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 POLG_CXB3W              Reviewed;        2185 AA.
Q66282;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-MAY-2017, entry version 151.
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 Woodruff).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Enterovirus B.
NCBI_TaxID=103904;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Knowlton K.U., Jeon E.S., Berkley R.W., Wessely R., Huber S.;
"A mutation in the puff region of VP2 attenuates the myocarditic
phenotype of an infectious cDNA of the Woodruff virus.";
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[2]
STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) OF 70-851, AND
MYRISTOYLATION AT GLY-2.
PubMed=8591043; DOI=10.1016/S0969-2126(01)00201-5;
Muckelbauer J.K., Kremer M., Minor I., Diana G., Dutko F.J.,
Groarke J., Pevear D.C., Rossmann M.G.;
"The structure of coxsackievirus B3 at 3.5 A resolution.";
Structure 3:653-667(1995).
-!- 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 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.
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
(By similarity). {ECO:0000250}.
-!- 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:0000250|UniProtKB:P03313};
Note=Requires the presence of 3CDpro or 3CPro.
{ECO:0000250|UniProtKB:P03313};
-!- 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). 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 and with protein 3CD (By similarity). {ECO:0000250}.
-!- 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:0000305}.
-!- 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}.
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1jew";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1cov";
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EMBL; U57056; AAB02228.1; -; Genomic_RNA.
PDB; 1COV; X-ray; 3.50 A; 1=571-851, 2=70-332, 3=333-570, 4=2-69.
PDB; 1JEW; EM; 22.00 A; 1=571-851, 2=70-332, 3=333-570, 4=2-69.
PDB; 3JD7; EM; 3.90 A; 1=571-851, 2=70-332, 3=333-570, 4=2-69.
PDBsum; 1COV; -.
PDBsum; 1JEW; -.
PDBsum; 3JD7; -.
ProteinModelPortal; Q66282; -.
SMR; Q66282; -.
IntAct; Q66282; 1.
DrugBank; DB08231; MYRISTIC ACID.
OrthoDB; VOG090000BA; -.
EvolutionaryTrace; Q66282; -.
Proteomes; UP000007530; 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: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; 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; 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:0039544; P:suppression by virus of host RIG-I activity by RIG-I proteolysis; ISS:UniProtKB.
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; IPR000081; Peptidase_C3.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR003138; Pico_P1A.
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.
CHAIN 2 2185 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426281.
CHAIN 2 848 P1. {ECO:0000250}.
/FTId=PRO_0000426282.
CHAIN 2 332 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426283.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426284.
CHAIN 70 332 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426285.
CHAIN 333 568 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426286.
CHAIN 568 851 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426287.
CHAIN 852 1429 P2. {ECO:0000250}.
/FTId=PRO_0000426288.
CHAIN 852 1001 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000426289.
CHAIN 1002 1100 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000039598.
CHAIN 1101 1429 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000039599.
CHAIN 1430 2185 P3. {ECO:0000250}.
/FTId=PRO_0000426290.
CHAIN 1430 1540 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426291.
CHAIN 1430 1518 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000039600.
CHAIN 1519 1540 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426292.
CHAIN 1541 2185 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426293.
CHAIN 1541 1722 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426294.
CHAIN 1723 2185 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426295.
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:0000250|UniProtKB:P03313}.
METAL 2053 2053 Magnesium.
{ECO:0000250|UniProtKB:P03313}.
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:0000269|PubMed:8591043}.
STRAND 4 7 {ECO:0000244|PDB:1COV}.
STRAND 26 29 {ECO:0000244|PDB:1COV}.
HELIX 36 38 {ECO:0000244|PDB:1COV}.
HELIX 50 52 {ECO:0000244|PDB:1COV}.
STRAND 57 59 {ECO:0000244|PDB:1COV}.
STRAND 83 87 {ECO:0000244|PDB:1COV}.
STRAND 90 96 {ECO:0000244|PDB:1COV}.
TURN 113 115 {ECO:0000244|PDB:1COV}.
HELIX 126 128 {ECO:0000244|PDB:1COV}.
STRAND 133 140 {ECO:0000244|PDB:1COV}.
STRAND 147 151 {ECO:0000244|PDB:1COV}.
TURN 152 154 {ECO:0000244|PDB:1COV}.
HELIX 159 167 {ECO:0000244|PDB:1COV}.
STRAND 168 180 {ECO:0000244|PDB:1COV}.
STRAND 188 197 {ECO:0000244|PDB:1COV}.
STRAND 203 205 {ECO:0000244|PDB:1COV}.
HELIX 212 215 {ECO:0000244|PDB:1COV}.
STRAND 218 220 {ECO:0000244|PDB:1COV}.
