POLG_CXA21
ID POLG_CXA21 Reviewed; 2206 AA.
AC P22055;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
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 Coxsackievirus A21 (strain Coe).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Enterovirus; Enterovirus C.
OX NCBI_TaxID=12070;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2584950; DOI=10.1099/0022-1317-70-11-2943;
RA Hughes P.J., North C., Minor P.D., Stanway G.;
RT "The complete nucleotide sequence of coxsackievirus A21.";
RL J. Gen. Virol. 70:2943-2952(1989).
RN [2]
RP FUNCTION (PROTEASE 2A).
RX PubMed=30867299; DOI=10.1128/jvi.00222-19;
RA Visser L.J., Langereis M.A., Rabouw H.H., Wahedi M., Muntjewerff E.M.,
RA de Groot R.J., van Kuppeveld F.J.M.;
RT "Essential Role of Enterovirus 2A Protease in Counteracting Stress Granule
RT Formation and the Induction of Type I Interferon.";
RL J. Virol. 93:0-0(2019).
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 to provide virion attachment to target host cells (By similarity). This
CC attachment induces virion internalization (By similarity). Tyrosine
CC kinases are probably involved in the entry process (By similarity).
CC After binding to its receptor, the capsid undergoes conformational
CC changes (By similarity). Capsid protein VP1 N-terminus (that contains
CC an amphipathic alpha-helix) and capsid protein VP4 are externalized (By
CC similarity). Together, they shape a pore in the host membrane through
CC which viral genome is translocated to host cell cytoplasm (By
CC similarity). {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 (By
CC similarity). Counteracts stress granule formation probably by
CC antagonizing its assembly or promoting its dissassembly (By
CC similarity). Cleaves and inhibits host IFIH1/MDA5, thereby inhibiting
CC the type-I IFN production and the establishment of the antiviral state
CC (By similarity). Cleaves and inhibits host MAVS, thereby inhibiting the
CC type-I IFN production and the establishment of the antiviral state (By
CC similarity). Counteracts stress granule formation probably by
CC antagonizing its assembly or promoting its dissassembly
CC (PubMed:30867299). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000250|UniProtKB:P03313, ECO:0000269|PubMed:30867299}.
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 ECO:0000250|UniProtKB:P03313}.
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: [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 -!- 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 NLRP1, triggers host N-glycine-mediated degradation of the
CC autoinhibitory NLRP1 N-terminal fragment (By similarity).
CC {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03303}.
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 Five protomers subsequently associate to form pentamers which serve as
CC building blocks for the capsid (By similarity). Interacts with capsid
CC protein VP2, capsid protein VP3 and capsid protein VP4 following
CC cleavage of capsid protein VP0 (By similarity).
CC {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=1z7s";
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DR EMBL; D00538; BAA00426.1; -; Genomic_RNA.
DR PIR; A33373; GNNY21.
DR PDB; 1Z7S; X-ray; 3.20 A; 1=582-879, 2=70-341, 3=342-581, 4=2-69.
DR PDB; 1Z7Z; EM; 8.00 A; 4=869-879.
DR PDBsum; 1Z7S; -.
DR PDBsum; 1Z7Z; -.
DR SMR; P22055; -.
DR DrugBank; DB08231; Myristic acid.
DR MEROPS; C03.001; -.
DR MEROPS; C03.020; -.
DR MEROPS; N08.001; -.
DR PRIDE; P22055; -.
DR EvolutionaryTrace; P22055; -.
