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Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; 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); 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_HRV1B              Reviewed;        2157 AA.
P12916; Q82106; Q82107; Q82108; Q82109; Q82110; Q82111; Q82112;
Q82113; Q82114; Q82115; Q89704;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 173.
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;
Human rhinovirus 1B (HRV-1B).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Rhinovirus A.
NCBI_TaxID=12129;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2826669; DOI=10.1099/0022-1317-69-1-49;
Hughes P.J., North C., Jellis C.H., Minor P.D., Stanway G.;
"The nucleotide sequence of human rhinovirus 1B: molecular
relationships within the rhinovirus genus.";
J. Gen. Virol. 69:49-58(1988).
[2]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1698-2157.
PubMed=15296746; DOI=10.1016/j.str.2004.05.024;
Love R.A., Maegley K.A., Yu X., Ferre R.A., Lingardo L.K., Diehl W.,
Parge H.E., Dragovich P.S., Fuhrman S.A.;
"The crystal structure of the RNA-dependent RNA polymerase from human
rhinovirus: a dual function target for common cold antiviral
therapy.";
Structure 12:1533-1544(2004).
[3]
REVIEW.
PubMed=23227049; DOI=10.1155/2012/826301;
Fuchs R., Blaas D.;
"Productive entry pathways of human rhinoviruses.";
Adv. Virol. 2012:826301-826301(2012).
-!- 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 mmbers 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.
-!- ACTIVITY 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}.
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EMBL; D00239; BAA00168.1; -; Genomic_RNA.
PIR; A28699; GNNY1B.
PDB; 1XR6; X-ray; 2.50 A; A=1698-2157.
PDBsum; 1XR6; -.
ProteinModelPortal; P12916; -.
SMR; P12916; -.
MEROPS; C03.007; -.
PRIDE; P12916; -.
OrthoDB; VOG0900001E; -.
EvolutionaryTrace; P12916; -.
Proteomes; UP000007681; 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:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
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: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.
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.
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.
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; 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 2157 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426491.
CHAIN 2 847 P1. {ECO:0000250}.
/FTId=PRO_0000426492.
CHAIN 2 332 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426493.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426494.
CHAIN 70 332 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426495.
CHAIN 333 567 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426496.
CHAIN 567 857 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426497.
CHAIN 858 1416 P2. {ECO:0000250}.
/FTId=PRO_0000426498.
CHAIN 858 999 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000426499.
CHAIN 1000 1094 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000040004.
CHAIN 1095 1416 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000040005.
CHAIN 1417 2157 P3. {ECO:0000250}.
/FTId=PRO_0000426500.
CHAIN 1417 1514 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426501.
CHAIN 1417 1493 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000040006.
CHAIN 1494 1514 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426502.
CHAIN 1515 2157 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426503.
CHAIN 1515 1696 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426504.
CHAIN 1697 2157 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426505.
TOPO_DOM 2 1470 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1471 1486 {ECO:0000255}.
TOPO_DOM 1487 2157 Cytoplasmic. {ECO:0000255}.
DOMAIN 1188 1350 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1515 1680 Peptidase C3.
DOMAIN 1925 2038 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
REGION 567 584 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1417 1431 Disordered. {ECO:0000250}.
ACT_SITE 875 875 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 892 892 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 963 963 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 1554 1554 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1585 1585 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1661 1661 For Protease 3C activity. {ECO:0000250}.
ACT_SITE 2024 2024 For RdRp activity. {ECO:0000250}.
SITE 332 333 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 857 858 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 999 1000 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1416 1417 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1493 1494 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1514 1515 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1697 1698 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1496 1496 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
STRAND 1699 1705 {ECO:0000244|PDB:1XR6}.
HELIX 1706 1709 {ECO:0000244|PDB:1XR6}.
TURN 1726 1730 {ECO:0000244|PDB:1XR6}.
HELIX 1751 1756 {ECO:0000244|PDB:1XR6}.
HELIX 1769 1783 {ECO:0000244|PDB:1XR6}.
HELIX 1794 1799 {ECO:0000244|PDB:1XR6}.
