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

 R1AB_FIPV               Reviewed;        6709 AA.
Q98VG9; Q4U5G1; Q4U5G2; Q52PA4;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 2.
25-OCT-2017, entry version 114.
RecName: Full=Replicase polyprotein 1ab;
Short=pp1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Non-structural protein 1;
Short=nsp1;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
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;
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;
Contains:
RecName: Full=Non-structural protein 11;
Short=nsp11;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=nsp12;
Contains:
RecName: Full=Helicase;
Short=Hel;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=nsp13;
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;
Feline coronavirus (strain FIPV WSU-79/1146) (FCoV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Alphacoronavirus.
NCBI_TaxID=33734;
NCBI_TaxID=9681; Felidae (cat family).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16033972; DOI=10.1099/vir.0.80985-0;
Dye C., Siddell S.G.;
"Genomic RNA sequence of Feline coronavirus strain FIPV WSU-79/1146.";
J. Gen. Virol. 86:2249-2253(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Haijema B.J., de Groot-Mijnes J.D.F., Vennema H., Raamsman M.J.,
Rottier P.J.M., de Groot R.J.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2894-3215, AND MUTAGENESIS OF
HIS-2944; ASN-2967; GLY-2986; SER-3041; CYS-3047; TYR-3063; MET-3064
AND HIS-3065.
PubMed=11842253;
Hegyi A., Friebe A., Gorbalenya A.E., Ziebuhr J.;
"Mutational analysis of the active centre of coronavirus 3C-like
proteases.";
J. Gen. Virol. 83:581-593(2002).
-!- 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).
-!- 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=Q98VG9-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=Q98VG9-2; Sequence=VSP_032885;
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}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAY16374.1; Type=Frameshift; Positions=4033; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DQ010921; AAY32594.1; -; Genomic_RNA.
EMBL; DQ010921; AAY32595.1; -; Genomic_RNA.
EMBL; AY994055; AAY16374.1; ALT_FRAME; Genomic_RNA.
EMBL; AF326575; AAK09095.1; -; Genomic_RNA.
PDB; 3ETI; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1331-1498.
PDB; 3EW5; X-ray; 3.10 A; A/B/C=1331-1498.
PDB; 3GZF; X-ray; 2.76 A; A/B/C/D/E=2808-2902.
PDB; 3JZT; X-ray; 3.91 A; A/B/C/D/E/F/G/H=1331-1498.
PDB; 3UB0; X-ray; 2.60 A; A/D=3583-3777, B/C/E/F=3500-3582.
PDB; 4ZRO; X-ray; 2.06 A; A/B/C/D=2904-3202.
PDB; 5EU8; X-ray; 2.45 A; A=2904-3205.
PDBsum; 3ETI; -.
PDBsum; 3EW5; -.
PDBsum; 3GZF; -.
PDBsum; 3JZT; -.
PDBsum; 3UB0; -.
PDBsum; 4ZRO; -.
PDBsum; 5EU8; -.
ProteinModelPortal; Q98VG9; -.
SMR; Q98VG9; -.
MEROPS; C30.004; -.
OrthoDB; VOG09000000; -.
EvolutionaryTrace; Q98VG9; -.
Proteomes; UP000000835; Genome.
Proteomes; UP000140386; 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:0019079; P:viral genome replication; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR032039; A-CoV_nsp1.
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; IPR009469; RNA_pol_N_coronovir.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR014827; Viral_protease.
Pfam; PF16688; CNV-Replicase_N; 1.
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; 2.
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.
1: Evidence at protein level;
3D-structure; 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 6709 Replicase polyprotein 1ab.
/FTId=PRO_0000283825.
CHAIN 1 110 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_5000140208.
CHAIN 111 879 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_5000140209.
CHAIN 880 2413 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_5000140210.
CHAIN 2414 2903 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_5000140211.
CHAIN 2904 3205 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_5000140212.
CHAIN 3206 3499 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_5000140213.
CHAIN 3500 3582 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_5000140214.
