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 POLG_FMDVC              Reviewed;        2333 AA.
P03309; I0AZ17; Q6PN18; Q9Q2N6;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
29-MAY-2013, sequence version 2.
22-NOV-2017, entry version 107.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Leader protease;
Short=Lpro;
EC=3.4.22.46;
Contains:
RecName: Full=Protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Protein VP4;
AltName: Full=P1A;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Protein VP2;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Protein 2A;
Short=P2A;
AltName: Full=P52;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Protein 3B-1;
Short=P3B-1;
AltName: Full=Genome-linked protein VPg1;
Contains:
RecName: Full=Protein 3B-2;
Short=P3B-2;
AltName: Full=Genome-linked protein VPg2;
Contains:
RecName: Full=Protein 3B-3;
Short=P3B-3;
AltName: Full=Genome-linked protein VPg3;
Contains:
RecName: Full=Picornain 3C;
EC=3.4.22.28;
AltName: Full=Protease 3C;
Short=P3C;
AltName: Full=Protease P20B;
Contains:
RecName: Full=RNA-directed RNA polymerase 3D-POL;
Short=P3D-POL;
EC=2.7.7.48;
AltName: Full=P56A;
Foot-and-mouth disease virus (isolate Bovine/Brazil/A24Cruzeiro/1955
serotype A) (FMDV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Aphthovirus.
NCBI_TaxID=12115;
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=9925; Capra hircus (Goat).
NCBI_TaxID=9850; Cervidae (deer).
NCBI_TaxID=9363; Erinaceidae (hedgehogs).
NCBI_TaxID=9785; Loxodonta africana (African elephant).
NCBI_TaxID=9940; Ovis aries (Sheep).
NCBI_TaxID=10116; Rattus norvegicus (Rat).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Abrams C.C.;
"Nucleotide sequence of foot-and-mouth disease virus
A24/Cruzeiro/Brazil/55 from the poly(C) tract to 2B.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Knowles N.J., Samuel A.R., Aktas S., Rowe C.A., Abrams C.C.,
Newman J.W.I., King A.M.Q.;
"Phylogenetic comparison of the capsid-coding region of all seven
foot-and-mouth disease virus serotypes.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15858032; DOI=10.1128/JVI.79.10.6487-6504.2005;
Carrillo C., Tulman E.R., Delhon G., Lu Z., Carreno A., Vagnozzi A.,
Kutish G.F., Rock D.L.;
"Comparative genomics of foot-and-mouth disease virus.";
J. Virol. 79:6487-6504(2005).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 726-938.
PubMed=22397938; DOI=10.1016/j.vetmic.2012.02.009;
Malirat V., Bergmann I.E., de Mendonca Campos R., Conde F.,
Quiroga J.L., Villamil M., Salgado G., Ortiz S.;
"Molecular epidemiology of foot-and-mouth disease virus type A in
South America.";
Vet. Microbiol. 158:82-94(2012).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 737-952.
PubMed=6298715; DOI=10.1093/nar/10.24.8285;
Makoff A.J., Paynter C.A., Rowlands D.J., Boothroyd J.C.;
"Comparison of the amino acid sequence of the major immunogen from
three serotypes of foot and mouth disease virus.";
Nucleic Acids Res. 10:8285-8295(1982).
-!- FUNCTION: The leader protease autocatalytically cleaves itself
from the polyprotein at the L/VP0 junction. It cleaves the host
translation initiation factors EIF4G1 and EIF4G3, in order to shut
down the capped cellular mRNA transcription. Increases translation
driven by the viral internal ribosome entry site (IRES).
{ECO:0000250|UniProtKB:P03305, ECO:0000250|UniProtKB:P03311}.
-!- FUNCTION: Capsid proteins VP1, VP2, VP3 and VP4 form a closed
capsid enclosing the viral positive strand RNA genome. VP4 lies on
the inner surface of the protein shell formed by VP1, VP2 and VP3.
All the three latter proteins contain a beta-sheet structure
called beta-barrel jelly roll. Together they form an icosahedral
capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with
a diameter of approximately 300 Angstroms. VP1 is situated at the
12 fivefold axes, whereas VP2 and VP3 are located at the quasi-
sixfold axes. The capsid interacts with host heparan sulfate and
various integrins (alphavbeta1, alphavbeta3, alpha5beta1,
alphavbeta6, alphavbeta8) to provide virion attachment to target
Attachment via host integrins induces virion internalization
predominantly through clathrin-mediated endocytosis (By
similarity). {ECO:0000250}.
-!- FUNCTION: Protein VP0: VP0 precursor is a component of immature
procapsids. {ECO:0000250}.
