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

 POLG_POL1M              Reviewed;        2209 AA.
P03300; P03299; Q84879; Q84880; Q89679;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 194.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=P1;
Contains:
RecName: Full=Capsid protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Capsid protein VP4;
AltName: Full=P1A;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Capsid protein VP2;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Capsid protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Capsid protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=P2;
Contains:
RecName: Full=Protease 2A;
Short=P2A;
EC=3.4.22.29;
AltName: Full=Picornain 2A;
AltName: Full=Protein 2A;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=P3;
Contains:
RecName: Full=Protein 3AB;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Viral protein genome-linked;
Short=VPg;
AltName: Full=Protein 3B;
Short=P3B;
Contains:
RecName: Full=Protein 3CD;
EC=3.4.22.28;
Contains:
RecName: Full=Protease 3C;
Short=P3C;
EC=3.4.22.28;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=3D polymerase;
Short=3Dpol;
AltName: Full=Protein 3D;
Short=3D;
Poliovirus type 1 (strain Mahoney).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Enterovirus C.
NCBI_TaxID=12081;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6264310; DOI=10.1038/291547a0;
Kitamura N., Semler B.L., Rothberg P.G., Larsen G.R., Adler C.J.,
Dorner A.J., Emini E.A., Hanecak R., Lee J.J., van der Werf S.,
Anderson C.W., Wimmer E.;
"Primary structure, gene organization and polypeptide expression of
poliovirus RNA.";
Nature 291:547-553(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6272282; DOI=10.1073/pnas.78.8.4887;
Racaniello V.R., Baltimore D.;
"Molecular cloning of poliovirus cDNA and determination of the
complete nucleotide sequence of the viral genome.";
Proc. Natl. Acad. Sci. U.S.A. 78:4887-4891(1981).
[3]
PROTEIN SEQUENCE OF 2-69.
PubMed=6284987;
Dorner A.J., Dorner L.F., Larsen G.R., Wimmer E., Anderson C.W.;
"Identification of the initiation site of poliovirus polyprotein
synthesis.";
J. Virol. 42:1017-1028(1982).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1539-1574, AND FUNCTION (VIRAL
PROTEIN GENOME-LINKED).
PubMed=6250717; DOI=10.1016/0092-8674(80)90137-3;
Kitamura N., Adler C.J., Rothberg P.G., Martinko J., Nathenson S.G.,
Wimmer E.;
"The genome-linked protein of picornaviruses. VII. Genetic mapping of
poliovirus VPg by protein and RNA sequence studies.";
Cell 21:295-302(1980).
[5]
FUNCTION (VIRAL PROTEIN GENOME-LINKED), AND COVALENT RNA LINKAGE AT
TYR-1546 (VPG).
PubMed=209034;
Ambros V., Baltimore D.;
"Protein is linked to the 5' end of poliovirus RNA by a phosphodiester
linkage to tyrosine.";
J. Biol. Chem. 253:5263-5266(1978).
[6]
ACTIVE SITE (RNA-DIRECTED RNA POLYMERASE).
PubMed=2196557; DOI=10.1093/protein/3.6.461;
Delarue M., Poch O., Tordo N., Moras D., Argos P.;
"An attempt to unify the structure of polymerases.";
Protein Eng. 3:461-467(1990).
[7]
MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF ALA-3.
PubMed=1850017;
Moscufo N., Simons J., Chow M.;
"Myristoylation is important at multiple stages in poliovirus
assembly.";
J. Virol. 65:2372-2380(1991).
[8]
MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
PubMed=1851815; DOI=10.1099/0022-1317-72-5-1151;
Marc D., Girard M., van der Werf S.;
"A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks
its myristoylation and prevents viral assembly.";
J. Gen. Virol. 72:1151-1157(1991).
[9]
FUNCTION (PROTEIN 2C).
PubMed=8385138;
Rodriguez P.L., Carrasco L.;
"Poliovirus protein 2C has ATPase and GTPase activities.";
J. Biol. Chem. 268:8105-8110(1993).
[10]
INTERACTION OF PROTEIN 3AB WITH PROTEIN 3CD.
PubMed=7929441;
Harris K.S., Xiang W., Alexander L., Lane W.S., Paul A.V., Wimmer E.;
"Interaction of poliovirus polypeptide 3CDpro with the 5' and 3'
termini of the poliovirus genome. Identification of viral and cellular
cofactors needed for efficient binding.";
J. Biol. Chem. 269:27004-27014(1994).
[11]
FUNCTION (PROTEASE 2A).
PubMed=9755863; DOI=10.1016/S0014-5793(98)01027-8;
Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.;
"Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-
4F complex.";
FEBS Lett. 435:79-83(1998).
[12]
FUNCTION (PROTEIN 3B), COVALENT RNA-LINKAGE AT TYR-1546 OF VPG, AND
URIDYLYLATION AT TYR-1546.
PubMed=12502805; DOI=10.1128/JVI.77.2.891-904.2003;
Paul A.V., Peters J., Mugavero J., Yin J., van Boom J.H., Wimmer E.;
"Biochemical and genetic studies of the VPg uridylylation reaction
catalyzed by the RNA polymerase of poliovirus.";
J. Virol. 77:891-904(2003).
[13]
HOMODIMERIZATION (PROTEIN 3A).
PubMed=12823963; DOI=10.1016/S0022-2836(03)00577-1;
Strauss D.M., Glustrom L.W., Wuttke D.S.;
"Towards an understanding of the poliovirus replication complex: the
solution structure of the soluble domain of the poliovirus 3A
protein.";
J. Mol. Biol. 330:225-234(2003).
[14]
SUBUNIT (PROTEIN 3A), AND CAUTION.
PubMed=16138011; DOI=10.4161/cc.4.10.2041;
Kondratova A.A., Neznanov N., Kondratov R.V., Gudkov A.V.;
"Poliovirus protein 3A binds and inactivates LIS1, causing block of
membrane protein trafficking and deregulation of cell division.";
Cell Cycle 4:1403-1410(2005).
[15]
FUNCTION (PROTEIN 3A).
PubMed=15914217; DOI=10.1016/j.virol.2005.03.036;
Choe S.S., Dodd D.A., Kirkegaard K.;
"Inhibition of cellular protein secretion by picornaviral 3A
proteins.";
Virology 337:18-29(2005).
[16]
FUNCTION (VIRAL PROTEIN GENOME-LINKED), COVALENT RNA-LINKAGE AT
TYR-1546 OF VPG, AND URIDYLYLATION AT TYR-1546.
PubMed=16840321; DOI=10.1128/JVI.02533-05;
Richards O.C., Spagnolo J.F., Lyle J.M., Vleck S.E., Kuchta R.D.,
Kirkegaard K.;
"Intramolecular and intermolecular uridylylation by poliovirus RNA-
dependent RNA polymerase.";
J. Virol. 80:7405-7415(2006).
[17]
INTERACTION OF PROTEIN 3A WITH HOST GBF1.
PubMed=17005635; DOI=10.1128/JVI.01225-06;
Wessels E., Duijsings D., Lanke K.H., van Dooren S.H., Jackson C.L.,
Melchers W.J., van Kuppeveld F.J.;
"Effects of picornavirus 3A Proteins on Protein Transport and GBF1-
dependent COP-I recruitment.";
J. Virol. 80:11852-11860(2006).
[18]
INTERACTION OF PROTEIN 2C WITH HUMAN RTN3.
PubMed=17182608; DOI=10.1074/jbc.M611145200;
Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H.,
Lin K.-H., Lai H.-C., Tang P., Horng J.-T.;
"Reticulon 3 binds the 2C protein of enterovirus 71 and is required
for viral replication.";
J. Biol. Chem. 282:5888-5898(2007).
[19]
FUNCTION (PROTEIN 3A).
