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 POLG_HAVMB              Reviewed;        2227 AA.
P13901; Q81083; Q81084; Q81085; Q81086; Q81087; Q81088; Q81089;
Q81090; Q81091; Q81092; Q81093;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
25-OCT-2017, entry version 141.
RecName: Full=Genome polyprotein;
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 VP1-2A;
AltName: Full=PX;
Contains:
RecName: Full=Protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Protein 2A;
Short=P2A;
Contains:
RecName: Full=Protein 2BC;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=Protein 3ABCD;
Short=P3;
Contains:
RecName: Full=Protein 3ABC;
Contains:
RecName: Full=Protein 3AB;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Protein 3B;
Short=P3B;
AltName: Full=VPg;
Contains:
RecName: Full=Protein 3CD;
Contains:
RecName: Full=Protease 3C;
Short=P3C;
EC=3.4.22.28;
AltName: Full=Picornain 3C;
Contains:
RecName: Full=RNA-directed RNA polymerase 3D-POL;
Short=P3D-POL;
EC=2.7.7.48;
Human hepatitis A virus genotype IB (isolate MBB) (HHAV) (Human
hepatitis A virus (isolate Human/Northern Africa/MBB/1978)).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Hepatovirus.
NCBI_TaxID=12100;
NCBI_TaxID=9536; Cercopithecus hamlyni (Owl-faced monkey) (Hamlyn's monkey).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9539; Macaca (macaques).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2823500; DOI=10.1016/0168-1702(87)90026-8;
Paul A.V., Tada H., der Helm K., Wissel T., Kiehn R., Wimmer E.,
Deinhardt F.;
"The entire nucleotide sequence of the genome of human hepatitis A
virus (isolate MBB).";
Virus Res. 8:153-171(1987).
[2]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1520-1738 IN COMPLEX WITH THE
INHIBITOR N-CBZ-L-SERINE B-LACTONE.
PubMed=16288920; DOI=10.1016/j.jmb.2005.09.074;
Yin J., Bergmann E.M., Cherney M.M., Lall M.S., Jain R.P.,
Vederas J.C., James M.N.G.;
"Dual modes of modification of hepatitis A virus 3C protease by a
serine-derived beta-lactone: selective crystallization and formation
of a functional catalytic triad in the active site.";
J. Mol. Biol. 354:854-871(2005).
-!- FUNCTION: Capsid proteins VP1, VP2, and VP3 form a closed capsid
enclosing the viral positive strand RNA genome. All these 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 HAVCR1 to provide virion attachment to target cell
(By similarity). {ECO:0000250}.
-!- FUNCTION: Protein VP0: VP0 precursor is a component of immature
procapsids. The N-terminal domain of VP0, protein VP4, is needed
for the assembly of 12 pentamers into the icosahedral structure.
Unlike other picornaviruses, HAV VP4 does not seem to be
myristoylated and has not been detected in mature virions,
supposedly owing to its small size (By similarity). {ECO:0000250}.
-!- FUNCTION: VP1-2A precursor is a component of immature procapsids
and corresponds to an extended form of the structural protein VP1.
The C-terminal domain of VP1-2A, protein 2A, acts as an assembly
signal that allows multimerization of VP1-2A and formation of
pentamers of VP1-VP2-VP3 trimers. It is proteolytically removed
from the precursor by a host protease and does not seem to be
found in mature particles (By similarity). {ECO:0000250}.
-!- FUNCTION: Protein 2B and 2BC precursor affect 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 to the 3AB and 3ABC precursors. {ECO:0000250}.
-!- FUNCTION: The 3AB precursor interacts with the 3CD precursor and
with RNA structures found at both the 5'- and 3'-termini of the
viral genome. Since the 3AB precursor contains the hydrophobic
domain 3A, it probably anchors the whole viral replicase complex
to intracellular membranes on which viral RNA synthesis occurs (By
similarity). {ECO:0000250}.
-!- FUNCTION: The 3ABC precursor is targeted to the mitochondrial
membrane where protease 3C activity cleaves and inhibits the host
antiviral protein MAVS, thereby disrupting activation of IRF3
through the IFIH1/MDA5 pathway. In vivo, the protease activity of
3ABC precursor is more efficient in cleaving the 2BC precursor
than that of protein 3C. The 3ABC precursor may therefore play a
role in the proteolytic processing of the polyprotein (By
similarity). {ECO:0000250}.
-!- FUNCTION: Protein 3B is covalently linked to the 5'-end of both
the positive-strand and negative-strand genomic RNAs. It 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. Also cleaves host proteins such as PCBP2 (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: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- 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: NTP + H(2)O = NDP + phosphate.