STRAND 1802 1804 {ECO:0000244|PDB:1XR6}.
STRAND 1809 1811 {ECO:0000244|PDB:1XR6}.
HELIX 1817 1820 {ECO:0000244|PDB:1XR6}.
HELIX 1824 1827 {ECO:0000244|PDB:1XR6}.
TURN 1830 1833 {ECO:0000244|PDB:1XR6}.
HELIX 1836 1845 {ECO:0000244|PDB:1XR6}.
STRAND 1851 1855 {ECO:0000244|PDB:1XR6}.
HELIX 1862 1866 {ECO:0000244|PDB:1XR6}.
STRAND 1872 1875 {ECO:0000244|PDB:1XR6}.
HELIX 1878 1897 {ECO:0000244|PDB:1XR6}.
TURN 1901 1904 {ECO:0000244|PDB:1XR6}.
HELIX 1911 1921 {ECO:0000244|PDB:1XR6}.
STRAND 1924 1929 {ECO:0000244|PDB:1XR6}.
STRAND 1931 1934 {ECO:0000244|PDB:1XR6}.
HELIX 1936 1938 {ECO:0000244|PDB:1XR6}.
HELIX 1941 1953 {ECO:0000244|PDB:1XR6}.
HELIX 1959 1961 {ECO:0000244|PDB:1XR6}.
HELIX 1962 1965 {ECO:0000244|PDB:1XR6}.
STRAND 1966 1971 {ECO:0000244|PDB:1XR6}.
STRAND 1974 1981 {ECO:0000244|PDB:1XR6}.
HELIX 1989 2008 {ECO:0000244|PDB:1XR6}.
HELIX 2014 2016 {ECO:0000244|PDB:1XR6}.
STRAND 2018 2022 {ECO:0000244|PDB:1XR6}.
STRAND 2025 2032 {ECO:0000244|PDB:1XR6}.
HELIX 2036 2041 {ECO:0000244|PDB:1XR6}.
HELIX 2042 2046 {ECO:0000244|PDB:1XR6}.
TURN 2064 2066 {ECO:0000244|PDB:1XR6}.
STRAND 2072 2076 {ECO:0000244|PDB:1XR6}.
STRAND 2078 2080 {ECO:0000244|PDB:1XR6}.
STRAND 2083 2087 {ECO:0000244|PDB:1XR6}.
HELIX 2090 2097 {ECO:0000244|PDB:1XR6}.
STRAND 2099 2101 {ECO:0000244|PDB:1XR6}.
HELIX 2103 2105 {ECO:0000244|PDB:1XR6}.
HELIX 2106 2117 {ECO:0000244|PDB:1XR6}.
HELIX 2118 2120 {ECO:0000244|PDB:1XR6}.
HELIX 2122 2132 {ECO:0000244|PDB:1XR6}.
HELIX 2136 2140 {ECO:0000244|PDB:1XR6}.
HELIX 2146 2154 {ECO:0000244|PDB:1XR6}.
