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Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Protein VP2 (P1B) (Virion protein 2); Protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (PX); Protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Protein 3B (P3B) (VPg); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)] (Fragments)

 POLG_HAVHA              Reviewed;        2052 AA.
Q05794; Q67800; Q67801; Q67802; Q67803; Q67804; Q67805; Q67806;
Q67807;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
12-SEP-2018, entry version 92.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=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=Protein VP1-2A;
AltName: Full=VPX;
Contains:
RecName: Full=Capsid protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Assembly signal 2A;
AltName: Full=pX {ECO:0000250|UniProtKB:P08617};
Contains:
RecName: Full=Protein 2BC;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=Protein 3ABCD;
Short=P3;
Contains:
RecName: Full=Protein 3ABC;
Contains:
RecName: Full=Protein 3AB;
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;
Contains:
RecName: Full=Protease 3C;
Short=P3C;
EC=3.4.22.28 {ECO:0000250|UniProtKB:P08617};
AltName: Full=Picornain 3C;
Contains:
RecName: Full=RNA-directed RNA polymerase 3D-POL;
Short=P3D-POL;
EC=2.7.7.48 {ECO:0000250|UniProtKB:P08617};
Flags: Fragments;
Human hepatitis A virus genotype IA (isolate HAS-15) (HHAV) (Human
hepatitis A virus (isolate Human/Arizona/HAS-15/1979)).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Hepatovirus.
NCBI_TaxID=470424;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Sverdlov S.D., Tsarev S.A., Markova S.V., Vasilenko S.K.,
Chizhikov V.E., Petrov N.A., Kusov Y.Y., Nastashenko T.A.,
Balayan M.S.;
"Cloning and expression of hepatitis A virus genome in E. coli
cells.";
Mol. Genet. Microbiol. Virol. 6:129-133(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-906.
PubMed=3000718;
Ovchinnikov Y.A., Sverdlov E.D., Tsarev S.A., Arsenian S.G.,
Rokhlina T.O.;
"Sequence of 3372 RNA nucleotide links in the hepatitis A virus coding
for capsid VP4-VP1 and nonstructural proteins.";
Dokl. Akad. Nauk SSSR 285:1014-1018(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 758-813.
PubMed=1318940; DOI=10.1099/0022-1317-73-6-1365;
Robertson B.H., Jansen R.W., Khanna B., Totsuka A., Nainan O.V.,
Siegl G., Widell A., Margolis H.S., Isomura S., Ito K., Ishizu T.,
Moritsugu Y., Lemon S.M.;
"Genetic relatedness of hepatitis A virus strains recovered from
different geographical regions.";
J. Gen. Virol. 73:1365-1377(1992).
-!- FUNCTION: Capsid protein VP1: Capsid proteins VP1, VP2, and VP3
form a closed capsid enclosing the viral positive strand RNA
genome. All these proteins contain a beta-sheet structure called
beta-barrel jelly roll. Together they form an icosahedral capsid
(T=3) composed of 60 copies of each VP1, VP2, and VP3, with a
diameter of approximately 300 Angstroms. VP1 is situated at the 12
fivefold axes, whereas VP2 and VP3 are located at the quasi-
sixfold axes. The naked capsid interacts with the host receptor
HAVCR1 to provide virion attachment to and probably entry into the
target cell. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Capsid protein VP2: Capsid proteins VP1, VP2, and VP3
form a closed capsid enclosing the viral positive strand RNA
genome. All these proteins contain a beta-sheet structure called
beta-barrel jelly roll. Together they form an icosahedral capsid
(T=3) composed of 60 copies of each VP1, VP2, and VP3, with a
diameter of approximately 300 Angstroms. VP1 is situated at the 12
fivefold axes, whereas VP2 and VP3 are located at the quasi-
sixfold axes. The naked capsid interacts with the host receptor
HAVCR1 to provide virion attachment to and probably entry into the
target cell. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Capsid protein VP3: Capsid proteins VP1, VP2, and VP3
form a closed capsid enclosing the viral positive strand RNA
genome. All these proteins contain a beta-sheet structure called
beta-barrel jelly roll. Together they form an icosahedral capsid
(T=3) composed of 60 copies of each VP1, VP2, and VP3, with a
diameter of approximately 300 Angstroms. VP1 is situated at the 12
fivefold axes, whereas VP2 and VP3 are located at the quasi-
sixfold axes. The naked capsid interacts with the host receptor
HAVCR1 to provide virion attachment to and probably entry into the
target cell. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein VP0: VP0 precursor is a component of the
immature procapsids. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein VP4: Plays a role in the assembly of the 12
pentamers into an icosahedral structure. Has not been detected in
mature virions, supposedly owing to its small size.
{ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein VP1-2A: Precursor component of immature
procapsids that corresponds to an extended form of the structural
protein VP1. After maturation, possibly by the host Cathepsin L,
the assembly signal 2A is cleaved to give rise to the mature VP1
protein. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein 2B: Function as a viroporin. Affects membrane
integrity and causes an increase in membrane permeability.
Involved in host intracellular membrane rearrangements probably to
give rise to the viral factories. Does not disrupt calcium
homeostasis or glycoprotein trafficking. Antagonizes the innate
immune response of the host by suppressing IFN-beta synthesis,
which it achieves by interfering with the DDX58/IFIH1 (RIG-I/MDA5)
pathway. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein 2BC: Affects membrane integrity and causes an
increase in membrane permeability. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein 2C: Associates with and induces structural
rearrangements of intracellular membranes. Displays RNA-binding
activity. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein 3ABC: The precursor 3ABC is targeted to the
mitochondrial membrane where protease 3C activity cleaves and
inhibits the host antiviral protein MAVS, thereby disrupting
activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the
protease activity of 3ABC precursor is more efficient in cleaving
the 2BC precursor than that of protein 3C. The 3ABC precursor may
therefore play a role in the proteolytic processing of the
polyprotein. Possible viroporin. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein 3AB: Interacts with the 3CD precursor and with
RNA structures found at both the 5'- and 3'-termini of the viral
genome. Since the 3AB precursor contains the hydrophobic domain
3A, it probably anchors the whole viral replicase complex to
intracellular membranes on which viral RNA synthesis occurs.
{ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein 3A: May serve as membrane anchor to the 3AB and
3ABC precursors via its hydrophobic domain. May interact with RNA.
{ECO:0000250|UniProtKB:P08617}.
-!- 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 VPg-pUpU is then used as primer on the genomic RNA poly(A) by
the RNA-dependent RNA polymerase to replicate the viral genome.
{ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protease 3C: Cysteine protease that generates mature
viral proteins from the precursor polyprotein. In addition to its
proteolytic activity, it binds to viral RNA, and thus influences
viral genome replication. RNA and substrate bind cooperatively to
the protease. Cleaves IKBKG/NEMO to impair innate immune
signaling. Cleaves host PABPC1 which may participate to the switch
of viral translation to RNA synthesis.
{ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein 3CD: Interacts with the 3AB precursor and with
RNA structures found at both the 5'- and 3'-termini of the viral
genome. Disrupts TLR3 signaling by degrading the host adapter
protein TICAM1/TRIF. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic
and antigenomic RNA by recognizing replications specific signals.
{ECO:0000250|UniProtKB:P08617}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000250|UniProtKB:P08617, ECO:0000255|PROSITE-
ProRule:PRU00539}.
-!- 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.
