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 POLG_CXB3N              Reviewed;        2185 AA.
P03313; Q66322; Q66323; Q66324; Q66325; Q66326; Q66327; Q66328;
Q83744;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 179.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=P3;
Contains:
RecName: Full=Protein 3AB;
Contains:
RecName: Full=P2;
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=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=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;
Coxsackievirus B3 (strain Nancy).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Enterovirus B.
NCBI_TaxID=103903;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2157045;
Klump W.M., Bergmann I., Mueller B.C., Ameis D., Kandolf R.;
"Complete nucleotide sequence of infectious Coxsackievirus B3 cDNA:
two initial 5' uridine residues are regained during plus-strand RNA
synthesis.";
J. Virol. 64:1573-1583(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3027968; DOI=10.1016/0042-6822(87)90435-1;
Lindberg A.M., Staalhandske P.O.K., Pettersson U.;
"Genome of coxsackievirus B3.";
Virology 156:50-63(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1724-2185.
PubMed=6088796;
Staalhandske P.O.K., Lindberg A.M., Pettersson U.;
"Replicase gene of coxsackievirus B3.";
J. Virol. 51:742-746(1984).
[4]
INTERACTION WITH HOST CD55.
PubMed=7538177;
Shafren D.R., Bates R.C., Agrez M.V., Herd R.L., Burns G.F.,
Barry R.D.;
"Coxsackieviruses B1, B3, and B5 use decay accelerating factor as a
receptor for cell attachment.";
J. Virol. 69:3873-3877(1995).
[5]
INTERACTION WITH HOST CXADR.
PubMed=10814575; DOI=10.1006/viro.2000.0324;
Martino T.A., Petric M., Weingartl H., Bergelson J.M., Opavsky M.A.,
Richardson C.D., Modlin J.F., Finberg R.W., Kain K.C., Willis N.,
Gauntt C.J., Liu P.P.;
"The coxsackie-adenovirus receptor (CAR) is used by reference strains
and clinical isolates representing all six serotypes of coxsackievirus
group B and by swine vesicular disease virus.";
Virology 271:99-108(2000).
[6]
INDUCTION.
PubMed=12384597; DOI=10.1093/nar/gkf583;
Ray P.S., Das S.;
"La autoantigen is required for the internal ribosome entry site-
mediated translation of Coxsackievirus B3 RNA.";
Nucleic Acids Res. 30:4500-4508(2002).
[7]
FUNCTION OF PROTEIN 3A.
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).
[8]
COFACTOR.
PubMed=23667424; DOI=10.1371/journal.pone.0060272;
Gong P., Kortus M.G., Nix J.C., Davis R.E., Peersen O.B.;
"Structures of coxsackievirus, rhinovirus, and poliovirus polymerase
elongation complexes solved by engineering RNA mediated crystal
contacts.";
PLoS ONE 8:E60272-E60272(2013).
[9]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1541-1723.
PubMed=17037602; DOI=10.1007/978-0-387-33012-9_106;
Hilgenfeld R., Anand K., Mesters J.R., Rao Z., Shen X., Jiang H.,
Tan J., Verschueren K.H.;
"Structure and dynamics of SARS coronavirus main proteinase (Mpro).";
Adv. Exp. Med. Biol. 581:585-591(2006).
[10]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1724-2185 IN COMPLEX WITH
VPG; GTP AND DUTP, INTERACTION OF RNA-DIRECTED RNA POLYMERASE WITH
VPG, COFACTOR, AND FUNCTION (RNA-DIRECTED RNA POLYMERASE).
PubMed=18632861; DOI=10.1128/JVI.00631-08;
Gruez A., Selisko B., Roberts M., Bricogne G., Bussetta C., Jabafi I.,
Coutard B., De Palma A.M., Neyts J., Canard B.;
"The crystal structure of coxsackievirus B3 RNA-dependent RNA
polymerase in complex with its protein primer VPg confirms the
existence of a second VPg binding site on Picornaviridae
polymerases.";
J. Virol. 82:9577-9590(2008).
[11]
X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 1541-1723.
