POLG_POL2L
ID POLG_POL2L Reviewed; 2207 AA.
AC P06210;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1;
DE Contains:
DE RecName: Full=Capsid protein VP0;
DE AltName: Full=VP4-VP2;
DE Contains:
DE RecName: Full=Capsid protein VP4;
DE AltName: Full=P1A;
DE AltName: Full=Virion protein 4;
DE Contains:
DE RecName: Full=Capsid protein VP2;
DE AltName: Full=P1B;
DE AltName: Full=Virion protein 2;
DE Contains:
DE RecName: Full=Capsid protein VP3;
DE AltName: Full=P1C;
DE AltName: Full=Virion protein 3;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Contains:
DE RecName: Full=P2;
DE Contains:
DE RecName: Full=Protease 2A;
DE Short=P2A;
DE EC=3.4.22.29 {ECO:0000250|UniProtKB:P03300};
DE AltName: Full=Picornain 2A;
DE AltName: Full=Protein 2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=P2C;
DE EC=3.6.1.15 {ECO:0000250|UniProtKB:P03300};
DE Contains:
DE RecName: Full=P3;
DE Contains:
DE RecName: Full=Protein 3AB;
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=Viral protein genome-linked;
DE Short=VPg;
DE AltName: Full=Protein 3B;
DE Short=P3B;
DE Contains:
DE RecName: Full=Protein 3CD;
DE EC=3.4.22.28;
DE Contains:
DE RecName: Full=Protease 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE EC=3.4.22.28 {ECO:0000255|PROSITE-ProRule:PRU01222};
DE AltName: Full=Picornain 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE Short=P3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE Short=RdRp;
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE AltName: Full=3D polymerase;
DE Short=3Dpol;
DE AltName: Full=Protein 3D;
DE Short=3D;
OS Poliovirus type 2 (strain Lansing).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Enterovirus; Enterovirus C.
OX NCBI_TaxID=12084;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3003384; DOI=10.1128/jvi.57.2.515-525.1986;
RA la Monica N., Meriam C., Racaniello V.R.;
RT "Mapping of sequences required for mouse neurovirulence of poliovirus type
RT 2 Lansing.";
RL J. Virol. 57:515-525(1986).
CC -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
CC capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC capsid protein and enclosing the viral positive strand RNA genome (By
CC similarity). Capsid protein VP1 mainly forms the vertices of the capsid
CC (By similarity). Capsid protein VP1 interacts with host cell receptor
CC PVR to provide virion attachment to target host cells (By similarity).
CC This attachment induces virion internalization predominantly through
CC clathrin- and caveolin-independent endocytosis in Hela cells and
CC through caveolin-mediated endocytosis in brain microvascular
CC endothelial cells (By similarity). Tyrosine kinases are probably
CC involved in the entry process (By similarity). Virus binding to PVR
CC induces increased junctional permeability and rearrangement of
CC junctional proteins (By similarity). Modulation of endothelial tight
CC junctions, as well as cytolytic infection of endothelial cells
CC themselves, may result in loss of endothelial integrity which may help
CC the virus to reach the CNS (By similarity). After binding to its
CC receptor, the capsid undergoes conformational changes (By similarity).
CC Capsid protein VP1 N-terminus (that contains an amphipathic alpha-
CC helix) and capsid protein VP4 are externalized (By similarity).