PubMed=17079330; DOI=10.1128/JVI.01820-06;
Belov G.A., Altan-Bonnet N., Kovtunovych G., Jackson C.L.,
Lippincott-Schwartz J., Ehrenfeld E.;
"Hijacking components of the cellular secretory pathway for
replication of poliovirus RNA.";
J. Virol. 81:558-567(2007).
[20]
FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), AND
FUNCTION (CAPSID PROTEIN VP3).
PubMed=17622193; DOI=10.1371/journal.pbio.0050183;
Brandenburg B., Lee L.Y., Lakadamyali M., Rust M.J., Zhuang X.,
Hogle J.M.;
"Imaging poliovirus entry in live cells.";
PLoS Biol. 5:E183-E183(2007).
[21]
FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), AND
FUNCTION (CAPSID PROTEIN VP3).
STRAIN=Sabin 2;
PubMed=17717529; DOI=10.1038/sj.emboj.7601831;
Coyne C.B., Kim K.S., Bergelson J.M.;
"Poliovirus entry into human brain microvascular cells requires
receptor-induced activation of SHP-2.";
EMBO J. 26:4016-4028(2007).
[22]
INTERACTION OF PROTEIN 3B WITH PROTEIN 3D.
PubMed=17409142; DOI=10.1128/JVI.02252-06;
Strauss D.M., Wuttke D.S.;
"Characterization of protein-protein interactions critical for
poliovirus replication: analysis of 3AB and VPg binding to the RNA-
dependent RNA polymerase.";
J. Virol. 81:6369-6378(2007).
[23]
TOPOLOGY (PROTEIN 3A AND PROTEIN 3AB).
PubMed=17417822; DOI=10.1021/bi6024758;
Fujita K., Krishnakumar S.S., Franco D., Paul A.V., London E.,
Wimmer E.;
"Membrane topography of the hydrophobic anchor sequence of poliovirus
3A and 3AB proteins and the functional effect of 3A/3AB membrane
association upon RNA replication.";
Biochemistry 46:5185-5199(2007).
[24]
FUNCTION (PROTEASE 3C).
PubMed=18632855; DOI=10.1128/JVI.00006-08;
Bonderoff J.M., Larey J.L., Lloyd R.E.;
"Cleavage of poly(A)-binding protein by poliovirus 3C proteinase
inhibits viral internal ribosome entry site-mediated translation.";
J. Virol. 82:9389-9399(2008).
[25]
FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), AND
FUNCTION (CAPSID PROTEIN VP3).
PubMed=18191571; DOI=10.1016/j.tim.2007.12.004;
Bergelson J.M.;
"New (fluorescent) light on poliovirus entry.";
Trends Microbiol. 16:44-47(2008).
[26]
REVIEW (PROTEIN 2B).
PubMed=18216106; DOI=10.1128/JVI.02076-07;
de Jong A.S., de Mattia F., Van Dommelen M.M., Lanke K.,
Melchers W.J., Willems P.H., van Kuppeveld F.J.;
"Functional analysis of picornavirus 2B proteins: effects on calcium
homeostasis and intracellular protein trafficking.";
J. Virol. 82:3782-3790(2008).
[27]
FUNCTION (PROTEASE 3C).
PubMed=17993457; DOI=10.1074/jbc.M707907200;
Shen M., Reitman Z.J., Zhao Y., Moustafa I., Wang Q., Arnold J.J.,
Pathak H.B., Cameron C.E.;
"Picornavirus genome replication. Identification of the surface of the
poliovirus (PV) 3C dimer that interacts with PV 3Dpol during VPg
uridylylation and construction of a structural model for the PV 3C2-
3Dpol complex.";
J. Biol. Chem. 283:875-888(2008).
[28]
FUNCTION (PROTEIN 2A).
PubMed=19789179; DOI=10.1242/jcs.055988;
Castello A., Izquierdo J.M., Welnowska E., Carrasco L.;
"RNA nuclear export is blocked by poliovirus 2A protease and is
concomitant with nucleoporin cleavage.";
J. Cell Sci. 122:3799-3809(2009).
[29]
FUNCTION (PROTEIN 2C).
PubMed=19520852; DOI=10.1074/jbc.M109.031807;
Adams P., Kandiah E., Effantin G., Steven A.C., Ehrenfeld E.;
"Poliovirus 2C protein forms homo-oligomeric structures required for
ATPase activity.";
J. Biol. Chem. 284:22012-22021(2009).
[30]
REVIEW (RNA-DIRECTED RNA POLYMERASE).
PubMed=18487072; DOI=10.1016/j.biocel.2008.03.019;
Kok C.C., McMinn P.C.;
"Picornavirus RNA-dependent RNA polymerase.";
Int. J. Biochem. Cell Biol. 41:498-502(2009).
[31]
INTERACTION OF CAPSID PROTEIN VP3 WITH PROTEIN 2C, AND FUNCTION OF
CAPSID PROTEIN VP3.
PubMed=20865167; DOI=10.1371/journal.ppat.1001066;
Liu Y., Wang C., Mueller S., Paul A.V., Wimmer E., Jiang P.;
"Direct interaction between two viral proteins, the nonstructural
protein 2C and the capsid protein VP3, is required for enterovirus
morphogenesis.";
PLoS Pathog. 6:E1001066-E1001066(2010).
[32]
FUNCTION (VIRAL PROTEIN GENOME-LINKED).
PubMed=20441784; DOI=10.1016/j.peptides.2010.04.021;
Schein C.H., Oezguen N., van der Heden van Noort G.J., Filippov D.V.,
Paul A., Kumar E., Braun W.;
"NMR solution structure of poliovirus uridylyated peptide linked to
the genome (VPgpU).";
Peptides 31:1441-1448(2010).
[33]
FUNCTION (PROTEIN 3AB).
PubMed=21045553; DOI=10.4161/rna.7.6.13781;
Gangaramani D.R., Eden E.L., Shah M., Destefano J.J.;
"The twenty-nine amino acid C-terminal cytoplasmic domain of
poliovirus 3AB is critical for nucleic acid chaperone activity.";
RNA Biol. 7:820-829(2010).
[34]
TOPOLOGY (PROTEIN 2B).
PubMed=21835803; DOI=10.1128/JVI.05421-11;
Martinez-Gil L., Bano-Polo M., Redondo N., Sanchez-Martinez S.,
Nieva J.L., Carrasco L., Mingarro I.;
"Membrane integration of poliovirus 2B viroporin.";
J. Virol. 85:11315-11324(2011).
[35]
SUBUNIT OF PROTEIN 3A AND PROTEIN 3AB.
PubMed=21345960; DOI=10.1128/JVI.02398-10;
Teterina N.L., Pinto Y., Weaver J.D., Jensen K.S., Ehrenfeld E.;
"Analysis of poliovirus protein 3A interactions with viral and
cellular proteins in infected cells.";
J. Virol. 85:4284-4296(2011).
[36]
FUNCTION (PROTEIN 2C).
PubMed=22761387; DOI=10.1128/JVI.00914-12;
Wang C., Jiang P., Sand C., Paul A.V., Wimmer E.;
"Alanine scanning of poliovirus 2CATPase reveals new genetic evidence
that capsid protein/2CATPase interactions are essential for
morphogenesis.";
J. Virol. 86:9964-9975(2012).
[37]
CHARACTERIZATION OF N-TERMINUS (CAPSID PROTEIN VP1).
PubMed=23085162; DOI=10.1016/j.jmgm.2012.06.009;
Roberts J.A., Kuiper M.J., Thorley B.R., Smooker P.M., Hung A.;
"Investigation of a predicted N-terminal amphipathic alpha-helix using
atomistic molecular dynamics simulation of a complete prototype
poliovirus virion.";
J. Mol. Graph. Model. 38:165-173(2012).
[38]
FUNCTION (CAPSID PROTEIN VP1 AND CAPSID PROTEIN VP4).