PubMed=19144641; DOI=10.1074/jbc.M807947200;
Lee C.C., Kuo C.J., Ko T.P., Hsu M.F., Tsui Y.C., Chang S.C., Yang S.,
Chen S.J., Chen H.C., Hsu M.C., Shih S.R., Liang P.H., Wang A.H.;
"Structural basis of inhibition specificities of 3C and 3C-like
proteases by zinc-coordinating and peptidomimetic compounds.";
J. Biol. Chem. 284:7646-7655(2009).
[12]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1724-2185.
PubMed=25320316; DOI=10.1128/JVI.01574-14;
Campagnola G., McDonald S., Beaucourt S., Vignuzzi M., Peersen O.B.;
"Structure-function relationships underlying the replication fidelity
of viral RNA-dependent RNA polymerases.";
J. Virol. 89:275-286(2015).
[13]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1724-2185.
PubMed=25799064; DOI=10.1371/journal.ppat.1004733;
van der Linden L., Vives-Adrian L., Selisko B., Ferrer-Orta C.,
Liu X., Lanke K., Ulferts R., De Palma A.M., Tanchis F., Goris N.,
Lefebvre D., De Clercq K., Leyssen P., Lacroix C., Purstinger G.,
Coutard B., Canard B., Boehr D.D., Arnold J.J., Cameron C.E.,
Verdaguer N., Neyts J., van Kuppeveld F.J.;
"The RNA template channel of the RNA-dependent RNA polymerase as a
target for development of antiviral therapy of multiple genera within
a virus family.";
PLoS Pathog. 11:E1004733-E1004733(2015).
-!- 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 CD55 and CXADR to provide virion
attachment to target host cells. This attachment induces virion
internalization. Tyrosine kinases are probably involved in the
entry process. 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 (By
similarity). {ECO:0000250}.
-!- 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 (By
similarity). {ECO:0000250}.
-!- 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 (By
similarity). {ECO:0000250}.
-!- 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 (By
similarity). {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- FUNCTION: Protein 2C: Induces and associates with structural
rearrangements of intracellular membranes. 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 (By similarity). {ECO:0000250}.
-!- 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
(By similarity). {ECO:0000250}.
-!- 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 (By
similarity). {ECO:0000250}.
-!- FUNCTION: Viral protein genome-linked: Acts as a primer for viral
RNA replication and remains covalently bound to viral genomic RNA
(PubMed:18632861). 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 (PubMed:18632861). 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 (By similarity).
{ECO:0000250, ECO:0000269|PubMed:18632861}.
-!- 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 (By similarity). {ECO:0000250}.
-!- FUNCTION: Protease 3C: cleaves host DDX58/RIG-I and thus
contributes to the inhibition of type I interferon production.
Cleaves also host PABPC1 (By similarity). {ECO:0000250}.
-!- 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 (By similarity). {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 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.
-!- COFACTOR: RNA-directed RNA polymerase:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:18632861,
ECO:0000269|PubMed:23667424};
Note=Requires the presence of 3CDpro or 3CPro.
{ECO:0000269|PubMed:18632861};
-!- 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 capsid protein VP4
in the mature capsid (By similarity). Interacts with host CD55 and
CXADR. 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 (By
similarity). 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 (By similarity). Capsid protein VP4:
Interacts with capsid protein VP1 and capsid protein VP3 (By
similarity). Protein 2C: interacts with capsid protein VP3; this
interaction may be important for virion morphogenesis (By
similarity). Protein 3AB: interacts with protein 3CD (By
similarity). Viral protein genome-linked: interacts with RNA-
directed RNA polymerase (By similarity). Protein 3CD: interacts
with protein 3AB and with RNA-directed RNA polymerase. RNA-
directed RNA polymerase: interacts with viral protein genome-
linked (PubMed:18632861). RNA-directed RNA polymerase: interacts
with protein 3CD (By similarity). {ECO:0000250,
ECO:0000269|PubMed:18632861}.
-!- SUBCELLULAR LOCATION: Capsid protein VP0: Virion {ECO:0000250}.
Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP4: Virion {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion {ECO:0000250}.
Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP3: Virion {ECO:0000250}.
Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP1: Virion {ECO:0000250}.
