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 POLG_CXA9               Reviewed;        2201 AA.
P21404;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 163.
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 A9 (strain Griggs).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Enterovirus B.
NCBI_TaxID=12068;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2558158; DOI=10.1099/0022-1317-70-12-3269;
Chang K.H., Auvinen P., Hyypiae T., Stanway G.;
"The nucleotide sequence of coxsackievirus A9; implications for
receptor binding and enterovirus classification.";
J. Gen. Virol. 70:3269-3280(1989).
[2]
INTERACTION WITH HUMAN ITGAV/ITGB6 INTEGRIN.
PubMed=15194773; DOI=10.1128/JVI.78.13.6967-6973.2004;
Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D.,
Stanway G.;
"Integrin alpha v beta 6 is an RGD-dependent receptor for
coxsackievirus A9.";
J. Virol. 78:6967-6973(2004).
[3]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-870.
PubMed=10647183; DOI=10.1016/S0969-2126(00)88343-4;
Hendry E., Hatanaka H., Fry E., Smyth M., Tate J., Stanway G.,
Santti J., Maaronen M., Hyypia T., Stuart D.;
"The crystal structure of coxsackievirus A9: new insights into the
uncoating mechanisms of enteroviruses.";
Structure 7:1527-1538(1999).
-!- 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 integrin ITGAV/ITGB6 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). Interacts with host integrin
ITGAV/ITGB6 heterodimer. 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=1d4m";
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EMBL; D00627; BAA00518.1; -; Genomic_RNA.
PIR; JQ0523; GNNYA9.
PDB; 1D4M; X-ray; 2.90 A; 1=569-867, 2=70-330, 3=331-568, 4=2-69.
PDB; 3J2J; EM; 9.54 A; A=631-852, B=331-568, C=79-330.
PDBsum; 1D4M; -.
PDBsum; 3J2J; -.
ProteinModelPortal; P21404; -.
SMR; P21404; -.
ELM; P21404; -.
DrugBank; DB08231; MYRISTIC ACID.
MEROPS; C03.011; -.
OrthoDB; VOG0900006M; -.
EvolutionaryTrace; P21404; -.
Proteomes; UP000000288; 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; ISS: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: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 2201 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426164.
CHAIN 2 849 P1. {ECO:0000250}.
/FTId=PRO_0000426165.
CHAIN 2 330 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426166.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426167.
CHAIN 70 330 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426168.
CHAIN 331 566 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426169.
CHAIN 566 867 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426170.
CHAIN 868 1445 P2. {ECO:0000250}.
/FTId=PRO_0000426171.
CHAIN 868 1017 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000426172.
CHAIN 1018 1116 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000039508.
CHAIN 1117 1445 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000039509.
CHAIN 1446 2201 P3. {ECO:0000250}.
/FTId=PRO_0000426173.
CHAIN 1446 1556 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426174.
CHAIN 1446 1534 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000039510.
CHAIN 1535 1556 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426175.
CHAIN 1557 2201 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426176.
CHAIN 1557 1738 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426177.
CHAIN 1739 2201 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426178.
TOPO_DOM 2 1511 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1512 1527 {ECO:0000255}.
TOPO_DOM 1528 2201 Cytoplasmic. {ECO:0000255}.
DOMAIN 1221 1377 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1557 1722 Peptidase C3.
DOMAIN 1966 2082 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
REGION 566 582 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1446 1469 Disordered. {ECO:0000250}.
MOTIF 858 860 Cell attachment site.
ACT_SITE 888 888 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 906 906 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 977 977 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 1596 1596 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1627 1627 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1703 1703 For Protease 3C activity. {ECO:0000250}.
ACT_SITE 2068 2068 For RdRp activity. {ECO:0000250}.
METAL 1972 1972 Magnesium.
{ECO:0000250|UniProtKB:P03313}.
METAL 2069 2069 Magnesium.
{ECO:0000250|UniProtKB:P03313}.
SITE 69 70 Cleavage; by autolysis. {ECO:0000255}.
SITE 330 331 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 867 868 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 1017 1018 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1445 1446 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1534 1535 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1556 1557 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1739 1740 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1537 1537 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
STRAND 3 7 {ECO:0000244|PDB:1D4M}.
STRAND 26 29 {ECO:0000244|PDB:1D4M}.
STRAND 33 35 {ECO:0000244|PDB:1D4M}.
HELIX 36 38 {ECO:0000244|PDB:1D4M}.
HELIX 51 54 {ECO:0000244|PDB:1D4M}.
STRAND 57 59 {ECO:0000244|PDB:1D4M}.
STRAND 63 65 {ECO:0000244|PDB:1D4M}.
STRAND 83 87 {ECO:0000244|PDB:1D4M}.
STRAND 90 96 {ECO:0000244|PDB:1D4M}.
TURN 113 115 {ECO:0000244|PDB:1D4M}.
HELIX 126 128 {ECO:0000244|PDB:1D4M}.
