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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_HRV16              Reviewed;        2153 AA.
Q82122;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
23-MAY-2018, entry version 164.
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 16 (HRV-16).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Rhinovirus A.
NCBI_TaxID=31708;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7732663; DOI=10.1007/BF01702661;
Lee W.M., Wang W., Rueckert R.R.;
"Complete sequence of the RNA genome of human rhinovirus 16, a
clinically useful common cold virus belonging to the ICAM-1 receptor
group.";
Virus Genes 9:177-181(1995).
[2]
FUNCTION OF PROTEASE 3C.
PubMed=19403669; DOI=10.1128/JVI.01748-08;
Ghildyal R., Jordan B., Li D., Dagher H., Bardin P.G., Gern J.E.,
Jans D.A.;
"Rhinovirus 3C protease can localize in the nucleus and alter active
and passive nucleocytoplasmic transport.";
J. Virol. 83:7349-7352(2009).
[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).
[4]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-853.
PubMed=7915182; DOI=10.1016/0969-2126(93)90008-5;
Oliveira M.A., Zhao R., Lee W.M., Kremer M.J., Minor I.,
Rueckert R.R., Diana G.D., Pevear D.C., Dutko F.J., McKinlay M.A.,
Rossmann M.G.;
"The structure of human rhinovirus 16.";
Structure 1:51-68(1993).
[5]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-853, AND SEQUENCE REVISION
TO 547-548.
PubMed=9083115; DOI=10.1016/S0969-2126(97)00199-8;
Hadfield A.T., Lee W.M., Zhao R., Oliveira M.A., Minor I.,
Rueckert R.R., Rossmann M.G.;
"The refined structure of human rhinovirus 16 at 2.15-A resolution:
implications for the viral life cycle.";
Structure 5:427-441(1997).
-!- 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: 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 at high resolution;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1aym";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1ayn";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with antiviral drug VP63843
(pleconaril);
URL="http://viperdb.scripps.edu/info_page.php?VDB=1c8m";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with a two-domain fragment of its
cellular receptor ICAM1;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1d3e";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with antiviral compound pleconaril;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1ncr";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1nd2";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with antiviral compound pleconaril;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1nd3";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with antiviral compound VP61209;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1qju";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with antiviral compound WIN68934;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1qjx";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with antiviral compound VP65099;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1qjy";
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EMBL; L24917; AAA69862.1; -; Genomic_RNA.
PDB; 1AYM; X-ray; 2.15 A; 1=569-853, 2=70-330, 3=331-568.
PDB; 1AYN; X-ray; 2.90 A; 1=569-853, 2=70-330, 3=331-568.
PDB; 1C8M; X-ray; 2.80 A; 1=569-853, 2=79-330, 3=331-568, 4=2-78.
PDB; 1D3E; EM; 28.00 A; 1=570-853, 2=79-330, 3=331-568, 4=2-69.
PDB; 1NCR; X-ray; 2.70 A; A=569-853, B=70-330, C=331-568, D=2-69.
PDB; 1ND2; X-ray; 2.50 A; A=569-853, B=70-330, C=331-568, D=2-69.
PDB; 1ND3; X-ray; 2.80 A; A=569-853, B=70-330, C=331-568, D=2-69.
PDB; 1QJU; X-ray; 2.80 A; 1=569-853, 2=70-330, 3=331-568, 4=2-69.
PDB; 1QJX; X-ray; 2.80 A; 1=569-853, 2=70-330, 3=331-568, 4=2-69.
PDB; 1QJY; X-ray; 2.80 A; 1=569-853, 2=70-330, 3=331-568, 4=2-69.
PDB; 1TP7; X-ray; 2.40 A; A/B/C/D=1694-2153.
PDB; 1XR7; X-ray; 2.30 A; A/B=1694-2153.
PDB; 4K50; X-ray; 2.93 A; A/E/I/M=1694-2153.
PDBsum; 1AYM; -.
PDBsum; 1AYN; -.
PDBsum; 1C8M; -.
PDBsum; 1D3E; -.
PDBsum; 1NCR; -.
PDBsum; 1ND2; -.
PDBsum; 1ND3; -.
PDBsum; 1QJU; -.