STRAND 225 227 {ECO:0000244|PDB:1COV}.
HELIX 241 243 {ECO:0000244|PDB:1COV}.
TURN 244 247 {ECO:0000244|PDB:1COV}.
HELIX 250 255 {ECO:0000244|PDB:1COV}.
STRAND 256 262 {ECO:0000244|PDB:1COV}.
TURN 263 265 {ECO:0000244|PDB:1COV}.
STRAND 267 273 {ECO:0000244|PDB:1COV}.
STRAND 278 280 {ECO:0000244|PDB:1COV}.
TURN 284 286 {ECO:0000244|PDB:1COV}.
STRAND 290 301 {ECO:0000244|PDB:1COV}.
STRAND 310 326 {ECO:0000244|PDB:1COV}.
TURN 340 343 {ECO:0000244|PDB:1COV}.
STRAND 355 357 {ECO:0000244|PDB:1COV}.
STRAND 369 374 {ECO:0000244|PDB:1COV}.
HELIX 376 379 {ECO:0000244|PDB:1COV}.
HELIX 391 395 {ECO:0000244|PDB:1COV}.
HELIX 397 400 {ECO:0000244|PDB:1COV}.
STRAND 402 405 {ECO:0000244|PDB:1COV}.
STRAND 408 410 {ECO:0000244|PDB:1COV}.
STRAND 413 419 {ECO:0000244|PDB:1COV}.
TURN 421 423 {ECO:0000244|PDB:1COV}.
TURN 425 429 {ECO:0000244|PDB:1COV}.
HELIX 431 436 {ECO:0000244|PDB:1COV}.
STRAND 439 443 {ECO:0000244|PDB:1COV}.
STRAND 446 452 {ECO:0000244|PDB:1COV}.
STRAND 461 467 {ECO:0000244|PDB:1COV}.
STRAND 469 471 {ECO:0000244|PDB:1COV}.
HELIX 477 480 {ECO:0000244|PDB:1COV}.
STRAND 483 489 {ECO:0000244|PDB:1COV}.
STRAND 491 493 {ECO:0000244|PDB:1COV}.
STRAND 495 500 {ECO:0000244|PDB:1COV}.
STRAND 505 512 {ECO:0000244|PDB:1COV}.
STRAND 521 528 {ECO:0000244|PDB:1COV}.
STRAND 538 548 {ECO:0000244|PDB:1COV}.
STRAND 553 557 {ECO:0000244|PDB:1COV}.
STRAND 599 602 {ECO:0000244|PDB:1COV}.
HELIX 604 606 {ECO:0000244|PDB:1COV}.
HELIX 614 617 {ECO:0000244|PDB:1COV}.
HELIX 634 638 {ECO:0000244|PDB:1COV}.
STRAND 642 654 {ECO:0000244|PDB:1COV}.
STRAND 656 661 {ECO:0000244|PDB:1COV}.
HELIX 668 674 {ECO:0000244|PDB:1COV}.
STRAND 677 694 {ECO:0000244|PDB:1COV}.
STRAND 708 714 {ECO:0000244|PDB:1COV}.
HELIX 727 730 {ECO:0000244|PDB:1COV}.
STRAND 732 734 {ECO:0000244|PDB:1COV}.
STRAND 736 740 {ECO:0000244|PDB:1COV}.
STRAND 747 750 {ECO:0000244|PDB:1COV}.
STRAND 755 761 {ECO:0000244|PDB:1COV}.
STRAND 765 768 {ECO:0000244|PDB:1COV}.
TURN 769 771 {ECO:0000244|PDB:1COV}.
STRAND 772 776 {ECO:0000244|PDB:1COV}.
HELIX 777 779 {ECO:0000244|PDB:1COV}.
STRAND 785 791 {ECO:0000244|PDB:1COV}.
STRAND 795 797 {ECO:0000244|PDB:1COV}.
STRAND 799 817 {ECO:0000244|PDB:1COV}.
STRAND 828 830 {ECO:0000244|PDB:1COV}.