DR Proteomes; UP000007758; 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:0075509; P:endocytosis involved in viral entry into host cell; 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: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: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: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; 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; 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; Covalent protein-RNA linkage;
KW DNA replication; Eukaryotic host gene expression 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 host innate immune response 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..2206
FT /note="Genome polyprotein"
FT /id="PRO_0000426207"
FT CHAIN 2..879
FT /note="P1"
FT /id="PRO_0000426208"
FT CHAIN 2..341
FT /note="Capsid protein VP0"
FT /id="PRO_0000426209"
FT CHAIN 2..69
FT /note="Capsid protein VP4"
FT /id="PRO_0000426210"
FT CHAIN 70..341
FT /note="Capsid protein VP2"
FT /id="PRO_0000426211"
FT CHAIN 342..581
FT /note="Capsid protein VP3"
FT /id="PRO_0000426212"
FT CHAIN 582..879
FT /note="Capsid protein VP1"
FT /id="PRO_0000426213"
FT CHAIN 880..1453
FT /note="P2"
FT /id="PRO_0000426214"
FT CHAIN 880..1028
FT /note="Protease 2A"
FT /id="PRO_0000039540"
FT CHAIN 1029..1125
FT /note="Protein 2B"
FT /id="PRO_0000039541"
FT CHAIN 1126..1453
FT /note="Protein 2C"
FT /id="PRO_0000039542"
FT CHAIN 1454..2206
FT /note="P3"
FT /id="PRO_0000426215"
FT CHAIN 1454..1562
FT /note="Protein 3AB"
FT /id="PRO_0000426216"
FT CHAIN 1454..1540
FT /note="Protein 3A"
FT /id="PRO_0000039543"
FT CHAIN 1541..1562
FT /note="Viral protein genome-linked"
FT /id="PRO_0000426217"
FT CHAIN 1563..2206
FT /note="Protein 3CD"
FT /id="PRO_0000426218"
FT CHAIN 1563..1745
FT /note="Protease 3C"
FT /id="PRO_0000426219"
FT CHAIN 1746..2206
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000426220"
FT TOPO_DOM 2..1517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1518..1533
FT /evidence="ECO:0000255"
FT TOPO_DOM 1534..2206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1230..1385
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1563..1741
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1972..2087
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ZN_FING 1393..1410
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 581..602
FT /note="Amphipathic alpha-helix"
FT /evidence="ECO:0000255"
FT REGION 582..602
FT /note="Amphipathic alpha-helix"
FT /evidence="ECO:0000255"
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 1437..1444
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1448..1453
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
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 1602
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1633
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1709
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 1393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1978
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 1978
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 2073
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 2073
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 341..342
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 1453..1454
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1540..1541
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1562..1563
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1745..1746
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT MOD_RES 1543
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:1Z7S"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1Z7S"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 168..180
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1Z7S"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:1Z7S"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:1Z7S"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 296..310
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 315..332
FT /evidence="ECO:0007829|PDB:1Z7S"
FT TURN 349..352
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:1Z7S"
FT TURN 400..404