CC Together, they shape a pore in the host membrane through which viral
CC genome is translocated to host cell cytoplasm (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
CC capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC capsid protein and enclosing the viral positive strand RNA genome (By
CC similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
CC capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC capsid protein and enclosing the viral positive strand RNA genome (By
CC similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC shell (By similarity). After binding to the host receptor, the capsid
CC undergoes conformational changes (By similarity). Capsid protein VP4 is
CC released, Capsid protein VP1 N-terminus is externalized, and together,
CC they shape a pore in the host membrane through which the viral genome
CC is translocated into the host cell cytoplasm (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which
CC is cleaved into capsid proteins VP4 and VP2 after maturation (By
CC similarity). Allows the capsid to remain inactive before the maturation
CC step (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protease 2A]: Cysteine protease that cleaves viral
CC polyprotein and specific host proteins (By similarity). It is
CC responsible for the autocatalytic cleavage between the P1 and P2
CC regions, which is the first cleavage occurring in the polyprotein (By
CC similarity). Cleaves also the host translation initiation factor
CC EIF4G1, in order to shut down the capped cellular mRNA translation (By
CC similarity). Inhibits the host nucleus-cytoplasm protein and RNA
CC trafficking by cleaving host members of the nuclear pores including
CC NUP98, NUP62 and NUP153 (By similarity). Counteracts stress granule
CC formation probably by antagonizing its assembly or promoting its
CC dissassembly (By similarity). Cleaves and inhibits host IFIH1/MDA5,
CC thereby inhibiting the type-I IFN production and the establishment of
CC the antiviral state (By similarity). Cleaves and inhibits host MAVS,
CC thereby inhibiting the type-I IFN production and the establishment of
CC the antiviral state (By similarity). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000250|UniProtKB:P03301}.
CC -!- FUNCTION: [Protein 2B]: Plays an essential role in the virus
CC replication cycle by acting as a viroporin. Creates a pore in the host
CC reticulum endoplasmic and as a consequence releases Ca2+ in the
CC cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium
CC may trigger membrane trafficking and transport of viral ER-associated
CC proteins to viroplasms, sites of viral genome replication.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protein 2C]: Induces and associates with structural
CC rearrangements of intracellular membranes. Displays RNA-binding,
CC nucleotide binding and NTPase activities. May play a role in virion
CC morphogenesis and viral RNA encapsidation by interacting with the
CC capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protein 3AB]: Localizes the viral replication complex to the
CC surface of membranous vesicles. Together with protein 3CD binds the
CC Cis-Active RNA Element (CRE) which is involved in RNA synthesis
CC initiation. Acts as a cofactor to stimulate the activity of 3D
CC polymerase, maybe through a nucleid acid chaperone activity.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protein 3A]: Localizes the viral replication complex to the
CC surface of membranous vesicles (By similarity). It inhibits host cell
CC endoplasmic reticulum-to-Golgi apparatus transport and causes the
CC disassembly of the Golgi complex, possibly through GBF1 interaction (By
CC similarity). This would result in depletion of MHC, trail receptors and
CC IFN receptors at the host cell surface (By similarity). Plays an
CC essential role in viral RNA replication by recruiting ACBD3 and PI4KB
CC at the viral replication sites, thereby allowing the formation of the
CC rearranged membranous structures where viral replication takes place
CC (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA
CC replication and remains covalently bound to viral genomic RNA. VPg is
CC uridylylated prior to priming replication into VPg-pUpU (By
CC similarity). The oriI viral genomic sequence may act as a template for
CC this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by
CC the RNA-dependent RNA polymerase to replicate the viral genome (By
CC similarity). Following genome release from the infecting virion in the
CC cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By
CC similarity). During the late stage of the replication cycle, host TDP2
CC is excluded from sites of viral RNA synthesis and encapsidation,
CC allowing for the generation of progeny virions (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protein 3CD]: Involved in the viral replication complex and
CC viral polypeptide maturation. It exhibits protease activity with a
CC specificity and catalytic efficiency that is different from protease
CC 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the
CC 5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic
CC processing of the polyprotein (By similarity). Cleaves host EIF5B,
CC contributing to host translation shutoff (By similarity). Cleaves also
CC host PABPC1, contributing to host translation shutoff (By similarity).
CC Cleaves host DDX58/RIG-I and thus contributes to the inhibition of type
CC I interferon production (By similarity). Cleaves host NLRP1, triggers
CC host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-
CC terminal fragment (By similarity). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000250|UniProtKB:P03303}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genomic
CC RNA on the surface of intracellular membranes. May form linear arrays
CC of subunits that propagate along a strong head-to-tail interaction
CC called interface-I. Covalently attaches UMP to a tyrosine of VPg, which
CC is used to prime RNA synthesis. The positive stranded RNA genome is
CC first replicated at virus induced membranous vesicles, creating a dsRNA
CC genomic replication form. This dsRNA is then used as template to
CC synthesize positive stranded RNA genomes. ss(+)RNA genomes are either
CC translated, replicated or encapsidated. {ECO:0000250|UniProtKB:P03300}.
