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 POLG_POL3L              Reviewed;        2206 AA.
P03302; Q84783; Q84784; Q84785; Q84786; Q84787; Q84788; Q84789;
Q84790; Q98592; Q98593; Q98594;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 181.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=P3;
Contains:
RecName: Full=Protein 3AB;
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=P2;
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;
Poliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Enterovirus C.
NCBI_TaxID=12088;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=P3/Leon/37;
PubMed=6324200; DOI=10.1073/pnas.81.5.1539;
Stanway G., Hughes P.J., Mountford R.C., Reeve P., Minor P.D.,
Schild G.C., Almond J.W.;
"Comparison of the complete nucleotide sequences of the genomes of the
neurovirulent poliovirus P3/Leon/37 and its attenuated Sabin vaccine
derivative P3/Leon 12a1b.";
Proc. Natl. Acad. Sci. U.S.A. 81:1539-1543(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=P3/Leon 12A[1]B;
PubMed=6310508; DOI=10.1093/nar/11.16.5629;
Stanway G., Cann A.J., Hauptmann R., Hughes P.J., Clarke L.D.,
Mountford R.C., Minor P.D., Schild G.C., Almond J.W.;
"The nucleotide sequence of poliovirus type 3 Leon 12 a1b: comparison
with poliovirus type 1.";
Nucleic Acids Res. 11:5629-5643(1983).
[3]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-878.
PubMed=7820548; DOI=10.1016/S0960-9822(00)00176-7;
Grant R.A., Hiremath C.N., Filman D.J., Syed R., Andries K.,
Hogle J.M.;
"Structures of poliovirus complexes with anti-viral drugs:
implications for viral stability and drug design.";
Curr. Biol. 4:784-797(1994).
[4]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-878.
PubMed=15299834; DOI=10.1107/S090744499401084X;
Hiremath C.N., Grant R.A., Filman D.J., Hogle J.M.;
"Binding of the antiviral drug win51711 to the Sabin strain of type-3
poliovirus -structural comparison with drug-binding in rhinovirus-
14.";
Acta Crystallogr. D 51:473-489(1995).
-!- 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 through clathrin- and caveolin-independent
endocytosis in Hela cells and through caveolin-mediated
endocytosis in brain microvascular endothelial cells. 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}.
-!- MISCELLANEOUS: The sequence of strain Sabin vaccine P3/Leon/37 is
shown.
-!- MISCELLANEOUS: The strain Sabin vaccine P3/Leon/37 is the
progenitor of the strain Sabin vaccine P3/Leon 12a[1]b.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with antiviral compound R78206;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1vba";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with antiviral compound R80633;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1vbb";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with antiviral compound R77975;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1vbc";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure of mutant F700L, F710L in complex with antiviral
compound R78206;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1vbe";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure in complex with antiviral compound WIN51711;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1piv";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1pvc";
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EMBL; K01392; AAA46914.1; -; Genomic_RNA.
EMBL; X00925; CAA25444.1; -; Genomic_RNA.
PIR; A93987; GNNY4P.
PDB; 1PIV; X-ray; 2.90 A; 1=578-878, 2=70-340, 3=341-578, 4=2-69.
PDB; 1PVC; X-ray; 2.40 A; 1=578-878, 2=70-340, 3=341-578, 4=2-69.
PDB; 1VBA; X-ray; 2.90 A; 1=579-878, 2=70-340, 3=341-575, 4=2-69.
PDB; 1VBB; X-ray; 2.80 A; 1=579-878, 2=70-340, 3=341-575, 4=2-69.
PDB; 1VBC; X-ray; 2.80 A; 1=579-878, 2=70-340, 3=341-575, 4=2-69.
PDB; 1VBE; X-ray; 2.80 A; 1=579-878, 2=70-340, 3=341-575, 4=2-69.
PDB; 3EPD; EM; -; 1=600-878, 2=75-340, 3=341-575, 4=2-69.