-!- FUNCTION: Protein 2B: Affects membrane integrity and cause an
increase in membrane permeability. {ECO:0000250}.
-!- FUNCTION: Protein 2C: Associates with and induces structural
rearrangements of intracellular membranes. It displays RNA-
binding, nucleotide binding and NTPase activities (By similarity).
{ECO:0000250}.
-!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as
membrane anchor. {ECO:0000250}.
-!- FUNCTION: Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the
5'-end of both the positive-strand and negative-strand genomic
RNAs. They acts as a genome-linked replication primer (By
similarity). {ECO:0000250}.
-!- FUNCTION: Protease 3C: cysteine protease that generates mature
viral proteins from the precursor polyprotein. In addition to its
proteolytic activity, it binds to viral RNA, and thus influences
viral genome replication. RNA and substrate bind cooperatively to
the protease (By similarity). {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic
and antigenomic RNA by recognizing replications specific signals.
{ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Autocatalytically cleaves itself from the
polyprotein of the foot-and-mouth disease virus by hydrolysis of a
Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-
4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the
poliovirus polyprotein. In other picornavirus reactions Glu may be
substituted for Gln, and Ser or Thr for Gly.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBUNIT: VP1 interacts (via RGD) with integrins heterodimers
alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein VP2: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP3: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP1: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 2C: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3A: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3B-1: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 3B-2: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 3B-3: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Picornain 3C: Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host
cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Note=Probably localizes to the surface of intracellular membrane
vesicles that are induced after virus infection as the site for
viral RNA replication. These vesicles are derived from the
endoplasmic reticulum (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Lab;
IsoId=P03309-1; Sequence=Displayed;
Name=Lb;
IsoId=P03309-2; Sequence=VSP_046530;
-!- PTM: Specific enzymatic cleavages in vivo by the viral proteases
yield a variety of precursors and mature proteins. Polyprotein
processing intermediates such as VP0 which is a VP4-VP2 precursor
are produced. During virion maturation, non-infectious particles
are rendered infectious following cleavage of VP0. This maturation
cleavage is followed by a conformational change of the particle.
The polyprotein seems to be cotranslationally cleaved at the 2A/2B
junction by a ribosomal skip from one codon to the next without
formation of a peptide bond. This process would release the L-P1-
2A peptide from the translational complex (By similarity).
{ECO:0000250}.
-!- PTM: Myristoylation of VP4 is required during RNA encapsidation
and formation of the mature virus particle. {ECO:0000250}.
-!- PTM: Protein 3B-1, 3B-2 and 3B-3 are uridylylated by the
polymerase and are covalently linked to the 5'-end of genomic RNA.
These uridylylated forms act as a nucleotide-peptide primer for
the polymerase (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The capsid protein VP1 contains the main antigenic
determinants of the virion; therefore, changes in its sequence
must be responsible for the high antigenic variability of the
virus. {ECO:0000250}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000305}.
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EMBL; AJ251476; CAB62583.1; -; Genomic_RNA.
EMBL; AY593768; AAT01711.1; -; Genomic_RNA.
EMBL; J02183; AAA42596.1; -; Genomic_RNA.
EMBL; JQ082960; AFH54505.1; -; Genomic_RNA.
PIR; A03911; A03911.
ProteinModelPortal; P03309; -.
SMR; P03309; -.
IntAct; P03309; 1.
OrthoDB; VOG090000RZ; -.
Proteomes; UP000012667; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0019030; C:icosahedral viral capsid; IEA:InterPro.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C: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:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
GO; GO:0039525; P:modulation by virus of host chromatin organization; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 3.
Gene3D; 4.10.90.10; -; 1.
InterPro; IPR015031; Capsid_VP4_Picornavir.
InterPro; IPR037080; Capsid_VP4_sf_Picornavirus.
InterPro; IPR004080; FMDV_VP1_coat.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008739; Peptidase_C28.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF05408; Peptidase_C28; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 3.
Pfam; PF00910; RNA_helicase; 1.
Pfam; PF08935; VP4_2; 1.
PRINTS; PR00918; CALICVIRUSNS.
PRINTS; PR01542; FMDVP1COAT.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
3: Inferred from homology;
Alternative initiation; ATP-binding; Capsid protein;
Clathrin- and caveolin-independent endocytosis of virus by host;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Covalent protein-RNA linkage; Disulfide bond; Helicase;
Host cytoplasm; Host cytoplasmic vesicle; Host membrane;
Host-virus interaction; Hydrolase; Ion channel; Ion transport;
Lipoprotein; Membrane; Modulation of host chromatin by virus;
Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; RNA-binding; RNA-directed RNA polymerase; Thiol protease;
Transferase; Translation regulation; Transport;
Viral attachment to host cell; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 2333 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000422490.