PDBsum; 1QJX; -.
PDBsum; 1QJY; -.
PDBsum; 1TP7; -.
PDBsum; 1XR7; -.
PDBsum; 4K50; -.
ProteinModelPortal; Q82122; -.
SMR; Q82122; -.
BindingDB; Q82122; -.
ChEMBL; CHEMBL5296; -.
DrugBank; DB03017; Lauric Acid.
DrugBank; DB08231; MYRISTIC ACID.
MEROPS; C03.007; -.
PRIDE; Q82122; -.
OrthoDB; VOG0900001E; -.
BRENDA; 2.7.7.48; 2703.
EvolutionaryTrace; Q82122; -.
Proteomes; UP000007680; 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; IDA: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; IDA:UniProtKB.
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; 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.
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 2153 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426551.
CHAIN 2 853 P1. {ECO:0000250}.
/FTId=PRO_0000426552.
CHAIN 2 330 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426553.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426554.
CHAIN 70 330 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426555.
CHAIN 331 565 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426556.
CHAIN 565 853 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426557.
CHAIN 854 1412 P2. {ECO:0000250}.
/FTId=PRO_0000426558.
CHAIN 854 995 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000426559.
CHAIN 996 1090 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000040041.
CHAIN 1091 1412 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000040042.
CHAIN 1413 2153 P3. {ECO:0000250}.
/FTId=PRO_0000426560.
CHAIN 1413 1510 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426561.
CHAIN 1413 1489 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000040043.
CHAIN 1490 1510 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426562.
CHAIN 1511 2153 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426563.
CHAIN 1511 1692 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426564.
CHAIN 1693 2153 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426565.
TOPO_DOM 2 1466 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1467 1482 {ECO:0000255}.
TOPO_DOM 1483 2153 Cytoplasmic. {ECO:0000255}.
DOMAIN 1186 1346 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1511 1676 Peptidase C3.
DOMAIN 1921 2034 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
REGION 565 582 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1413 1427 Disordered. {ECO:0000250}.
ACT_SITE 871 871 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 1550 1550 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1581 1581 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1657 1657 For Protease 3C activity. {ECO:0000250}.
ACT_SITE 2020 2020 For RdRp activity. {ECO:0000250}.
SITE 330 331 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 853 854 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 995 996 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1412 1413 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1489 1490 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1510 1511 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1693 1694 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1492 1492 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
CONFLICT 547 548 KD -> NH (in Ref. 1; AAA69862).
{ECO:0000305}.
STRAND 3 5 {ECO:0000244|PDB:1ND2}.
STRAND 28 30 {ECO:0000244|PDB:1ND2}.
STRAND 33 35 {ECO:0000244|PDB:1ND2}.
HELIX 36 38 {ECO:0000244|PDB:1ND2}.
STRAND 83 87 {ECO:0000244|PDB:1AYM}.
STRAND 90 96 {ECO:0000244|PDB:1AYM}.
HELIX 103 105 {ECO:0000244|PDB:1AYM}.
TURN 113 115 {ECO:0000244|PDB:1AYM}.
HELIX 126 128 {ECO:0000244|PDB:1AYM}.
STRAND 138 140 {ECO:0000244|PDB:1AYM}.
STRAND 147 151 {ECO:0000244|PDB:1AYM}.
HELIX 153 155 {ECO:0000244|PDB:1AYM}.
HELIX 159 167 {ECO:0000244|PDB:1AYM}.
STRAND 168 180 {ECO:0000244|PDB:1AYM}.
STRAND 188 197 {ECO:0000244|PDB:1AYM}.
STRAND 204 206 {ECO:0000244|PDB:1AYM}.
HELIX 213 216 {ECO:0000244|PDB:1AYM}.
HELIX 219 221 {ECO:0000244|PDB:1AYM}.
TURN 225 227 {ECO:0000244|PDB:1AYM}.
HELIX 239 241 {ECO:0000244|PDB:1AYM}.
TURN 242 245 {ECO:0000244|PDB:1AYM}.
HELIX 248 253 {ECO:0000244|PDB:1AYM}.
STRAND 254 260 {ECO:0000244|PDB:1AYM}.