CC -!- CATALYTIC ACTIVITY: [Protein 2C]:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000250|UniProtKB:P03300};
CC -!- CATALYTIC ACTIVITY: [Protease 2A]:
CC Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus
CC polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300};
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY: [Protease 3C]:
CC Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus
CC polyprotein. In other picornavirus reactions Glu may be substituted
CC for Gln, and Ser or Thr for Gly.; EC=3.4.22.28;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
CC -!- COFACTOR: [RNA-directed RNA polymerase]:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P03300};
CC Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal
CC center (By similarity). The magnesium ions are not prebound but only
CC present for catalysis (By similarity). Requires the presence of 3CDpro
CC or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000250|UniProtKB:P03313};
CC -!- ACTIVITY REGULATION: [RNA-directed RNA polymerase]: Replication or
CC transcription is subject to high level of random mutations by the
CC nucleotide analog ribavirin. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 and
CC capsid protein VP3 to form heterotrimeric protomers.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0, and
CC capsid protein VP3 to form heterotrimeric protomers (By similarity).
CC Interacts with human PVR (By similarity). Five protomers subsequently
CC associate to form pentamers which serve as building blocks for the
CC capsid (By similarity). Interacts with capsid protein VP2, capsid
CC protein VP3 and capsid protein VP4 following cleavage of capsid protein
CC VP0 (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP2]: Interacts with capsid protein VP1 and
CC capsid protein VP3 in the mature capsid.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP3]: Interacts with capsid protein VP0 and
CC capsid protein VP1 to form heterotrimeric protomers (By similarity).
CC Five protomers subsequently associate to form pentamers which serve as
CC building blocks for the capsid (By similarity). Interacts with capsid
CC protein VP4 in the mature capsid (By similarity). Interacts with
CC protein 2C; this interaction may be important for virion morphogenesis
CC (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP4]: Interacts with capsid protein VP1 and
CC capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Protease 2A]: Homodimer. {ECO:0000250|UniProtKB:P04936}.
CC -!- SUBUNIT: [Protein 2C]: Homohexamer; forms a hexameric ring structure
CC with 6-fold symmetry characteristic of AAA+ ATPases (By similarity).
CC Interacts (via N-terminus) with host RTN3 (via reticulon domain); this
CC interaction is important for viral replication (By similarity).
CC Interacts with capsid protein VP3; this interaction may be important
CC for virion morphogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Protein 3AB]: Interacts with protein 3CD.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Protein 3A]: Homodimer (By similarity). Interacts with host
CC GBF1 (By similarity). Interacts (via GOLD domain) with host ACBD3 (via
CC GOLD domain); this interaction allows the formation of a viral protein
CC 3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will stimulate
CC the recruitment of host PI4KB in order to synthesize PI4P at the viral
CC RNA replication sites (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Viral protein genome-linked]: Interacts with RNA-directed RNA
CC polymerase. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Protein 3CD]: Interacts with protein 3AB and with RNA-
CC directed RNA polymerase. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with Viral protein
CC genome-linked and with protein 3CD. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [Protein 3AB]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q66478}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P03300}. Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
CC vesicle membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes
CC to the surface of intracellular membrane vesicles that are induced
CC after virus infection as the site for viral RNA replication. These
CC vesicles are derived from the endoplasmic reticulum.
CC -!- DOMAIN: [Protein 2C]: The N-terminus has membrane-binding (By
CC similarity). The N-terminus also displays RNA-binding properties (By
CC similarity). The N-terminus is involved in oligomerization (By
CC similarity). The central part contains an ATPase domain and a C4-type
CC zinc-finger (By similarity). The C-terminus is involved in RNA-binding
CC (By similarity). The extreme C-terminus contains a region involved in
CC oligomerization (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the
CC viral proteases yield processing intermediates and the mature proteins.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Capsid protein VP0]: Myristoylation is required for the formation
CC of pentamers during virus assembly. Further assembly of 12 pentamers
CC and a molecule of genomic RNA generates the provirion.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Capsid protein VP0]: During virion maturation, immature virions
CC are rendered infectious following cleavage of VP0 into VP4 and VP2.