PubMed=23365424; DOI=10.1128/JVI.03209-12;
Strauss M., Levy H.C., Bostina M., Filman D.J., Hogle J.M.;
"RNA transfer from poliovirus 135S particles across membranes is
mediated by long umbilical connectors.";
J. Virol. 87:3903-3914(2013).
[39]
MULTIMERIZATION (RNA-DIRECTED RNA POLYMERASE).
PubMed=23583774; DOI=10.1016/j.jmb.2013.04.007;
Wang J., Lyle J.M., Bullitt E.;
"Surface for catalysis by poliovirus RNA-dependent RNA polymerase.";
J. Mol. Biol. 425:2529-2540(2013).
[40]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881.
PubMed=2994218; DOI=10.1126/science.2994218;
Hogle J.M., Chow M., Filman D.J.;
"Three-dimensional structure of poliovirus at 2.9-A resolution.";
Science 229:1358-1365(1985).
[41]
X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 2-880.
PubMed=2548847;
Filman D.J., Syed R., Chow M., Macadam A.J., Minor P.D., Hogle J.M.;
"Structural factors that control conformational transitions and
serotype specificity in type 3 poliovirus.";
EMBO J. 8:1567-1579(1989).
[42]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-880.
PubMed=7849583; DOI=10.1002/pro.5560031005;
Basavappa R., Syed R., Flore O., Icenogle J.P., Filman D.J.,
Hogle J.M.;
"Role and mechanism of the maturation cleavage of VP0 in poliovirus
assembly: structure of the empty capsid assembly intermediate at 2.9 A
resolution.";
Protein Sci. 3:1651-1669(1994).
[43]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881.
PubMed=7820548; DOI=10.1016/S0960-9822(00)00176-7;
Grant R.A., Hiremath C.N., Filman D.J., Syed R., Andries K.,
Hogle J.M.;
"Structures of poliovirus complexes with anti-viral drugs:
implications for viral stability and drug design.";
Curr. Biol. 4:784-797(1994).
[44]
STRUCTURE BY ELECTRON MICROSCOPY (2.0 ANGSTROMS) OF 1-881, AND
MYRISTOYLATION AT GLY-2.
PubMed=10618374; DOI=10.1073/pnas.97.1.79;
He Y., Bowman V.D., Mueller S., Bator C.M., Bella J., Peng X.,
Baker T.S., Wimmer E., Kuhn R.J., Rossmann M.G.;
"Interaction of the poliovirus receptor with poliovirus.";
Proc. Natl. Acad. Sci. U.S.A. 97:79-84(2000).
[45]
STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS) OF 2-881.
PubMed=12663789; DOI=10.1128/JVI.77.8.4827-4835.2003;
He Y., Mueller S., Chipman P.R., Bator C.M., Peng X., Bowman V.D.,
Mukhopadhyay S., Wimmer E., Kuhn R.J., Rossmann M.G.;
"Complexes of poliovirus serotypes with their common cellular
receptor, CD155.";
J. Virol. 77:4827-4835(2003).
[46]
STRUCTURE BY ELECTRON MICROSCOPY (11.0 ANGSTROMS) OF 97-880.
PubMed=15919927; DOI=10.1128/JVI.79.12.7745-7755.2005;
Bubeck D., Filman D.J., Cheng N., Steven A.C., Hogle J.M.,
Belnap D.M.;
"The structure of the poliovirus 135S cell entry intermediate at 10-
angstrom resolution reveals the location of an externalized
polypeptide that binds to membranes.";
J. Virol. 79:7745-7755(2005).
[47]
STRUCTURE BY ELECTRON MICROSCOPY (8.0 ANGSTROMS) OF 2-881.
PubMed=19011098; DOI=10.1073/pnas.0807848105;
Zhang P., Mueller S., Morais M.C., Bator C.M., Bowman V.D.,
Hafenstein S., Wimmer E., Rossmann M.G.;
"Crystal structure of CD155 and electron microscopic studies of its
complexes with polioviruses.";
Proc. Natl. Acad. Sci. U.S.A. 105:18284-18289(2008).
[48]
STRUCTURE BY ELECTRON MICROSCOPY OF 97-341 AND 647-881.
PubMed=20181687; DOI=10.1128/JVI.02393-09;
Levy H.C., Bostina M., Filman D.J., Hogle J.M.;
"Catching a virus in the act of RNA release: a novel poliovirus
uncoating intermediate characterized by cryo-electron microscopy.";
J. Virol. 84:4426-4441(2010).
-!- FUNCTION: Capsid protein VP1: Forms an icosahedral capsid of
pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid
is 300 Angstroms in diameter, composed of 60 copies of each capsid
protein and enclosing the viral positive strand RNA genome. Capsid
protein VP1 mainly forms the vertices of the capsid. Capsid
protein VP1 interacts with host cell receptor PVR to provide
virion attachment to target host epithelial cells. This attachment
induces virion internalization predominantly through clathrin- and
caveolin-independent endocytosis in Hela cells and through
caveolin-mediated endocytosis in brain microvascular endothelial
cells. Tyrosine kinases are probably involved in the entry
process. Virus binding to PVR induces increased junctional
permeability and rearrangement of junctional proteins. Modulation
of endothelial tight junctions, as well as cytolytic infection of
endothelial cells themselves, may result in loss of endothelial
integrity which may help the virus to reach the CNS. After binding
to its receptor, the capsid undergoes conformational changes.
Capsid protein VP1 N-terminus (that contains an amphipathic alpha-
helix) and capsid protein VP4 are externalized. Together, they
shape a pore in the host membrane through which viral genome is
translocated to host cell cytoplasm. After genome has been
released, the channel shrinks.
-!- FUNCTION: Capsid protein VP2: Forms an icosahedral capsid of
pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid
is 300 Angstroms in diameter, composed of 60 copies of each capsid
protein and enclosing the viral positive strand RNA genome.
-!- FUNCTION: Capsid protein VP3: Forms an icosahedral capsid of
pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid
is 300 Angstroms in diameter, composed of 60 copies of each capsid
protein and enclosing the viral positive strand RNA genome.
-!- FUNCTION: Capsid protein VP4: Lies on the inner surface of the
capsid shell. After binding to the host receptor, the capsid
undergoes conformational changes. Capsid protein VP4 is released,
Capsid protein VP1 N-terminus is externalized, and together, they
shape a pore in the host membrane through which the viral genome
is translocated into the host cell cytoplasm. After genome has
been released, the channel shrinks (By similarity). {ECO:0000250}.
-!- FUNCTION: Capsid protein VP0: Component of immature procapsids,
which is cleaved into capsid proteins VP4 and VP2 after
maturation. Allows the capsid to remain inactive before the
maturation step (By similarity). {ECO:0000250}.
-!- FUNCTION: Protein 2A: Cysteine protease that cleaves viral
polyprotein and specific host proteins. It is responsible for the
cleavage between the P1 and P2 regions, first cleavage occurring
in the polyprotein. Cleaves also the host translation initiation
factor EIF4G1, in order to shut down the capped cellular mRNA
translation. Inhibits the host nucleus-cytoplasm protein and RNA
trafficking by cleaving host members of the nuclear pores
including NUP98, NUP62 and NUP153.
-!- FUNCTION: Protein 2B: Plays an essential role in the virus
replication cycle by acting as a viroporin. Creates a pore in the
host reticulum endoplasmic and as a consequence releases Ca2+ in
the cytoplasm of infected cell. In turn, high levels of
cyctoplasmic calcium may trigger membrane trafficking and
transport of viral ER-associated proteins to viroplasms, sites of
viral genome replication.