TURN 261 263 {ECO:0000244|PDB:1AYM}.
STRAND 265 271 {ECO:0000244|PDB:1AYM}.
STRAND 276 280 {ECO:0000244|PDB:1AYM}.
TURN 282 284 {ECO:0000244|PDB:1AYM}.
STRAND 288 299 {ECO:0000244|PDB:1AYM}.
STRAND 307 323 {ECO:0000244|PDB:1AYM}.
TURN 338 341 {ECO:0000244|PDB:1AYM}.
STRAND 353 355 {ECO:0000244|PDB:1AYM}.
STRAND 369 372 {ECO:0000244|PDB:1ND2}.
HELIX 374 377 {ECO:0000244|PDB:1AYM}.
TURN 389 393 {ECO:0000244|PDB:1AYM}.
HELIX 395 398 {ECO:0000244|PDB:1AYM}.
STRAND 399 402 {ECO:0000244|PDB:1AYM}.
STRAND 406 409 {ECO:0000244|PDB:1C8M}.
STRAND 411 416 {ECO:0000244|PDB:1AYM}.
TURN 422 426 {ECO:0000244|PDB:1AYM}.
HELIX 428 433 {ECO:0000244|PDB:1AYM}.
STRAND 436 441 {ECO:0000244|PDB:1AYM}.
STRAND 443 449 {ECO:0000244|PDB:1AYM}.
STRAND 458 464 {ECO:0000244|PDB:1AYM}.
STRAND 466 468 {ECO:0000244|PDB:1AYM}.
HELIX 474 478 {ECO:0000244|PDB:1AYM}.
STRAND 480 486 {ECO:0000244|PDB:1AYM}.
STRAND 488 490 {ECO:0000244|PDB:1AYM}.
STRAND 492 497 {ECO:0000244|PDB:1AYM}.
STRAND 502 504 {ECO:0000244|PDB:1AYM}.
STRAND 506 509 {ECO:0000244|PDB:1AYM}.
HELIX 512 514 {ECO:0000244|PDB:1ND2}.
STRAND 518 525 {ECO:0000244|PDB:1AYM}.
STRAND 537 545 {ECO:0000244|PDB:1AYM}.
STRAND 550 554 {ECO:0000244|PDB:1AYM}.
HELIX 570 579 {ECO:0000244|PDB:1AYM}.
STRAND 582 584 {ECO:0000244|PDB:1AYM}.
HELIX 605 607 {ECO:0000244|PDB:1AYM}.
HELIX 615 618 {ECO:0000244|PDB:1AYM}.
HELIX 631 633 {ECO:0000244|PDB:1AYM}.
HELIX 635 639 {ECO:0000244|PDB:1AYM}.
STRAND 643 651 {ECO:0000244|PDB:1AYM}.
HELIX 656 659 {ECO:0000244|PDB:1AYM}.
STRAND 660 665 {ECO:0000244|PDB:1AYM}.
HELIX 672 678 {ECO:0000244|PDB:1AYM}.
STRAND 681 701 {ECO:0000244|PDB:1AYM}.
STRAND 707 713 {ECO:0000244|PDB:1AYM}.
HELIX 726 729 {ECO:0000244|PDB:1AYM}.
STRAND 731 739 {ECO:0000244|PDB:1AYM}.
STRAND 746 749 {ECO:0000244|PDB:1AYM}.
STRAND 754 760 {ECO:0000244|PDB:1AYM}.
STRAND 764 769 {ECO:0000244|PDB:1AYM}.
TURN 776 779 {ECO:0000244|PDB:1AYM}.
STRAND 784 789 {ECO:0000244|PDB:1AYM}.
STRAND 798 816 {ECO:0000244|PDB:1AYM}.
HELIX 838 840 {ECO:0000244|PDB:1AYM}.
STRAND 847 849 {ECO:0000244|PDB:1AYM}.
STRAND 1695 1701 {ECO:0000244|PDB:1XR7}.
HELIX 1702 1705 {ECO:0000244|PDB:1XR7}.
TURN 1722 1726 {ECO:0000244|PDB:1XR7}.
HELIX 1747 1751 {ECO:0000244|PDB:1XR7}.
