3545 3834 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338128.
CHAIN 3835 3917 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338129.
CHAIN 3918 4115 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338130.
CHAIN 4116 4228 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338131.
CHAIN 4229 4367 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338132.
CHAIN 4368 4380 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338133.
TRANSMEM 2201 2221 Helical. {ECO:0000255}.
TRANSMEM 2312 2334 Helical. {ECO:0000255}.
TRANSMEM 2349 2369 Helical. {ECO:0000255}.
TRANSMEM 2753 2773 Helical. {ECO:0000255}.
TRANSMEM 3020 3040 Helical. {ECO:0000255}.
TRANSMEM 3059 3079 Helical. {ECO:0000255}.
TRANSMEM 3081 3101 Helical. {ECO:0000255}.
TRANSMEM 3103 3123 Helical. {ECO:0000255}.
TRANSMEM 3140 3160 Helical. {ECO:0000255}.
TRANSMEM 3562 3582 Helical. {ECO:0000255}.
TRANSMEM 3584 3604 Helical. {ECO:0000255}.
TRANSMEM 3610 3630 Helical. {ECO:0000255}.
TRANSMEM 3657 3676 Helical. {ECO:0000255}.
TRANSMEM 3683 3702 Helical. {ECO:0000255}.
TRANSMEM 3726 3746 Helical. {ECO:0000255}.
TRANSMEM 3754 3774 Helical. {ECO:0000255}.
DOMAIN 1001 1167 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1609 1873 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3239 3544 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1727 1764 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4302 4318 {ECO:0000250}.
ZN_FING 4345 4358 {ECO:0000250}.
REGION 2201 2369 HD1. {ECO:0000250}.
REGION 2753 3160 HD2. {ECO:0000250}.
REGION 3562 3774 HD3. {ECO:0000250}.
COMPBIAS 930 999 Glu-rich.
COMPBIAS 2208 2211 Poly-Leu.
COMPBIAS 3764 3767 Poly-Cys.
ACT_SITE 1649 1649 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1810 1810 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3279 3279 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3383 3383 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 179 180 Cleavage. {ECO:0000250}.
SITE 818 819 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 3238 3239 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 3544 3545 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3834 3835 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3917 3918 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4115 4116 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4228 4229 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4367 4368 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 4380 AA; 486337 MW; 0DDA57CD3DF1535B CRC64;
MESLVLGINE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKSGT CGIVELEKGV
LPQPEQPYVF IKRSDAQGTD HGHRVRELVA ELDGVQYGRS GITLGVLVPH VGETPIAYRN
VLLRKNGNKG AGGHSFGIDL KSYDLGDELG TDPIEDYEQN WNTKHGSGVL RELTRELNGG
ALTRYVDNNF CGPDGYPLEC IKDLLARAGK SMCTLSEQLD YIESKRGVYC CRDHGHEIAW
FTERSDKSYE HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