CHAIN 3583 3777 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_5000140215.
CHAIN 3778 3888 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_5000140216.
CHAIN 3889 4023 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_5000140217.
CHAIN 4024 4952 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_5000140219.
CHAIN 4024 4042 Non-structural protein 11. {ECO:0000250}.
/FTId=PRO_5000140218.
CHAIN 4953 5551 Helicase. {ECO:0000250}.
/FTId=PRO_5000140220.
CHAIN 5552 6070 Exoribonuclease. {ECO:0000255}.
/FTId=PRO_5000140221.
CHAIN 6071 6409 Uridylate-specific endoribonuclease.
{ECO:0000255}.
/FTId=PRO_5000140222.
CHAIN 6410 6709 Putative 2'-O-methyl transferase.
{ECO:0000255}.
/FTId=PRO_5000140223.
TRANSMEM 1860 1878 Helical. {ECO:0000255}.
TRANSMEM 1921 1941 Helical. {ECO:0000255}.
TRANSMEM 2006 2026 Helical. {ECO:0000255}.
TRANSMEM 2043 2065 Helical. {ECO:0000255}.
TRANSMEM 2426 2446 Helical. {ECO:0000255}.
TRANSMEM 2691 2711 Helical. {ECO:0000255}.
TRANSMEM 2720 2740 Helical. {ECO:0000255}.
TRANSMEM 2771 2791 Helical. {ECO:0000255}.
TRANSMEM 3212 3232 Helical. {ECO:0000255}.
TRANSMEM 3242 3262 Helical. {ECO:0000255}.
TRANSMEM 3267 3287 Helical. {ECO:0000255}.
TRANSMEM 3306 3326 Helical. {ECO:0000255}.
TRANSMEM 3339 3359 Helical. {ECO:0000255}.
TRANSMEM 3396 3416 Helical. {ECO:0000255}.
TRANSMEM 3419 3439 Helical. {ECO:0000255}.
DOMAIN 1079 1330 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1329 1500 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1561 1814 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 2904 3205 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 4632 4794 RdRp catalytic.
DOMAIN 4953 5036 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5200 5391 (+)RNA virus helicase ATP-binding.
DOMAIN 5392 5561 (+)RNA virus helicase C-terminal.
ZN_FING 1188 1219 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1678 1707 C4-type 2; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ZN_FING 3962 3978 {ECO:0000250}.
ZN_FING 4004 4017 {ECO:0000250}.
NP_BIND 5235 5242 ATP. {ECO:0000250}.
REGION 1860 2065 HD1. {ECO:0000250}.
REGION 2426 2791 HD2. {ECO:0000250}.
REGION 3212 3439 HD3. {ECO:0000250}.
ACT_SITE 1117 1117 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1268 1268 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1599 1599 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1752 1752 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 2944 2944 For 3CL-PRO activity.
ACT_SITE 3047 3047 For 3CL-PRO activity.
METAL 4957 4957 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4960 4960 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4968 4968 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4971 4971 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4978 4978 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4981 4981 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4985 4985 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 4991 4991 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5002 5002 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5007 5007 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5024 5024 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5027 5027 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 110 111 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 879 880 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2413 2414 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 2903 2904 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3053 3053 Important for substrate recognition.
SITE 3205 3206 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3499 3500 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3582 3583 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3777 3778 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3888 3889 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4023 4024 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4952 4953 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5551 5552 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6070 6071 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6409 6410 Cleavage; by 3CL-PRO. {ECO:0000250}.
VAR_SEQ 4043 6709 Missing (in isoform Replicase polyprotein
1a). {ECO:0000305}.
/FTId=VSP_032885.
VARIANT 162 162 W -> C.
VARIANT 177 177 D -> G.
VARIANT 388 388 W -> C.
VARIANT 808 808 K -> T.
VARIANT 1784 1784 A -> V.
VARIANT 2889 2889 M -> K.
VARIANT 3280 3280 A -> V.