Host cytoplasm {ECO:0000250}.
-!- 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
{ECO:0000250}. Host cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protease 3C: Host cytoplasm {ECO:0000250}.
-!- 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.
-!- INDUCTION: Translated cap independently from an internal ribosome
entry site (IRES). {ECO:0000269|PubMed:12384597}.
-!- 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
(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}.
-!- PTM: Myristoylation of VP4 is required during RNA encapsidation
and formation of the mature virus particle. {ECO:0000250}.
-!- 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. {ECO:0000250}.
-!- 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 (By similarity).
{ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000305}.
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EMBL; M33854; AAA42931.1; -; Genomic_RNA.
EMBL; K02709; AAA42932.1; -; Genomic_RNA.
EMBL; M16572; AAA74400.1; -; Genomic_RNA.
PIR; A26354; GNNYB3.
PIR; A34664; GNNYBT.
PDB; 2VB0; X-ray; 2.40 A; A=1541-1723.
PDB; 2ZTX; X-ray; 1.72 A; A=1541-1723.
PDB; 2ZTY; X-ray; 1.72 A; A=1541-1723.
PDB; 2ZTZ; X-ray; 2.00 A; A/B=1541-1723.
PDB; 2ZU1; X-ray; 1.38 A; A/B=1541-1723.
PDB; 2ZU3; X-ray; 1.75 A; A=1541-1723.
PDB; 3CDU; X-ray; 2.10 A; A=1724-2185.
PDB; 3CDW; X-ray; 2.50 A; A=1724-2185, H=1519-1540.
PDB; 4WFX; X-ray; 1.81 A; A=1724-2185.
PDB; 4WFY; X-ray; 2.06 A; A=1724-2185.
PDB; 4WFZ; X-ray; 1.80 A; A=1724-2185.
PDB; 4Y2A; X-ray; 2.90 A; A=1724-2185.
PDBsum; 2VB0; -.
PDBsum; 2ZTX; -.
PDBsum; 2ZTY; -.
PDBsum; 2ZTZ; -.
PDBsum; 2ZU1; -.
PDBsum; 2ZU3; -.
PDBsum; 3CDU; -.
PDBsum; 3CDW; -.
PDBsum; 4WFX; -.
PDBsum; 4WFY; -.
PDBsum; 4WFZ; -.
PDBsum; 4Y2A; -.
ProteinModelPortal; P03313; -.
SMR; P03313; -.
BindingDB; P03313; -.
ChEMBL; CHEMBL2396505; -.
MEROPS; C03.011; -.
OrthoDB; VOG0900001E; -.
EvolutionaryTrace; P03313; -.
Proteomes; UP000007760; Genome.
Proteomes; UP000181225; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IDA:CACAO.
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:0046872; F:metal ion binding; 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
GO; GO:0039656; P:modulation by virus of host gene expression; IDA:BHF-UCL.
GO; GO:0061765; P:modulation by virus of host NIK/NF-kappaB signaling; IDA:BHF-UCL.
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:0044832; P:positive regulation by virus of host cytokine production; IDA:BHF-UCL.
GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
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:0039522; P:suppression by virus of host mRNA export from nucleus; ISS: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; ISS: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; IPR003593; AAA+_ATPase.
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.
SMART; SM00382; AAA; 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;
DNA replication; 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; Magnesium; Membrane; Metal-binding; Myristate;
Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Pore-mediated penetration of viral genome into host cell; Protease;
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 2185 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426266.
CHAIN 2 848 P1. {ECO:0000250}.
/FTId=PRO_0000426267.
CHAIN 2 332 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426268.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426269.
CHAIN 70 332 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426270.
CHAIN 333 568 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426271.
CHAIN 568 851 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426272.
CHAIN 852 1429 P2. {ECO:0000250}.
/FTId=PRO_0000426273.
CHAIN 852 1001 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000426274.
CHAIN 1002 1100 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000039587.
CHAIN 1101 1429 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000039588.
CHAIN 1430 2185 P3. {ECO:0000250}.
/FTId=PRO_0000426275.
CHAIN 1430 1540 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426276.
CHAIN 1430 1518 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000039589.
