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 POLG_CXB4J              Reviewed;        2183 AA.
P08292;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 161.
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 B4 (strain JVB / Benschoten / New York/51).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Enterovirus B.
NCBI_TaxID=103906;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3037008; DOI=10.1099/0022-1317-68-7-1835;
Jenkins O., Booth J.D., Minor P.D., Almond J.W.;
"The complete nucleotide sequence of coxsackievirus B4 and its
comparison to other members of the Picornaviridae.";
J. Gen. Virol. 68:1835-1848(1987).
[2]
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).
-!- 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 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.
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 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 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}.
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EMBL; X05690; CAA29172.1; -; Genomic_RNA.
PDB; 1Z8R; NMR; -; A=842-999.
PDBsum; 1Z8R; -.
ProteinModelPortal; P08292; -.
SMR; P08292; -.
MEROPS; C03.011; -.
OrthoDB; VOG0900001E; -.
EvolutionaryTrace; P08292; -.
Proteomes; UP000007531; 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; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 3.
Gene3D; 4.10.80.10; -; 1.
InterPro; 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 2183 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426311.
CHAIN 2 849 P1. {ECO:0000250}.
/FTId=PRO_0000426312.
CHAIN 2 330 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426313.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426314.
CHAIN 70 330 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426315.
CHAIN 331 566 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426316.
CHAIN 566 849 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426317.
CHAIN 850 1427 P2. {ECO:0000250}.
/FTId=PRO_0000426318.
CHAIN 850 999 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000426319.
CHAIN 1000 1098 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000039620.
CHAIN 1099 1427 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000039621.
CHAIN 1428 2183 P3. {ECO:0000250}.
/FTId=PRO_0000426320.
CHAIN 1428 1538 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426321.
CHAIN 1428 1516 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000039622.
CHAIN 1517 1538 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426322.
CHAIN 1539 2183 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426323.
CHAIN 1539 1720 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426324.
CHAIN 1721 2183 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426325.
TOPO_DOM 2 1493 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1494 1509 {ECO:0000255}.
TOPO_DOM 1510 2183 Cytoplasmic. {ECO:0000255}.
DOMAIN 1203 1359 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1539 1704 Peptidase C3.
DOMAIN 1948 2064 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
REGION 566 582 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1428 1451 Disordered. {ECO:0000250}.
ACT_SITE 870 870 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 888 888 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 959 959 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 1578 1578 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1609 1609 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1685 1685 For Protease 3C activity. {ECO:0000250}.
ACT_SITE 2050 2050 For RdRp activity. {ECO:0000250}.
METAL 1954 1954 Magnesium.
{ECO:0000250|UniProtKB:P03313}.
METAL 2051 2051 Magnesium.
{ECO:0000250|UniProtKB:P03313}.
SITE 69 70 Cleavage; by autolysis. {ECO:0000255}.
SITE 330 331 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 849 850 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 999 1000 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1427 1428 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1516 1517 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1538 1539 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1721 1722 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1519 1519 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
STRAND 858 861 {ECO:0000244|PDB:1Z8R}.
STRAND 864 868 {ECO:0000244|PDB:1Z8R}.
HELIX 869 871 {ECO:0000244|PDB:1Z8R}.
HELIX 874 878 {ECO:0000244|PDB:1Z8R}.
STRAND 880 884 {ECO:0000244|PDB:1Z8R}.
TURN 885 888 {ECO:0000244|PDB:1Z8R}.
STRAND 889 893 {ECO:0000244|PDB:1Z8R}.
STRAND 908 914 {ECO:0000244|PDB:1Z8R}.
TURN 915 917 {ECO:0000244|PDB:1Z8R}.
STRAND 919 924 {ECO:0000244|PDB:1Z8R}.
STRAND 929 933 {ECO:0000244|PDB:1Z8R}.
STRAND 941 951 {ECO:0000244|PDB:1Z8R}.
STRAND 953 955 {ECO:0000244|PDB:1Z8R}.
STRAND 960 964 {ECO:0000244|PDB:1Z8R}.
STRAND 966 976 {ECO:0000244|PDB:1Z8R}.
STRAND 978 986 {ECO:0000244|PDB:1Z8R}.