STRAND 138 140 {ECO:0000244|PDB:1D4M}.
STRAND 147 151 {ECO:0000244|PDB:1D4M}.
HELIX 153 155 {ECO:0000244|PDB:1D4M}.
HELIX 159 167 {ECO:0000244|PDB:1D4M}.
STRAND 168 180 {ECO:0000244|PDB:1D4M}.
STRAND 188 197 {ECO:0000244|PDB:1D4M}.
STRAND 203 205 {ECO:0000244|PDB:1D4M}.
HELIX 212 214 {ECO:0000244|PDB:1D4M}.
STRAND 225 227 {ECO:0000244|PDB:1D4M}.
HELIX 239 241 {ECO:0000244|PDB:1D4M}.
TURN 242 245 {ECO:0000244|PDB:1D4M}.
HELIX 248 253 {ECO:0000244|PDB:1D4M}.
STRAND 254 260 {ECO:0000244|PDB:1D4M}.
TURN 261 263 {ECO:0000244|PDB:1D4M}.
STRAND 265 271 {ECO:0000244|PDB:1D4M}.
STRAND 276 280 {ECO:0000244|PDB:1D4M}.
TURN 282 284 {ECO:0000244|PDB:1D4M}.
STRAND 288 299 {ECO:0000244|PDB:1D4M}.
STRAND 308 324 {ECO:0000244|PDB:1D4M}.
TURN 338 341 {ECO:0000244|PDB:1D4M}.
STRAND 353 355 {ECO:0000244|PDB:1D4M}.
HELIX 374 377 {ECO:0000244|PDB:1D4M}.
HELIX 394 398 {ECO:0000244|PDB:1D4M}.
STRAND 400 404 {ECO:0000244|PDB:1D4M}.
STRAND 411 416 {ECO:0000244|PDB:1D4M}.
TURN 419 421 {ECO:0000244|PDB:1D4M}.
TURN 423 427 {ECO:0000244|PDB:1D4M}.
HELIX 429 434 {ECO:0000244|PDB:1D4M}.
STRAND 437 442 {ECO:0000244|PDB:1D4M}.
STRAND 444 450 {ECO:0000244|PDB:1D4M}.
STRAND 459 465 {ECO:0000244|PDB:1D4M}.
HELIX 475 478 {ECO:0000244|PDB:1D4M}.
STRAND 481 487 {ECO:0000244|PDB:1D4M}.
STRAND 493 498 {ECO:0000244|PDB:1D4M}.
STRAND 503 505 {ECO:0000244|PDB:1D4M}.
STRAND 507 510 {ECO:0000244|PDB:1D4M}.
STRAND 519 526 {ECO:0000244|PDB:1D4M}.
STRAND 536 546 {ECO:0000244|PDB:1D4M}.
STRAND 551 555 {ECO:0000244|PDB:1D4M}.
HELIX 602 604 {ECO:0000244|PDB:1D4M}.
HELIX 612 615 {ECO:0000244|PDB:1D4M}.
HELIX 628 630 {ECO:0000244|PDB:1D4M}.
HELIX 632 636 {ECO:0000244|PDB:1D4M}.
STRAND 640 650 {ECO:0000244|PDB:1D4M}.
HELIX 654 657 {ECO:0000244|PDB:1D4M}.
STRAND 658 662 {ECO:0000244|PDB:1D4M}.
STRAND 665 668 {ECO:0000244|PDB:1D4M}.
HELIX 669 675 {ECO:0000244|PDB:1D4M}.
STRAND 678 695 {ECO:0000244|PDB:1D4M}.
STRAND 709 715 {ECO:0000244|PDB:1D4M}.
HELIX 728 731 {ECO:0000244|PDB:1D4M}.
STRAND 733 735 {ECO:0000244|PDB:1D4M}.
STRAND 737 741 {ECO:0000244|PDB:1D4M}.
STRAND 748 751 {ECO:0000244|PDB:1D4M}.
STRAND 756 762 {ECO:0000244|PDB:1D4M}.
STRAND 766 769 {ECO:0000244|PDB:1D4M}.
TURN 770 772 {ECO:0000244|PDB:1D4M}.
STRAND 773 777 {ECO:0000244|PDB:1D4M}.
HELIX 778 781 {ECO:0000244|PDB:1D4M}.
STRAND 786 793 {ECO:0000244|PDB:1D4M}.
STRAND 800 818 {ECO:0000244|PDB:1D4M}.
STRAND 843 845 {ECO:0000244|PDB:1D4M}.