CHAIN 1519 1540 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426277.
CHAIN 1541 2185 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426278.
CHAIN 1541 1722 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426279.
CHAIN 1723 2185 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426280.
TOPO_DOM 2 1495 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1496 1511 {ECO:0000255}.
TOPO_DOM 1512 2185 Cytoplasmic. {ECO:0000255}.
DOMAIN 1205 1361 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1541 1706 Peptidase C3.
DOMAIN 1950 2066 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
REGION 568 584 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1430 1453 Disordered. {ECO:0000250}.
ACT_SITE 872 872 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 890 890 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 961 961 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 1580 1580 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1611 1611 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1687 1687 For Protease 3C activity. {ECO:0000250}.
ACT_SITE 2052 2052 For RdRp activity. {ECO:0000250}.
METAL 1956 1956 Magnesium. {ECO:0000305|PubMed:23667424}.
METAL 2053 2053 Magnesium. {ECO:0000305|PubMed:23667424}.
SITE 69 70 Cleavage; by autolysis. {ECO:0000255}.
SITE 332 333 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 851 852 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 1001 1002 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1429 1430 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1518 1519 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1540 1541 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1723 1724 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1521 1521 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
CONFLICT 16 16 R -> G (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 177 177 V -> D (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 469 469 P -> L (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 487 487 I -> V (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 510 510 F -> Y (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 516 516 Y -> C (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 566 566 Q -> E (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 593 593 T -> N (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 650 650 K -> E (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 854 865 FGQQSGAVYVGN -> IWTTIRGSVCGD (in Ref. 2;
AAA74400). {ECO:0000305}.
CONFLICT 873 873 L -> S (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 1097 1097 A -> P (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 1280 1280 Q -> H (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 1437 1437 I -> F (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 1503 1503 V -> M (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 1616 1616 K -> E (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 1624 1624 R -> G (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 1627 1627 R -> G (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 1630 1630 L -> V (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 1718 1718 Y -> N (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 1734 1734 D -> V (in Ref. 2; AAA74400).
{ECO:0000305}.
CONFLICT 1758 1758 E -> V (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 1824 1824 V -> R (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 1867 1867 C -> R (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 1880 1880 Y -> H (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 2001 2001 D -> N (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 2095 2095 A -> V (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 2115 2115 V -> A (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 2175 2175 S -> T (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 2178 2178 R -> G (in Ref. 2 and 3). {ECO:0000305}.
TURN 1528 1530 {ECO:0000244|PDB:3CDW}.
HELIX 1542 1554 {ECO:0000244|PDB:2ZU1}.
STRAND 1555 1560 {ECO:0000244|PDB:2ZU1}.
STRAND 1563 1572 {ECO:0000244|PDB:2ZU1}.
STRAND 1574 1578 {ECO:0000244|PDB:2ZU1}.
HELIX 1579 1581 {ECO:0000244|PDB:2ZU1}.
STRAND 1585 1589 {ECO:0000244|PDB:2ZU1}.
STRAND 1592 1603 {ECO:0000244|PDB:2ZU1}.
STRAND 1609 1617 {ECO:0000244|PDB:2ZU1}.
HELIX 1627 1629 {ECO:0000244|PDB:2ZU1}.
STRAND 1637 1644 {ECO:0000244|PDB:2ZU1}.
STRAND 1646 1649 {ECO:0000244|PDB:2ZU1}.
STRAND 1652 1667 {ECO:0000244|PDB:2ZU1}.
STRAND 1670 1680 {ECO:0000244|PDB:2ZU1}.
STRAND 1690 1693 {ECO:0000244|PDB:2ZU1}.
STRAND 1696 1705 {ECO:0000244|PDB:2ZU1}.
STRAND 1708 1713 {ECO:0000244|PDB:2ZU1}.
HELIX 1716 1719 {ECO:0000244|PDB:2ZU1}.
STRAND 1725 1731 {ECO:0000244|PDB:4WFZ}.
HELIX 1732 1735 {ECO:0000244|PDB:4WFZ}.
TURN 1752 1756 {ECO:0000244|PDB:4WFZ}.