VARIANT 3992 3992 Q -> R.
VARIANT 4304 4304 H -> Q.
VARIANT 5846 5846 Y -> H.
MUTAGEN 2944 2944 H->Y,R: Complete loss of 3CL-PRO
activity. {ECO:0000269|PubMed:11842253}.
MUTAGEN 2967 2967 N->A,D: Increase of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253}.
MUTAGEN 2986 2986 G->A: 5% loss of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253}.
MUTAGEN 2986 2986 G->D: Increase of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253}.
MUTAGEN 2986 2986 G->E: 50% loss of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253}.
MUTAGEN 2986 2986 G->P,V: 95% loss of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253}.
MUTAGEN 2986 2986 G->R,T,W: 70% loss of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253}.
MUTAGEN 3041 3041 S->A: 80% loss of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253}.
MUTAGEN 3041 3041 S->T: 40% loss of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253}.
MUTAGEN 3047 3047 C->A,S: Complete loss of 3CL-PRO
activity. {ECO:0000269|PubMed:11842253}.
MUTAGEN 3063 3063 Y->A,F,G,T: Almost complete loss of 3CL-
PRO activity.
{ECO:0000269|PubMed:11842253}.
MUTAGEN 3064 3064 M->A: Increase of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253}.
MUTAGEN 3065 3065 H->A: Complete loss of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253}.
CONFLICT 1016 1092 Missing (in Ref. 1; AAY32594).
{ECO:0000305}.
STRAND 1336 1339 {ECO:0000244|PDB:3ETI}.
STRAND 1342 1347 {ECO:0000244|PDB:3ETI}.
HELIX 1349 1356 {ECO:0000244|PDB:3ETI}.
STRAND 1359 1365 {ECO:0000244|PDB:3ETI}.
HELIX 1376 1382 {ECO:0000244|PDB:3ETI}.
TURN 1383 1385 {ECO:0000244|PDB:3ETI}.
HELIX 1386 1395 {ECO:0000244|PDB:3ETI}.
STRAND 1405 1413 {ECO:0000244|PDB:3ETI}.
STRAND 1416 1422 {ECO:0000244|PDB:3ETI}.
HELIX 1431 1443 {ECO:0000244|PDB:3ETI}.
STRAND 1449 1451 {ECO:0000244|PDB:3ETI}.
HELIX 1463 1473 {ECO:0000244|PDB:3ETI}.
STRAND 1479 1483 {ECO:0000244|PDB:3ETI}.
HELIX 1486 1497 {ECO:0000244|PDB:3ETI}.
HELIX 2818 2823 {ECO:0000244|PDB:3GZF}.
STRAND 2826 2828 {ECO:0000244|PDB:3GZF}.
HELIX 2830 2837 {ECO:0000244|PDB:3GZF}.
TURN 2838 2840 {ECO:0000244|PDB:3GZF}.
HELIX 2842 2850 {ECO:0000244|PDB:3GZF}.
HELIX 2852 2856 {ECO:0000244|PDB:3GZF}.
HELIX 2864 2884 {ECO:0000244|PDB:3GZF}.
STRAND 2889 2891 {ECO:0000244|PDB:3GZF}.
STRAND 2895 2899 {ECO:0000244|PDB:3GZF}.
TURN 2914 2916 {ECO:0000244|PDB:4ZRO}.
HELIX 2917 2919 {ECO:0000244|PDB:4ZRO}.
STRAND 2920 2925 {ECO:0000244|PDB:4ZRO}.
STRAND 2928 2935 {ECO:0000244|PDB:4ZRO}.
STRAND 2938 2942 {ECO:0000244|PDB:4ZRO}.
HELIX 2943 2946 {ECO:0000244|PDB:4ZRO}.
STRAND 2950 2952 {ECO:0000244|PDB:5EU8}.
HELIX 2956 2962 {ECO:0000244|PDB:4ZRO}.
HELIX 2965 2967 {ECO:0000244|PDB:4ZRO}.