{ECO:0000250|UniProtKB:P08617}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBUNIT: Protein 2B: Homodimer. Homomultimer; probably interacts
with membranes in a multimeric form. Seems to assemble into
amyloid-like fibers. Protein 3AB: Homodimer. Monomer. Protein 3AB:
Interacts with protein 3CD. Protein 3CD: Interacts with protein
3AB. Protein 3ABC: Interacts with human MAVS. Protease 3C:
Homodimer; disulfide-linked. Protein VP1-2A: Homopentamer. Protein
VP1-2A: Homooligomer. Capsid protein VP1: Interacts with capsid
protein VP2. Capsid protein VP1: Interacts with capsid protein
VP3. Capsid protein VP2: Interacts with capsid protein VP1. Capsid
protein VP2: Interacts with capsid protein VP3. Capsid protein
VP3: Interacts with capsid protein VP1. Capsid protein VP3:
Interacts with capsid protein VP2. {ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion
{ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular
body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly
formed virions occurs through an exosome-like mechanism involving
endosomal budding of viral capsids into multivesicular bodies.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Capsid protein VP3: Virion
{ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular
body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly
formed virions occurs through an exosome-like mechanism involving
endosomal budding of viral capsids into multivesicular bodies.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Capsid protein VP1: Virion
{ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular
body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly
formed virions occurs through an exosome-like mechanism involving
endosomal budding of viral capsids into multivesicular bodies.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Protein VP4: Virion
{ECO:0000250|UniProtKB:P08617}. Note=Present in the full mature
virion. The egress of newly formed virions occurs through an
exosome-like mechanism involving endosomal budding of viral
capsids into multivesicular bodies.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host membrane
{ECO:0000250|UniProtKB:P08617}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to
intracellular membrane vesicles that are induced after virus
infection as the site for viral RNA replication.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Protein 2C: Host membrane
{ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein
{ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to
intracellular membrane vesicles that are induced after virus
infection as the site for viral RNA replication. May associate
with membranes through a N-terminal amphipathic helix.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Protein 3ABC: Host membrane
{ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein
{ECO:0000255}. Host mitochondrion outer membrane
{ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein
{ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to
intracellular membrane vesicles that are induced after virus
infection as the site for viral RNA replication.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Protein 3AB: Host membrane
{ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein
{ECO:0000255}. Note=Probably localizes to intracellular membrane
vesicles that are induced after virus infection as the site for
viral RNA replication. {ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Protein 3A: Host membrane
{ECO:0000250|UniProtKB:P08617}; Single-pass membrane protein
{ECO:0000255}. Note=Probably localizes to intracellular membrane
vesicles that are induced after virus infection as the site for
viral RNA replication. {ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Viral protein genome-linked: Virion
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Protease 3C: Host cytoplasm
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host
cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P08617};
Peripheral membrane protein {ECO:0000250|UniProtKB:P08617};
Cytoplasmic side {ECO:0000250|UniProtKB:P08617}. Note=Interacts
with membranes in a complex with viral protein 3AB. 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. {ECO:0000250|UniProtKB:P08617}.
-!- DOMAIN: Protein VP1-2A: The assembly signal 2A region mediates
pentamerization of P1-2A. {ECO:0000250|UniProtKB:P08617}.
-!- DOMAIN: Genome polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle budding. They
recruit proteins of the host ESCRT machinery (Endosomal Sorting
Complex Required for Transport) or ESCRT-associated proteins. The
genome polyprotein contains two L domains: a tandem of (L)YPX(n)L
domain which is known to bind the PDCD6IP/ALIX adaptater protein.
{ECO:0000250|UniProtKB:P08617}.
-!- DOMAIN: Capsid protein VP2: Late-budding domains (L domains) are
short sequence motifs essential for viral particle budding. They
recruit proteins of the host ESCRT machinery (Endosomal Sorting
Complex Required for Transport) or ESCRT-associated proteins.
Capsid protein VP2 contains two L domains: a tandem of (L)YPX(n)L
domain which is known to bind the Alix adaptater protein.
{ECO:0000250|UniProtKB:P08617}.
-!- DOMAIN: Protein 2B: The C-terminus displays a membrane-penetrating
ability. {ECO:0000250|UniProtKB:P08617}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages by viral
protease in vivo yield a variety of precursors and mature
proteins. Polyprotein processing intermediates are produced, such
as P1-2A which is a functional precursor of the structural
proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC
precursor which is a stable and catalytically active precursor of
3A, 3B and 3C proteins, 3AB and 3CD precursors. The assembly
signal 2A is removed from VP1-2A by a host protease, possibly host
Cathepsin L. This cleavage occurs over a region of 3 amino-acids
probably generating VP1 proteins with heterogeneous C-termini.
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.
{ECO:0000250|UniProtKB:P08617}.
-!- PTM: Protein VP1-2A: The assembly signal 2A is removed from VP1-2A
by a host protease, possibly host Cathepsin L in nacked virions.
