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Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

 POLG_POL2L              Reviewed;        2207 AA.
P06210;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 173.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=P3;
Contains:
RecName: Full=Protein 3AB;
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=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 2 (strain Lansing).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Enterovirus C.
NCBI_TaxID=12084;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3003384;
la Monica N., Meriam C., Racaniello V.R.;
"Mapping of sequences required for mouse neurovirulence of poliovirus
type 2 Lansing.";
J. Virol. 57:515-525(1986).
-!- 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 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. 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
cytoplasmic 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.
-!- 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.
-!- 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=1eah";
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EMBL; M12197; AAA46912.1; -; Genomic_RNA.
PIR; A29507; GNNY5P.
PDB; 1EAH; X-ray; 2.90 A; 1=579-879, 2=70-340, 3=341-578, 4=2-69.
PDB; 3EPF; EM; 9.00 A; 1=602-879, 2=79-340, 3=341-575, 4=2-69.
PDBsum; 1EAH; -.
PDBsum; 3EPF; -.
ProteinModelPortal; P06210; -.
SMR; P06210; -.
DrugBank; DB08231; MYRISTIC ACID.
PRIDE; P06210; -.
OrthoDB; VOG0900001E; -.
EvolutionaryTrace; P06210; -.
Proteomes; UP000007638; 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; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006260; P:DNA replication; 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 complex oligomerization; IEA:UniProtKB-KW.
GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; 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; 1.10.10.870; -; 1.
Gene3D; 2.60.120.20; -; 3.
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; IPR002527; Pico_P2B.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR029053; Viral_coat.
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;
Clathrin- and caveolin-independent endocytosis of virus by host;
Complete proteome; Covalent protein-RNA linkage; DNA replication;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host transcription 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 eukaryotic host transcription initiation by virus;
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;
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 2207 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426611.
CHAIN 2 879 P1. {ECO:0000250}.
/FTId=PRO_0000426612.
CHAIN 2 340 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426613.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426614.
CHAIN 70 340 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426615.
CHAIN 341 578 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426616.
CHAIN 579 879 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426617.
CHAIN 880 1454 P2. {ECO:0000250}.
/FTId=PRO_0000426618.
CHAIN 880 1028 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000426619.
CHAIN 1029 1125 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000040107.
CHAIN 1126 1454 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000040108.
CHAIN 1455 2207 P3. {ECO:0000250}.
/FTId=PRO_0000426620.
CHAIN 1455 1563 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426621.
CHAIN 1455 1541 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000040109.
CHAIN 1542 1563 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426622.
CHAIN 1564 2207 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426623.
CHAIN 1564 1745 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426624.
CHAIN 1746 2207 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426625.
TOPO_DOM 2 1518 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1519 1534 {ECO:0000255}.
TOPO_DOM 1535 2207 Cytoplasmic. {ECO:0000255}.
DOMAIN 1230 1386 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1564 1729 Peptidase C3.
DOMAIN 1973 2088 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1254 1261 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
REGION 579 599 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1455 1477 Disordered. {ECO:0000250}.
ACT_SITE 899 899 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 917 917 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 988 988 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 1603 1603 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1634 1634 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1710 1710 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 2074 2074 For RdRp activity. {ECO:0000250}.
SITE 69 70 Cleavage; by autolysis. {ECO:0000255}.
SITE 340 341 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 879 880 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 1028 1029 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1125 1126 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1454 1455 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1541 1542 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1563 1564 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1746 1747 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1544 1544 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
STRAND 4 7 {ECO:0000244|PDB:1EAH}.
HELIX 17 19 {ECO:0000244|PDB:1EAH}.
HELIX 23 25 {ECO:0000244|PDB:1EAH}.
STRAND 26 29 {ECO:0000244|PDB:1EAH}.
HELIX 36 38 {ECO:0000244|PDB:1EAH}.
HELIX 51 54 {ECO:0000244|PDB:1EAH}.
STRAND 57 59 {ECO:0000244|PDB:1EAH}.
STRAND 63 65 {ECO:0000244|PDB:1EAH}.
STRAND 83 87 {ECO:0000244|PDB:1EAH}.
STRAND 90 96 {ECO:0000244|PDB:1EAH}.
HELIX 103 105 {ECO:0000244|PDB:1EAH}.
TURN 113 115 {ECO:0000244|PDB:1EAH}.
HELIX 126 128 {ECO:0000244|PDB:1EAH}.
STRAND 138 140 {ECO:0000244|PDB:1EAH}.
STRAND 147 151 {ECO:0000244|PDB:1EAH}.
HELIX 153 155 {ECO:0000244|PDB:1EAH}.
HELIX 159 167 {ECO:0000244|PDB:1EAH}.
STRAND 168 180 {ECO:0000244|PDB:1EAH}.