-!- FUNCTION: Protein 2C: Induces and associates with structural
rearrangements of intracellular membranes. Triggers host autophagy
by interacting with host BECN1 and thereby promotes viral
replication. Participates in viral replication and interacts with
host DHX9. Displays RNA-binding, nucleotide binding and NTPase
activities. May play a role in virion morphogenesis and viral RNA
encapsidation by interacting with the capsid protein VP3.
-!- FUNCTION: Protein 3AB: Localizes the viral replication complex to
the surface of membranous vesicles. Together with protein 3CD
binds the Cis-Active RNA Element (CRE) which is involved in RNA
synthesis initiation. Acts as a cofactor to stimulate the activity
of 3D polymerase, maybe through a nucleid acid chaperone activity.
-!- FUNCTION: Protein 3A: Localizes the viral replication complex to
the surface of membranous vesicles. It inhibits host cell
endoplasmic reticulum-to-Golgi apparatus transport and causes the
dissassembly of the Golgi complex, possibly through GBF1
interaction. This would result in depletion of MHC, trail
receptors and IFN receptors at the host cell surface.
-!- FUNCTION: Viral protein genome-linked: acts as a primer for viral
RNA replication and remains covalently bound to viral genomic RNA.
VPg is uridylylated prior to priming replication into VPg-pUpU.
The oriI viral genomic sequence may act as a template for this.
The VPg-pUpU is then used as primer on the genomic RNA poly(A) by
the RNA-dependent RNA polymerase to replicate the viral genome.
VPg may be removed in the cytoplasm by an unknown enzyme termed
"unlinkase". VPg is not cleaved off virion genomes because
replicated genomic RNA are encapsidated at the site of
replication.
-!- FUNCTION: Protein 3CD: Is involved in the viral replication
complex and viral polypeptide maturation. It exhibits protease
activity with a specificity and catalytic efficiency that is
different from protease 3C. Protein 3CD lacks polymerase activity.
The 3C domain in the context of protein 3CD may have an RNA
binding activity.
-!- FUNCTION: Protease 3C: May cleave host PABP and contribute to host
translation shutoff.
-!- FUNCTION: RNA-directed RNA polymerase: Replicates the viral
genomic RNA on the surface of intracellular membranes. May form
linear arrays of subunits that propagate along a strong head-to-
tail interaction called interface-I. Covalently attaches UMP to a
tyrosine of VPg, which is used to prime RNA synthesis. The
positive stranded RNA genome is first replicated at virus induced
membranous vesicles, creating a dsRNA genomic replication form.
This dsRNA is then used as template to synthesize positive
stranded RNA genomes. ss(+)RNA genomes are either translated,
replicated or encapsidated.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the
picornavirus polyprotein.
-!- 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.
-!- ENZYME REGULATION: RNA-directed RNA polymerase: replication or
transcription is subject to high level of random mutations by the
nucleotide analog ribavirin.
-!- SUBUNIT: Capsid protein VP1: Interacts with capsid protein VP0,
and capsid protein VP3 to form heterotrimeric protomers. Five
protomers subsequently associate to form pentamers which serve as
building blocks for the capsid. Interacts with human PVR.
Interacts with capsid protein VP4 in the mature capsid. Capsid
protein VP0: interacts with capsid protein VP1 and capsid protein
VP3 to form heterotrimeric protomers. Five protomers subsequently
associate to form pentamers which serve as building blocks for the
capsid. Capsid protein VP2: Interacts with capsid protein VP1 and
capsid protein VP3 in the mature capsid. Capsid protein VP3:
interacts with capsid protein VP0 and capsid protein VP1 to form
heterotrimeric protomers. Five protomers subsequently associate to
form pentamers which serve as building blocks for the capsid.
Interacts with capsid protein VP4 in the mature capsid. Capsid
protein VP4: Interacts with capsid protein VP1 and capsid protein
VP3. Protein 2C: interacts with cellular Vimentin/VIM and BECN1;
these interactions play important roles in the viral replication
(By similarity). Protein 2C: interacts with capsid protein VP3;
this interaction may be important for virion morphogenesis.
Protein 2C: interacts with host BECN1 and DHX9 and possibly
presents a hexameric ring structure with 6-fold symmetry
characteristic of AAA+ ATPases. Protein 2C: N-terminus interacts
with human RTN3. This interaction is important for viral
replication (By similarity). Protein 3AB: interacts with protein
3CD. Protein 3A: homodimerizes and interacts with host GBF1. Viral
protein genome-linked: interacts with RNA-directed RNA polymerase.
Protein 3CD: interacts with protein 3AB and with RNA-directed RNA
polymerase. RNA-directed RNA polymerase: interacts with Viral
protein genome-linked and with protein 3CD. {ECO:0000250,
ECO:0000269|PubMed:16138011, ECO:0000269|PubMed:17005635,
ECO:0000269|PubMed:17182608, ECO:0000269|PubMed:17409142,
ECO:0000269|PubMed:20865167, ECO:0000269|PubMed:21345960,
ECO:0000269|PubMed:7929441}.
-!- SUBCELLULAR LOCATION: Capsid protein VP0: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein VP4: Virion.
-!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein VP3: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid 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.
-!- 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.
-!- 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.
-!- 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.
-!- SUBCELLULAR LOCATION: Viral protein genome-linked: Virion. Host
cytoplasm.
-!- SUBCELLULAR LOCATION: Protease 3C: Host cytoplasm.
-!- SUBCELLULAR LOCATION: Protein 3CD: 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.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase: 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.
-!- PTM: Capsid protein VP0: Myristoylation is required for the
formation of pentamers during virus assembly. Further assembly of
12 pentamers and a molecule of genomic RNA generates the provirion
(By similarity). {ECO:0000250}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages in vivo by
the viral proteases yield processing intermediates and the mature
proteins.
-!- PTM: Capsid protein VP0: During virion maturation, immature
virions are rendered infectious following cleavage of VP0 into VP4
and VP2. This maturation seems to be an autocatalytic event
triggered by the presence of RNA in the capsid and it is followed
by a conformational change infectious virion.
-!- PTM: Viral protein genome-linked: VPg is uridylylated by the
polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer
for the genomic RNA replication.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000305}.
-!- CAUTION: Protein 3A: Has been proposed to interact with host
LIS1/NUF (PubMed:16138011), but this has not been confirmed by
other studies (PubMed:21345960). {ECO:0000305|PubMed:16138011,
ECO:0000305|PubMed:21345960}.
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure associated with cellular receptor;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1dgi";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure associated with cellular receptor;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1nn8";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with R80633, an inhibitor of viral
replication;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1po1";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with R77975, an inhibitor of viral
replication;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1po2";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
empty capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1pov";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure complexed with R78206;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1vbd";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2plv";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure of 135S cell entry intermediate;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1xyr";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1hxs";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; V01149; CAA24461.1; -; Genomic_RNA.
EMBL; V01148; CAA24446.1; -; Genomic_RNA.
PIR; A03898; GNNY2P.
PIR; A93258; GNNY1P.
RefSeq; NP_041277.1; NC_002058.3.
PDB; 1AL2; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 1AR6; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 1AR7; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 1AR8; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 1AR9; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 1ASJ; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 1DGI; EM; 22.00 A; 1=599-881, 2=74-341, 3=342-576, 4=2-69.
PDB; 1FPT; X-ray; 3.00 A; P=665-682.
PDB; 1HXS; X-ray; 2.20 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
PDB; 1L1N; X-ray; 2.10 A; A/B=1566-1748.
PDB; 1NG7; NMR; -; A/B=1457-1515.