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:1Z7S"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:1Z7S"
FT TURN 433..437
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 439..444
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 513..520
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 529..536
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 546..556
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 633..636
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 653..656
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 661..670
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 678..680
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 681..685
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 693..698
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 701..717
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 730..736
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 749..752
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 754..756
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 758..762
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 769..772
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 777..783
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 787..790
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 793..796
FT /evidence="ECO:0007829|PDB:1Z7S"
FT TURN 798..803
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:1Z7S"
FT HELIX 807..809
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 815..820
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 829..847
FT /evidence="ECO:0007829|PDB:1Z7S"
FT STRAND 857..860
FT /evidence="ECO:0007829|PDB:1Z7S"
SQ SEQUENCE 2206 AA; 246051 MW; 537F6A13AD37723B CRC64;
MGAQVSTQKT GAHENQNVAA NGSTINYTTI NYYKDSASNS ATRQDLSQDP SKFTEPVKDL
MLKTAPALNS PNVEACGYSD RVRQITLGNS TITTQEAANA IVAYGEWPTY INDSEANPVD
APTEPDVSSN RFYTLESVSW KTTSRGWWWK LPDCLKDMGM FGQNMYYHYL GRSGYTIHVQ
CNASKFHQGA LGVFLIPEFV MACNTESKTS YVSYINANPG ERGGEFTNTY NPSNTDVSEG
RQFAALDYLL GSGVLAGNAF VYPHQIINLR TNNSATIVVP YVNSLVIDCM AKHNNWGIVI
LPLAPLAFAA TSSPQVPITV TIAPMCTEFN GLRNITIPVH QGLPTMNTPG SNQFLTSDDF
QSPCALPNFD VTPPIHIPGE VKNMMELAEI DTLIPMNAVD GKVNTMEMYQ IPLNDNLSKA
PIFCLSLSPA SDKRLSHTML GEILNYYTHW TGSIRFTFLF CGSMMATGKL LLSYSPPGAK
PPTNRKDAML GTHIIWDLGL QSSCSMVAPW ISNTVYRRCA RDDFTEGGFI TCFYQTRIVV
PASTPTSMFM LGFVSACPDF SVRLLRDTSH ISQSKLIART QGIEDLIDTA IKNALRVSQP
LRPSQLKQPN GVNSQEVPAL TAVETGASGQ AIPSDVVETR HVINYKTRSE SCLESFFGRA
ACVTILSLTN SSKSGEEKKH FNIWNITYTD TVQLRRKLEF FTYSRFDLEM TFVFTENYPS
TASGEVRNQC DQIMYIPPGA PRPSSWDDYT WQSSSNPSIF YMYGNAPPRM SIPYVGIANA
YSHFYDGFAR VPLEGENTDA GDTFYGLVSI NDFGVLAVRA VNRSNPHTIH TSVRVYMKPK
HIRCWCPRPP RAVLYRGEGV DMISSAIQPL TKVDSITTFG FGHQNKAVYV AGYKICNYHL
ATPSDHLNAI SVLWDRDLMV VESRAQGTDT IARCSCRCGV YYCESRRKYY LVTFTGPTFR
FMEANDYYPA RYQSHMLIGC GFAEPGDCGG ILRCTHGVIG IITAGGEGIV AFADIRDLWV
YEEEAMEQGI TSYIESLGTA FGAGFTHTIS EKVTELTTMV TSTITEKLLK NLVKIVSALV
IVVRNYEDTT TILATLALLG CDISPWQWLK KKACDLLEIP HVMRQGDGWM KKFTEACNAA
KGLRWVSNKI SKFVDWLKCK IIPEAKDKVE FLTKLKQLDM LENQIATIHQ SCPSQEQQEI
LFNNVRWLAV QSRRFAPLYA VEARRISKME STINNYIQFK SKHRIEPVCM LVHGSPGTGK
GIASSLIGRA IAERETTSVY SVPLAPSHFD GYKQQGYDMD DLNQNPDGMD MKLFCQMVST
VEFIPPMASL EEKGILFTSD YVLASTNSHS IAPPTVAHSD ALTRRFAFDV EVYTMSEHSV
KGKLNMATAT QLCKDCPTPA NFKKCCPLVC GKALQLMDRY TRQRFTVDEI TTLIMNEKNR
RANIGNCMEA LFQGPLRYKD LKIDVKTVPP PECISDLLQA VDSQEVRDYC EKKGWIVNVT
SQIQLERNIN RAMTILQAVT TFAAVAGVVY VMYKLFAGQQ GAYTGLPNKK PNVPTIRIAK
VQGPGFDYAV AMAKRNIVTA TTTKGEFTML GVHDNVAILP THAAPGETII VDGKEVEILD
ARALEDQAGT NLEITIITLK RNEKFRDIRP HIPTQITETN DGVLIVNTSK YPNMYVPVGA
VTEQGYLNLS GRQTARTLMY NFPTRAGQCG GIITCTGKVI GMHVGGNGSH GFAAALKRSY
FTQNQGEIQW MRSSKEVGYP IINAPSKTKL EPSAFHYVFE GVKEPAVLTK NDPRLKTDFE
EAIFSKYVGN KITEVDEYMK EAVDHYAGQL MSLDINTEQM CLEDAMYGTD GLEALDLSTS
AGYPYVAMGK KKRDILDKQT RDTKEMQRLL DTYGINLPLV TYVKDELRSK TKVEQGKSRL
IEASSLNDSV AMRMAFGNLY AAFHKNPGVV TGSAVGCDPD LFWSKIPVLM EEKLFAFDYT
GYDASLSPAW FEALKMVLEK IGFGNRVDYI DYLNHSHHLY KNKTYCVKGG MPSGCSGTSI
FNSMINNLII RTLLLRTYKG IDLDHLKMIA YGDDVIASYP HEVDASLLAQ SGKDYGLTMT
PADKSATFET VTWENVTFLK RFFRADEKYP FLVHPVMPMK EIHESIRWTK DPRNTQDHVR
SLCLLAWHNG EEEYNKFLAK IRSVPIGRAL LLPEYSTLYR RWLDSF