STRAND 1761 1763 {ECO:0000244|PDB:4Y2A}.
HELIX 1777 1782 {ECO:0000244|PDB:4WFZ}.
HELIX 1795 1809 {ECO:0000244|PDB:4WFZ}.
TURN 1810 1812 {ECO:0000244|PDB:4WFZ}.
HELIX 1820 1825 {ECO:0000244|PDB:4WFZ}.
STRAND 1835 1837 {ECO:0000244|PDB:4WFZ}.
HELIX 1843 1845 {ECO:0000244|PDB:4WFZ}.
HELIX 1850 1853 {ECO:0000244|PDB:4WFZ}.
TURN 1856 1859 {ECO:0000244|PDB:4WFZ}.
HELIX 1862 1871 {ECO:0000244|PDB:4WFZ}.
STRAND 1877 1881 {ECO:0000244|PDB:4WFZ}.
STRAND 1885 1887 {ECO:0000244|PDB:4Y2A}.
HELIX 1888 1892 {ECO:0000244|PDB:4WFZ}.
STRAND 1898 1901 {ECO:0000244|PDB:4WFZ}.
HELIX 1904 1923 {ECO:0000244|PDB:4WFZ}.
TURN 1927 1930 {ECO:0000244|PDB:4WFZ}.
HELIX 1937 1947 {ECO:0000244|PDB:4WFZ}.
STRAND 1950 1953 {ECO:0000244|PDB:4WFZ}.
STRAND 1955 1959 {ECO:0000244|PDB:4WFZ}.
HELIX 1960 1963 {ECO:0000244|PDB:4WFZ}.
HELIX 1966 1978 {ECO:0000244|PDB:4WFZ}.
TURN 1983 1986 {ECO:0000244|PDB:4WFZ}.
HELIX 1987 1993 {ECO:0000244|PDB:4WFZ}.
STRAND 1994 1999 {ECO:0000244|PDB:4WFZ}.
STRAND 2002 2008 {ECO:0000244|PDB:4WFZ}.
HELIX 2017 2036 {ECO:0000244|PDB:4WFZ}.
HELIX 2042 2044 {ECO:0000244|PDB:4WFZ}.
STRAND 2046 2050 {ECO:0000244|PDB:4WFZ}.
STRAND 2053 2060 {ECO:0000244|PDB:4WFZ}.
HELIX 2064 2073 {ECO:0000244|PDB:4WFZ}.
STRAND 2078 2080 {ECO:0000244|PDB:4WFZ}.
STRAND 2083 2085 {ECO:0000244|PDB:4WFZ}.
TURN 2092 2094 {ECO:0000244|PDB:4WFZ}.
STRAND 2100 2104 {ECO:0000244|PDB:4WFZ}.
STRAND 2106 2108 {ECO:0000244|PDB:4WFZ}.
STRAND 2111 2115 {ECO:0000244|PDB:4WFZ}.
HELIX 2118 2125 {ECO:0000244|PDB:4WFZ}.
STRAND 2127 2129 {ECO:0000244|PDB:4WFZ}.
HELIX 2131 2133 {ECO:0000244|PDB:4WFZ}.
HELIX 2134 2145 {ECO:0000244|PDB:4WFZ}.
HELIX 2146 2148 {ECO:0000244|PDB:4WFZ}.
HELIX 2150 2160 {ECO:0000244|PDB:4WFZ}.
HELIX 2164 2168 {ECO:0000244|PDB:4WFZ}.
HELIX 2174 2184 {ECO:0000244|PDB:4WFZ}.