PDB; 3IYB; EM; -; 2=83-96.
PDB; 3IYC; EM; -; 2=83-96.
PDB; 5O5B; EM; 3.60 A; 4=1-69.
PDB; 5O5P; EM; 4.10 A; 4=1-69.
PDBsum; 1PIV; -.
PDBsum; 1PVC; -.
PDBsum; 1VBA; -.
PDBsum; 1VBB; -.
PDBsum; 1VBC; -.
PDBsum; 1VBE; -.
PDBsum; 3EPD; -.
PDBsum; 3IYB; -.
PDBsum; 3IYC; -.
PDBsum; 5O5B; -.
PDBsum; 5O5P; -.
ProteinModelPortal; P03302; -.
SMR; P03302; -.
DrugBank; DB08014; (METHYLPYRIDAZINE PIPERIDINE BUTYLOXYPHENYL)ETHYLACETATE.
DrugBank; DB08012; (METHYLPYRIDAZINE PIPERIDINE ETHYLOXYPHENYL)ETHYLACETATE.
DrugBank; DB08013; (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE.
DrugBank; DB08231; MYRISTIC ACID.
DrugBank; DB03203; Sphingosine.
MEROPS; C03.020; -.
OrthoDB; VOG0900006M; -.
EvolutionaryTrace; P03302; -.
Proteomes; UP000008147; Genome.
Proteomes; UP000008995; 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:0075513; P:caveolin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; 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; 1.10.10.870; -; 1.
Gene3D; 2.60.120.20; -; 3.
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; 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; Caveolin-mediated endocytosis of virus by host;
Clathrin- and caveolin-independent endocytosis of virus by host;
Complete proteome; Covalent protein-RNA linkage; DNA replication;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host transcription 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 eukaryotic host transcription initiation by virus;
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 2206 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000426656.
CHAIN 2 878 P1. {ECO:0000250}.
/FTId=PRO_0000426657.
CHAIN 2 340 Capsid protein VP0. {ECO:0000255}.
/FTId=PRO_0000426658.
CHAIN 2 69 Capsid protein VP4. {ECO:0000255}.
/FTId=PRO_0000426659.
CHAIN 70 340 Capsid protein VP2. {ECO:0000255}.
/FTId=PRO_0000426660.
CHAIN 341 578 Capsid protein VP3. {ECO:0000255}.
/FTId=PRO_0000426661.
CHAIN 579 878 Capsid protein VP1. {ECO:0000255}.
/FTId=PRO_0000426662.
CHAIN 879 1453 P2. {ECO:0000250}.
/FTId=PRO_0000426663.
CHAIN 879 1027 Protease 2A. {ECO:0000255}.
/FTId=PRO_0000426664.
CHAIN 1028 1124 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000040140.
CHAIN 1125 1453 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000040141.
CHAIN 1454 2206 P3. {ECO:0000250}.
/FTId=PRO_0000426665.
CHAIN 1454 1562 Protein 3AB. {ECO:0000255}.
/FTId=PRO_0000426666.
CHAIN 1454 1540 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000040142.
CHAIN 1541 1562 Viral protein genome-linked.
{ECO:0000255}.
/FTId=PRO_0000426667.
CHAIN 1563 2206 Protein 3CD. {ECO:0000255}.
/FTId=PRO_0000426668.
CHAIN 1563 1744 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000426669.
CHAIN 1745 2206 RNA-directed RNA polymerase.
{ECO:0000250}.
/FTId=PRO_0000426670.
TOPO_DOM 2 1517 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1518 1533 {ECO:0000255}.
TOPO_DOM 1534 2206 Cytoplasmic. {ECO:0000255}.
DOMAIN 1229 1385 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1563 1728 Peptidase C3.
DOMAIN 1972 2087 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1253 1260 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
REGION 579 603 Amphipatic alpha-helix. {ECO:0000255}.
REGION 1454 1476 Disordered. {ECO:0000250}.