CHAIN 1 201 Leader protease. {ECO:0000250}.
/FTId=PRO_0000422491.
CHAIN 202 504 Protein VP0. {ECO:0000255}.
/FTId=PRO_0000422492.
CHAIN 202 286 Protein VP4. {ECO:0000255}.
/FTId=PRO_0000422493.
CHAIN 287 504 Protein VP2. {ECO:0000255}.
/FTId=PRO_0000422494.
CHAIN 505 725 Protein VP3. {ECO:0000255}.
/FTId=PRO_0000422495.
CHAIN 726 936 Protein VP1. {ECO:0000250}.
/FTId=PRO_0000039867.
CHAIN 937 954 Protein 2A. {ECO:0000255}.
/FTId=PRO_0000039868.
CHAIN 955 1108 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000422496.
CHAIN 1109 1426 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000422497.
CHAIN 1427 1579 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000422498.
CHAIN 1580 1602 Protein 3B-1. {ECO:0000255}.
/FTId=PRO_0000422499.
CHAIN 1603 1626 Protein 3B-2. {ECO:0000255}.
/FTId=PRO_0000422500.
CHAIN 1627 1650 Protein 3B-3. {ECO:0000255}.
/FTId=PRO_0000422501.
CHAIN 1651 1863 Picornain 3C. {ECO:0000255}.
/FTId=PRO_0000422502.
CHAIN 1864 2333 RNA-directed RNA polymerase 3D-POL.
{ECO:0000255}.
/FTId=PRO_0000422503.
TOPO_DOM 1 1481 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1482 1502 {ECO:0000255}.
TOPO_DOM 1503 2333 Cytoplasmic. {ECO:0000255}.
DOMAIN 1 201 Peptidase C28.
DOMAIN 1190 1354 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1653 1837 Peptidase C3.
DOMAIN 2097 2215 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1218 1225 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
MOTIF 869 871 Cell attachment site. {ECO:0000250}.
ACT_SITE 51 51 For leader protease activity.
{ECO:0000250}.
ACT_SITE 148 148 For leader protease activity.
{ECO:0000250}.
ACT_SITE 163 163 For leader protease activity.
{ECO:0000250}.
ACT_SITE 1696 1696 For picornain 3C activity; Proton
donor/acceptor.
{ECO:0000250|UniProtKB:P03306,
ECO:0000255}.
ACT_SITE 1734 1734 For picornain 3C activity.
{ECO:0000250|UniProtKB:P03306}.
ACT_SITE 1813 1813 For picornain 3C activity.
{ECO:0000250|UniProtKB:P03306,
ECO:0000255}.
SITE 201 202 Cleavage; by leader protease.
{ECO:0000255}.
SITE 286 287 Cleavage. {ECO:0000255}.
SITE 504 505 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 725 726 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 936 937 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 954 955 Cleavage; by ribosomal skip.
{ECO:0000255}.
SITE 1108 1109 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1426 1427 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1579 1580 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1602 1603 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1626 1627 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1650 1651 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1863 1864 Cleavage; by picornain 3C. {ECO:0000255}.
MOD_RES 1582 1582 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MOD_RES 1605 1605 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MOD_RES 1629 1629 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 202 202 N-myristoyl glycine; by host.
{ECO:0000250}.
DISULFID 511 511 Interchain; in VP3 dimer. {ECO:0000250}.
VAR_SEQ 1 28 Missing (in isoform Lb). {ECO:0000305}.
/FTId=VSP_046530.
VARIANT 12 12 H -> T.
VARIANT 165 165 E -> D.
VARIANT 220 220 G -> S.
VARIANT 293 293 T -> M.
VARIANT 728 728 A -> T.
VARIANT 794 794 A -> T.
VARIANT 851 851 L -> P.