This cleavage does not occur in enveloped virions. This cleavage
occurs over a region of 3 amino-acids probably generating VP1
proteins with heterogeneous C-termini.
{ECO:0000250|UniProtKB:P08617}.
-!- PTM: Viral protein genome-linked: VPg is uridylylated prior to
priming replication into VPg-pUpU. {ECO:0000250|UniProtKB:P03300}.
-!- PTM: Protein VP4: Unlike other picornaviruses, does not seem to be
myristoylated. {ECO:0000250|UniProtKB:P08617}.
-!- MISCELLANEOUS: Genome polyprotein: The need for an intact eIF4G
factor for the initiation of translation of HAV results in an
inability to shut off host protein synthesis by a mechanism
similar to that of other picornaviruses.
{ECO:0000250|UniProtKB:P08617}.
-!- MISCELLANEOUS: Genome polyprotein: During infection, enveloped
virions (eHAV) are released from cells. These eHAV are cloaked in
host-derived membranes and resemble exosomes. The membrane of eHAV
is devoid of viral proteins and thus prevents their neutralization
by antibodies. eHAV budding is dependent on ESCRT-associated
proteins VPS4B and PDCD6IP/ALIX. eHAV are produced and released in
the serum and plasma, but not in bile and feces which only contain
the naked, nonenveloped virions. It is likely that eHAV also use
HAVCR1 as a functional receptor to infect cells, an evolutionary
trait that may enhance HAV infectivity.
{ECO:0000250|UniProtKB:P08617}.
-!- SIMILARITY: Belongs to the picornaviridae polyprotein family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
{ECO:0000250|UniProtKB:P08617}.
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EMBL; X15463; CAA33491.1; -; Genomic_RNA.
EMBL; X15464; CAA33492.1; -; Genomic_RNA.
EMBL; L07669; -; NOT_ANNOTATED_CDS; Genomic_RNA.
ProteinModelPortal; Q05794; -.
PRIDE; Q05794; -.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0044193; C:host cell mitochondrial outer 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:0019028; C: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:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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; 2.
Gene3D; 2.60.120.20; -; 3.
InterPro; IPR024354; Hepatitis_A_VP1-2A.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
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; PF12944; HAV_VP; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 2.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
3: Inferred from homology;
ATP-binding; Capsid protein; Coiled coil;
Covalent protein-RNA linkage; Disulfide bond; Helicase;
Host cytoplasm; Host cytoplasmic vesicle; Host endosome;
Host membrane; Host mitochondrion; Host mitochondrion outer membrane;
Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host MAVS by virus;
Inhibition of host RLR pathway by virus;
Interferon antiviral system evasion; Ion channel; Ion transport;
Membrane; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; RNA-binding; RNA-directed RNA polymerase; Thiol protease;
Transferase; Transmembrane; Transmembrane helix; Transport;
Viral attachment to host cell; Viral immunoevasion; Viral ion channel;
Viral RNA replication; Virion; Virus entry into host cell.
CHAIN 1 2052 Genome polyprotein.
/FTId=PRO_0000311062.
CHAIN 1 245 Protein VP0.
/FTId=PRO_0000311063.
CHAIN 1 23 Protein VP4.
/FTId=PRO_5000145525.
CHAIN 24 245 Capsid protein VP2.
/FTId=PRO_5000145526.
CHAIN 246 491 Capsid protein VP3.
/FTId=PRO_5000145527.
CHAIN 492 830 Protein VP1-2A.
/FTId=PRO_0000311064.
CHAIN 492 759 Capsid protein VP1.
/FTId=PRO_5000145528.
CHAIN 760 830 Assembly signal 2A.
/FTId=PRO_5000145529.
CHAIN 831 1258 Protein 2BC.
/FTId=PRO_0000311065.
CHAIN 831 1081 Protein 2B.
/FTId=PRO_5000145530.
CHAIN 1082 1258 Protein 2C.
/FTId=PRO_5000145531.
CHAIN 1259 2052 Protein 3ABCD.
/FTId=PRO_0000311066.
CHAIN 1259 1572 Protein 3ABC.