RSVYPVATPQ ECNNMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV SEGPNTCGYL
PTNAVVKMPC PACQDPEIGP EHSAADYHNH SNIETRLRKG GRTRCFGGCV FAYVGCYNKR
AYWVPRASAD IGSGHTGITG DNVETLNEDL LEILSRERVN INIVGDFQLN EEVAIILASF
SASTSAFIDT IKSLDYKSFK TIVESCGNYK VTKGKPIKGA WNIGQHRSVL TPLCGFPSQA
AGVIRSIFSR TLDAANHSIP DLQRAAVTIL DSISEQSLRL VDAMVYTSNL LTNSVIIMAY
VTGGLVQQTS QWLSNLLDTT VEKLRPIFAW IEAKLSAGVE FLKDAWEILK FLITGVFDIV
KGQIQVASDN IKDCVKCFVD VVNKALEMCI DQVTIAGAKL RSLNLGEVFI AQSKGLYRQC
IRGKEQLQLL MPLKAPKEVT FLEGDSHDTV LTSEEVVLKN GELEALETPV DSFTNGAVVG
TPVCINGLML LEIKANEQYC ALSPGLLATN NVFRLKGGAP TKGVTFGEDT VVEVQGYKNV
RITFELDERV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
WSVATFYLFD DSGEEKLSSR MYCSFYPPDE EEDCEEYEEE EEVSERTCEH EYGTEEDYKG
LPLEFGASTD IIQVEEQEEE DWLDDAVEAE PEPEPLHEEP VNQLTGYLKL TDNVAIKCVD
IVEEAQNANP MVIVNAANIH LKHGGGVAGA LNKATNGAMQ KESDHYIKLN GPLTVGGSCL
LSGHNLAKKC LHVVGPNLNA GEDIQLLKAA YENFNSQDIL LAPLLSAGIF GAKPLQSLQM
CVQTVRTQVY IVVNDKVLYE QVVMDYLDSL KPKVEAPKQE VLPKAEYPKV DEKSVVQKTI
DVKPKIKACI DEVTTTLEET KFLTNKLLLF TDINGKLYQD SKNMLRGEDM SFLEKDAPYM
VGDVITSGDI TCVVIPSKKA GGTTEMLSRA LKKVPINEYI TTYPGQGCAG YTLEEAKTAL
KKCKSAFYVL PSETPNAKEE ILGTVSWNLR EMLAHAEETR KLMPVCMDVR AIMATIQRKY
KGIKIQEGIV DYGVRFFFYT SKEPVASIIT KLNSLNEPLV TMPIGYVTHG FNLEEAARCM
RSLKAPAIVS VSSPDAVTTY NGYLTSSSKT SEDHFVETVS LAGSYRDWSY SGQRTELGVE
FLKRGEKIVY HTLESPVKFH LDGEVLPLDK LKSLLSLREV KTIKVFTTVD NTNLHTQLVD
MSMTYGQQLG PTYLEGADVT KIKPHVNHEG KTFFVLPSDD TLRSEAFEYY HTLDESFLGR
YMSALNHTKK WKFPQVGGLT SIKWADNNCY LSSVLLALQQ IEVKFNAPAL QEAYYRARAG
DAANFCALIL AYSNKTVGEL GDVRETMTHL LQHANLESAK RVLNVVCKHC GQKTTTLTGV
EAVMYMGTLS YDNLKMGVSI PCVCGRDATQ YLVQQESSFV MMSAPPAEYK LQQGTFLCAN
EYTGNYQCGH YTHITAKETL YRIDGAHLTK MSEYKGPVTD VFYKETSYTT TIKPVSYKLD
GVTYTEIEPK LDGYYKKDNA YYTEQPIDLI PTQPLPNASF DNFKLTCSNT KFADDLNQMT
GFTKPASREL SVTFFPDLNG DVVAIDYRHY SASFKKGAKL LHKPIVWHIN QATTKTTFKP
NTWCLRCLWS TKPVDTSNSF EVLAVEDTQG MDNLACESQQ PTPEEVVENP TIQKEVIECD
VKTTEVVGNV ILKPSDEGVK VTQELDHEDL MAAYVENTSI TIKKPNELSL ALGLKTIATH
GIAAINSVPW GKILAYVKPF LGQAAVTTSN CAKRLVQRMF NNYMPYVLTL LFQLCTFTKS
TNSRIRASLP TTIAKNSVRG IVRLCLDAGI NYVKSPKFSK LFTIAMWLLL LSICLGSLIY
VTAALGVLLS NFGAPSYCSG VRESYLNSSN VTTMDFCEGS FPCSVCLSGL DSLDSYPALE
TIQVTISSYK LDLTILGLAA EWFFAYMLFT KFFYLLGLSA IMQVFFGYFA SHFISNSWLM
WFIISIVQMA PVSAMVRMYI FFASFYYIWK SYVHIMDGCT SSTCMMCYKR NRATRVECTT
IVNGMKRSFY VYANGGRGFC KTHNWNCLNC DTFCAGSTFI SDEVARDLSL QFKRPINPTD
QSSYVVDSVA VKNGALHLYF DKAGQKTYER HPLSHFVNLD NLRANNTKGS LPINVIVFDG
KSKCDESAAK SASVYYSQLM CQPILLLDQA LVSDVGDSTE VSVKMFDAYV DTFSATFSVP
MEKLKALVAT AHSELAKGVA LDGVLSTFVS ASRQGVVDTD VDTKDVIECL KLSHHSDLEV
TGDSCNNFML TYNKVENMTP RDLGACIDCN ARHINAQVAR SHNVSLIWNV KDYMSLSEQL
RKQIRSAAKK NNIPFRLTCA TTRQVVNVIT TKISLKGGKI VSTWFKIMLK ATLLCVLAAL
VCYIVMPVHI LSVHGGYTNE IIGYKAIQDG VTRDIVSTDD CFANKHAGFD SWFSQRGGSY
KNDKSCPVVA AIITREIGFI VPGLPGTVLR AINGDFLHFL PRVFSAVGNI CYTPSKLIEY
SDFSTSACVL AAECTIFKDA MGKPVPYCYD TNLLEGSISY SELRPDTRYV LMDGSIIQFP