CC This maturation seems to be an autocatalytic event triggered by the
CC presence of RNA in the capsid and it is followed by a conformational
CC change infectious virion. {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
CC encapsidation and formation of the mature virus particle.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [Viral protein genome-linked]: VPg is uridylylated by the
CC polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for
CC the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1eah";
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DR EMBL; M12197; AAA46912.1; -; Genomic_RNA.
DR PIR; A29507; GNNY5P.
DR PDB; 1EAH; X-ray; 2.90 A; 1=579-879, 2=70-340, 3=341-578, 4=2-69.
DR PDB; 3EPF; EM; 9.00 A; 1=602-879, 2=79-340, 3=341-575, 4=2-69.
DR PDBsum; 1EAH; -.
DR PDBsum; 3EPF; -.
DR SMR; P06210; -.
DR DrugBank; DB08231; Myristic acid.
DR MEROPS; C03.020; -.
DR PRIDE; P06210; -.
DR EvolutionaryTrace; P06210; -.
DR Proteomes; UP000007638; Genome.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0039554; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host MDA-5 activity; IEA:UniProtKB-KW.
DR GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IEA:UniProtKB-KW.
DR GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd00205; rhv_like; 3.
DR Gene3D; 2.40.10.10; -; 4.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 6.10.20.20; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014838; P3A.
DR InterPro; IPR036203; P3A_soluble_dom.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000081; Peptidase_C3.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR003138; Pico_P1A.
DR InterPro; IPR002527; Pico_P2B.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF08727; P3A; 1.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF02226; Pico_P1A; 1.
DR Pfam; PF00947; Pico_P2A; 1.
DR Pfam; PF01552; Pico_P2B; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 3.
DR Pfam; PF00910; RNA_helicase; 1.
DR SUPFAM; SSF50494; SSF50494; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF89043; SSF89043; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Autocatalytic cleavage; Capsid protein;
KW Clathrin- and caveolin-independent endocytosis of virus by host;
KW Covalent protein-RNA linkage; DNA replication;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host transcription shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Helicase; Host cytoplasm;
KW Host cytoplasmic vesicle; Host gene expression shutoff by virus;
KW Host membrane; Host mRNA suppression by virus; Host nucleus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of eukaryotic host transcription initiation by virus;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host MAVS by virus; Inhibition of host MDA5 by virus;
KW Inhibition of host mRNA nuclear export by virus;
KW Inhibition of host RIG-I by virus; Inhibition of host RLR pathway by virus;
KW Ion channel; Ion transport; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Pore-mediated penetration of viral genome into host cell;
KW Protease; Repeat; RNA-binding; RNA-directed RNA polymerase;
KW T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
KW Transport; Viral attachment to host cell; Viral immunoevasion;
KW Viral ion channel; Viral penetration into host cytoplasm;
KW Viral RNA replication; Virion; Virus endocytosis by host;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT CHAIN 2..2207
FT /note="Genome polyprotein"
FT /id="PRO_0000426611"
FT CHAIN 2..879
FT /note="P1"
FT /id="PRO_0000426612"
FT CHAIN 2..340
FT /note="Capsid protein VP0"
FT /id="PRO_0000426613"
FT CHAIN 2..69
FT /note="Capsid protein VP4"
FT /id="PRO_0000426614"
FT CHAIN 70..340
FT /note="Capsid protein VP2"
FT /id="PRO_0000426615"
FT CHAIN 341..578
FT /note="Capsid protein VP3"
FT /id="PRO_0000426616"
FT CHAIN 579..879
FT /note="Capsid protein VP1"
FT /id="PRO_0000426617"
FT CHAIN 880..1454
FT /note="P2"