STRAND 2968 2972 {ECO:0000244|PDB:4ZRO}.
STRAND 2975 2977 {ECO:0000244|PDB:4ZRO}.
STRAND 2979 2985 {ECO:0000244|PDB:4ZRO}.
STRAND 2988 2995 {ECO:0000244|PDB:4ZRO}.
STRAND 3013 3020 {ECO:0000244|PDB:4ZRO}.
STRAND 3023 3031 {ECO:0000244|PDB:4ZRO}.
STRAND 3050 3055 {ECO:0000244|PDB:4ZRO}.
STRAND 3058 3068 {ECO:0000244|PDB:4ZRO}.
STRAND 3074 3077 {ECO:0000244|PDB:4ZRO}.
STRAND 3079 3081 {ECO:0000244|PDB:5EU8}.
HELIX 3084 3086 {ECO:0000244|PDB:4ZRO}.
STRAND 3089 3092 {ECO:0000244|PDB:4ZRO}.
HELIX 3103 3115 {ECO:0000244|PDB:4ZRO}.
HELIX 3129 3136 {ECO:0000244|PDB:4ZRO}.
TURN 3137 3140 {ECO:0000244|PDB:4ZRO}.
HELIX 3147 3150 {ECO:0000244|PDB:4ZRO}.
HELIX 3151 3157 {ECO:0000244|PDB:4ZRO}.
HELIX 3161 3171 {ECO:0000244|PDB:4ZRO}.
STRAND 3183 3185 {ECO:0000244|PDB:4ZRO}.
HELIX 3192 3200 {ECO:0000244|PDB:4ZRO}.
HELIX 3510 3518 {ECO:0000244|PDB:3UB0}.
HELIX 3521 3523 {ECO:0000244|PDB:3UB0}.
HELIX 3525 3540 {ECO:0000244|PDB:3UB0}.
HELIX 3544 3561 {ECO:0000244|PDB:3UB0}.
HELIX 3568 3577 {ECO:0000244|PDB:3UB0}.
HELIX 3579 3581 {ECO:0000244|PDB:3UB0}.
STRAND 3583 3585 {ECO:0000244|PDB:3UB0}.
HELIX 3587 3609 {ECO:0000244|PDB:3UB0}.
HELIX 3614 3652 {ECO:0000244|PDB:3UB0}.
HELIX 3663 3680 {ECO:0000244|PDB:3UB0}.
HELIX 3683 3693 {ECO:0000244|PDB:3UB0}.
STRAND 3697 3702 {ECO:0000244|PDB:3UB0}.
STRAND 3709 3714 {ECO:0000244|PDB:3UB0}.
HELIX 3717 3723 {ECO:0000244|PDB:3UB0}.
STRAND 3728 3731 {ECO:0000244|PDB:3UB0}.
STRAND 3734 3742 {ECO:0000244|PDB:3UB0}.
HELIX 3751 3753 {ECO:0000244|PDB:3UB0}.
HELIX 3756 3761 {ECO:0000244|PDB:3UB0}.
STRAND 3766 3772 {ECO:0000244|PDB:3UB0}.
