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 POLG_HRV3               Reviewed;        2178 AA.
Q82081; A5GZD4; A7KC14;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
24-JUL-2013, sequence version 4.
25-OCT-2017, entry version 120.
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 3 (HRV-3).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus.
NCBI_TaxID=44130;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=17477878; DOI=10.1186/1743-422X-4-40;
Kistler A.L., Webster D.R., Rouskin S., Magrini V., Credle J.J.,
Schnurr D.P., Boushey H.A., Mardis E.R., Li H., DeRisi J.L.;
"Genome-wide diversity and selective pressure in the human
rhinovirus.";
Virol. J. 4:40-40(2007).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Tapparel C., Junier T., Gerlach D., Cordey S., Van Belle S.,
Perrin L., Zdobnov E.M., Kaiser L.;
"New complete genome sequences of human rhinoviruses shed light on
their phylogeny and genomic features.";
BMC Genomics 8:224-224(2007).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-855, AND X-RAY CRYSTALLOGRAPHY
(3.0 ANGSTROMS).
PubMed=8939746; DOI=10.1016/S0969-2126(96)00128-1;
Zhao R., Pevear D.C., Kremer M.J., Giranda V.L., Kofron J.A.,
Kuhn R.J., Rossmann M.G.;
"Human rhinovirus 3 at 3.0-A resolution.";
Structure 4:1205-1220(1996).
[4]
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 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.
-!- 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: Myristoylation of VP4 is required during RNA encapsidation
and formation of the mature virus particle. {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: 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=1rhi";
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EMBL; DQ473485; ABF51179.1; -; Genomic_RNA.
EMBL; EF173422; ABO69378.1; -; Genomic_RNA.
EMBL; U60874; AAB05616.1; -; Genomic_RNA.
PDB; 1RHI; X-ray; 3.00 A; 1=568-855, 2=70-331, 3=332-567, 4=2-69.
PDBsum; 1RHI; -.
ProteinModelPortal; Q82081; -.
SMR; Q82081; -.
MEROPS; C03.013; -.
OrthoDB; VOG0900006M; -.
EvolutionaryTrace; Q82081; -.
Proteomes; UP000013737; Genome.
Proteomes; UP000165566; 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; 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; 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.
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 2178 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426521.
CHAIN 2 855 P1. {ECO:0000250}.
/FTId=PRO_0000426522.
CHAIN 2 331 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426523.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426524.
CHAIN 70 331 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426525.
CHAIN 332 563 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426526.
CHAIN 564 857 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426527.
CHAIN 858 1428 P2. {ECO:0000250}.
/FTId=PRO_0000426528.
CHAIN 858 1001 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000423099.
CHAIN 1002 1098 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000423100.
CHAIN 1100 1428 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000426529.
CHAIN 1429 2178 P3. {ECO:0000250}.
/FTId=PRO_0000426530.
CHAIN 1429 1536 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426531.
CHAIN 1429 1513 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000423102.
CHAIN 1514 1536 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426532.
CHAIN 1537 2178 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426533.
CHAIN 1537 1717 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426534.
CHAIN 1718 2178 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426535.
TOPO_DOM 2 1490 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1491 1506 {ECO:0000255}.
TOPO_DOM 1507 2178 Cytoplasmic. {ECO:0000255}.
DOMAIN 1204 1360 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1537 1701 Peptidase C3.
DOMAIN 1946 2059 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
REGION 564 584 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1429 1450 Disordered. {ECO:0000250}.
ACT_SITE 875 875 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 893 893 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 964 964 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 1576 1576 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1607 1607 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1682 1682 For Protease 3C activity. {ECO:0000250}.
ACT_SITE 2045 2045 For RdRp activity. {ECO:0000250}.
SITE 69 70 Cleavage; by autolysis. {ECO:0000255}.
SITE 331 332 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 857 858 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 1001 1002 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1428 1429 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1513 1514 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1536 1537 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1718 1719 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1516 1516 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
VARIANT 87 87 L -> M.
VARIANT 98 98 A -> R.
VARIANT 260 260 L -> M.
VARIANT 475 475 E -> K.
VARIANT 523 523 Q -> L.
VARIANT 846 846 I -> V.
VARIANT 1349 1349 M -> L.
VARIANT 1389 1389 I -> V.
VARIANT 1703 1703 R -> Q.
VARIANT 1925 1925 E -> G.
VARIANT 1978 1978 Q -> H.
STRAND 33 35 {ECO:0000244|PDB:1RHI}.
HELIX 36 38 {ECO:0000244|PDB:1RHI}.
HELIX 51 54 {ECO:0000244|PDB:1RHI}.
STRAND 57 59 {ECO:0000244|PDB:1RHI}.
STRAND 83 87 {ECO:0000244|PDB:1RHI}.
STRAND 90 96 {ECO:0000244|PDB:1RHI}.
HELIX 103 105 {ECO:0000244|PDB:1RHI}.