-!- SUBUNIT: 3AB precursor is a homodimer. 3AB precursor interacts
with 3CD precursor. Protein 3ABC interacts with human MAVS (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein VP2: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP3: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP1: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP1-2A: Virion {ECO:0000250}. 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. May associate
with membranes through a N-terminal amphipathic helix (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3ABC: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Host mitochondrion outer 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 3AB: 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: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protease 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=Interacts with membranes in a complex with viral protein 3AB.
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}.
-!- PTM: Specific enzymatic cleavages by the viral protease in vivo
yield a variety of precursors and mature proteins. Polyprotein
processing intermediates are produced, such as P1-2A which is a
functional precursor of the structural proteins, VP0 which is a
VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a
stable and catalytically active precursor of 3A, 3B and 3C
proteins, 3AB and 3CD precursors. The assembly signal 2A is
removed from VP1-2A by a host protease. 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 (By similarity).
{ECO:0000250}.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
linked to the 5'-end of genomic RNA. This uridylylated form acts
as a nucleotide-peptide primer for the polymerase (By similarity).
{ECO:0000250}.
-!- MISCELLANEOUS: The need for an intact eIF4G factor for the
initiation of translation of HAV results in an inability to shut
off host protein synthesis by a mechanism similar to that of other
picornaviruses.
-!- SIMILARITY: Belongs to the picornaviridae polyprotein family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
{ECO:0000305}.
-!- CAUTION: Protein VP1 seems to have a heterogeneous C-terminus in
cell culture. It may be reduced by a few amino acids compared to
the sequence shown. {ECO:0000305}.
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EMBL; M20273; AAA45474.1; -; Genomic_RNA.
PDB; 2A4O; X-ray; 1.55 A; A=1520-1738.
PDB; 2CXV; X-ray; 1.40 A; A=1520-1738.
PDBsum; 2A4O; -.
PDBsum; 2CXV; -.
ProteinModelPortal; P13901; -.
SMR; P13901; -.
DrugBank; DB04634; N-BENZYLOXYCARBONYL-L-SERINE-BETALACTONE.
DrugBank; DB04029; Phenylalanine Amide.
OrthoDB; VOG0900006M; -.
EvolutionaryTrace; P13901; -.
Proteomes; UP000007904; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0044193; C:host cell mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; 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:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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; 2.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR024354; Hepatitis_A_VP1-2A.
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; PF12944; HAV_VP; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 2.
Pfam; PF00910; RNA_helicase; 1.
PRINTS; PR00918; CALICVIRUSNS.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Capsid protein; Coiled coil;
Complete proteome; Covalent protein-RNA linkage;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Helicase;
Host cytoplasm; Host cytoplasmic vesicle;
Host gene expression shutoff by virus; Host membrane;
Host mitochondrion; Host mitochondrion outer membrane;
Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host MAVS by virus;
Inhibition of host RLR pathway by virus;
Interferon antiviral system evasion; Ion channel; Ion transport;
Membrane; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; RNA-binding; RNA-directed RNA polymerase; Thiol protease;
Transferase; Transport; Viral attachment to host cell;
Viral immunoevasion; Viral ion channel; Viral RNA replication; Virion;
Virus entry into host cell.
CHAIN 1 2227 Genome polyprotein.
/FTId=PRO_0000311015.
CHAIN 1 245 Protein VP0. {ECO:0000255}.
/FTId=PRO_0000311016.
CHAIN 1 23 Protein VP4. {ECO:0000255}.
/FTId=PRO_0000039968.
CHAIN 24 245 Protein VP2. {ECO:0000255}.
/FTId=PRO_0000039969.
CHAIN 246 491 Protein VP3. {ECO:0000255}.
/FTId=PRO_0000039970.
CHAIN 492 836 Protein VP1-2A. {ECO:0000255}.
/FTId=PRO_0000039971.
CHAIN 492 769 Protein VP1. {ECO:0000255}.
/FTId=PRO_0000311017.
CHAIN 770 836 Protein 2A. {ECO:0000255}.
/FTId=PRO_0000039972.
CHAIN 837 1422 Protein 2BC. {ECO:0000255}.
/FTId=PRO_0000311018.
CHAIN 837 1087 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000039973.
CHAIN 1088 1422 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000039974.
CHAIN 1423 2227 Protein 3ABCD. {ECO:0000255}.
/FTId=PRO_0000311019.