PDB; 1NN8; EM; 15.00 A; 1=580-881, 2=70-341, 3=342-576, 4=2-69.
PDB; 1PO1; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 1PO2; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 1POV; X-ray; 2.80 A; 0=2-341, 1=580-881, 3=342-579.
PDB; 1RA6; X-ray; 2.00 A; A=1749-2209.
PDB; 1RA7; X-ray; 2.35 A; A=1749-2209.
PDB; 1RAJ; X-ray; 2.50 A; A=1817-2209.
PDB; 1RDR; X-ray; 2.40 A; A=1749-2209.
PDB; 1TQL; X-ray; 2.30 A; A=1749-2209.
PDB; 1VBD; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 1XYR; EM; 11.00 A; 1=650-881, 2=97-333, 3=391-572, 5=342-353, 6=355-390, 7=82-95, 8=621-631.
PDB; 2BBL; NMR; -; A=1544-1565.
PDB; 2BBP; NMR; -; A=1544-1565.
PDB; 2IJD; X-ray; 3.40 A; 1/2=1566-2208.
PDB; 2IJF; X-ray; 3.00 A; A=1749-2208.
PDB; 2ILY; X-ray; 2.60 A; A=1749-2208.
PDB; 2ILZ; X-ray; 2.50 A; A=1749-2208.
PDB; 2IM0; X-ray; 2.25 A; A=1749-2208.
PDB; 2IM1; X-ray; 2.50 A; A=1749-2208.
PDB; 2IM2; X-ray; 2.35 A; A=1749-2208.
PDB; 2IM3; X-ray; 2.60 A; A=1749-2208.
PDB; 2PLV; X-ray; 2.88 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 3EPC; EM; 8.00 A; 1=599-881, 2=74-341, 3=342-576, 4=2-69.
PDB; 3IYB; EM; 10.00 A; 1=647-881, 3=342-572, 4=97-341.
PDB; 3IYC; EM; -; 1=647-881, 4=97-341.
PDB; 3J3O; EM; 11.10 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 3J3P; EM; 9.10 A; 1=580-881, 2=70-341, 3=342-579.
PDB; 3J48; EM; 5.50 A; 1=580-881, 2=70-341, 3=342-579.
PDB; 3J8F; EM; 3.70 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 3J9F; EM; 9.00 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.
PDB; 3JBC; EM; 5.60 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
PDB; 3JBD; EM; 4.70 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
PDB; 3JBE; EM; 4.20 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
PDB; 3JBF; EM; 4.60 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
PDB; 3JBG; EM; 3.80 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.
PDB; 3OL7; X-ray; 2.70 A; A/E/I/M=1749-2209.
PDB; 4DCD; X-ray; 1.69 A; A=1566-1748.
PDB; 4K4S; X-ray; 2.40 A; A/E=1749-2209.
PDB; 4K4T; X-ray; 2.75 A; A/E=1749-2209.
PDB; 4K4U; X-ray; 2.85 A; A/E=1749-2209.
PDB; 4K4V; X-ray; 2.63 A; A/E=1749-2209.
PDB; 4K4W; X-ray; 2.69 A; A/E=1749-2209.
PDB; 4NLO; X-ray; 2.20 A; A=1749-2209.
PDB; 4NLP; X-ray; 2.20 A; A=1749-2209.
PDB; 4NLQ; X-ray; 2.30 A; A=1749-2209.
PDB; 4NLR; X-ray; 2.00 A; A=1749-2209.
PDB; 4NLS; X-ray; 2.00 A; A=1749-2209.
PDB; 4NLT; X-ray; 2.50 A; A=1749-2209.
PDB; 4NLU; X-ray; 2.10 A; A=1749-2209.
PDB; 4NLV; X-ray; 2.30 A; A=1749-2209.
PDB; 4NLW; X-ray; 2.10 A; A=1749-2209.
PDB; 4NLX; X-ray; 2.60 A; A=1749-2209.
PDB; 4NLY; X-ray; 2.30 A; A=1749-2209.
PDB; 4R0E; X-ray; 3.00 A; A=1749-2209.
PDB; 5KTZ; EM; 4.30 A; 1=636-858, 2=70-338, 3=342-572.
PDB; 5KU0; EM; 4.20 A; 1=636-858, 2=70-338, 3=342-572.
PDB; 5KU2; EM; 4.50 A; 1=650-858, 2=70-337, 3=342-571.
PDB; 5KWL; EM; 4.50 A; 1=650-858, 2=70-337, 3=342-571.
PDBsum; 1AL2; -.
PDBsum; 1AR6; -.
PDBsum; 1AR7; -.
PDBsum; 1AR8; -.
PDBsum; 1AR9; -.
PDBsum; 1ASJ; -.
PDBsum; 1DGI; -.
PDBsum; 1FPT; -.
PDBsum; 1HXS; -.
PDBsum; 1L1N; -.
PDBsum; 1NG7; -.
PDBsum; 1NN8; -.
PDBsum; 1PO1; -.
PDBsum; 1PO2; -.
PDBsum; 1POV; -.
PDBsum; 1RA6; -.
PDBsum; 1RA7; -.
PDBsum; 1RAJ; -.
PDBsum; 1RDR; -.
PDBsum; 1TQL; -.
PDBsum; 1VBD; -.
PDBsum; 1XYR; -.
PDBsum; 2BBL; -.
PDBsum; 2BBP; -.
PDBsum; 2IJD; -.
PDBsum; 2IJF; -.
PDBsum; 2ILY; -.
PDBsum; 2ILZ; -.
PDBsum; 2IM0; -.
PDBsum; 2IM1; -.
PDBsum; 2IM2; -.
PDBsum; 2IM3; -.
PDBsum; 2PLV; -.
PDBsum; 3EPC; -.
PDBsum; 3IYB; -.
PDBsum; 3IYC; -.
PDBsum; 3J3O; -.
PDBsum; 3J3P; -.
PDBsum; 3J48; -.
PDBsum; 3J8F; -.
PDBsum; 3J9F; -.
PDBsum; 3JBC; -.
PDBsum; 3JBD; -.
PDBsum; 3JBE; -.
PDBsum; 3JBF; -.
PDBsum; 3JBG; -.
PDBsum; 3OL7; -.
PDBsum; 4DCD; -.
PDBsum; 4K4S; -.
PDBsum; 4K4T; -.
PDBsum; 4K4U; -.
PDBsum; 4K4V; -.
PDBsum; 4K4W; -.
PDBsum; 4NLO; -.
PDBsum; 4NLP; -.
PDBsum; 4NLQ; -.
PDBsum; 4NLR; -.
PDBsum; 4NLS; -.
PDBsum; 4NLT; -.
PDBsum; 4NLU; -.
PDBsum; 4NLV; -.
PDBsum; 4NLW; -.
PDBsum; 4NLX; -.
PDBsum; 4NLY; -.
PDBsum; 4R0E; -.
PDBsum; 5KTZ; -.
PDBsum; 5KU0; -.
PDBsum; 5KU2; -.
PDBsum; 5KWL; -.
ProteinModelPortal; P03300; -.
SMR; P03300; -.
ELM; P03300; -.
BindingDB; P03300; -.
ChEMBL; CHEMBL5127; -.
DrugBank; DB08014; (METHYLPYRIDAZINE PIPERIDINE BUTYLOXYPHENYL)ETHYLACETATE.
DrugBank; DB08012; (METHYLPYRIDAZINE PIPERIDINE ETHYLOXYPHENYL)ETHYLACETATE.
DrugBank; DB08013; (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE.
DrugBank; DB04137; Guanosine-5'-Triphosphate.
DrugBank; DB08231; MYRISTIC ACID.
DrugBank; DB03963; S-(Dimethylarsenic)Cysteine.