NAYLEGSVRV VTTFDAEYCR HGTCERSEAG ICLSTSGRWV LNNEHYRALP GVFCGVDAMN
LIANIFTPLV QPVGALDVSA SVVAGGIIAI LVTCAAYYFM KFRRAFGEYN HVVAANAPLF
LMSFTILCLA PAYSFLPGVY SVFYLYLTFY FTNDVSFLAH LQWFAMFSPI VPFWITAIYV
FCISLKHFHW FFNNYLRKRV VFNGVTFSTF EEAALCTFLL NKEMYLKLRS ETLLPLTQYN
RYLALYNKYK YFSGALDTTS YREAACCHLA KALNDFSNSG ADVLYQPPQT SITSAVLQSG
FRKMAFPSGK VEGCMVQVTC GTTTLNGLWL DDTVYCPRHV ICTAEDMLNP NYEDLLIRKS
NHSFLVQAGN VQLRVIGHSM QNCLLRLKVD TSNPKTPKYK FVRIQPGQTF SVLACYNGSP
SGVYQCAMRP NHTIKGSFLN GSCGSVGFNI DYDCVSFCYM HHMELPTEVH AGTDLEGKFY
GPFVDRQTAQ AAGTDTTITL NVLAWLYAAV INGDRWFLNR FTTTLNDFNL VAMKYNYEPL
TQDHVDILGP LSAQTGIAVL DMCAALKELL QNGMNGRTIL GSTILEDEFT PFDVVRQCSG
VTFQGKFKRI VKGTHHWMLL TFLTSLLILV QSTQWSLFFF VYENAFLPFT LGIMAVAACA
MLLVKHKHAF LCLFLLPSLA TVAYFNMVYM PASWVMRIMT WLELADTSLS GYRLKDCVMY
ASALVLLVLM TARTVYDDAA RRVWTLMNVI TLVYKVYYGN ALDQAISMWA LVISVTSNYS
GVVTTIMFLA RAIVFVCVEY YPLLFITGNT LQCIMLVYCF LGYCCCCYFG LFCLLNRYFR
LTLGVYDYLV STQEFRYMNS QGLLPPKSSI DAFKLNIKLL GIGGKPCIKV ATVQSKMSDV
KCTSVVLLSV LQQLRVESSS KLWAQCVQLH NDILLAKDTT EAFEKMVSLL SVLLSMQGAV
DINKLCEEML DNRATLQAIA SEFSSLPSYA AYATAQEAYE QAVANGDSEV VLKKLKKSLN
VAKSEFDRNA AMQRKLEKMA DQAMTQMYKQ ARSEDKRAKV TSAMQTMLFT MLRKLDNDAL
NNIINNARDG CVPLNIIPLT TAAKLMVVVP DYGTYKNTCD GNTFTYASAL WEIQQVVDAD
SKIVQLSEIN MENSSNLAWP LIVTALRANS AVKLQNNELS PVALRQMSCA AGTTQTACTD
DNALAYYNNS KGGRFVLALL SDHQDLKWAR FPKSDGTGTI YTELEPPCRF VTDTPKGPKV
KYLHFIKGLN NLNRGMVLGS LAATVRLQAG NATEVPANST VLSFCAFAVD PAKAYKDYLA
SGGQPITNCV KMLCTHTGTG QAITVTPEAN MDQESFGGAS CCLYCRCHID HPNPKGFCDL
KGKYVQIPTT CANDPVGFTL RNTVCTVCGM WKGYGCSCDQ LREPMMQSAD ASTFLNGFAV


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Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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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

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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
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IBAN lautet DE8839050000107569353
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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
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San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
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GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
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София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
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GENTAUR Poland Sp. z o.o.


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TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

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GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
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Fax 02 36 00 65 94
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