STRAND 187 197 {ECO:0000244|PDB:1EAH}.
STRAND 203 207 {ECO:0000244|PDB:1EAH}.
HELIX 213 216 {ECO:0000244|PDB:1EAH}.
HELIX 219 221 {ECO:0000244|PDB:1EAH}.
STRAND 226 228 {ECO:0000244|PDB:1EAH}.
STRAND 235 237 {ECO:0000244|PDB:1EAH}.
HELIX 246 248 {ECO:0000244|PDB:1EAH}.
TURN 249 252 {ECO:0000244|PDB:1EAH}.
HELIX 255 260 {ECO:0000244|PDB:1EAH}.
STRAND 261 267 {ECO:0000244|PDB:1EAH}.
TURN 268 270 {ECO:0000244|PDB:1EAH}.
STRAND 272 278 {ECO:0000244|PDB:1EAH}.
STRAND 282 287 {ECO:0000244|PDB:1EAH}.
TURN 289 291 {ECO:0000244|PDB:1EAH}.
STRAND 295 307 {ECO:0000244|PDB:1EAH}.
STRAND 315 331 {ECO:0000244|PDB:1EAH}.
TURN 348 351 {ECO:0000244|PDB:1EAH}.
STRAND 363 365 {ECO:0000244|PDB:1EAH}.
STRAND 379 382 {ECO:0000244|PDB:1EAH}.
HELIX 384 387 {ECO:0000244|PDB:1EAH}.
TURN 399 403 {ECO:0000244|PDB:1EAH}.
HELIX 405 408 {ECO:0000244|PDB:1EAH}.
STRAND 410 413 {ECO:0000244|PDB:1EAH}.
STRAND 422 427 {ECO:0000244|PDB:1EAH}.
TURN 429 431 {ECO:0000244|PDB:1EAH}.
TURN 433 437 {ECO:0000244|PDB:1EAH}.
HELIX 439 444 {ECO:0000244|PDB:1EAH}.
STRAND 447 452 {ECO:0000244|PDB:1EAH}.
STRAND 454 460 {ECO:0000244|PDB:1EAH}.
STRAND 469 475 {ECO:0000244|PDB:1EAH}.
STRAND 477 479 {ECO:0000244|PDB:1EAH}.
HELIX 485 488 {ECO:0000244|PDB:1EAH}.
STRAND 491 497 {ECO:0000244|PDB:1EAH}.
STRAND 499 501 {ECO:0000244|PDB:1EAH}.
STRAND 503 508 {ECO:0000244|PDB:1EAH}.
STRAND 513 520 {ECO:0000244|PDB:1EAH}.
STRAND 529 536 {ECO:0000244|PDB:1EAH}.
STRAND 546 556 {ECO:0000244|PDB:1EAH}.
STRAND 561 565 {ECO:0000244|PDB:1EAH}.
HELIX 625 627 {ECO:0000244|PDB:1EAH}.
HELIX 635 637 {ECO:0000244|PDB:1EAH}.
HELIX 655 659 {ECO:0000244|PDB:1EAH}.
STRAND 663 671 {ECO:0000244|PDB:1EAH}.
STRAND 683 687 {ECO:0000244|PDB:1EAH}.
HELIX 695 700 {ECO:0000244|PDB:1EAH}.
STRAND 703 725 {ECO:0000244|PDB:1EAH}.
STRAND 732 738 {ECO:0000244|PDB:1EAH}.
HELIX 751 754 {ECO:0000244|PDB:1EAH}.
STRAND 756 758 {ECO:0000244|PDB:1EAH}.
STRAND 760 764 {ECO:0000244|PDB:1EAH}.
STRAND 770 774 {ECO:0000244|PDB:1EAH}.
STRAND 779 785 {ECO:0000244|PDB:1EAH}.
TURN 800 803 {ECO:0000244|PDB:1EAH}.
STRAND 812 815 {ECO:0000244|PDB:1EAH}.
STRAND 817 822 {ECO:0000244|PDB:1EAH}.
STRAND 831 849 {ECO:0000244|PDB:1EAH}.
STRAND 859 862 {ECO:0000244|PDB:1EAH}.