DrugBank; DB03203; Sphingosine.
MEROPS; C03.001; -.
iPTMnet; P03300; -.
GeneID; 919920; -.
KEGG; vg:919920; -.
OrthoDB; VOG0900001E; -.
EvolutionaryTrace; P03300; -.
PMAP-CutDB; P03299; -.
Proteomes; UP000000356; Genome.
Proteomes; UP000149468; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle 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:0039618; C:T=pseudo3 icosahedral 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; IDA:CACAO.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IDA:UniProtKB.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
GO; GO:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IDA:UniProtKB.
GO; GO:0039540; P:suppression by virus of host RIG-I activity; IEA:UniProtKB-KW.
GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; 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; 4.10.80.10; -; 1.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014838; P3A.
InterPro; IPR036203; P3A_soluble_dom.
InterPro; IPR000081; Peptidase_C3.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR003138; Pico_P1A.
InterPro; IPR036988; Pico_P1A_sf.
InterPro; IPR002527; Pico_P2B.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF08727; P3A; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF02226; Pico_P1A; 1.
Pfam; PF00947; Pico_P2A; 1.
Pfam; PF01552; Pico_P2B; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 3.
Pfam; PF00910; RNA_helicase; 1.
ProDom; PD001306; Peptidase_C3; 1.
ProDom; PD649346; Pico_P2B; 1.
SUPFAM; SSF50494; SSF50494; 2.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF89043; SSF89043; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Capsid protein; Complete proteome; Covalent protein-RNA linkage;
Direct protein sequencing;
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 mRNA suppression by virus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host mRNA nuclear export by virus;
Inhibition of host RIG-I by virus;
Inhibition of host RLR pathway by virus; Ion channel; Ion transport;
Lipoprotein; Membrane; Myristate; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein;
Pore-mediated penetration of viral genome into host cell; Protease;
Reference proteome; Repeat; RNA-binding; RNA-directed RNA polymerase;
T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
Transport; Viral attachment to host cell; Viral immunoevasion;
Viral ion channel; Viral penetration into host cytoplasm;
Viral RNA replication; Virion; Virus endocytosis by host;
Virus entry into host cell.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 2209 Genome polyprotein.
/FTId=PRO_0000424686.
CHAIN 2 881 P1.
/FTId=PRO_0000424687.
CHAIN 2 341 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000424688.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000040080.
CHAIN 70 341 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000040081.
CHAIN 342 579 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000040082.
CHAIN 580 881 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000040083.
CHAIN 882 1456 P2.
/FTId=PRO_0000424689.
CHAIN 882 1030 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000040084.
CHAIN 1031 1127 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000040085.
CHAIN 1128 1456 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000040086.
CHAIN 1457 2209 P3.
/FTId=PRO_0000424690.
CHAIN 1457 1565 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000424691.
CHAIN 1457 1543 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000424692.
CHAIN 1544 1565 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000040088.
CHAIN 1566 2209 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000424693.
CHAIN 1566 1747 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000040089.
CHAIN 1748 2209 RNA-directed RNA polymerase.
/FTId=PRO_0000040090.
TOPO_DOM 2 1520 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1521 1536 {ECO:0000255}.
TOPO_DOM 1537 2209 Cytoplasmic. {ECO:0000255}.
DOMAIN 882 1031 Peptidase C3 1.
DOMAIN 1232 1388 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1566 1731 Peptidase C3 2.
DOMAIN 1975 2090 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1256 1263 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
REGION 580 600 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1457 1479 Disordered.
ACT_SITE 901 901 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 919 919 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 990 990 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 1605 1605 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1636 1636 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1712 1712 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 2076 2076 For RdRp activity.
{ECO:0000269|PubMed:2196557}.
SITE 25 25 Involved in the interaction with human
RTN3. {ECO:0000250}.
SITE 69 70 Cleavage; by autolysis. {ECO:0000255}.
SITE 341 342 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 881 882 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 1030 1031 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1127 1128 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1456 1457 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1543 1544 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1565 1566 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1748 1749 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1546 1546 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000269|PubMed:209034}.
MOD_RES 1546 1546 O-UMP-tyrosine; transient.
{ECO:0000269|PubMed:12502805,
ECO:0000269|PubMed:16840321}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000269|PubMed:10618374,
ECO:0000269|PubMed:1850017,
ECO:0000269|PubMed:1851815}.
MUTAGEN 2 2 G->A: 100% loss of myristoylation.
Impaired viral assembly.
{ECO:0000269|PubMed:1851815}.
MUTAGEN 3 3 A->D: 50% loss of myristoylation. Severe
reduction in specific infectivity.
{ECO:0000269|PubMed:1850017}.
MUTAGEN 3 3 A->G,L,V: No effect on myristoylation and
virus growth.
{ECO:0000269|PubMed:1850017}.
MUTAGEN 3 3 A->H: No effect on myristoylation. Severe
reduction in specific infectivity.
{ECO:0000269|PubMed:1850017}.
CONFLICT 242 264 RFCPVDYLLGNGTLLGNAFVFPH -> SSARWITSLEMARC
WGMPLCSA (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 287 287 I -> L (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 309 309 A -> V (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 420 422 DDP -> AAS (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 464 464 F -> S (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 515 515 T -> S (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 855 856 AV -> QL (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 972 972 A -> V (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 985 985 A -> E (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 1140 1141 NA -> QR (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 1619 1619 V -> A (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 1626 1627 AL -> VF (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 1635 1635 L -> F (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 1682 1682 G -> R (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 1722 1730 VIGMHVGGN -> SSGCMLVD (in Ref. 2;
CAA24446). {ECO:0000305}.
CONFLICT 1743 1743 Y -> L (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 1752 1752 Q -> P (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 1759 1760 EV -> DA (in Ref. 2; CAA24446).
{ECO:0000305}.
CONFLICT 1840 1840 T -> I (in Ref. 2; CAA24446).
{ECO:0000305}.
STRAND 3 7 {ECO:0000244|PDB:1HXS}.
STRAND 17 23 {ECO:0000244|PDB:1HXS}.
STRAND 26 29 {ECO:0000244|PDB:1HXS}.
STRAND 33 35 {ECO:0000244|PDB:1AL2}.
HELIX 36 38 {ECO:0000244|PDB:1HXS}.
HELIX 51 54 {ECO:0000244|PDB:1HXS}.
STRAND 57 59 {ECO:0000244|PDB:1HXS}.
HELIX 66 69 {ECO:0000244|PDB:1POV}.
HELIX 74 76 {ECO:0000244|PDB:1POV}.
STRAND 83 87 {ECO:0000244|PDB:1HXS}.
STRAND 90 96 {ECO:0000244|PDB:1HXS}.
STRAND 100 102 {ECO:0000244|PDB:1POV}.
HELIX 103 105 {ECO:0000244|PDB:1HXS}.
HELIX 113 115 {ECO:0000244|PDB:1HXS}.
HELIX 126 128 {ECO:0000244|PDB:1HXS}.
STRAND 138 141 {ECO:0000244|PDB:1HXS}.
STRAND 147 151 {ECO:0000244|PDB:1HXS}.
HELIX 153 155 {ECO:0000244|PDB:1HXS}.
HELIX 159 167 {ECO:0000244|PDB:1HXS}.
STRAND 168 180 {ECO:0000244|PDB:1HXS}.
STRAND 187 197 {ECO:0000244|PDB:1HXS}.
STRAND 206 210 {ECO:0000244|PDB:1HXS}.
HELIX 214 217 {ECO:0000244|PDB:1HXS}.
HELIX 220 222 {ECO:0000244|PDB:1HXS}.
STRAND 227 229 {ECO:0000244|PDB:1HXS}.
STRAND 236 238 {ECO:0000244|PDB:1HXS}.