SEQUENCE 6709 AA; 751196 MW; F26AC0FFF5FE27F9 CRC64;
MSSKQFKILV NEDYQVNVPS LPFRDALQEI KYCYRNGFDG YVFVPEYRRD LVDCNRKDHY
VIGVLGNGIS DLKPVLLTEP SVMLQGFIVR ANCNGVLEDF DLKFARTGNG AIYVDQYMCG
ADGKPVIEGE FKDYFGDEDV IIYEGEEYHC AWLTVRDEKP LWQQTLLTIR EIQYNLDIPH
KLPNCAIREV APPVKKNSKV VLSEEYRKLY DIFGSPFMGN GDSLNTCFDS LHFIAATLKC
PCGAESSGVG DWTGFKTACC GLHGKVKGVT LGAVKPGDAI VTSMSAGKGV KFFANSVLQY
AGDVENVSVW KVIKTFTVNE TVCTTDFEGE LNDFIRPEST SPVSCSIKRA FITGEVDDAV
HDCIIAGKLD LSTNLFGSAN LLFKKMPWFV QKCGAIFADA WKVVEELLCS LKLTYKQIYD
VVASLCTSAF TIMDYKPVFV VSSNSVKDLV DKCVKILVKA FDVFTQTITI AGVEAKCFVL
GSKYLLFNNA LVKLVSVKIL GKRQKGLDSA FFATNLIGAT VNVTPQRTES AYISLNKVDD
VVTPGGGHIV IIGDMAFYKS EEYYFMMASP DSVLVNNVFK AARVPSYNIV YDVNDDTKSK
MVVKIGTSFD FDGDLDAAIA KVNDLLIEFR QEKLCFRALK DGENILVEAY LKKYKMPVCL
KNHVGLWDII RQDSGKKGFL DTFNHLNELE DVKDIKIQTI KNIICPDLLL ELDFGAIWYR
CMPACSDKSI LGNVKIMLGN GVKVVCDGCH SFANRLTINY NKLCDTARKD IEIGGIPFST
FKTPSSSFID MKDAIYSVVE YGEALSFKTA SVPVTNSGII TTDDWSDPIL LEPADYVEPK
DNGDVIVIAG YTFYKDEDDH FYPYGSGMVV QKMYNKMGGG DKSVSFSDNV NVREIEPVTR
VRLEFEFDNE VVTQVLEKVI GTKYKFIGTT WEEFEDSISE KLDKIFDTLA EQGVELEGYF
IYDTCGGFDI NNPDGVMISQ YDLNTAADDK SDSDASVEDI SLISDNEDVE QIEEDNTSTD
DAEDVSSVEG ETVSVVDVED FVEQVSLVEE NNVLTPAVNP DEQLSSVEKK DEVSAKNDPW
AAAVDEQEAE QPKPSLTPFK TTNLNGKIIL KQQDNNCWIN ACCYQLQAFD FFNHDLWDGF
KKDDVMPFVD FCYAALTLKQ GDSGDAEYLL ETMLNDYSTA KVTLSAKCGC GVKEIVLERT
VFKLTPLRNE FKYGVCGDCK QINMCKFASV EGSGVFVHDR IEKQTPVSQF IVTPTMHAVY
TGTTQSGHYM IEDCIHDYCV DGMGIKPRKH KFYTSTLFLN ANVMTAKSKT MVEPPVPVED
KCVEDCQSPK DLILPFYKAG KVSFYQGDLD VLINFLEPDV LVNAANGDLR HVGGVARAID
VFTGGKLTKR SKEYLKSSKA IAPGNAVLFE NVLEHLSVLN AVGPRNGDSR VEGKLCNVYK
AIAKCDGKIL TPLISVGIFK VKLEVSLQCL LKTVTDRDLN VFVYTDQERV TIENFFNGTI
PIKVTEDTVN QKRVSVALDK TYGEQLKGTV VIKDKDVTNQ LPSVSDVGEK VVKALDVDWN
AYYGFPNAAA FSASSHDAYE FDVVTHNNFI VHKQTDNNCW VNAICLALQR LKPTWKFPGV
KSLWDAFLTR KTAGFVHMLY HISGLTKGQP GDAELTLHKL VDLMSSDSAV TVTHTTACDK