HELIX 1752 1754 {ECO:0000244|PDB:1XR7}.
HELIX 1765 1779 {ECO:0000244|PDB:1XR7}.
HELIX 1790 1795 {ECO:0000244|PDB:1XR7}.
STRAND 1805 1807 {ECO:0000244|PDB:1XR7}.
TURN 1811 1817 {ECO:0000244|PDB:1XR7}.
HELIX 1820 1823 {ECO:0000244|PDB:1XR7}.
TURN 1826 1829 {ECO:0000244|PDB:1XR7}.
HELIX 1832 1841 {ECO:0000244|PDB:1XR7}.
STRAND 1847 1851 {ECO:0000244|PDB:1XR7}.
STRAND 1854 1856 {ECO:0000244|PDB:1TP7}.
HELIX 1859 1862 {ECO:0000244|PDB:1XR7}.
STRAND 1868 1871 {ECO:0000244|PDB:1XR7}.
HELIX 1874 1893 {ECO:0000244|PDB:1XR7}.
TURN 1897 1900 {ECO:0000244|PDB:1XR7}.
HELIX 1907 1917 {ECO:0000244|PDB:1XR7}.
STRAND 1920 1930 {ECO:0000244|PDB:1XR7}.
HELIX 1931 1934 {ECO:0000244|PDB:1XR7}.
HELIX 1937 1949 {ECO:0000244|PDB:1XR7}.
HELIX 1958 1961 {ECO:0000244|PDB:1XR7}.
STRAND 1962 1967 {ECO:0000244|PDB:1XR7}.
STRAND 1970 1977 {ECO:0000244|PDB:1XR7}.
HELIX 1985 2004 {ECO:0000244|PDB:1XR7}.
HELIX 2010 2012 {ECO:0000244|PDB:1XR7}.
STRAND 2014 2018 {ECO:0000244|PDB:1XR7}.
STRAND 2021 2028 {ECO:0000244|PDB:1XR7}.
HELIX 2032 2037 {ECO:0000244|PDB:1XR7}.
HELIX 2038 2042 {ECO:0000244|PDB:1XR7}.
STRAND 2046 2049 {ECO:0000244|PDB:1XR7}.
TURN 2060 2062 {ECO:0000244|PDB:1XR7}.
STRAND 2068 2072 {ECO:0000244|PDB:1XR7}.
STRAND 2079 2083 {ECO:0000244|PDB:1XR7}.
HELIX 2086 2093 {ECO:0000244|PDB:1XR7}.
STRAND 2095 2097 {ECO:0000244|PDB:1XR7}.
HELIX 2099 2101 {ECO:0000244|PDB:1XR7}.
HELIX 2102 2113 {ECO:0000244|PDB:1XR7}.
HELIX 2114 2116 {ECO:0000244|PDB:1XR7}.
HELIX 2118 2128 {ECO:0000244|PDB:1XR7}.
HELIX 2132 2135 {ECO:0000244|PDB:1XR7}.
HELIX 2142 2150 {ECO:0000244|PDB:1XR7}.