CHAIN 1423 1738 Protein 3ABC. {ECO:0000255}.
/FTId=PRO_0000311020.
CHAIN 1423 1519 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000311021.
CHAIN 1423 1496 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000039975.
CHAIN 1497 1519 Protein 3B. {ECO:0000255}.
/FTId=PRO_0000039976.
CHAIN 1520 2227 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000311022.
CHAIN 1520 1738 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000039977.
CHAIN 1739 2227 RNA-directed RNA polymerase 3D-POL.
/FTId=PRO_0000039978.
TOPO_DOM 1 1467 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1468 1482 {ECO:0000255}.
TOPO_DOM 1483 2227 Cytoplasmic. {ECO:0000255}.
DOMAIN 1204 1366 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1520 1716 Peptidase C3.
DOMAIN 1976 2097 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1230 1237 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
COILED 1127 1152 {ECO:0000255}.
COMPBIAS 636 639 Poly-Ile.
ACT_SITE 1563 1563 For protease 3C activity.
ACT_SITE 1603 1603 For protease 3C activity.
ACT_SITE 1691 1691 For protease 3C activity.
SITE 23 24 Cleavage. {ECO:0000255}.
SITE 245 246 Cleavage; by protease 3C. {ECO:0000255}.
SITE 491 492 Cleavage; by protease 3C. {ECO:0000255}.
SITE 769 770 Cleavage; by host. {ECO:0000255}.
SITE 769 769 Important for VP1 folding and capsid
assembly. {ECO:0000250}.
SITE 836 837 Cleavage; by protease 3C. {ECO:0000250}.
SITE 1087 1088 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1422 1423 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1496 1497 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1519 1520 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1738 1739 Cleavage; by protease 3C. {ECO:0000250}.
MOD_RES 1499 1499 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
HELIX 1521 1531 {ECO:0000244|PDB:2CXV}.
STRAND 1532 1538 {ECO:0000244|PDB:2CXV}.
STRAND 1545 1555 {ECO:0000244|PDB:2CXV}.
STRAND 1557 1561 {ECO:0000244|PDB:2CXV}.
HELIX 1562 1564 {ECO:0000244|PDB:2CXV}.
TURN 1565 1567 {ECO:0000244|PDB:2CXV}.
HELIX 1571 1573 {ECO:0000244|PDB:2CXV}.
STRAND 1574 1580 {ECO:0000244|PDB:2CXV}.
STRAND 1583 1588 {ECO:0000244|PDB:2CXV}.
HELIX 1589 1591 {ECO:0000244|PDB:2CXV}.
STRAND 1592 1600 {ECO:0000244|PDB:2CXV}.
STRAND 1603 1608 {ECO:0000244|PDB:2CXV}.
HELIX 1619 1621 {ECO:0000244|PDB:2CXV}.
HELIX 1625 1631 {ECO:0000244|PDB:2CXV}.
STRAND 1636 1642 {ECO:0000244|PDB:2CXV}.
STRAND 1645 1651 {ECO:0000244|PDB:2CXV}.
STRAND 1655 1665 {ECO:0000244|PDB:2CXV}.
STRAND 1671 1683 {ECO:0000244|PDB:2CXV}.
STRAND 1694 1698 {ECO:0000244|PDB:2CXV}.
HELIX 1700 1702 {ECO:0000244|PDB:2CXV}.
STRAND 1706 1714 {ECO:0000244|PDB:2CXV}.
STRAND 1717 1722 {ECO:0000244|PDB:2CXV}.
HELIX 1725 1730 {ECO:0000244|PDB:2CXV}.