CAKVETFTGP VVAAPLLVCG TDEICVHGVH VNVKVTSIRG TVAITSLIGP VVGDVIDATG
YICYTGLNSR GHYTYYDNRN GLMVDADKAY HFEKNLLQVT TAIASNFVAN TPKKEIMPKT
QAKESKAKES NTARVFSEVE ENPKNIVRKE KLLAIESGVD YTITTLGKYA DVFFMAGDKI
LRFLLEVFKY LLVVFMCLRK SKMPKVKVKP PHVFRNLGAK VRTLNYVRQL NKPALWRYIK
LVLLLIALYH FFYLFVSIPV VHKLACSGSV QAYSNSSFVK SEVCGNSILC KACLASYDEL
ADFDHLQVSW DYKSDPLWNR VIQLSYFIFL AVFGNNYVRC LLMYFVSQYL NLWLSYFGYV
KYSWFLHVVN FESISVEFVI IVVVFKAVLA LKHIFLPCNN PSCKTCSKIA RQTRIPIQVV
VNGSMKTVYV HANGTGKLCK KHNFYCKNCD SYGFDHTFIC DEIVRDLSNS IKQTVYATDR
SYQEVTKVEC TDGFYRFYVG EEFTAYDYDV KHKKYSSQEV LKTMFLLDDF IVYNPSGSSL
ASVRNVCVYF SQLIGRPIKI VNSELLEDLS VDFKGALFNA KKNVIKNSFN VDVSECKNLE
ECYKLCNLDV TFSTFEMAIN NAHRFGILIT DRSFNNFWPS KIKPGSSGVS AMDIGKCMTF
DAKIVNAKVL TQRGKSVVWL SQDFSTLSST AQKVLVKTFV EEGVNFSLTF NAVGSDEDLP
YERFTESVSA KSGSGFFDVL KQLKQLFWCL VLFITLYGLC SVYSVATQSY IDSAEGYDYM
VIKNGVVQSF DDSINCVHNT YKGFAVWFKA KHGFVPTFDK SCPIVLGTVF DLGNMRPIPD
VPAYVALVGR SLVFAINAAF GVTNVCYDHT GAAVSKNSYF DTCVFNSACT TLTGIGGTVV
YCAKQGLVEG AKLYSELLPD YYYEHASGNM VKIPAIIRSF GLRFVKTQAT TYCRVGECTE
SQAGFCFGGD NWFVYDKEFG DGYICGSSTL GFFKNVFALF NSNMSVVATS GAMLANIVIA
CLAIAVCYGV LKFKKIFGDC TLLVVMIIVT LVVNNVSYFV TQNTFFMIVY AIIYYFTTRK
LAYPGVLDAG FIIAYLNMAP WYVLVLYIMV FLYDSLPSLF KLKVTTNLFE GDKFVGSFES
AAMGTFVIDM RSYETLVNST SLDRIKSYAN SFNKYKYYTG SMGEADYRMA CYAHLGKALM
DYSVSRNDML YTPPTVSVNS TLQSGLRKMA QPSGVVEPCI VRVAYGNNVL NGLWLGDEVI
CPRHVIASDT SRVINYENEL SSVRLHNFSI AKNNAFLGVV SAKYKGVNLV LKVNQVNPNT
PEHKFKSVRP GESFNILACY EGCPGSVYGV NMRSQGTIKG SFIAGTCGSV GYVLENGTLY
FVYMHHLELG NGSHVGSNLE GEMYGGYEDQ PSMQLEGTNV MSSDNVVAFL YAALINGERW
FVTNTSMTLE SYNAWAKTNS FTEIVSTDAF NMLAAKTGYS VEKLLECIVR LNKGFGGRTI
LSYGSLCDEF TPTEVIRQMY GVNLQSGKVK SIFYPMMTAI AILFAFWLEF FMYTPFTWIN
PTFVSVVLAI TTLVSVLLVA GIKHKMLFFM SFVMPSVILA TAHNVVWDMT YYESLQVLVE
NVNTTFLPVD MQGVMLALFC VVVFVICTIR FFTCKQSWFS LFATTIFVMF NIVKLLGMIG