TURN 113 115 {ECO:0000244|PDB:1RHI}.
HELIX 126 128 {ECO:0000244|PDB:1RHI}.
STRAND 138 140 {ECO:0000244|PDB:1RHI}.
STRAND 147 151 {ECO:0000244|PDB:1RHI}.
HELIX 153 155 {ECO:0000244|PDB:1RHI}.
HELIX 159 165 {ECO:0000244|PDB:1RHI}.
STRAND 168 180 {ECO:0000244|PDB:1RHI}.
STRAND 188 197 {ECO:0000244|PDB:1RHI}.
STRAND 203 205 {ECO:0000244|PDB:1RHI}.
HELIX 213 216 {ECO:0000244|PDB:1RHI}.
HELIX 219 221 {ECO:0000244|PDB:1RHI}.
TURN 238 244 {ECO:0000244|PDB:1RHI}.
HELIX 247 252 {ECO:0000244|PDB:1RHI}.
STRAND 253 259 {ECO:0000244|PDB:1RHI}.
TURN 260 262 {ECO:0000244|PDB:1RHI}.
STRAND 264 270 {ECO:0000244|PDB:1RHI}.
STRAND 275 279 {ECO:0000244|PDB:1RHI}.
STRAND 281 284 {ECO:0000244|PDB:1RHI}.
STRAND 286 298 {ECO:0000244|PDB:1RHI}.
STRAND 307 323 {ECO:0000244|PDB:1RHI}.
TURN 339 342 {ECO:0000244|PDB:1RHI}.
STRAND 354 356 {ECO:0000244|PDB:1RHI}.
TURN 374 379 {ECO:0000244|PDB:1RHI}.
STRAND 390 392 {ECO:0000244|PDB:1RHI}.
HELIX 395 398 {ECO:0000244|PDB:1RHI}.
STRAND 399 402 {ECO:0000244|PDB:1RHI}.
STRAND 410 415 {ECO:0000244|PDB:1RHI}.
HELIX 421 423 {ECO:0000244|PDB:1RHI}.
HELIX 427 432 {ECO:0000244|PDB:1RHI}.
STRAND 435 440 {ECO:0000244|PDB:1RHI}.
STRAND 442 448 {ECO:0000244|PDB:1RHI}.
STRAND 457 463 {ECO:0000244|PDB:1RHI}.
HELIX 473 476 {ECO:0000244|PDB:1RHI}.
STRAND 479 485 {ECO:0000244|PDB:1RHI}.
STRAND 487 489 {ECO:0000244|PDB:1RHI}.
STRAND 491 496 {ECO:0000244|PDB:1RHI}.
STRAND 501 503 {ECO:0000244|PDB:1RHI}.
STRAND 505 508 {ECO:0000244|PDB:1RHI}.
HELIX 511 513 {ECO:0000244|PDB:1RHI}.
STRAND 517 524 {ECO:0000244|PDB:1RHI}.
STRAND 536 544 {ECO:0000244|PDB:1RHI}.
STRAND 549 553 {ECO:0000244|PDB:1RHI}.
STRAND 585 587 {ECO:0000244|PDB:1RHI}.
HELIX 604 606 {ECO:0000244|PDB:1RHI}.
HELIX 614 616 {ECO:0000244|PDB:1RHI}.
HELIX 630 632 {ECO:0000244|PDB:1RHI}.
HELIX 634 637 {ECO:0000244|PDB:1RHI}.
STRAND 642 651 {ECO:0000244|PDB:1RHI}.
HELIX 660 663 {ECO:0000244|PDB:1RHI}.
STRAND 665 669 {ECO:0000244|PDB:1RHI}.
STRAND 673 676 {ECO:0000244|PDB:1RHI}.
HELIX 677 683 {ECO:0000244|PDB:1RHI}.
STRAND 686 702 {ECO:0000244|PDB:1RHI}.
STRAND 714 720 {ECO:0000244|PDB:1RHI}.
HELIX 733 736 {ECO:0000244|PDB:1RHI}.
STRAND 738 740 {ECO:0000244|PDB:1RHI}.
STRAND 742 746 {ECO:0000244|PDB:1RHI}.
STRAND 749 755 {ECO:0000244|PDB:1RHI}.
STRAND 760 766 {ECO:0000244|PDB:1RHI}.
STRAND 770 774 {ECO:0000244|PDB:1RHI}.
STRAND 776 778 {ECO:0000244|PDB:1RHI}.
HELIX 784 786 {ECO:0000244|PDB:1RHI}.
STRAND 790 795 {ECO:0000244|PDB:1RHI}.
STRAND 804 822 {ECO:0000244|PDB:1RHI}.