SEQUENCE 2227 AA; 251427 MW; EC983ED2A7C86349 CRC64;
MNMSRQGIFQ TVGSGLDHIL SLADIEEEQM IQSVDRTAVT GASYFTSVDQ SSVHTAEVGS
HQVEPLRTSV DKPGSKKTQG EKFFLIHSAD WLTTHALFHE VAKLDVVKLL YNEQFAVQGL
LRYHTYARFG IEIQVQINPT PFQQGGLICA MVPGDQSYGS IASLTVYPHG LLNCNINNVV
RIKVPFIYTR GAYHFKDPQY PVWELTIRVW SELNIGTGTS AYTSLNVLAR FTDLELHGLT
PLSTQMMRNE FRVSTTENVV NLSNYEDARA KMSFALDQED WKSDPSQGGG IKITHFTTWT
SIPTLAAQFP FNASDSVGQQ IKVIPVDPYF FQMTNTNPDQ KCITALASIC QMFCFWRGDL
VFDFQVFPTK YHSGRLLFCF VPGNELIDVS GITLKQATTA PCAVMDITGV QSTLRFRVPW
ISDTPYRVNR YTKSAHQKGE YTAIGKLIVY CYNRLTSPSN VASHVRVNVY LSAINLECFA
PLYHAMDVTT QVGDDSGGFS TTVSTEQNVP DPQVGITTMK DLKGKANRGK MDVSGVQAPV
GAITTIEDPV LAKKVPETFP ELKPGESRHT SDHMSIYKFM GRSHFLCTFT FNSNNKEYTF
PITLSSTSNP PHGLPSTLRW FFNLFQLYRG PLDLTIIIIG ATDVDGMAWF TPVGLAVDTP
WVEKESALSI DYKTALGAVR FNTRRTGNIQ IRLPWYSYLY AVSGALDGLG DKTDSTFGLV
SIQIANYNHS DEYLSFSCYL SVTEQSEFYF PRAPLNSNAM LSTESMMSRI AAGDLESSVD
DPRSEEDKRF ESHIECRKPY KELRLEVGKQ RLKYAQEELS NEVLPPPRKK KGLFSQAKIS
LFYTEEHEIM KFSWRGVTAD TRALRRFGFS LAAGRSVWTL EMDAGVLTGR LIRLNDEKWT
EMKDDKIVSL IEKFTSNKYW SKVNFPHGML DLEEIAANSK DFPNMSETDL CFLLHWLNPK
KINLADRMLG LSGVQEIKEQ GVGLIAECRT FLDSIAGTLK SMMFGFHHSV TVEIINTVLC
FVKSGILLYV MQQLNQDEHS HIIGLLRVMN YVDIGCSVIS CGKVFSKMLE TVFNWQMDSR
MMELRTQSFS NWLRDICSGI TIFKNFKDAI YWLYTKLNDF YEVNYGKKKD ILNILKDNQQ
KIEKAIEEAD KFSILQIQDV EKFEQYQKGV DLIQKLRTVH SMAQVDPNLM VHLSPLRDCI
ARVHQKLKNL GSINQAMVTR CEPVVCYLYG KRGGGKSLTS IALATKICKH YGVEPEKNIY
TKPVASDYWD GYSGQLVCII DDIGQNTTDE DWSDFCQLVS GCPLRLNMAS LEEKGRHFSS
PFIIATSNWS NPSPKTVYVK EAIDRRLHFK VEVNPASFSK NPHNDMLNVN LAKTNDAIKD
MSCVDLIMDG HNVSLMDLLS SLVMTVEIRK QNMTAFMELW SQGISDDDND SAMAEFFQSF
PSGEPSNSKL SGFFQSVTNH KWVAVGAAVG ILGVLVGGWF VYKHFSRKEE EPIPAEGVYH
GVTKPKQVIK LDADPVESQS TLEIAGLVRK NLVQFGVGEK NGCVRWVMNA LGVKDDWLLV
PSHAYKFEKD YEMMEFYFNR GGTYYSISAG NVVIQSLDVG FQDVVLMKVP TIPKFRDITQ
HFIKKGDVPR ALNRLATLVT TVNGTPMLIS EGPLKMEEKA TYVHKKNDGT TVDLTVDQAW
RGKGEGLPGM CGGALVSSNQ SIQNAILGIH VAGGNSILVA KLVTQEMFQN IDKKIESQRI
MKVEFTQCSM NVVSKTLFRK SPIHHHIDKT MINFPAAMPF SKAEIDPMAM MLSKYSLPIV
EEPEDYKEAS IFYQNKIVGK TQLVDDFLDL DMAITGAPGI DAINMDSSPG FPYVQERLTK
RDLIWLDENG LLLGVHPRLA QRILFNTVMM ENCSDLDVVF TTCPKDELRP LEKVLESKTR
AIDACPLDYT ILCRMYWGPA ISYFHLNPGF HTGVAIGIDP DCQWDELFKT MIRFGDVGLD
LDFSAFDASL SPFMIREAGR IMSELSGTPS HFGTALMNTI IYSKHLLYNC CYHVCGSMPS
GSPCTALLNS IINNVNLYYV FSKIFGKSPV FFCQALKILC YGDDVLIVFS RDVQIDNLDL
IGQKIVDEFK KLGMTATSAD KNVPQLKPVS ELTFLKRSFN LVEDRIRPAI SEKTIWSLIA
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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
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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

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GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
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Fax 02 36 00 65 94
italia@gentaur.com | Gentaur