SEQUENCE 2333 AA; 259559 MW; B12EDE7A43D0492A CRC64;
MNTTDCFIAL VHAIREIRAF FLPRATGRME FTLHNGERKV FYSRPNNHDN CWLNTILQLF
RYVGEPFFDW VYDSPENLTL EAIEQLEELT GLELHEGGPP ALVIWNIKHL LHTGIGTASR
PSEVCMVDGT NMCLADFHAG IFLKGQEHAV FACVTSNGWY AIDDEDFYPW TPDPSDVLVF
VPYDQEPLNG EWKTKVQQKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFTGL FGALLADKKT EETTLLEDRI
LTTRNGHTTS TTQSSVGVTH GYSTEEDHVA GPNTSGLETR VVQAERFYKK YLFDWTTDKA
FGHLEKLELP SDHHGVFGHL VDSYAYMRNG WDVEVSAVGN QFNGGCLLVA MVPEWKEFDT
REKYQLTLFP HQFISPRTNM TAHITVPYLG VNRYDQYKKH KPWTLVVMVV SPLTVNNTSA
AQIKVYANIA PTYVHVAGEL PSKEGIFPVA CADGYGGLVT TDPKTADPAY GKVYNPPRTN
YPGRFTNLLD VAEACPTFLC FDDGKPYVTT RTDDTRLLAK FDLSLAAKHM SNTYLSGIAQ
YYTQYSGTIN LHFMFTGSTD SKARYMVAYI PPGVETPPDT PERAAHCIHA EWDTGLNSKF
TFSIPYVSAA DYAYTASDTA ETINVQGWVC IYQITHGKAE NDTLVVSVSA GKDFELRLPI
DPRQQTTATG ESADPVTTTV ENYGGETQIQ RRHHTDIGFI MDRFVKIQSL SPTHVIDLMQ
THQHGLVGAL LRAATYYFSD LEIVVRHEGN LTWVPNGAPE SALLNTSNPT AYNKAPFTRL
ALPYTAPHRV LATVYNGTSK YAVGGSGRRG DMGSLAARVV KQLPASFNYG AIKADAIHEL
LVRMKRAELY CPRPLLAIEV SSQDRHKQKI IAPAKQLLNF DLLKLAGDVE SNPGPFFFSD
VRSNFSKLVD TINQMQEDMS TKHGPDFNRL VSAFEELATG VKAIRTGLDE AKPWYKLIKL
LSRLSCMAAV AARSKDPVLV AIMLADTGLE ILDSTFVVKK ISDSLSSLFH VPAPVFSFGA
PILLAGLVKV ASSFFRSTPE DLERAEKQLK ARDINDIFAI LKNGEWLVKL ILAIRDWIKA
WIASEEKFVT TTDLVPGILE KQRDLNDPSK YKEAKEWLDN ARQACLKSGN VHIANLCKVV
APAPSRSRPE PVVVCLRGKS GQGKSFLANV LAQAISTHFT GRTDSVWYCP PDPDHFDGYN
QQTVVVMDDL GQNPDGKDFK YFAQMVSTTG FIPPMASLED KGKPFNSKVI IATTNLYSGF
TPRTMVCPDA LNRRFHFDID VSAKDGYKIN NKLDIIKALE DTHTNPVAMF QYDCALLNGM
AVEMKRMQQD MFKPQPPLQN VYQLVQEVIE RVELHEKVSS HPIFKQISIP SQKSVLYFLI
EKGQHEAAIE FFEGMVHDSI KEELRPLIQQ TSFVKRAFKR LKENFEIVAL CLTLLANIVI
MIRETRKRQK MVDDAVSEYI ERANITTDDK TLDEAEKNPL ETSGASTVGF RERPLPGQKA
RNDENSEPAQ PAEEQPQAEG PYAGPLERQK PLKVRAKLPQ QEGPYAGPME RQKPLKVKAK
APVVKEGPYE GPVKKPVALK VKAKNLIVTE SGAPPTDLQK LVMGNTKPVE LILDGKTVAI
CCATGVFGTA YLVPRHLFAE KYDKIMLDGR AMTDSDYRVF EFEIKVKGQD MLSDAALMVL
HRGNRVRDIT KHFRDTARMK KGTPVVGVIN NADVGRLIFS GEALTYKDIV VCMDGDTMPG
LFAYKAATKA GYCGGAVLAK DGADTFIVGT HSAGGNGVGY CSCVSRSMLL KMKAHVDPEP
HHEGLIVDTR DVEERVHVMR KTKLAPTVAH GVFNPEFGPA ALSNKDPRLN DGVVLDEVIF
SKHKGDTKMS EEDKALFRRC AADYASRLHS VLGTANAPLS IYEAIKGVDG LDAMEPDTAP
GLPWALQGKR RGALIDFENG TVGPEVEAAL KLMEKREYKF ACQTFLKDEI RPMEKVRAGK
TRIVDVLPVE HILYTRMMIG RFCAQMHSNN GPQIGSAVGC NPDVDWQRFG THFAQYRNVW
DVDYSAFDAN HCSDAMNIMF EEVFRTEFGF HPNAEWILKT LVNTEHAYEN KRITVEGGMP
SGCSATSIIN TILNNIYVLY ALRRHYEGVE LDTYTMISYG DDIVVASDYD LDFEALKPHF
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