SEQUENCE 2185 AA; 243453 MW; 1B5ECE3DA47338FF CRC64;
MGAQVSTQKT GAHETRLNAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP GKFTEPVKDI
MIKSLPALNS PTVEECGYSD RARSITLGNS TITTQECANV VVGYGVWPDY LKDSEATAED
QPTQPDVATC RFYTLDSVQW QKTSPGWWWK LPDALSNLGL FGQNMQYHYL GRTGYTVHVQ
CNASKFHQGC LLVVCVPEAE MGCATLDNTP SSAELLGGDT AKEFADKPVA SGSNKLVQRV
VYNAGMGVGV GNLTIFPHQW INLRTNNSAT IVMPYTNSVP MDNMFRHNNV TLMVIPFVPL
DYCPGSTTYV PITVTIAPMC AEYNGLRLAG HQGLPTMNTP GSCQFLTSDD FQSPSAMPQY
DVTPEMRIPG EVKNLMEIAE VDSVVPVQNV GEKVNSMEAY QIPVRSNEGS GTQVFGFPLQ
PGYSSVFSRT LLGEILNYYT HWSGSIKLTF MFCGSAMATG KFLLAYSPPG AGAPTKRVDA
MLGTHVIWDV GLQSSCVLCI PWISQTHYRF VASDEYTAGG FITCWYQTNI VVPADAQSSC
YIMCFVSACN DFSVRLLKDT PFISQQNFFQ GPVEDAITAA IGRVADTVGT GPTNSEAIPA
LTAAETGHTS QVVPGDTMQT RHVKNYHSRS ESTIENFLCR SACVYFTEYK NSGAKRYAEW
VLTPRQAAQL RRKLEFFTYV RFDLELTFVI TSTQQPSTTQ NQDAQILTHQ IMYVPPGGPV
PDKVDSYVWQ TSTNPSVFWT EGNAPPRMSI PFLSIGNAYS NFYDGWSEFS RNGVYGINTL
NNMGTLYARH VNAGSTGPIK STIRIYFKPK HVKAWIPRPP RLCQYEKAKN VNFQPSGVTT
TRQSITTMTN TGAFGQQSGA VYVGNYRVVN RHLATSADWQ NCVWESYNRD LLVSTTTAHG
CDIIARCQCT TGVYFCASKN KHYPISFEGP GLVEVQESEY YPRRYQSHVL LAAGFSEPGD
CGGILRCEHG VIGIVTMGGE GVVGFADIRD LLWLEDDAME QGVKDYVEQL GNAFGSGFTN
QICEQVNLLK ESLVGQDSIL EKSLKALVKI ISALVIVVRN HDDLITVTAT LALIGCTSSP
WRWLKQKVSQ YYGIPMAERQ NNSWLKKFTE MTNACKGMEW IAVKIQKFIE WLKVKILPEV
REKHEFLNRL KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYAAEAKR
VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL NSSVYSLPPD
PDHFDGYKQQ AVVIMDDLCQ NPDGKDVSLF CQMVSSVDFV PPMAALEEKG ILFTSPFVLA
STNAGSINAP TVSDSRALAR RFHFDMNIEV ISMYSQNGKI NMPMSVKTCD DECCPVNFKK
CCPLVCGKAI QFIDRRTQVR YSLDMLVTEM FREYNHRHSV GTTLEALFQG PPVYREIKIS
VAPETPPPPA IADLLKSVDS EAVREYCKEK GWLVPEINST LQIEKHVSRA FICLQALTTF
VSVAGIIYII YKLFAGFQGA YTGVPNQKPR VPTLRQAKVQ GPAFEFAVAM MKRNSSTVKT
EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVLDAK ELVDKDGTNL ELTLLKLNRN
EKFRDIRGFL AKEEVEVNEA VLAINTSKFP NMYIPVGQVT EYGFLNLGGT PTKRMLMYNF
PTRAGQCGGV LMSTGKVLGI HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKDAGFPVI
NTPSKTKLEP SVFHQVFEGN KEPAVLRSGD PRLKANFEEA IFSKYIGNVN THVDEYMLEA
VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK RDILSKKTKD
LTKLKECMDK YGLNLPMVTY VKDELRSIEK VAKGKSRLIE ASSLNDSVAM RQTFGNLYKT
FHLNPGVVTG SAVGCDPDLF WSKIPVMLDG HLIAFDYSGY DASLSPVWFA CLKMLLEKLG
YTHKETNYID YLCNSHHLYR DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI
DLDQFRMIAY GDDVIASYPW PIDASLLAEA GKGYGLIMTP ADKGECFNEV TWTNATFLKR
YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE HEYEEFIRKI
RSVPVGRCLT LPAFSTLRRK WLDSF


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