HELIX 247 249 {ECO:0000244|PDB:1HXS}.
TURN 250 253 {ECO:0000244|PDB:1HXS}.
HELIX 256 261 {ECO:0000244|PDB:1HXS}.
STRAND 262 268 {ECO:0000244|PDB:1HXS}.
TURN 269 271 {ECO:0000244|PDB:1HXS}.
STRAND 273 279 {ECO:0000244|PDB:1HXS}.
STRAND 284 288 {ECO:0000244|PDB:1HXS}.
TURN 290 292 {ECO:0000244|PDB:1HXS}.
STRAND 296 308 {ECO:0000244|PDB:1HXS}.
STRAND 311 313 {ECO:0000244|PDB:1AR7}.
STRAND 315 332 {ECO:0000244|PDB:1HXS}.
TURN 349 352 {ECO:0000244|PDB:1HXS}.
STRAND 364 366 {ECO:0000244|PDB:1HXS}.
STRAND 380 383 {ECO:0000244|PDB:1HXS}.
HELIX 384 388 {ECO:0000244|PDB:1HXS}.
TURN 400 404 {ECO:0000244|PDB:1HXS}.
HELIX 406 409 {ECO:0000244|PDB:1HXS}.
STRAND 411 414 {ECO:0000244|PDB:1HXS}.
STRAND 423 428 {ECO:0000244|PDB:1HXS}.
TURN 430 432 {ECO:0000244|PDB:1HXS}.
TURN 434 438 {ECO:0000244|PDB:1HXS}.
HELIX 440 445 {ECO:0000244|PDB:1HXS}.
STRAND 448 453 {ECO:0000244|PDB:1HXS}.
STRAND 455 461 {ECO:0000244|PDB:1HXS}.
STRAND 470 476 {ECO:0000244|PDB:1HXS}.
STRAND 478 480 {ECO:0000244|PDB:1HXS}.
HELIX 486 489 {ECO:0000244|PDB:1HXS}.
STRAND 492 498 {ECO:0000244|PDB:1HXS}.
STRAND 500 502 {ECO:0000244|PDB:1HXS}.
STRAND 504 509 {ECO:0000244|PDB:1HXS}.
STRAND 514 521 {ECO:0000244|PDB:1HXS}.
HELIX 524 526 {ECO:0000244|PDB:1POV}.
STRAND 530 537 {ECO:0000244|PDB:1HXS}.
STRAND 547 557 {ECO:0000244|PDB:1HXS}.
STRAND 562 566 {ECO:0000244|PDB:1HXS}.
STRAND 570 572 {ECO:0000244|PDB:1POV}.
STRAND 586 589 {ECO:0000244|PDB:1HXS}.
STRAND 594 596 {ECO:0000244|PDB:2PLV}.
HELIX 626 628 {ECO:0000244|PDB:1HXS}.
HELIX 636 638 {ECO:0000244|PDB:1HXS}.
HELIX 652 654 {ECO:0000244|PDB:1HXS}.
HELIX 656 660 {ECO:0000244|PDB:1HXS}.
STRAND 664 673 {ECO:0000244|PDB:1HXS}.
STRAND 685 688 {ECO:0000244|PDB:1HXS}.
STRAND 693 695 {ECO:0000244|PDB:1HXS}.
HELIX 696 701 {ECO:0000244|PDB:1HXS}.
STRAND 704 721 {ECO:0000244|PDB:1HXS}.
STRAND 723 725 {ECO:0000244|PDB:1AR7}.
STRAND 733 739 {ECO:0000244|PDB:1HXS}.
HELIX 752 755 {ECO:0000244|PDB:1HXS}.
STRAND 757 759 {ECO:0000244|PDB:1HXS}.
STRAND 761 765 {ECO:0000244|PDB:1HXS}.
STRAND 771 775 {ECO:0000244|PDB:1HXS}.
STRAND 780 786 {ECO:0000244|PDB:1HXS}.
STRAND 790 793 {ECO:0000244|PDB:1POV}.
STRAND 796 799 {ECO:0000244|PDB:1POV}.
TURN 801 804 {ECO:0000244|PDB:1HXS}.
HELIX 812 814 {ECO:0000244|PDB:1HXS}.
STRAND 818 823 {ECO:0000244|PDB:1HXS}.
STRAND 832 850 {ECO:0000244|PDB:1HXS}.
STRAND 860 863 {ECO:0000244|PDB:1HXS}.
HELIX 1478 1484 {ECO:0000244|PDB:1NG7}.
HELIX 1487 1496 {ECO:0000244|PDB:1NG7}.
STRAND 1546 1550 {ECO:0000244|PDB:2BBL}.
STRAND 1556 1558 {ECO:0000244|PDB:2BBL}.
HELIX 1560 1564 {ECO:0000244|PDB:2BBL}.
HELIX 1567 1579 {ECO:0000244|PDB:4DCD}.
STRAND 1580 1585 {ECO:0000244|PDB:4DCD}.
STRAND 1588 1597 {ECO:0000244|PDB:4DCD}.
STRAND 1599 1603 {ECO:0000244|PDB:4DCD}.
HELIX 1604 1606 {ECO:0000244|PDB:4DCD}.
STRAND 1610 1614 {ECO:0000244|PDB:4DCD}.
STRAND 1617 1628 {ECO:0000244|PDB:4DCD}.
STRAND 1634 1645 {ECO:0000244|PDB:4DCD}.
HELIX 1652 1654 {ECO:0000244|PDB:4DCD}.
STRAND 1662 1669 {ECO:0000244|PDB:4DCD}.
STRAND 1671 1674 {ECO:0000244|PDB:4DCD}.
STRAND 1677 1692 {ECO:0000244|PDB:4DCD}.
STRAND 1695 1705 {ECO:0000244|PDB:4DCD}.
STRAND 1715 1718 {ECO:0000244|PDB:4DCD}.
STRAND 1721 1729 {ECO:0000244|PDB:4DCD}.
STRAND 1734 1738 {ECO:0000244|PDB:4DCD}.
HELIX 1741 1744 {ECO:0000244|PDB:4DCD}.
STRAND 1750 1756 {ECO:0000244|PDB:1RA6}.
TURN 1757 1761 {ECO:0000244|PDB:1RA6}.
TURN 1763 1766 {ECO:0000244|PDB:1RDR}.
HELIX 1770 1772 {ECO:0000244|PDB:1RDR}.
TURN 1777 1781 {ECO:0000244|PDB:1RA6}.
STRAND 1786 1788 {ECO:0000244|PDB:4K4S}.
STRAND 1792 1794 {ECO:0000244|PDB:4K4S}.
HELIX 1802 1807 {ECO:0000244|PDB:1RA6}.
HELIX 1820 1834 {ECO:0000244|PDB:1RA6}.
TURN 1835 1837 {ECO:0000244|PDB:1RA7}.
HELIX 1845 1850 {ECO:0000244|PDB:1RA6}.
STRAND 1860 1862 {ECO:0000244|PDB:4NLR}.
TURN 1866 1872 {ECO:0000244|PDB:1RA6}.
HELIX 1875 1878 {ECO:0000244|PDB:1RA6}.
TURN 1881 1884 {ECO:0000244|PDB:1RA6}.
HELIX 1887 1895 {ECO:0000244|PDB:1RA6}.
STRAND 1902 1906 {ECO:0000244|PDB:1RA6}.
STRAND 1910 1912 {ECO:0000244|PDB:4K4S}.
HELIX 1913 1917 {ECO:0000244|PDB:1RA6}.
STRAND 1923 1926 {ECO:0000244|PDB:1RA6}.
HELIX 1929 1948 {ECO:0000244|PDB:1RA6}.
TURN 1952 1955 {ECO:0000244|PDB:1RA6}.
