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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_HRV2               Reviewed;        2150 AA.
P04936;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 182.
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 2 (HRV-2).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Rhinovirus A.
NCBI_TaxID=12130;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2987843; DOI=10.1093/nar/13.6.2111;
Skern T., Sommergruber W., Blaas D., Gruendler P., Fraundorfer F.,
Pieler C., Fogy I., Kuechler E.;
"Human rhinovirus 2: complete nucleotide sequence and proteolytic
processing signals in the capsid protein region.";
Nucleic Acids Res. 13:2111-2126(1985).
[2]
SEQUENCE REVISION.
Kuechler E.;
Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION OF THE LEADER PROTEASE.
PubMed=11034318; DOI=10.1016/S0014-5793(00)01928-1;
Glaser W., Skern T.;
"Extremely efficient cleavage of eIF4G by picornaviral proteinases L
and 2A in vitro.";
FEBS Lett. 480:151-155(2000).
[4]
FUNCTION OF VP1 AND VP4.
PubMed=12191477; DOI=10.1016/S1097-2765(02)00603-2;
Hewat E.A., Neumann E., Blaas D.;
"The concerted conformational changes during human rhinovirus 2
uncoating.";
Mol. Cell 10:317-326(2002).
[5]
FUNCTION OF PROTEASE 2A.
PubMed=20622012; DOI=10.1074/jbc.M110.143404;
Park N., Skern T., Gustin K.E.;
"Specific cleavage of the nuclear pore complex protein Nup62 by a
viral protease.";
J. Biol. Chem. 285:28796-28805(2010).
[6]
REVIEW.
PubMed=20629045; DOI=10.1002/rmv.654;
Fuchs R., Blaas D.;
"Uncoating of human rhinoviruses.";
Rev. Med. Virol. 20:281-297(2010).
[7]
REVIEW.
PubMed=23227049; DOI=10.1155/2012/826301;
Fuchs R., Blaas D.;
"Productive entry pathways of human rhinoviruses.";
Adv. Virol. 2012:826301-826301(2012).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-239.
PubMed=1338980; DOI=10.1002/pro.5560010909;
Tormo J., Stadler E., Skern T., Auer H., Kanzler O., Betzel C.,
Blaas D., Fita I.;
"Three-dimensional structure of the Fab fragment of a neutralizing
antibody to human rhinovirus serotype 2.";
Protein Sci. 1:1154-1161(1992).
[9]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 851-992.
PubMed=10523291; DOI=10.1093/emboj/18.20.5463;
Petersen J.F., Cherney M.M., Liebig H.D., Skern T., Kuechler E.,
James M.N.;
"The structure of the 2A proteinase from a common cold virus: a
proteinase responsible for the shut-off of host-cell protein
synthesis.";
EMBO J. 18:5463-5475(1999).
[10]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1508-1687.
PubMed=10500114; DOI=10.1073/pnas.96.20.11000;
Matthews D.A., Dragovich P.S., Webber S.E., Fuhrman S.A., Patick A.K.,
Zalman L.S., Hendrickson T.F., Love R.A., Prins T.J., Marakovits J.T.,
Zhou R., Tikhe J., Ford C.E., Meador J.W., Ferre R.A., Brown E.L.,
Binford S.L., Brothers M.A., DeLisle D.M., Worland S.T.;
"Structure-assisted design of mechanism-based irreversible inhibitors
of human rhinovirus 3C protease with potent antiviral activity against
multiple rhinovirus serotypes.";
Proc. Natl. Acad. Sci. U.S.A. 96:11000-11007(1999).
[11]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 71-856.
PubMed=10903863; DOI=10.1006/jmbi.2000.3943;
Verdaguer N., Blaas D., Fita I.;
"Structure of human rhinovirus serotype 2 (HRV2).";
J. Mol. Biol. 300:1179-1194(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 VLDLR 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
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). Interacts with host VLDLR.
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 associated with cellular receptor;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1fpn";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure complexed with cellular receptor fragment;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1v9u";
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EMBL; X02316; CAA26181.1; -; Genomic_RNA.
PIR; A03902; GNNYH2.
PDB; 1A3R; X-ray; 2.10 A; P=225-239.
PDB; 1CQQ; X-ray; 1.85 A; A=1508-1687.
PDB; 1FPN; X-ray; 2.60 A; 1=568-856, 2=70-330, 3=331-567, 4=2-69.