SEQUENCE 2157 AA; 242315 MW; 42DB649063B677B9 CRC64;
MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP SKFTDPVKDV
LEKGIPTLQS PSVEACGYSD RIIQITRGDS TITSQDVANA VVGYGVWPHY LTPQDATAID
KPTQPDTSSN RFYTLESKHW NGDSKGWWWK LPDALKEMGI FGENMYYHFL GRSGYTVHVQ
CNASKFHQGT LLVAMIPEHQ LASAKNGSVT AGYNLTHPGE AGRVVGQQRD ANLRQPSDDS
WLNFDGTLLG NLLIFPHQFI NLRSNNSATL IVPYVNAVPM DSMLRHNNWS LVIIPISPLR
SETTSSNIRP ITVSISPMCA EFSGARAKNV RQGLPVYITP GSGQFMTTDD MQSPCALPWY
HPTKEISIPG EVKNLIEMCQ VDTLIPVNNV GTNVGNISMY TVQLGNQMDM AQEVFAIKVD
ITSQPLATTL IGEIASYYTH WTGSLRFSFM FCGTANTTLK LLLAYTPPGI DKPATRKDAM
LGTHVVWDVG LQSTISLVVP WVSASHFRLT ANDKYSMAGY ITCWYQTNLV VPPNTPQTAD
MLCFVSACKD FCLRMARDTD LHIQSGPIEQ NPVENYIDEV LNEVLVVPNI KESHHTTSNS
APLLDAAETG HTSNVQPEDA IETRYVMTSQ TRDEMSIESF LGRSGCVHIS RIKVDYNDYN
GVNKNFTTWK ITLQEMAQIR RKFELFTYVR FDSEVTLVPC IAGRGDDIGH VVMQYMYVPP
GAPIPKTRND FSWQSGTNMS IFWQHGQPFP RFSLPFLSIA SAYYMFYDGY DGDNSSSKYG
SIVTNDMGTI CSRIVTEKQE HPVVITTHIY HKAKHTKAWC PRPPRAVPYT HSRVTNYVPK
TGDVTTAIVP RASMKTVGPS DLYVHVGNLI YRNLHLFNSE MHDSILVSYS SDLIIYRTNT
TGDDYIPSCN CTEATYYCKH KNRYYPIKVT PHDWYEIQES EYYPKHIQYN LLIGEGPCEP
GDCGGKLLCR HGVIGIITAG GEGHVAFTDL RQFQCAEEQG ITDYIHMLGE AFGNGFVDSV
KEQINAINPI NSISKKVIKW LLRIISAMVI IIRNSSDPQT IIATLTLIGC NGSPWRFLKE
KFCKWTQLTY IHKESDSWLK KFTEMCNAAR GLEWIGNKIS KFIDWMKSML PQAQLKVKYL
NEIKKLSLLE KQIENLRAAD NATQEKIKCE IDTLHDLSCK FLPLYAHEAK RIKVLYNKCS
NIIKQRKRSE PVAVMIHGPP GTGKSITTNF LARMITNESD VYSLPPDPKY FDGYDNQSVV
IMDDIMQNPD GEDMTLFCQM VSSVTFIPPM ADLPDKGKPF DSRFVLCSTN HSLLAPPTIS
SLPAMNRRFF FDLDIVVHDN YKDAQGKLNV SKAFQPCNVN TKIGNAKCCP FVCGKAVSFK
DRSTCSTYTL AQVYNHILEE DKRRRQVVDV MSAIFQGPIS LDAPPPPAIA DLLQSVRTPE
VIKYCQDNKW IVPAECQIER DLSIANSIIT IIANIISIAG IIFVIYKLFC TLQGPYSGEP
KPKTKMPERR VVAQGPEEEF GRSILKNNTC VITTDNGKFT GLGIYDRTLI IPTHADPGRE
VQVNGIHTKV LDSYDLYNRD GVKLEITVIQ LDRNEKFRDI RKYIPETEDD YPECNLALSA
NQVEPTIIKV GDVVSYGNIL LSGNQTARML KYNYPTKSGY CGGVLYKIGQ ILGIHVGGNG
RDGFSAMLLR SYFTDTQGQI KISKHANECG LPTIHTPSKT KLQPSVFYDV FPGSKEPAVS
RDNDPRLKVN FKEALFSKYK GNTECSLNQH MEIAIAHYSA QLITLDIDSK PIALEDSVFG
IEGLEALDLN TSAGFPYVTM GIKKRDLINN KTKDISRLKE ALDKYGVDLP MITFLKDELR
KKEKISAGKT RVIEASSIND TILFRTTFGN LFSKFHLNPG VVTGSAVGCD PETFWSKIPV
MLDGDCIMAF DYTNYDGSIH PVWFQALKKV LENLSFQSNL IDRLCYSKHL FKSTYYEVAG
GVPSGCSGTS IFNTMINNII IRTLVLDAYK NIDLDKLKII AYGDDVIFSY KYTLDMEAIA
NEGKKYGLTI TPADKSTEFK KLDYNNVTFL KRGFKQDEKH TFLIHPTFPV EEIYESIRWT
KKPSQMQEHV LSLCHLMWHN GRKVYEDFSS KIRSVSAGRA LYIPPYDLLK HEWYEKF


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