HELIX 1962 1965 {ECO:0000244|PDB:1RA6}.
TURN 1966 1968 {ECO:0000244|PDB:1RA6}.
HELIX 1969 1972 {ECO:0000244|PDB:1RA6}.
STRAND 1975 1978 {ECO:0000244|PDB:1RA6}.
STRAND 1981 1984 {ECO:0000244|PDB:1RA6}.
HELIX 1985 1988 {ECO:0000244|PDB:1RA6}.
HELIX 1991 2003 {ECO:0000244|PDB:1RA6}.
TURN 2004 2006 {ECO:0000244|PDB:1RA6}.
HELIX 2007 2010 {ECO:0000244|PDB:1RA6}.
HELIX 2011 2017 {ECO:0000244|PDB:1RA6}.
STRAND 2018 2023 {ECO:0000244|PDB:1RA6}.
STRAND 2026 2032 {ECO:0000244|PDB:1RA6}.
STRAND 2036 2038 {ECO:0000244|PDB:4NLV}.
HELIX 2041 2060 {ECO:0000244|PDB:1RA6}.
STRAND 2061 2063 {ECO:0000244|PDB:4K4V}.
HELIX 2066 2068 {ECO:0000244|PDB:1RA6}.
STRAND 2070 2074 {ECO:0000244|PDB:1RA6}.
STRAND 2077 2084 {ECO:0000244|PDB:1RA6}.
HELIX 2088 2097 {ECO:0000244|PDB:1RA6}.
STRAND 2102 2104 {ECO:0000244|PDB:1RA6}.
TURN 2105 2107 {ECO:0000244|PDB:1RA6}.
TURN 2116 2118 {ECO:0000244|PDB:1RA6}.
STRAND 2124 2128 {ECO:0000244|PDB:1RA6}.
STRAND 2130 2132 {ECO:0000244|PDB:1TQL}.
STRAND 2135 2139 {ECO:0000244|PDB:1RA6}.
HELIX 2142 2149 {ECO:0000244|PDB:1RA6}.
STRAND 2151 2153 {ECO:0000244|PDB:1RA6}.
HELIX 2155 2157 {ECO:0000244|PDB:1RA6}.
HELIX 2158 2169 {ECO:0000244|PDB:1RA6}.
HELIX 2170 2172 {ECO:0000244|PDB:1RA6}.
HELIX 2174 2184 {ECO:0000244|PDB:1RA6}.
HELIX 2188 2191 {ECO:0000244|PDB:1RA6}.
HELIX 2198 2208 {ECO:0000244|PDB:1RA6}.
SEQUENCE 2209 AA; 246540 MW; DF1754F87F2E97D6 CRC64;
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFSQDP SKFTEPIKDV
LIKTAPMLNS PNIEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEY LRDSEANPVD
QPTEPDVAAC RFYTLDTVSW TKESRGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ
CNASKFHQGA LGVFAVPEMC LAGDSNTTTM HTSYQNANPG EKGGTFTGTF TPDNNQTSPA
RRFCPVDYLL GNGTLLGNAF VFPHQIINLR TNNCATLVLP YVNSLSIDSM VKHNNWGIAI
LPLAPLNFAS ESSPEIPITL TIAPMCCEFN GLRNITLPRL QGLPVMNTPG SNQYLTADNF
QSPCALPEFD VTPPIDIPGE VKNMMELAEI DTMIPFDLSA TKKNTMEMYR VRLSDKPHTD
DPILCLSLSP ASDPRLSHTM LGEILNYYTH WAGSLKFTFL FCGFMMATGK LLVSYAPPGA
DPPKKRKEAM LGTHVIWDIG LQSSCTMVVP WISNTTYRQT IDDSFTEGGY ISVFYQTRIV
VPLSTPREMD ILGFVSACND FSVRLLRDTT HIEQKALAQG LGQMLESMID NTVRETVGAA
TSRDALPNTE ASGPTHSKEI PALTAVETGA TNPLVPSDTV QTRHVVQHRS RSESSIESFF
ARGACVTIMT VDNPASTTNK DKLFAVWKIT YKDTVQLRRK LEFFTYSRFD MELTFVVTAN
FTETNNGHAL NQVYQIMYVP PGAPVPEKWD DYTWQTSSNP SIFYTYGTAP ARISVPYVGI
SNAYSHFYDG FSKVPLKDQS AALGDSLYGA ASLNDFGILA VRVVNDHNPT KVTSKIRVYL
KPKHIRVWCP RPPRAVAYYG PGVDYKDGTL TPLSTKDLTT YGFGHQNKAV YTAGYKICNY
HLATQDDLQN AVNVMWSRDL LVTESRAQGT DSIARCNCNA GVYYCESRRK YYPVSFVGPT
FQYMEANNYY PARYQSHMLI GHGFASPGDC GGILRCHHGV IGIITAGGEG LVAFSDIRDL
YAYEEEAMEQ GITNYIESLG AAFGSGFTQQ ISDKITELTN MVTSTITEKL LKNLIKIISS
LVIITRNYED TTTVLATLAL LGCDASPWQW LRKKACDVLE IPYVIKQGDS WLKKFTEACN
AAKGLEWVSN KISKFIDWLK EKIIPQARDK LEFVTKLRQL EMLENQISTI HQSCPSQEHQ
EILFNNVRWL SIQSKRFAPL YAVEAKRIQK LEHTINNYIQ FKSKHRIEPV CLLVHGSPGT
GKSVATNLIA RAIAERENTS TYSLPPDPSH FDGYKQQGVV IMDDLNQNPD GADMKLFCQM
VSTVEFIPPM ASLEEKGILF TSNYVLASTN SSRISPPTVA HSDALARRFA FDMDIQVMNE
YSRDGKLNMA MATEMCKNCH QPANFKRCCP LVCGKAIQLM DKSSRVRYSI DQITTMIINE
RNRRSNIGNC MEALFQGPLQ YKDLKIDIKT SPPPECINDL LQAVDSQEVR DYCEKKGWIV
NITSQVQTER NINRAMTILQ AVTTFAAVAG VVYVMYKLFA GHQGAYTGLP NKKPNVPTIR
TAKVQGPGFD YAVAMAKRNI VTATTSKGEF TMLGVHDNVA ILPTHASPGE SIVIDGKEVE
ILDAKALEDQ AGTNLEITII TLKRNEKFRD IRPHIPTQIT ETNDGVLIVN TSKYPNMYVP
VGAVTEQGYL NLGGRQTART LMYNFPTRAG QCGGVITCTG KVIGMHVGGN GSHGFAAALK
RSYFTQSQGE IQWMRPSKEV GYPIINAPSK TKLEPSAFHY VFEGVKEPAV LTKNDPRLKT
DFEEAIFSKY VGNKITEVDE YMKEAVDHYA GQLMSLDINT EQMCLEDAMY GTDGLEALDL
STSAGYPYVA MGKKKRDILN KQTRDTKEMQ KLLDTYGINL PLVTYVKDEL RSKTKVEQGK
SRLIEASSLN DSVAMRMAFG NLYAAFHKNP GVITGSAVGC DPDLFWSKIP VLMEEKLFAF
DYTGYDASLS PAWFEALKMV LEKIGFGDRV DYIDYLNHSH HLYKNKTYCV KGGMPSGCSG
TSIFNSMINN LIIRTLLLKT YKGIDLDHLK MIAYGDDVIA SYPHEVDASL LAQSGKDYGL
TMTPADKSAT FETVTWENVT FLKRFFRADE KYPFLIHPVM PMKEIHESIR WTKDPRNTQD
HVRSLCLLAW HNGEEEYNKF LAKIRSVPIG RALLLPEYST LYRRWLDSF


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