/FTId=PRO_0000311067.
CHAIN 1259 1353 Protein 3AB.
/FTId=PRO_0000311068.
CHAIN 1259 1330 Protein 3A.
/FTId=PRO_5000145521.
CHAIN 1331 1353 Viral protein genome-linked.
/FTId=PRO_5000145522.
CHAIN 1354 2052 Protein 3CD.
/FTId=PRO_0000311069.
CHAIN 1354 1572 Protease 3C.
/FTId=PRO_5000145523.
CHAIN 1573 2052 RNA-directed RNA polymerase 3D-POL.
/FTId=PRO_5000145524.
TRANSMEM 1005 1025 Helical. {ECO:0000255}.
TRANSMEM 1296 1316 Helical. {ECO:0000255}.
DOMAIN 1354 1550 Peptidase C3.
DOMAIN 1810 1931 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
REGION 760 830 Involved in P1-2A pentamerization.
{ECO:0000250|UniProtKB:P08617}.
REGION 1037 1064 Membrane-penetrating ability.
{ECO:0000250|UniProtKB:P08617}.
COILED 1121 1146 {ECO:0000255}.
MOTIF 167 171 (L)YPX(n)L motif.
{ECO:0000250|UniProtKB:P08617}.
MOTIF 200 205 (L)YPX(n)L motif.
{ECO:0000250|UniProtKB:P08617}.
ACT_SITE 1397 1397 For protease 3C activity.
{ECO:0000250|UniProtKB:P13901}.
ACT_SITE 1437 1437 For protease 3C activity.
{ECO:0000250|UniProtKB:P13901}.
ACT_SITE 1525 1525 For protease 3C activity.
{ECO:0000250|UniProtKB:P13901}.
SITE 23 24 Cleavage. {ECO:0000255}.
SITE 245 246 Cleavage; by protease 3C.
{ECO:0000250|UniProtKB:P08617}.
SITE 491 492 Cleavage; by protease 3C.
{ECO:0000250|UniProtKB:P08617}.
SITE 759 760 Cleavage; partial; by host.
{ECO:0000250|UniProtKB:P08617}.
SITE 763 763 Important for VP1 folding and capsid
assembly. {ECO:0000250|UniProtKB:P08617}.
SITE 830 831 Cleavage; by protease 3C.
{ECO:0000250|UniProtKB:P08617}.
SITE 1081 1082 Cleavage; by protease 3C.
{ECO:0000250|UniProtKB:P08617}.
SITE 1258 1259 Cleavage; by protease 3C.
{ECO:0000250|UniProtKB:P08617}.
SITE 1330 1331 Cleavage; by protease 3C.
{ECO:0000250|UniProtKB:P08617}.
SITE 1353 1354 Cleavage; by protease 3C.
{ECO:0000250|UniProtKB:P08617}.
SITE 1572 1573 Cleavage; by protease 3C.
{ECO:0000250|UniProtKB:P08617}.
MOD_RES 1333 1333 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
DISULFID 1377 1377 Interchain.
{ECO:0000250|UniProtKB:P08617}.
NON_CONS 1161 1162 {ECO:0000305}.