PDB; 1V9U; X-ray; 3.60 A; 1=568-856, 2=70-330, 3=331-567, 4=2-69.
PDB; 2HRV; X-ray; 1.95 A; A/B=851-992.
PDB; 2XYA; X-ray; 2.40 A; A=1508-1687.
PDB; 3DPR; X-ray; 3.50 A; A=568-856, B=70-330, C=331-567, D=2-69.
PDB; 3TN9; X-ray; 3.00 A; 1=568-856, 2=70-330, 3=331-567.
PDB; 3VDD; X-ray; 3.20 A; A=568-850, B=70-330, C=331-567, D=1-69.
PDB; 4L3B; X-ray; 6.50 A; A=568-856, B=70-330, C=331-567.
PDB; 5FX5; X-ray; 1.70 A; A=1508-1687.
PDB; 5FX6; X-ray; 1.45 A; A=1508-1687.
PDB; 6FFN; X-ray; 1.75 A; A=1508-1687.
PDB; 6FFS; X-ray; 1.86 A; A=1508-1687.
PDBsum; 1A3R; -.
PDBsum; 1CQQ; -.
PDBsum; 1FPN; -.
PDBsum; 1V9U; -.
PDBsum; 2HRV; -.
PDBsum; 2XYA; -.
PDBsum; 3DPR; -.
PDBsum; 3TN9; -.
PDBsum; 3VDD; -.
PDBsum; 4L3B; -.
PDBsum; 5FX5; -.
PDBsum; 5FX6; -.
PDBsum; 6FFN; -.
PDBsum; 6FFS; -.
ProteinModelPortal; P04936; -.
SMR; P04936; -.
DrugBank; DB02313; 4-{2-(4-Fluoro-Benzyl)-6-Methyl-5-[(5-Methyl-Isoxazole-3-Carbonyl)-Amino]-4-Oxo-Heptanoylamino}-5-(2-Oxo-Pyrrolidin-3-Yl)-Pentanoic Acid Ethyl Ester.
DrugBank; DB03017; Lauric Acid.
MEROPS; C03.007; -.
PRIDE; P04936; -.
OrthoDB; VOG0900001E; -.
SABIO-RK; P04936; -.
EvolutionaryTrace; P04936; -.
Proteomes; UP000007682; 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; IDA:UniProtKB.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO: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; 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 2150 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426506.
CHAIN 2 844 P1. {ECO:0000250}.
/FTId=PRO_0000426507.
CHAIN 2 330 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426508.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426509.
CHAIN 70 330 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426510.
CHAIN 331 565 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426511.
CHAIN 565 850 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426512.
CHAIN 851 1409 P2. {ECO:0000250}.
/FTId=PRO_0000426513.
CHAIN 851 992 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000426514.
CHAIN 993 1087 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000040015.
CHAIN 1088 1409 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000040016.
CHAIN 1410 2150 P3. {ECO:0000250}.
/FTId=PRO_0000426515.
CHAIN 1410 1507 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426516.
CHAIN 1410 1486 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000040017.
CHAIN 1487 1507 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426517.
CHAIN 1508 2150 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426518.
CHAIN 1508 1689 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426519.
CHAIN 1690 2150 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426520.
TOPO_DOM 2 1463 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1464 1479 {ECO:0000255}.
TOPO_DOM 1480 2150 Cytoplasmic. {ECO:0000255}.
DOMAIN 1181 1343 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1508 1673 Peptidase C3.
DOMAIN 1918 2031 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
REGION 565 581 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1410 1424 Disordered. {ECO:0000250}.
ACT_SITE 868 868 For Protease 2A activity.
ACT_SITE 885 885 For Protease 2A activity.
ACT_SITE 956 956 For Protease 2A activity.
ACT_SITE 1547 1547 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1578 1578 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1654 1654 For Protease 3C activity. {ECO:0000305}.
ACT_SITE 2017 2017 For RdRp activity. {ECO:0000250}.
SITE 330 331 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 850 851 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 992 993 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1409 1410 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1486 1487 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1507 1508 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1690 1691 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1489 1489 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
STRAND 33 35 {ECO:0000244|PDB:1FPN}.
HELIX 36 38 {ECO:0000244|PDB:1FPN}.
TURN 52 54 {ECO:0000244|PDB:3VDD}.