SEQUENCE 2207 AA; 245831 MW; 2B1E2070B7D44F99 CRC64;
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFAQDP SKFTEPIKDV
LIKTAPTLNS PNIEACGYSD RVMQLTLGNS TITTQEAANS VVAYGRWPEY IKDSEANPVD
QPTEPDVAAC RFYTLDTVTW RKESRGWWWK LPDALKDMGL FGQNMFYHYL GRAGYTVHVQ
CNASKFHQGA LGVFAVPEMC LAGDSTTHMF TKYENANPGE KGGEFKGSFT LDTNATNPAR
NFCPVDYLFG SGVLAGNAFV YPHQIINLRT NNCATLVLPY VNSLSIDSMT KHNNWGIAIL
PLAPLDFATE SSTEIPITLT IAPMCCEFNG LRNITVPRTQ GLPVLNTPGS NQYLTADNYQ
SPCAIPEFDV TPPIDIPGEV RNMMELAEID TMIPLNLTNQ RKNTMDMYRV ELNDAAHSDT
PILCLSLSPA SDPRLAHTML GEILNYYTHW AGSLKFTFLF CGSMMATGKL LVSYAPPGAE
APKSRKEAML GTHVIWDIGL QSSCTMVVPW ISNTTYRQTI NDSFTEGGYI SMFYQTRVVV
PLSTPRKMDI LGFVSACNDF SVRLLRDTTH ISQEAMPQGL GDLIEGVVEG VTRNALTPLT
PANNLPDTQS SGPAHSKETP ALTAVETGAT NPLVPSDTVQ TRHVIQKRTR SESTVESFFA
RGACVAIIEV DNDAPTKRAS KLFSVWKITY KDTVQLRRKL EFFTYSRFDM EFTFVVTSNY
TDANNGHALN QVYQIMYIPP GAPIPGKWND YTWQTSSNPS VFYTYGAPPA RISVPYVGIA
NAYSHFYDGF AKVPLAGQAS TEGDSLYGAA SLNDFGSLAV RVVNDHNPTK LTSKIRVYMK
PKHVRVWCPR PPRAVPYYGP GVDYKDGLAP LPGKGLTTYG FGHQNKAVYT AGYKICNYHL
ATQEDLQNAV NIMWIRDLLV VESKAQGIDS IARCNCHTGV YYCESRRKYY PVSFTGPTFQ
YMEANEYYPA RYQSHMLIGH GFASPGDCGG ILRCQHGVIG IITAGGEGLV AFSDIRDLYA
YEEEAMEQGV SNYIESLGAA FGSGFTQQIG NKISELTSMV TSTITEKLLK NLIKIISSLV
IITRNYEDTT TVLATLALLG CDASPWQWLK KKACDILEIP YIMRQGDSWL KKFTEACNAA
KGLEWVSNKI SKFIDWLKEK IIPQARDKLE FVTKLKQLEM LENQIATIHQ SCPSQEHQEI
LFNNVRWLSI QSKRFAPLYA VEAKRIQKLE HTINNYVQFK SKHRIEPVCL LVHGSPGTGK
SVATNLIARA IAEKENTSTY SLPPDPSHFD GYKQQGVVIM DDLNQNPDGA DMKLFCQMVS
TVEFIPPMAS LEEKGILFTS NYVLASTNSS RITPPTVAHS DALARRFAFD MDIQIMSEYS
RDGKLNMAMA TEMCKNCHHP ANFKRCCPLV CGKAIQLMDK SSRVRYSIDQ ITTMIINERN
RRSSIGNCME ALFQGPLQYK DLKIDIKTTP PPECINDLLQ AVDSQEVRDY CEKKGWIVDI
TSQVQTERNI NRAMTILQAV TTFAAVAGVV YVMYKLFAGH QGAYTGLPNK RPNVPTIRTA
KVQGPGFDYA VAMAKRNILT ATTIKGEFTM LGVHDNVAIL PTHASPGETI VIDGKEVEVL
DAKALEDQAG TNLEITIVTL KRNEKFRDIR PHIPTQITET NDGVLIVNTS KYPNMYVPVG
AVTEQGYLNL SGRQTARTLM YNFPTRAGQC GGVITCTGKV IGMHVGGNGS HGFAAALKRS
YFTQSQGEIQ WMRPSKEVGY PVINAPSKTK LEPSAFHYVF EGVKEPAVLT KSDPRLKTDF
EEAIFSKYVG NKITEVDEYM KEAVDHYAGQ LMSLDINTEQ MCLEDAMYGT DGLEALDLST
SAGYPYVAMG KKKRDILNKQ TRDTKEMQRL LDTYGINLPL VTYVKDELRS KTKVEQGKSR
LIEASSLNDS VAMRMAFGNL YAAFHKNPGV VTGSAVGCDP DLFWSKIPVL MEEKLFAFDY
TGYDASLSPA WFEALKMVLE KIGFGDRVDY IDYLNHSHHL YKNKTYCVKG GMPSGCSGTS
IFNSMINNLI IRTLLLKTYK GIDLDHLKMI AYGDDVIASY PHEVDASLLA QSGKDYGLTM
TPADKSATFE TVTWENVTFL KRFFRADEKY PFLVHPVMPM KEIHESIRWT KDPRNTQDHV
RSLCLLAWHN GEEEYNKFLA KIRSVPIGRA LLLPEYSTLY RRWLDSF


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