ACT_SITE 898 898 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 916 916 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 987 987 For Protease 2A activity. {ECO:0000250}.
ACT_SITE 1602 1602 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1633 1633 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 1709 1709 For Protease 3C activity. {ECO:0000255}.
ACT_SITE 2073 2073 For RdRp activity. {ECO:0000250}.
SITE 69 70 Cleavage; by autolysis. {ECO:0000255}.
SITE 340 341 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 878 879 Cleavage; by Protease 2A. {ECO:0000255}.
SITE 1027 1028 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1124 1125 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1453 1454 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1540 1541 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1562 1563 Cleavage; by Protease 3C. {ECO:0000255}.
SITE 1745 1746 Cleavage; by Protease 3C. {ECO:0000255}.
MOD_RES 1543 1543 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
VARIANT 431 431 S -> F (in strain: P3/Leon 12a[1]b).
VARIANT 864 864 K -> R (in strain: P3/Leon 12a[1]b).
VARIANT 908 908 T -> A (in strain: P3/Leon 12a[1]b).
STRAND 4 8 {ECO:0000244|PDB:1PVC}.
STRAND 25 29 {ECO:0000244|PDB:1PVC}.
HELIX 36 38 {ECO:0000244|PDB:1PVC}.
HELIX 51 54 {ECO:0000244|PDB:1PVC}.
STRAND 57 59 {ECO:0000244|PDB:1PVC}.
STRAND 83 87 {ECO:0000244|PDB:1PVC}.
STRAND 90 96 {ECO:0000244|PDB:1PVC}.
HELIX 103 105 {ECO:0000244|PDB:1PVC}.
TURN 113 115 {ECO:0000244|PDB:1PVC}.
HELIX 126 128 {ECO:0000244|PDB:1PVC}.
STRAND 138 141 {ECO:0000244|PDB:1PVC}.
STRAND 147 151 {ECO:0000244|PDB:1PVC}.
HELIX 153 155 {ECO:0000244|PDB:1PVC}.
HELIX 159 167 {ECO:0000244|PDB:1PVC}.
STRAND 168 180 {ECO:0000244|PDB:1PVC}.
STRAND 187 197 {ECO:0000244|PDB:1PVC}.
STRAND 203 207 {ECO:0000244|PDB:1PVC}.
HELIX 213 216 {ECO:0000244|PDB:1PVC}.
HELIX 219 221 {ECO:0000244|PDB:1PVC}.
STRAND 226 228 {ECO:0000244|PDB:1PVC}.
HELIX 246 248 {ECO:0000244|PDB:1PVC}.
TURN 249 252 {ECO:0000244|PDB:1PVC}.
HELIX 255 260 {ECO:0000244|PDB:1PVC}.
STRAND 261 267 {ECO:0000244|PDB:1PVC}.
TURN 268 270 {ECO:0000244|PDB:1PVC}.
STRAND 272 278 {ECO:0000244|PDB:1PVC}.
STRAND 282 287 {ECO:0000244|PDB:1PVC}.
TURN 289 291 {ECO:0000244|PDB:1PVC}.
STRAND 295 307 {ECO:0000244|PDB:1PVC}.
STRAND 314 331 {ECO:0000244|PDB:1PVC}.
TURN 348 351 {ECO:0000244|PDB:1PVC}.
STRAND 363 365 {ECO:0000244|PDB:1PVC}.
STRAND 379 382 {ECO:0000244|PDB:1PVC}.
HELIX 384 387 {ECO:0000244|PDB:1PVC}.
TURN 399 403 {ECO:0000244|PDB:1PVC}.
HELIX 405 408 {ECO:0000244|PDB:1PVC}.
STRAND 410 413 {ECO:0000244|PDB:1PVC}.
STRAND 422 427 {ECO:0000244|PDB:1PVC}.
TURN 429 431 {ECO:0000244|PDB:1PVC}.
TURN 433 437 {ECO:0000244|PDB:1PVC}.