STRAND 83 86 {ECO:0000244|PDB:1FPN}.
STRAND 91 96 {ECO:0000244|PDB:1FPN}.
HELIX 103 105 {ECO:0000244|PDB:1FPN}.
TURN 113 115 {ECO:0000244|PDB:1FPN}.
STRAND 117 119 {ECO:0000244|PDB:3TN9}.
HELIX 126 128 {ECO:0000244|PDB:1FPN}.
STRAND 138 140 {ECO:0000244|PDB:1FPN}.
STRAND 147 151 {ECO:0000244|PDB:1FPN}.
HELIX 153 155 {ECO:0000244|PDB:1FPN}.
HELIX 159 167 {ECO:0000244|PDB:1FPN}.
STRAND 168 180 {ECO:0000244|PDB:1FPN}.
STRAND 187 197 {ECO:0000244|PDB:1FPN}.
STRAND 203 208 {ECO:0000244|PDB:1FPN}.
HELIX 213 216 {ECO:0000244|PDB:1FPN}.
HELIX 219 221 {ECO:0000244|PDB:1FPN}.
HELIX 233 235 {ECO:0000244|PDB:1A3R}.
HELIX 241 243 {ECO:0000244|PDB:1FPN}.
TURN 244 247 {ECO:0000244|PDB:1FPN}.
HELIX 253 255 {ECO:0000244|PDB:1FPN}.
STRAND 256 262 {ECO:0000244|PDB:1FPN}.
TURN 263 265 {ECO:0000244|PDB:1FPN}.
STRAND 267 273 {ECO:0000244|PDB:1FPN}.
STRAND 278 282 {ECO:0000244|PDB:1FPN}.
TURN 284 286 {ECO:0000244|PDB:1FPN}.
STRAND 290 305 {ECO:0000244|PDB:1FPN}.
STRAND 309 325 {ECO:0000244|PDB:1FPN}.
TURN 338 341 {ECO:0000244|PDB:1FPN}.
STRAND 353 355 {ECO:0000244|PDB:1FPN}.
STRAND 367 372 {ECO:0000244|PDB:3DPR}.
HELIX 374 377 {ECO:0000244|PDB:1FPN}.
TURN 389 393 {ECO:0000244|PDB:1FPN}.
HELIX 395 398 {ECO:0000244|PDB:1FPN}.
STRAND 399 403 {ECO:0000244|PDB:1FPN}.
STRAND 411 416 {ECO:0000244|PDB:1FPN}.
STRAND 418 421 {ECO:0000244|PDB:3VDD}.
HELIX 424 426 {ECO:0000244|PDB:1FPN}.
HELIX 428 433 {ECO:0000244|PDB:1FPN}.
STRAND 436 441 {ECO:0000244|PDB:1FPN}.
STRAND 443 449 {ECO:0000244|PDB:1FPN}.
STRAND 456 464 {ECO:0000244|PDB:1FPN}.
STRAND 466 468 {ECO:0000244|PDB:1FPN}.
HELIX 474 478 {ECO:0000244|PDB:1FPN}.
STRAND 480 489 {ECO:0000244|PDB:1FPN}.
STRAND 492 497 {ECO:0000244|PDB:1FPN}.
STRAND 502 504 {ECO:0000244|PDB:1FPN}.
STRAND 506 509 {ECO:0000244|PDB:1FPN}.
STRAND 517 524 {ECO:0000244|PDB:1FPN}.
STRAND 530 532 {ECO:0000244|PDB:3TN9}.
STRAND 534 544 {ECO:0000244|PDB:1FPN}.
STRAND 549 553 {ECO:0000244|PDB:1FPN}.
TURN 572 579 {ECO:0000244|PDB:3VDD}.
STRAND 581 583 {ECO:0000244|PDB:3VDD}.
STRAND 599 602 {ECO:0000244|PDB:3VDD}.
HELIX 604 606 {ECO:0000244|PDB:1FPN}.
HELIX 614 617 {ECO:0000244|PDB:1FPN}.
HELIX 630 632 {ECO:0000244|PDB:1FPN}.
HELIX 634 638 {ECO:0000244|PDB:1FPN}.
STRAND 642 650 {ECO:0000244|PDB:1FPN}.
TURN 654 658 {ECO:0000244|PDB:1FPN}.