EPWTDDHFLL CLVNMLTMLI SLTTKDWFVV FASYKVAYYI VVYVMQPAFV QDFGFVKCVS
IIYMACGYLF CCYYGILYWV NRFTCMTCGV YQFTVSPAEL KYMTANNLSA PKTAYDAMIL
SFKLMGIGGG RNIKISTVQS KLTEMKCTNV VLLGLLSKMH VESNSKEWNY CVGLHNEINL
CDDPDAVLEK LLALIAFFLS KHNTCDLSDL IESYFENTTI LQSVASAYAA LPSWIAYEKA
RADLEEAKKN DVSPQLLKQL TKACNIAKSE FEREASVQKK LDKMAEQAAA SMYKEARAVD
RKSKIVSAMH SLLFGMLKKL DMSSVNTIIE QARNGVLPLS IIPAASATRL IVVTPNLEVL
SKVRQENNVH YAGAIWSIVE VKDANGAQVH LKEVTAANEL NITWPLSITC ERTTKLQNNE
ILPGKLKEKA VKASATIDGD AYGSGKALMA SEGGKSFIYA FIASDSNLKY VKWESNNDVI
PIELEAPLRF YVDGVNGPEV KYLYFVKSLN TLRRGAVLGY IGATVRLQAG KPTEHPSNSG
LLTLCAFAPD PAKAYVDAVK RGMQPVTNCV KMLSNGAGNG MAITNGVESN TQQDSYGGAS
VCIYCRCHVE HPAIDGLCRF KGKFVQVPTG TQDPIRFCIE NEVCVVCGCW LTNGCMCDRT
SIQGTTIDQS YLNECGVLVQ LDLEPCNGTD PDHVSRAFDI YNKDVACIGK FLKTNCSRFR
NLDKHDAYYV VKRCTKSVMD HEQVCYNDLK DSGVVAEHDF FLYKEGRCEF GNVARKDLTK
YTMMDLCYAI RNFDEKNCEV LKEILVTLGA CNESFFENKD WFDPVENEAI HEVYARLGPI
VANAMLKCVA FCDAIVEKGY IGIITLDNQD LNGNFYDFGD FVKTTPGFGC ACVTSYYSYM
MPLMGMTSCL ESENFVKSDI YGADYKQYDL LAYDFTDHKE KLFHKYFKHW DRTYHPNCSD
CTSDECIIHC ANFNTLFSMT IPSTAFGPLV RKVHIDGVPV VVTAGYHFKQ LGIVWNLDVK
LDTMKLSMTD LLRFVTDPTL LVASSPALLD QRTVCFSIAA LSTGVTYQTV KPGHFNKDFY
DFITERGFFE EGSELTLKHF FFAQGGEAAM TDFNYYRYNR VTVLDICQAQ FVYKIVGKYF
ECYDGGCINA REVVVTNYDK SAGYPLNKFG KARLYYETLS YEEQDALFAL TKRNVLPTMT
QMNLKYAISG KARARTVGGV SLLSTMTTRQ YHQKHLKSIA ATRNATVVIG STKFYGGWDN
MLKNLMRDVD NGCLMGWDYP KCDRALPNMI RMASAMILGS KHVGCCTHSD RFYRLSNELA
QVLTEVVHCT GGFYFKPGGT TSGDGTTAYA NSAFNIFQAV SANVNKLLGV DSNACNNVTV
KSIQRKIYDN CYRSSSIDEE FVVEYFSYLR KHFSMMILSD DGVVCYNKDY ADLGYVADIN
AFKATLYYQN NVFMSTSKCW VEPDLSVGPH EFCSQHTLQI VGPDGDYYLP YPDPSRILSA
GVFVDDIVKT DNVIMLERYV SLAIDAYPLT KHPKPAYQKV FYTLLDWVKH LQKNLNAGVL
DSFSVTMLEE GQDKFWSEEF YASLYEKSTV LQAAGMCVVC GSQTVLRCGD CLRRPLLCTK
CAYDHVMGTK HKFIMSITPY VCSFNGCNVN DVTKLFLGGL SYYCMDHKPQ LSFPLCANGN