SEQUENCE 2178 AA; 242794 MW; 0DFED5280AF25CCF CRC64;
MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASSS SAGQSFSMDP SKFTEPVKDL
MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA IVCYAEWPEY LSDNDASDVN
KTSKPDISVC RFYTLDSKTW KATSKGWCWK LPDALKDMGV FGQNMFYHSL GRTGYTIHVQ
CNATKFHSGC LLVVVIPEHQ LASHEGGTVS VKYKYTHPGD RGIDLDTVEV AGGPTSDAIY
NMDGTLLGNL LIFPHQFINL RTNNTATIVV PYINSVPIDS MTRHNNVSLM VVPIAPLNAP
TGSSPTLPVT VTIAPMCTEF TGIRSRSIVP QGLPTTTLPG SGQFLTTDDR QSPSALPSYE
PTPRIHIPGK VRNLLEIIQV GTLIPMNNTG TNDNVTNYLI PLHADRQNEQ IFGTKLYIGD
GVFKTTLLGE IAQYYTHWSG SLRISLMYTG PALSSAKIIL AYTPPGTRGP EDRKEAMLGT
HVVWDIGLQS TIVMTIPWTS GVQFRYTDPD TYTSAGYLSC WYQTSLILPP QTSGQVYLLS
FISACPDFKL RLMKDTQTIS QTDALTEGLS DELEEVIVEK TKQTLASVSS GPKHTQSVPA
LTANETGATL PTRPSDNVET RTTYMHFNGS ETDVESFLGR AACVHVTEIK NKNAAGLDNH
RKEGLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT ASQPEASSYS SNLTVQAMYV
PPGAPNPKEW DDYTWQSASN PSVFFKVGET SRFSVPFVGI ASAYNCFYDG YSHDDPDTPY
GITVLNHMGS MAFRVVNEHD VHTTIVKIRV YHRAKHVEAW IPRAPRALPY VSIGRTNYPR
DSKTIIKKRT NIKTYGLGPR FGGVFTSNVK IINYHLMTPD DHLNLVAPYP NRDLAVVATG
AHGAETIPHC NCTSGVYYSR YYRKFYPIIC ERPTNIWIEG SSYYPSRYQA GVMKGVGPAE
PGDCGGILRC IHGPIGLLTA GGGGYVCFAD IRQLDFIADE QGLGDYITSL GRAFGTGFTD
QISAKVCELQ DVAKDFLTTK VLSKVVKMIS ALVIICRNHD DLVTVTATLA LLGCDGSPWR
FLKMYISKHF QVPYIERQAN DGWFRKFNDA CNAAKGLEWI ANKISKLIEW IKNKVLPQAR
EKLEFCSKLK QLDILERQIA SIHDSNPTQE KREQLFNNVL WLEQMSQKFS PLYASEAKRI
RDLKNKITNY MQFKSKQRTE PVCVLIHGTP GSGKSLTTSI VGRALAEHFN SSVYSLPPDP
KHFDGYQQQE VVIMDDLNQN PDGQDISMFC QMVSSVDFLP PMASLDNKGM LFTSNFVLAS
TNSNTLSPPT ILNPEALIRR FGFDLDICMH STYTKNGKLN AAMATSLCKD CHQPSNFKKC
CPLVCGKAIS LVDRVSNVRF SIDQLVTAII NDYKNKVKIT DSLEVLFQGP VYKDLEIDIC
NTPPPECISD LLKSVDSEEV REYCKKKKWI IPQISTNIER AVNQASMIIN TILMFVSTLG
IVYVIYKLFA QTQGPYSGNP VHNKLKPPTL KPVVVQGPNT EFALSLLRKN ILTITTEKGE
FTSLGIHDRI CVLPTHAQPG DNVLVNGQKI QIKDKYKLVD PDNTNLELTI IELDRNEKFR
DIRGFISEDL EGLDATLVVH SNGFTNTILD VGPITMAGLI NLSNTPTTRM IRYDYPTKTG
QCGGVLCTTG KIFGIHVGGN GRRGFSAQLK KQYFVEKQGL IVSKQKVRDI GLNPINTPTK
TKLHPSVFYN VFPGSKQPAV LNDNDPRLEV KLAESLFSKY KGNVQMEPTE NMLIAVDHYA
GQLMSLDIST KELTLKEALY GVDGLEPIDV TTSAGYPYVS LGIKKRDILN KETQDVEKMK
FYLDKYGIDL PLVTYIKDEL RSVDKVRLGK SRLIEASSLN DSVNMRMKLG NLYKAFHQNP
GIITESAVGC DPDVFWSVIP CLMDGHLMAF DYSNFDASLS PVWFECLEKV LNKLGFKQPS
LIQSICNTHH IFRDEIYRVE GGMPSGCSGT SIFNSMINNI IIRTLILDAY KGIDLDSLRI
LAYGDDLIVS YPFELDSNIL AAIGKNYGLT ITPPDKSDAF TKITWENITF LKRYFRPDPQ
FPFLIHPVMP MQDIYESIRW TRDPRNTQDH VRSLCMLAWH SGEKDYNDFI TKIRTTDIGK
CLNLPEYSVL RRRWLDLF


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