STRAND 661 665 {ECO:0000244|PDB:1FPN}.
HELIX 672 678 {ECO:0000244|PDB:1FPN}.
STRAND 681 698 {ECO:0000244|PDB:1FPN}.
STRAND 707 713 {ECO:0000244|PDB:1FPN}.
HELIX 726 729 {ECO:0000244|PDB:1FPN}.
STRAND 731 733 {ECO:0000244|PDB:1FPN}.
STRAND 735 739 {ECO:0000244|PDB:1FPN}.
STRAND 746 749 {ECO:0000244|PDB:1FPN}.
STRAND 754 760 {ECO:0000244|PDB:1FPN}.
TURN 774 777 {ECO:0000244|PDB:1FPN}.
STRAND 782 787 {ECO:0000244|PDB:1FPN}.
STRAND 796 814 {ECO:0000244|PDB:1FPN}.
STRAND 855 866 {ECO:0000244|PDB:2HRV}.
HELIX 867 869 {ECO:0000244|PDB:2HRV}.
HELIX 874 876 {ECO:0000244|PDB:2HRV}.
STRAND 878 881 {ECO:0000244|PDB:2HRV}.
HELIX 882 884 {ECO:0000244|PDB:2HRV}.
STRAND 886 896 {ECO:0000244|PDB:2HRV}.
STRAND 906 911 {ECO:0000244|PDB:2HRV}.
TURN 912 915 {ECO:0000244|PDB:2HRV}.
STRAND 916 921 {ECO:0000244|PDB:2HRV}.
STRAND 923 930 {ECO:0000244|PDB:2HRV}.
STRAND 938 948 {ECO:0000244|PDB:2HRV}.
STRAND 959 962 {ECO:0000244|PDB:2HRV}.
STRAND 965 973 {ECO:0000244|PDB:2HRV}.
STRAND 975 982 {ECO:0000244|PDB:2HRV}.
HELIX 983 986 {ECO:0000244|PDB:2HRV}.
HELIX 1509 1521 {ECO:0000244|PDB:5FX6}.
STRAND 1522 1527 {ECO:0000244|PDB:5FX6}.
STRAND 1530 1539 {ECO:0000244|PDB:5FX6}.
STRAND 1541 1545 {ECO:0000244|PDB:5FX6}.
HELIX 1546 1548 {ECO:0000244|PDB:5FX6}.
STRAND 1552 1556 {ECO:0000244|PDB:5FX6}.
STRAND 1559 1570 {ECO:0000244|PDB:5FX6}.
STRAND 1576 1584 {ECO:0000244|PDB:5FX6}.
HELIX 1594 1596 {ECO:0000244|PDB:5FX6}.
STRAND 1604 1611 {ECO:0000244|PDB:5FX6}.
STRAND 1615 1617 {ECO:0000244|PDB:5FX6}.
STRAND 1619 1634 {ECO:0000244|PDB:5FX6}.
STRAND 1637 1647 {ECO:0000244|PDB:5FX6}.
HELIX 1651 1653 {ECO:0000244|PDB:6FFN}.
STRAND 1657 1660 {ECO:0000244|PDB:5FX6}.
STRAND 1663 1671 {ECO:0000244|PDB:5FX6}.
STRAND 1676 1680 {ECO:0000244|PDB:5FX6}.
HELIX 1683 1685 {ECO:0000244|PDB:5FX6}.