HELIX 439 444 {ECO:0000244|PDB:1PVC}.
STRAND 447 452 {ECO:0000244|PDB:1PVC}.
STRAND 454 460 {ECO:0000244|PDB:1PVC}.
STRAND 469 475 {ECO:0000244|PDB:1PVC}.
STRAND 477 479 {ECO:0000244|PDB:1PVC}.
HELIX 485 488 {ECO:0000244|PDB:1PVC}.
STRAND 491 497 {ECO:0000244|PDB:1PVC}.
STRAND 499 501 {ECO:0000244|PDB:1PVC}.
STRAND 503 508 {ECO:0000244|PDB:1PVC}.
STRAND 513 520 {ECO:0000244|PDB:1PVC}.
HELIX 523 525 {ECO:0000244|PDB:1PVC}.
STRAND 529 536 {ECO:0000244|PDB:1PVC}.
STRAND 546 556 {ECO:0000244|PDB:1PVC}.
STRAND 561 565 {ECO:0000244|PDB:1PVC}.
HELIX 623 625 {ECO:0000244|PDB:1PVC}.
HELIX 633 635 {ECO:0000244|PDB:1PVC}.
HELIX 649 651 {ECO:0000244|PDB:1PVC}.
HELIX 653 657 {ECO:0000244|PDB:1PVC}.
STRAND 661 671 {ECO:0000244|PDB:1PVC}.
STRAND 675 677 {ECO:0000244|PDB:1VBB}.
STRAND 680 685 {ECO:0000244|PDB:1PVC}.
STRAND 690 692 {ECO:0000244|PDB:1PVC}.
HELIX 693 698 {ECO:0000244|PDB:1PVC}.
STRAND 701 718 {ECO:0000244|PDB:1PVC}.
STRAND 730 736 {ECO:0000244|PDB:1PVC}.
HELIX 749 752 {ECO:0000244|PDB:1PVC}.
STRAND 754 756 {ECO:0000244|PDB:1PVC}.
STRAND 758 762 {ECO:0000244|PDB:1PVC}.
STRAND 768 772 {ECO:0000244|PDB:1PVC}.
STRAND 777 783 {ECO:0000244|PDB:1PVC}.
TURN 799 802 {ECO:0000244|PDB:1PVC}.
STRAND 810 812 {ECO:0000244|PDB:1VBC}.
STRAND 816 821 {ECO:0000244|PDB:1PVC}.
STRAND 830 848 {ECO:0000244|PDB:1PVC}.
STRAND 858 861 {ECO:0000244|PDB:1PVC}.
SEQUENCE 2206 AA; 246165 MW; 4766B15C861F66D3 CRC64;
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYKDSASNA ASKQDYSQDP SKFTEPLKDV
LIKTAPALNS PNVEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEF IRDDEANPVD
QPTEPDVATC RFYTLDTVMW GKESKGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ
CNASKFHQGA LGVFAIPEYC LAGDSDKQRY TSYANANPGE RGGKFYSQFN KDNAVTSPKR
EFCPVDYLLG CGVLLGNAFV YPHQIINLRT NNSATIVLPY VNALAIDSMV KHNNWGIAIL
PLSPLDFAQD SSVEIPITVT IAPMCSEFNG LRNVTAPKFQ GLPVLNTPGS NQYLTSDNHQ
SPCAIPEFDV TPPIDIPGEV KNMMELAEID TMIPLNLEST KRNTMDMYRV TLSDSADLSQ
PILCLSLSPA SDPRLSHTML GEVLNYYTHW AGSLKFTFLF CGSMMATGKI LVAYAPPGAQ