SEQUENCE 2185 AA; 243682 MW; FD93A677904252FA CRC64;
MGAQVSTQKT GAHETGLNAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP SKFTEPVKDI
MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV VVGYGVWPDY LKDSEATAED
QPTQPDVATC RFYTLDSVQW QKTSPGWWWK LPDALSNLGL FGQNMQYHYL GRTGYTIHVQ
CNASKFHQGC LLVVCVPEAE MGCATLNNTP SSAELLGGDS AKEFADKPVA SGSNKLVQRV
VYNAGMGVGV GNLTIFPHQW INLRTNNSAT IVMPYTNSVP MDNMFRHNNV TLMVIPFVPL
DYCPGSTTYV PITITIAPMC AEYNGLRLAG HQGLPTMNTP GSCQFLTSDD FQSPSAMPQY
DVTPEMRIPG EVKNLMEIAE VDSVVPVQNV GEKVNSMEAY QIPVRSNEGS GTQVFGFPLQ
PGYSSVFSRT LLGEILNYYT HWSGSIKLTF MFCGSAMATG KFLLAYSPPG AGAPTKRVDA
MLGTHVVWDV GLQSSCVLCI PWISQTHYRY VASDEYTAGG FITCWYQTNI VVPADAQSSC
YIMCFVSACN DFSVRLLKDT PFISQQNFFQ GPVEDAITAA IGRVADTVGT GPTNSEAIPA
LTAAETGHTS QVVPSDTMQT RHVKNYHSRS ESTIENFLCR SACVYFTEYE NSGAKRYAEW
VITPRQAAQL RRKLEFFTYV RFDLELTFVI TSTQQPSTTQ NQDAQILTHQ IMYVPPGGPV
PDKVDSYVWQ TSTNPSVFWT EGNAPPRMSV PFLSIGNAYS NFYDGWSEFS RNGVYGINTL
NNMGTLYARH VNAGSTGPIK STIRIYFKPK HVKAWIPRPP RLCQYEKAKN VNFQPSGVTT
TRQSITTMTN TGAFGQQSGA VYVGNYRVVN RHLATSADWQ NCVWENYNRD LLVSTTTAHG
CDIIARCRCT TGVYFCASKN KHYPISFEGP GIVEVQESEY YPRRYQSHVL LAAGFSEPGD
CGGILRCEHG VIGIVTMGGE GVVGFADIRD LLWLEDDAME QGVKDYVEQL GNAFGSGFTN
QICEQVNLLK ESLVGQDSIL EKSLKALVKI ISALVIVVRN HDDLITVTAT LALIGCTSSP
WRWLKQKVSQ YYGIPMAERQ NNGWLKKFTE MTNACKGMEW IAIKIQKFIE WLKVKILPEV
REKHEFLNRL KQLPLLESQI ATIEQSAPSQ SDQEQLFSNV QYFAHYCRKY APLYASEAKR
VFSLEKKMSN YIQFKSKCRI EPVCLLLHGS PGAGKSVATN LIGRSLAEKL NSSVYSLPPD
PDHFDGYKQQ AVVIMDDLCQ KPDGKDVSLF CQMVSSVDFV PPMAALEEKG ILFTSPFVLA
STNAGSINAP TVSDSRALAR RFHFDMNIEV ISMYSQNGKI NMPMSVKTCD EECCPVNFKK
CCPLVCGKAI QFIDRRTQVR YSLDMLVTEM FREYNHRHSV GATLEALFQG PPVYREIKIS
VAPETPPPPR IADLLKSVDS EAVREYCKEK GWLVPEVNST LQIEKHVSRA FICLQAITTF
VSVAGIIYII YKLFAGFQGA YTGIPNQKPK VPTLRQAKVQ GPAFEFAVAM MKRNSSTVKT
EYGEFTMLGI YDRWAVLPRH AKPGPTILMN DQEVGVLDAK ELVDKDGTNL ELTLLKLNRN
EKFRDIRGFL AKEEVEVNEA VLAINTSKFP NMYIPVGQVT DYGFLNLGGT PTKRMLMYNF
PTRAGQCGGV LMSTGKVLGI HVGGNGHQGF SAALLKHYFN DEQGEIEFIE SSKEAGFPII
NTPSKTKLEP SVFHQVFEGD KEPAVLRNGD PRLKVNFEEA IFSKYIGNVN THVDEYMMEA
VDHYAGQLAT LDISTEPMKL EDAVYGTEGL EALDLTTSAG YPYVALGIKK RDILSKKTRD
LTKLKECMDK YGLNLPMVTY VKDELRSAEK VAKGKSRLIE ASSLNDSVAM RQTFGNLYKT
FHLNPGVVTG SAVGCDPDLF WSKIPVMLDG HLIAFDYSGY DASLSPVWFA CLKLLLEKLG
YSHKETNYID YLCNSHHLYR DKHYFVRGGM PSGCSGTSIF NSMINNIIIR TLMLKVYKGI
DLDQFRMIAY GDDVIASYPW PIDASLLAEA GKDYGLIMTP ADKGECFNEV TWTNVTFLKR
YFRADEQYPF LVHPVMPMKD IHESIRWTKD PKNTQDHVRS LCLLAWHNGE HEYEEFIRKI
RSVPVGRCLT LPAFSTIRRK WLDSF


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