SEQUENCE 2183 AA; 244014 MW; DEA069DE3AE91AF0 CRC64;
MGAQVSTQKT GAHETSLSAS GNSIIHYTNI NYYKDAASNS ANRQDFTQDP SKFTEPVKDV
MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV VVGYGVWPDY LSDEEATAED
QPTQPDVATC RFYTLNSVKW EMQSAGWWWK FPDALSEMGL FGQNMQYHYL GRSGYTIHVQ
CNASKFHQGC LLVVCVPEAE MGCTNAENAP AYGDLCGGET AKSFEQNAAT GKTAVQTAVC
NAGMGVGVGN LTIYPHQWIN LRTNNSATIV MPYINSVPMD NMFRHNNFTL MIIPFAPLDY
VTGASSYIPI TVTVAPMSAE YNGLRLAGHQ GLPTMLTPGS TQFLTSDDFQ SPSAMPQFDV
TPEMNIPGQV RNLMEIAEVD SVVPINNLKA NLMTMEAYRV QVRSTDEMGG QIFGFPLQPG
ASSVLQRTLL GEILNYYTHW SGSLKLTFVF CGSAMATGKF LLAYSPPGAG APDSRKNAML
GTHVIWDVGL QSSCVLCVPW ISQTHYRYVV DDKYTASGFI SCWYQTNVIV PAEAQKSCYI
MCFVSACNDF SVRMLRDTQF IKQTNFYQGP TEESVERAMG RVADTIARGP SNSEQIPALT
AVETGHTSQV DPSDTMQTRH VHNYHSRSES SIENFLCRSA CVIYIKYSSA ESNNLKRYAE
WVINTRQVAQ LRRKMEMFTY IRCDMELTFV ITSHQEMSTA TNSDVPVQTH QIMYVPPGGP
VPTSVNDYVW QTSTNPSIFW TEGNAPPRMS IPFMSIGNAY TMFYDGWSNF SRDGIYGYNS
LNNMGTIYAR HVNDSSPGGL TSTIRIYFKP KHVKAYVPRP PRLCQYKKAK SVNFDVEAVT
AERASLITTG PYGHQSGAVY VGNYKVVNRH LATHVDWQNC VWEDYNRDLL VSTTTAHGCD
TIARCQCTTG VYFCASKSKH YPVSFEGPGL VEVQESEYYP KRYQSHVLLA TGFSEPGDCG
GILRCEHGVI GLVTMGGEGV VGFADVRDLL WLEDDAMEQG VKDYVEQLGN AFGSGFTNQI
CEQVNLLKES LVGQDSILEK SLKALVKIIS ALVIVVRNHD DLITVTATLA LIGCTSSPWR
WLKHKVSQYY GIPMAERQNN GWLKKFTEMT NACKGMEWIA VKIQKFIEWL KVKILPEVKE
KHEFLSRLKQ LPLLESQIAT IEQSAPSQSD QEQLFSNVQY FAHYCRKYAP LYAAEAKRVF
SLEKKMSNYI QFKSKCRIEP VCLLLHGSPG AGKSVATNLI GRSLAEKLNS SVYSLPPDPD
HFDGYKQQAV VIMDDLCQNP DGKDVSLFCQ MVSSVDFVPP MAALEEKGIL FTSPFVLAST
NAGSINAPTV SDSRALARRF HFDMNIEVIS MYSQNGKINM PMSVKTCDEE CCPVNFKRCC
PLVCGKAIQF IDRKTQVRYS LDMLVTEMFR EYNHRHSVGA TLEALFQGPP VYREIKISVT
PETPPPPVIA DLLKSVDRQA IREYCKEKGW LVPEIDSILQ IEKHVSRAFI CLQALTTFVS
VAGIIYIIYK LFAGFQGAYT GMPNQKPKVP TLRQAKVQGP AFEFAVAMMK RNSSTVKTEY
GEFTMLGIYD RWAVLPRHAK PGPTILMNDQ EVGVLDAKEL IDRDGTNLEL TLLKLNRNEK
FRDIRGFLAK EEVEVNEAVL AINTSKFPNM YIPVGRVTDY GFLNLGGTPT KRMLMYNFPT
RAGQCGGVLM STGKVLGIHV GGNGHQGFSA GLLKHYFNDE QGEIEFIESS KDAGFPVINT
PSRTKLEPSV FHHVFEGNKE PAVLRNGDPR LKVNFEEAIF FKYIGNVNTH VDEYMLEAVD
HYAGQLATLD INTEPMKLED AVYGTEGLEA LDLTTSAGYP YVALGIKKRD ILSKKTKDLT
KLKECMDKYG LNLPMVTYVK DELRSAEKVA KGKSRLIEAS SLNDSVAMRQ TFGNLYKAFH
LNPGIVTGSA VGCDPDVFWS KIPVMLDGHL IAFDYSGYDA SLSPVWFACL KLLLEKLGYT
HKETNYIDYL CNSHHLYRDK HYFVRGGMPS GCSGTSIFNS MINNIIIRTL MLKVYKGIDL
DQFRMIAYGD DVIASYPWPI DASLLAEAGK DYGLIMTPAD KGECFNEVTW TNVTFLKRYF
RADEQYPFLV HPVMPMKDIH ESIRWTKDPK NTQDHVRSLC LLAWHNGEHE YEEFIQKIRS
VPVGRCLTLP AFSTLRRKWL DSF


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