VFGLYKSSAV GSEDVEDFNK LAVSDWTNVE DYKLANNVKE SLKIFAAETV KAKEESVKSE
YAYAILKEVI GPKEIVLQWE ASKTKPPLNR NSVFTCFQIS KDTKIQLGEF VFEQSEYGSD
SVYYKSTSTY KLTPGMIFVL TSHNVSPLKA TILVNQEKYN TISKLYPVFN IAEAYNTLVP
YYQMIGKQKF TTIQGPPGSG KSHCVIGLGL YYPQARIVYT ACSHAAVDAL CEKAAKNFNV
DRCSRIIPQR IRVDCYTGFK PNNTNAQYLF CTVNALPEAS CDIVVVDEVS MCTNYDLSVI
NSRLSYKHIV YVGDPQQLPA PRTLINKGVL QPQDYNVVTQ RVCTLGPDVF LHKCYRCPAE
IVKTVSALVY ENKFVPVNPE SKQCFKMFVK GQVQIESNSS INNKQLEVVK AFLAHNPKWR
KAVFISPYNS QNYVARRLLG LQTQTVDSAQ GSEYDYVIYT QTSDTQHATN VNRFNVAITR
AKVGILCIMC DRTMYENLDF YELKDSKIGL QAKPETCGLF KDCSKSEQYI PPAYATTYMS
LSDNFKTSDG LAVNIGTKDV KYANVISYMG FRFEANIPGY HTLFCTRDFA MRNVRAWLGF
DVEGAHVCGD NVGTNVPLQL GFSNGVDFVV QTEGCVVTEK GNSIEVVKAR APPGEQFAHL
IPLMRKGQPW HIVRRRIVQM VCDYFDGLSD ILIFVLWAGG LELTTMRYFV KIGRPQKCEC
GKSATCYSSS QCVYACFKHA LGCDYLYNPY CIDIQQWGYT GSLSMNHHEV CNIHRNEHVA
SGDAIMTRCL AIHDCFVKRV DWSIVYPFID NEEKINKAGR IVQSHVMKAA LKIFNPAAIH
DVGNPKGIRC ATTPIPWFCY DRDPINNNVR CLEYDYMVHG QMNGLMLFWN CNVDMYPEFS
IVCRFDTRTR SKLSLEGCNG GALYVNNHAF HTPAYDRRAF AKLKPMPFFY YDDSNCELVD
GQPNYVPLKS NVCITKCNIG GAVCKKHAAL YRAYVEDYNM FMQAGFTIWC PQNFDTYMLW
HGFVNSKALQ SLENVAFNVV KKGAFTGLKG DLPTAVIADK IMVRDGPTDK CIFTNKTSLP
TNVAFELYAK RKLGLTPPLT ILRNLGVVAT YKFVLWDYEA ECPFSNFTKQ VCSYTDLDSE
VVTCFDNSIA GSFERFTTTK DAVLISNNAV KGLSAIKLQY GFLNDLPVST VGNKPVTWYI
YVRKNGEYVE QIDSYYTHGR TFETFKPRST MEEDFLSMDT TLFIQKYGLE DYGFEHVVFG
DVSKTTIGGM HLLISQVRLA KMGLFSVQEF MTNSDSTLKS CCITYADDPS SKNVCTYMDI
LLDDFVTIIK SLDLNVVSKV VDVIVDCKAW RWMLWCENSQ IKTFYPQLQS AEWNPGYSMP
TLYKIQRMCL ERCNLYNYGA QVRLPDGITT NVVKYTQLCQ YLNTTTVCVP HKMRVLHLGA
AGASGVAPGS TVLRRWLPDD AILVDNDLRD YVSDADFSVT GDCTSLYIED KFDLLISDLY
DGSTKSIDGE NTSKDGFFTY INGFIKEKLS LGGSAAIKIT EFSWNKDLYE LIQRFEYWTV
FCTSVNTSSS EGFLIGINYL GPYCDKAIVD GNIMHANYIF WRNSTIMALS HNSVLDTPKF
KCRCNNALIV NLKEKELNEM VVGLLRKGKL LIRNNGKLLN FGNHLVNVP


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