SEQUENCE 2052 AA; 231976 MW; 971E03905B81110A CRC64;
MNMSKQGIFQ TVGSGLDHIL SLADIEEEQM IQSVDRTAVT GASYFTSVDQ SSVHTAEVGS
HQIEPLKTSV DKPGSKKTQG EKFFLIHSAD WLTTHALFHE VAKLDVVKLL YNEQFAVQGL
LRYHTYARFG IEIQVQINPT PFQQGGLICA MVPGDQSYGS IASLTVYPHG LLNCNINNVV
RIKVPFIYTR GAYHFKDPQY PVWELTIRVW SELNIGTGTS AYTSLNVLAR FTDLELHGLT
PLSTQMMRNE FRVSTTENVV NLSNYEDARA KMSFALDQED WKSDPSQGGG IKITHFTTWT
SIPTLAAQFP FNASDSVGQQ IKVIPVDPYF FQMTNTNPDQ KCITALASIC QMFCFWRGDL
VFDFQVFPTK YHSGRLLFCF VPGNELIDVT GITLKQATTA PCAVMDITGV QSTLRFRVPW
ISDTPYRVNR YTKSAHQKGE YTAIGKLIVY CYNRLTSPSN VASHVRVNVY LSAINLECFA
PLYHAMDVTT QVGDDSGGFS TTVSTEQNVP DPQVGIKGKA NRGKMDVSGV QAPVGAITTI
EDPVLAKKVP ETFPELKPGE SRHTSDHMSI YKFMGRSHFL CTFTFNSNNK EYTFPITLSS
TSNPPHGLPS TLRWFFNLFQ LYRGPLDLTI IITGATDVDG MAWFTPVGLA VDTPWVEKKS
ALSIDYKTAL GAVRFNTRRT GNIQIRLPWY SYLYAVSGAL DGLGDKTDST FGLVSIQIAN
YNHSDEYLSF SCYLSVTEQS EFYFPRAPLN SNAMLSTESM MSRIAAGDLE SSVDDPRSEE
DRRFESHIEC RKPYKELRLE VGKQRLKYAQ EELSNEVLPP PRKMKGLFSQ AKISLFYTEE
HEIMKFSWRG VTADTRALRR FGFSLAAGRS VWTLEMDAGV LTGRLIRLND EKWTEMKDDK
IVSLIEKFTS NKYWSKVNFP HGMLDLEEIA ANSKDFPNMS ETDLCFLLHW LNPKKINLAD
RMLGLSGVQE IKEQGVGLIA ECRTFLDSIA GTLKSMIFGF HHSVTVEIIN IVLCFIKSGI
LLYVIQQLNQ DEHSHIIGLL RVMNYADIGC SVISCGKVFS KMLETVFNWQ MDSRMMELRT
QSFSNWLRDI CSGITIFKSF KDAIYWLCTK LKDFYEVNYG KKKDVLNILK DNQQKIEKAI
EEADNFCILQ IQDVEKFDQY QTSNWSNPSP KTVYVKEAID RRLHFKVEVK PASFFKNPHN
DMLNVNLAKT NDAIKDMSCV DLIMDGHNIS LMDLLSSLVM TVEIRKQNMS EFMELWSQGI
SDDDSAVAEF FQSFPSGEPS NSKLSSFFQS VTNHKWVAVG AAVGILGLLV GGWFVYKHFS
RKEEEPIPAE GVYHGVTKPK QVIKLDADPV ESQSTLEIAG LVRKNLVQFG VGEKNGCVRW
VMNALGVKDD WLLVPSHAYK FEKDYEMMEF YFNRGGTYYS ISAGNVVIQS LDVGFQDVVL
MKVPTIPKFR DITQHFIKKG DVPRALNRLA TLVTTVNGTP MLISEGPLKM EEKATYVHKK
NDGTTVDLTV DQAWRGKGEG LPGMCGGALV SSNQSIQNAI LGIHVAGGNS ILVAKLITQE
MFQNIDKKIE SQRIMKVEFT QCSMNVVSKT LFRKSPIHHH IDKTMINFPA AMPFSKAEID
PMAMMLSKYS LPIVEEPEDY KEASVFYQNK IVGKTQLVDD FLDLDMAITG APGIDAINMD
SSPGFPYVQE KLTKRDLIWL DENGLLLGVH PRLAQRILFN TVMMENCSDL DVVFTTCPKD
ELRPLEKVLE SKTRAIDACP LDYTILCRMY WGPAISYFHL NPGFHTGVAI GIDPDRQWDE
LFKTMIRFGD VGLDLDFSAF DASLSPFMIR EAGRIMSELS GTPSHFGTAL INTIIYSKHL
LYNCCYHVCG SMPSGSPCTA LLNSIINNIN LYYVFSKIFG KSPVFFCQAL RILCYGDDVL
IVFSRDVQID NLDLIGQKIV DEFKKLGMTA TSADKNVPQL KPVSELTFLK RSFNLVEDRI
RPAISEKTIW SLIAWQRSNA EFEQNLENAQ WFAFMHGYEF YQKFYYFVQS CLEKEMIEYR
LKSYDWWRMR FY


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