PPTSRKEAML GTHVIWDLGL QSSCTMVVPW ISNVTYRQTT QDSFTEGGYI SMFYQTRIVV
PLSTPKSMSM LGFVSACNDF SVRLLRDTTH ISQSALPQGI EDLISEVAQG ALTLSLPKQQ
DSLPDTKASG PAHSKEVPAL TAVETGATNP LAPSDTVQTR HVVQRRSRSE STIESFFARG
ACVAIIEVDN EQPTTRAQKL FAMWRITYKD TVQLRRKLEF FTYSRFDMEF TFVVTANFTN
ANNGHALNQV YQIMYIPPGA PTPKSWDDYT WQTSSNPSIF YTYGAAPARI SVPYVGLANA
YSHFYDGFAK VPLKTDANDQ IGDSLYSAMT VDDFGVLAVR VVNDHNPTKV TSKVRIYMKP
KHVRVWCPRP PRAVPYYGPG VDYKNNLDPL SEKGLTTYGF GHQNKAVYTA GYKICNYHLA
TKEDLQNTVS IMWNRDLLVV ESKAQGTDSI ARCNCNAGVY YCESRRKYYP VSFVGPTFQY
MEANDYYPAR YQSHMLIGHG FASPGDCGGI LRCQHGVIGI VTAGGEGLVA FSDIRDLYAY
EEEAMEQGIS NYIESLGAAF GSGFTQQIGD KISELTSMVT STITEKLLKN LIKIISSLVI
ITRNYEDTTT VLATLALLGC DVSPWQWLKK KACDTLEIPY VIRQGDSWLK KFTEACNAAK
GLEWVSNKIS KFIDWLRERI IPQARDKLEF VTKLKQLEML ENQISTIHQS CPSQEHQEIL
FNNVRWLSIQ SKRFAPLYAL EAKRIQKLEH TINNYIQFKS KHRIEPVCLL VHGSPGTGKS
VATNLIARAI AEKENTSTYS LPPDPSHFDG YKQQGVVIMD DLNQNPDGAD MKLFCQMVST
VEFIPPMASL EEKGILFTSN YVLASTNSSR ITPPTVAHSD ALARRFAFDM DIQVMGEYSR
DGKLNMAMAT ETCKDCHQPA NFKRCCPLVC GKAIQLMDKS SRVRYSVDQI TTMIINERNR
RSNIGNCMEA LFQGPLQYKD LKIDIKTRPP PECINDLLQA VDSQEVRDYC EKKGWIVNIT
SQVQTERNIN RAMTILQAVT TFAAVAGVVY VMYKLFAGHQ GAYTGLPNKR PNVPTIRAAK
VQGPGFDYAV AMAKRNIVTA TTSKGEFTML GVHDNVAILP THASPGESIV IDGKEVEILD
AKALEDQAGT NLEITIITLK RNEKFRDIRQ HIPTQITETN DGVLIVNTSK YPNMYVPVGA
VTEQGYLNLG GRQTARILMY NFPTRAGQCG GVITCTGKVI GMHVGGNGSH GFAAALKRSY
FTQSQGEIQW MRPSKEAGYP IINAPTKTKL EPSAFHYVFE GVKEPAVLTK NDPRLKTDFE
EAIFSKYVGN KITEVDEYMK EAVDHYAGQL MSLDISTEQM CLEDAMYGTD GLEALDLSTS
AGYPYVAMGK KKRDILNKQT RDTKEMQRLL DAYGINLPLV TYVKDELRSK TKVEQGKSRL
IEASSLNDSV AMRMAFGNLY AAFHRNPGVV TGSAVGCDPD LFWSKIPVLM EEKLFAFDYT
GYDASLSPAW FEALKMVLEK IGFGDRVDYI DYLNHSHHLY KNKIYCVKGG MPSGCSGTSI
FNSMINNLII RTLLLKTYKG IDLDHLKMIA YGDDVIASYP HEVDASLLAQ SGKDYGLTMT
PADKSATFET VTWENVTFLK RFFRADEKYP FLIHPVMPMK EIHESIRWTK DPRNTQDHVR
SLCLLAWHNG EEEYNKFLAK IRSVPIGRAL LLPEYSTLYR RWLDSF


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