SEQUENCE 2153 AA; 242244 MW; 6B11D0D93DF11C04 CRC64;
MGAQVSRQNV GTHSTQNMVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP SKFTDPVKDV
LEKGIPTLQS PSVEACGYSD RIIQITRGDS TITSQDVANA VVGYGVWPHY LTPQDATAID
KPTQPDTSSN RFYTLDSKMW NSTSKGWWWK LPDALKDMGI FGENMFYHFL GRSGYTVHVQ
CNASKFHQGT LLVVMIPEHQ LATVNKGNVN AGYKYTHPGE AGREVGTQVE NEKQPSDDNW
LNFDGTLLGN LLIFPHQFIN LRSNNSATLI VPYVNAVPMD SMVRHNNWSL VIIPVCQLQS
NNISNIVPIT VSISPMCAEF SGARAKTVVQ GLPVYVTPGS GQFMTTDDMQ SPCALPWYHP
TKEIFIPGEV KNLIEMCQVD TLIPINSTQS NIGNVSMYTV TLSPQTKLAE EIFAIKVDIA
SHPLATTLIG EIASYFTHWT GSLRFSFMFC GTANTTLKVL LAYTPPGIGK PRSRKEAMLG
THVVWDVGLQ STVSLVVPWI SASQYRFTTP DTYSSAGYIT CWYQTNFVVP PNTPNTAEML
CFVSGCKDFC LRMARDTDLH KQTGPITQNP VERYVDEVLN EVLVVPNINQ SHPTTSNAAP
VLDAAETGHT NKIQPEDTIE TRYVQSSQTL DEMSVESFLG RSGCIHESVL DIVDNYNDQS
FTKWNINLQE MAQIRRKFEM FTYARFDSEI TMVPSVAAKD GHIGHIVMQY MYVPPGAPIP
TTRDDYAWQS GTNASVFWQH GQPFPRFSLP FLSIASAYYM FYDGYDGDTY KSRYGTVVTN
DMGTLCSRIV TSEQLHKVKV VTRIYHKAKH TKAWCPRPPR AVQYSHTHTT NYKLSSEVHN
DVAIRPRTNL TTVGPSDMYV HVGNLIYRNL HLFNSDIHDS ILVSYSSDLI IYRTSTQGDG
YIPTCNCTEA TYYCKHKNRY YPINVTPHDW YEIQESEYYP KHIQYNLLIG EGPCEPGDCG
GKLLCKHGVI GIITAGGEGH VAFIDLRHFH CAEEQGITDY IHMLGEAFGS GFVDSVKDQI
NSINPINNIS SKMVKWMLRI ISAMVIIIRN SSDPQTIIAT LTLIGCNGSP WRFLKEKFCK
WTQLTYIHKE SDSWLKKFTE MCNAARGLEW IGNKISKFID WMKSMLPQAQ LKVKYLSELK
KLNFLEKQVE NLRAADTNTQ EKIKCEIDTL HDLSCKFLPL YASEAKRIKV LYHKCTNIIK
QKKRSEPVAV MIHGPPGTGK SITTSFLARM ITNESDIYSL PPDPKYFDGY DNQSVVIMDD
IMQNPGGEDM TLFCQMVSSV TFIPPMADLP DKGKPFDSRF VLCSTNHSLL APPTISSLPA
MNRRFYLDLD ILVHDNYKDN QGKLDVSRAF RLCDVDSKIG NAKCCPFVCG KAVTFKDRNT
CRTYSLSQIY NQILEEDKRR RQVVDVMSAI FQGPISMDKP PPPAITDLLR SVRTPEVIKY
CQDNKWIVPA DCQIERDLNI ANSIITIIAN IISIAGIIYI IYKLFCSLQG PYSGEPKPKT
KVPERRVVAQ GPEEEFGMSI IKNNTCVVTT TNGKFTGLGI YDRILILPTH ADPGSEIQVN
GIHTKVLDSY DLFNKEGVKL EITVLKLDRN EKFRDIRKYI PESEDDYPEC NLALVANQTE
PTIIKVGDVV SYGNILLSGT QTARMLKYNY PTKSGYCGGV LYKIGQILGI HVGGNGRDGF
SSMLLRSYFT EQQGQIQISK HVKDVGLPSI HTPTKTKLQP SVFYDIFPGS KEPAVLTEKD
PRLKVDFDSA LFSKYKGNTE CSLNEHIQVA VAHYSAQLAT LDIDPQPIAM EDSVFGMDGL
EALDLNTSAG YPYVTLGIKK KDLINNKTKD ISKLKLALDK YDVDLPMITF LKDELRKKDK
IAAGKTRVIE ASSINDTILF RTVYGNLFSK FHLNPGVVTG CAVGCDPETF WSKIPLMLDG
DCIMAFDYTN YDGSIHPIWF KALGMVLDNL SFNPTLINRL CNSKHIFKST YYEVEGGVPS
GCSGTSIFNS MINNIIIRTL VLDAYKHIDL DKLKIIAYGD DVIFSYKYKL DMEAIAKEGQ
KYGLTITPAD KSSEFKELDY GNVTFLKRGF RQDDKYKFLI HPTFPVEEIY ESIRWTKKPS
QMQEHVLSLC HLMWHNGPEI YKDFETKIRS VSAGRALYIP PYELLRHEWY EKF


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