SEQUENCE 2201 AA; 246535 MW; CCEA86F9E80F385F CRC64;
MGAQVSTQKT GAHETSLSAA GNSIIHYTNI NYYKDAASNS ANRQDFTQDP SKFTEPVKDV
MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV VVGYGRWPTY LRDDEATAED
QPTQPDVATC RFYTLDSIKW EKGSVGWWWK FPEALSDMGL FGQNMQYHYL GRAGYTIHLQ
CNASKFHQGC LLVVCVPEAE MGGAVVGQAF SATAMANGDK AYEFTSATQS DQTKVQTAIH
NAGMGVGVGN LTIYPHQWIN LRTNNSATIV MPYINSVPMD NMFRHYNFTL MVIPFVKLDY
ADTASTYVPI TVTVAPMCAE YNGLRLAQAQ GLPTMNTPGS TQFLTSDDFQ SPCALPQFDV
TPSMNIPGEV KNLMEIAEVD SVVPVNNVQD TTDQMEMFRI PVTINAPLQQ QVFGLRLQPG
LDSVFKHTLL GEILNYYAHW SGSMKLTFVF CGSAMATGKF LIAYSPPGAN PPKTRKDAML
GTHIIWDIGL QSSCVLCVPW ISQTHYRLVQ QDEYTSAGYV TCWYQTGMIV PPGTPNSSSI
MCFASACNDF SVRMLRDTPF ISQDNKLQGD VEEAIERARC TVADTMRTGP SNSASVPALT
AVETGHTSQV TPSDTMQTRH VKNYHSRSES TVENFLGRSA CVYMEEYKTT DKHVNKKFVA
WPINTKQMVQ MRRKLEMFTY LRFDMEVTFV ITSRQDPGTT LAQDMPVLTR QIMYVPPGGP
IPAKVDDYAW QTSTNPSIFW TEGNAPARMS IPFISIGNAY SNFYDGWSNF DQRGSYGYNT
LNNLGHIYVR HVSGSSPHPI TSTIRVYFKP KHTRAWVPRP PRLCQYKKAF SVDFTPTPIT
DTRKDINTVT TVAQSRRRGD MSTLNTHGAF GQQSGAVYVG NYRVINRHLA THTDWQNCVW
EDYNRDLLVS TTTAHGCDVI ARCQCTTGVY FCASKNKHYP VSFEGPGLVE VQESEYYPKR
YQSHVLLAAG FSEPGDCGGI LRCEHGVIGI VTMGGEGVVG FADVRDLLWL EDDAMEQGVK
DYVEQLGNAF GSGFTNQICE QVNLLKESLV GQDSILEKSL KALVKIISAL VIVVRNHDDL
ITVTAILALI GCTSSPWRWL KQKVSQYYGI PMAERQNDSW LKKFTEMTNA CKRMEWIAIK
IQKFIEWLKV KILPEVREKH EFLNRLKQLP LLESQIATIE QSAPSQSDQE QLFSNVQYFA
HYCRKYAPLY AAEAKRVFSL EKKMSNYIQF KSKCRIEPVC LLLHGSPGAG KSVATNLIGR
SLAEKLNSSV YSLPPDPDHF DGYKQQAVVI MDDLCQNPDG KDVSLFCQMV SSVDFVPPMA
ALEEKGILFT SPFVLASTNA GSINAPTVSD SRALARRFHF DMNIEVISMY SQNGKINMPM
SVKTCDEECC PVNFKKCCPL VCGKAIQFID RRTQVRYSLD MLVTEMFREY NHRHSVGATL
EALFQGPPIY REIKISVAPE TPPPPVIADL LKSVDSEDVR EYCKEKGWLI PEVNSTLQIE
KYVSRAFICL QAITTFVSVA GIIYIIYKLF AGFQGAYTGI PNQKPKVPTL RQAKVQGPAF
EFAVAMMKRN SSTVKTEYGE FTMLGIYDRW AVLPRHAKPG PTILMNDQEV GVMDAKELVD
KDGTNLELTL LKLNRNEKFR DIRGFLAKEE MEVNEAVLAI NTSKFPNMYI PVGQVTDYGF
LNLGGTPTKR MLMYNFPTRA GQCGGVLMST GKVLGIHVGG NGHQGFSAAL LKHYFNDEQG
EIEFIESSKD AGFPIINTPS KTKLEPSVFH QVFEGVKEPA VLRNGDPRLK ANFEEAIFSK
YIGNVNTHVD EYMLEAVDHY AGQLATLDIS TEPMKLEDAV YGTEGLEALD LTTSAGYPYV
ALGIKKRDIL SKKTRDLTKL KECMDKYGLN LPMITYVKDQ LRSAEKVAKG KSRLIEASSL
NDSVAMRQTF GNLYKTFHLN PGIVTGSAVG CDPDLFWSKI PVMLNGHLIA FDYSGYDASL
SPVWFACLKL LLEKLGYSHK ETNYIDYLCN SHHLYRDKHY FVRGGMPSGC SGTSIFNSMI
NNIIIRTLML KVYKGIDLDQ FRMIAYGDDV IASYPWPIDA SLLAEAGKDY GLIMTPADKG
ECFNEVTWTN VTFLKRYFRA DEQYPFLVHP VMPMKDIHES IRWTKDPKNT QDHVRSLCLL
AWHNGEHEYE EFIRKIRSVP VGRCLTLPAF STLRRKWLDS F


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