FT /id="PRO_0000426618"
FT CHAIN 880..1028
FT /note="Protease 2A"
FT /id="PRO_0000426619"
FT CHAIN 1029..1125
FT /note="Protein 2B"
FT /id="PRO_0000040107"
FT CHAIN 1126..1454
FT /note="Protein 2C"
FT /id="PRO_0000040108"
FT CHAIN 1455..2207
FT /note="P3"
FT /id="PRO_0000426620"
FT CHAIN 1455..1563
FT /note="Protein 3AB"
FT /id="PRO_0000426621"
FT CHAIN 1455..1541
FT /note="Protein 3A"
FT /id="PRO_0000040109"
FT CHAIN 1542..1563
FT /note="Viral protein genome-linked"
FT /id="PRO_0000426622"
FT CHAIN 1564..2207
FT /note="Protein 3CD"
FT /id="PRO_0000426623"
FT CHAIN 1564..1746
FT /note="Protease 3C"
FT /id="PRO_0000426624"
FT CHAIN 1747..2207
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000426625"
FT TOPO_DOM 2..1518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1519..1534
FT /evidence="ECO:0000255"
FT TOPO_DOM 1535..2207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1230..1386
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1564..1742
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1973..2088
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ZN_FING 1394..1411
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 579..599
FT /note="Amphipathic alpha-helix"
FT /evidence="ECO:0000255"
FT REGION 597..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1264
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1126..1198
FT /note="Membrane-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1147..1151
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1438..1445
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1449..1454
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT COMPBIAS 628..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 899
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 917
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 988
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 1603
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1634
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1710
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 934
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT BINDING 936
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT BINDING 994
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT BINDING 996
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q9QF31"
FT BINDING 1254..1261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT BINDING 1394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1979
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1979
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 2074
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 2074
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT SITE 69..70
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT SITE 340..341
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 879..880
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1028..1029
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1125..1126
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1150
FT /note="Involved in the interaction with host RTN3"
FT /evidence="ECO:0000250|UniProtKB:Q66478"
FT SITE 1454..1455
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1541..1542
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1563..1564
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1746..1747
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT MOD_RES 1544
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1EAH"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 168..180
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 187..197
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1EAH"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:1EAH"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:1EAH"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 295..307
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 315..331