SEQUENCE 2150 AA; 241978 MW; 6E0DF9F4945D9D0C CRC64;
MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASNG ASKLEFTQDP SKFTDPVKDV
LEKGIPTLQS PTVEACGYSD RIIQITRGDS TITSQDVANA IVAYGVWPHY LSSKDASAID
KPSQPDTSSN RFYTLRSVTW SSSSKGWWWK LPDALKDMGI FGENMFYHYL GRSGYTIHVQ
CNASKFHQGT LIVALIPEHQ IASALHGNVN VGYNYTHPGE TGREVKAETR LNPDLQPTEE
YWLNFDGTLL GNITIFPHQF INLRSNNSAT IIAPYVNAVP MDSMRSHNNW SLVIIPICPL
ETSSAINTIP ITISISPMCA EFSGARAKRQ GLPVFITPGS GQFLTTDDFQ SPCALPWYHP
TKEISIPGEV KNLVEICQVD SLVPINNTDT YINSENMYSV VLQSSINAPD KIFSIRTDVA
SQPLATTLIG EISSYFTHWT GSLRFSFMFC GTANTTVKLL LAYTPPGIAE PTTRKDAMLG
THVIWDVGLQ STISMVVPWI SASHYRNTSP GRSTSGYITC WYQTRLVIPP QTPPTARLLC
FVSGCKDFCL RMARDTNLHL QSGAIAQNPV ENYIDEVLNE VLVVPNINSS NPTTSNSAPA
LDAAETGHTS SVQPEDVIET RYVQTSQTRD EMSLESFLGR SGCIHESKLE VTLANYNKEN
FTVWAINLQE MAQIRRKFEL FTYTRFDSEI TLVPCISALS QDIGHITMQY MYVPPGAPVP
NSRDDYAWQS GTNASVFWQH GQAYPRFSLP FLSVASAYYM FYDGYDEQDQ NYGTANTNNM
GSLCSRIVTE KHIHKVHIMT RIYHKAKHVK AWCPRPPRAL EYTRAHRTNF KIEDRSIQTA
IVTRPIITTA GPSDMYVHVG NLIYRNLHLF NSEMHESILV SYSSDLIIYR TNTVGDDYIP
SCDCTQATYY CKHKNRYFPI TVTSHDWYEI QESEYYPKHI QYNLLIGEGP CEPGDCGGKL
LCKHGVIGIV TAGGDNHVAF IDLRHFHCAE EQGVTDYIHM LGEAFGNGFV DSVKEHIHAI
NPVGNISKKI IKWMLRIISA MVIIIRNSSD PQTILATLTL IGCSGSPWRF LKEKFCKWTQ
LNYIHKESDS WLKKFTEACN AARGLEWIGN KISKFIEWMK SMLPQAQLKV KYLNELKKLN
LYEKQVESLR VADMKTQEKI KMEIDTLHDL SRKFLPLYAS EAKRIKTLYI KCDNIIKQKK
RCEPVAIVIH GPPGAGKSIT TNFLAKMITN DSDIYSLPPD PKYFDGYDQQ SVVIMDDIMQ
NPAGDDMTLF CQMVSSVTFI PPMADLPDKG KAFDSRFVLC STNHSLLTPP TITSLPAMNR
RFFLDLDIIV HDNFKDPQGK LNVAAAFRPC DVDNRIGNAR CCPFVCGKAV SFKDRNSCNK
YSLAQVYNIM IEEDRRRRQV VDVMTAIFQG PIDMKNPPPP AITDLLQSVR TPEVIKYCEG
NRWIIPAECK IEKELNLANT IITIIANVIG MARIIYVIYK LFCTLQGPYS GEPKPKTKIP
ERRVVTQGPE EEFGMSLIKH NSCVITTENG KFTGLGVYDR FVVVPTHADP GKEIQVDGIT
TKVIDSYDLY NKNGIKLEIT VLKLDRNEKF RDIRRYIPNN EDDYPNCNLA LLANQPEPTI
INVGDVVSYG NILLSGNQTA RMLKYSYPTK SGYCGGVLYK IGQVLGIHVG GNGRDGFSAM
LLRSYFTDVQ GQITLSKKTS ECNLPSIHTP CKTKLQPSVF YDVFPGSKEP AVLSEKDARL
QVDFNEALFS KYKGNTDCSI NDHIRIASSH YAAQLITLDI DPKPITLEDS VFGTDGLEAL
DLNTSAGFPY IAMGVKKRDL INNKTKDISK LKEAIDKYGV DLPMVTFLKD ELRKHEKVIK
GKTRVIEASS VNDTLLFRTT FGNLFSKFHL NPGIVTGSAV GCDPEVFWSK IPAMLDDKCI
MAFDYTNYDG SIHPIWFEAL KQVLVDLSFN PTLIDRLCKS KHIFKNTYYE VEGGVPSGCS
GTSIFNTMIN NIIIRTLVLD AYKNIDLDKL KIIAYGDDVI FSYIHELDME AIAIEGVKYG
LTITPADKSN TFVKLDYSNV TFLKRGFKQD EKYNFLIHPT FPEDEIFESI RWTKKPSQMH
EHVLSLCHLM WHNGRDAYKK FVEKIRSVSA GRALYIPPYD LLLHEWYEKF


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