FT /evidence="ECO:0007829|PDB:1EAH"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:1EAH"
FT TURN 399..403
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:1EAH"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:1EAH"
FT TURN 433..437
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 439..444
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 513..520
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 529..536
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 546..556
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 655..659
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 663..671
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 683..687
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 695..700
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 703..725
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 732..738
FT /evidence="ECO:0007829|PDB:1EAH"
FT HELIX 751..754
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 760..764
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 770..774
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 779..785
FT /evidence="ECO:0007829|PDB:1EAH"
FT TURN 800..803
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 812..815
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 817..822
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 831..849
FT /evidence="ECO:0007829|PDB:1EAH"
FT STRAND 859..862
FT /evidence="ECO:0007829|PDB:1EAH"
SQ SEQUENCE 2207 AA; 245831 MW; 2B1E2070B7D44F99 CRC64;
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYRDSASNA ASKQDFAQDP SKFTEPIKDV
LIKTAPTLNS PNIEACGYSD RVMQLTLGNS TITTQEAANS VVAYGRWPEY IKDSEANPVD
QPTEPDVAAC RFYTLDTVTW RKESRGWWWK LPDALKDMGL FGQNMFYHYL GRAGYTVHVQ
CNASKFHQGA LGVFAVPEMC LAGDSTTHMF TKYENANPGE KGGEFKGSFT LDTNATNPAR
NFCPVDYLFG SGVLAGNAFV YPHQIINLRT NNCATLVLPY VNSLSIDSMT KHNNWGIAIL
PLAPLDFATE SSTEIPITLT IAPMCCEFNG LRNITVPRTQ GLPVLNTPGS NQYLTADNYQ
SPCAIPEFDV TPPIDIPGEV RNMMELAEID TMIPLNLTNQ RKNTMDMYRV ELNDAAHSDT
PILCLSLSPA SDPRLAHTML GEILNYYTHW AGSLKFTFLF CGSMMATGKL LVSYAPPGAE
APKSRKEAML GTHVIWDIGL QSSCTMVVPW ISNTTYRQTI NDSFTEGGYI SMFYQTRVVV
PLSTPRKMDI LGFVSACNDF SVRLLRDTTH ISQEAMPQGL GDLIEGVVEG VTRNALTPLT
PANNLPDTQS SGPAHSKETP ALTAVETGAT NPLVPSDTVQ TRHVIQKRTR SESTVESFFA
RGACVAIIEV DNDAPTKRAS KLFSVWKITY KDTVQLRRKL EFFTYSRFDM EFTFVVTSNY
TDANNGHALN QVYQIMYIPP GAPIPGKWND YTWQTSSNPS VFYTYGAPPA RISVPYVGIA
NAYSHFYDGF AKVPLAGQAS TEGDSLYGAA SLNDFGSLAV RVVNDHNPTK LTSKIRVYMK
PKHVRVWCPR PPRAVPYYGP GVDYKDGLAP LPGKGLTTYG FGHQNKAVYT AGYKICNYHL
ATQEDLQNAV NIMWIRDLLV VESKAQGIDS IARCNCHTGV YYCESRRKYY PVSFTGPTFQ
YMEANEYYPA RYQSHMLIGH GFASPGDCGG ILRCQHGVIG IITAGGEGLV AFSDIRDLYA
YEEEAMEQGV SNYIESLGAA FGSGFTQQIG NKISELTSMV TSTITEKLLK NLIKIISSLV
IITRNYEDTT TVLATLALLG CDASPWQWLK KKACDILEIP YIMRQGDSWL KKFTEACNAA
KGLEWVSNKI SKFIDWLKEK IIPQARDKLE FVTKLKQLEM LENQIATIHQ SCPSQEHQEI
LFNNVRWLSI QSKRFAPLYA VEAKRIQKLE HTINNYVQFK SKHRIEPVCL LVHGSPGTGK
SVATNLIARA IAEKENTSTY SLPPDPSHFD GYKQQGVVIM DDLNQNPDGA DMKLFCQMVS
TVEFIPPMAS LEEKGILFTS NYVLASTNSS RITPPTVAHS DALARRFAFD MDIQIMSEYS
RDGKLNMAMA TEMCKNCHHP ANFKRCCPLV CGKAIQLMDK SSRVRYSIDQ ITTMIINERN
RRSSIGNCME ALFQGPLQYK DLKIDIKTTP PPECINDLLQ AVDSQEVRDY CEKKGWIVDI
TSQVQTERNI NRAMTILQAV TTFAAVAGVV YVMYKLFAGH QGAYTGLPNK RPNVPTIRTA
KVQGPGFDYA VAMAKRNILT ATTIKGEFTM LGVHDNVAIL PTHASPGETI VIDGKEVEVL
DAKALEDQAG TNLEITIVTL KRNEKFRDIR PHIPTQITET NDGVLIVNTS KYPNMYVPVG
AVTEQGYLNL SGRQTARTLM YNFPTRAGQC GGVITCTGKV IGMHVGGNGS HGFAAALKRS
YFTQSQGEIQ WMRPSKEVGY PVINAPSKTK LEPSAFHYVF EGVKEPAVLT KSDPRLKTDF
EEAIFSKYVG NKITEVDEYM KEAVDHYAGQ LMSLDINTEQ MCLEDAMYGT DGLEALDLST
SAGYPYVAMG KKKRDILNKQ TRDTKEMQRL LDTYGINLPL VTYVKDELRS KTKVEQGKSR
LIEASSLNDS VAMRMAFGNL YAAFHKNPGV VTGSAVGCDP DLFWSKIPVL MEEKLFAFDY
TGYDASLSPA WFEALKMVLE KIGFGDRVDY IDYLNHSHHL YKNKTYCVKG GMPSGCSGTS
IFNSMINNLI IRTLLLKTYK GIDLDHLKMI AYGDDVIASY PHEVDASLLA QSGKDYGLTM
TPADKSATFE TVTWENVTFL KRFFRADEKY PFLVHPVMPM KEIHESIRWT KDPRNTQDHV
RSLCLLAWHN GEEEYNKFLA KIRSVPIGRA LLLPEYSTLY RRWLDSF
