POLG_CXA9
ID POLG_CXA9 Reviewed; 2201 AA.
AC P21404;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 188.
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 A9 (strain Griggs).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Enterovirus; Enterovirus B.
OX NCBI_TaxID=12068;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2558158; DOI=10.1099/0022-1317-70-12-3269;
RA Chang K.H., Auvinen P., Hyypiae T., Stanway G.;
RT "The nucleotide sequence of coxsackievirus A9; implications for receptor
RT binding and enterovirus classification.";
RL J. Gen. Virol. 70:3269-3280(1989).
RN [2]
RP INTERACTION WITH HOST ITGAV/ITGB6 INTEGRIN (CAPSID PROTEIN VP1).
RX PubMed=15194773; DOI=10.1128/jvi.78.13.6967-6973.2004;
RA Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D., Stanway G.;
RT "Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus
RT A9.";
RL J. Virol. 78:6967-6973(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-870.
RX PubMed=10647183; DOI=10.1016/s0969-2126(00)88343-4;
RA Hendry E., Hatanaka H., Fry E., Smyth M., Tate J., Stanway G., Santti J.,
RA Maaronen M., Hyypia T., Stuart D.;
RT "The crystal structure of coxsackievirus A9: new insights into the
RT uncoating mechanisms of enteroviruses.";
RL Structure 7:1527-1538(1999).
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 integrin
CC ITGAV/ITGB6 to provide virion attachment to target host cells
CC (Probable). This attachment induces virion internalization (By
CC similarity). Tyrosine kinases are probably involved in the entry
CC process (By similarity). After binding to its receptor, the capsid
CC undergoes conformational changes (By similarity). Capsid protein VP1 N-
CC terminus (that contains an amphipathic alpha-helix) and capsid protein
CC VP4 are externalized (By similarity). Together, they shape a pore in
CC the host membrane through which viral genome is translocated to host
CC cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000305|PubMed:15194773}.
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). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000250|UniProtKB:P03313}.
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). Interacts with host
CC integrin heterodimer ITGAV/ITGB6 (PubMed:15194773).
CC {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:15194773}.
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 ECO:0000250|UniProtKB:P03313}.
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
CC degenerate C4-type zinc-finger with only 3 cysteines (By similarity).
CC The C-terminus is involved in RNA-binding (By similarity). The extreme
CC C-terminus contains a region involved in oligomerization (By
CC similarity). {ECO:0000250|UniProtKB:B9VUU3,
CC 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=1d4m";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D00627; BAA00518.1; -; Genomic_RNA.
DR PIR; JQ0523; GNNYA9.
DR PDB; 1D4M; X-ray; 2.90 A; 1=569-867, 2=70-330, 3=331-568, 4=2-69.
DR PDB; 3J2J; EM; 9.54 A; A=631-852, B=331-568, C=79-330.
DR PDBsum; 1D4M; -.
DR PDBsum; 3J2J; -.
DR SMR; P21404; -.
DR ELM; P21404; -.
DR DrugBank; DB08726; 5-(7-(4-(4,5-dihydro-2-oxazolyl)phenoxy)heptyl)-3-methyl isoxazole.
DR DrugBank; DB08231; Myristic acid.
DR MEROPS; C03.011; -.
DR MEROPS; C03.020; -.
DR MEROPS; N08.001; -.
DR PRIDE; P21404; -.
DR EvolutionaryTrace; P21404; -.
DR Proteomes; UP000000288; 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; 4.10.80.10; -; 1.
DR Gene3D; 6.10.20.20; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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; IPR036988; Pico_P1A_sf.
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 SMART; SM00382; AAA; 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; 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..2201
FT /note="Genome polyprotein"
FT /id="PRO_0000426164"
FT CHAIN 2..867
FT /note="P1"
FT /id="PRO_0000426165"
FT CHAIN 2..330
FT /note="Capsid protein VP0"
FT /id="PRO_0000426166"
FT CHAIN 2..69
FT /note="Capsid protein VP4"
FT /id="PRO_0000426167"
FT CHAIN 70..330
FT /note="Capsid protein VP2"
FT /id="PRO_0000426168"
FT CHAIN 331..568
FT /note="Capsid protein VP3"
FT /id="PRO_0000426169"
FT CHAIN 569..867
FT /note="Capsid protein VP1"
FT /id="PRO_0000426170"
FT CHAIN 868..1445
FT /note="P2"
FT /id="PRO_0000426171"
FT CHAIN 868..1017
FT /note="Protease 2A"
FT /id="PRO_0000426172"
FT CHAIN 1018..1116
FT /note="Protein 2B"
FT /id="PRO_0000039508"
FT CHAIN 1117..1445
FT /note="Protein 2C"
FT /id="PRO_0000039509"
FT CHAIN 1446..2201
FT /note="P3"
FT /id="PRO_0000426173"
FT CHAIN 1446..1556
FT /note="Protein 3AB"
FT /id="PRO_0000426174"
FT CHAIN 1446..1534
FT /note="Protein 3A"
FT /id="PRO_0000039510"
FT CHAIN 1535..1556
FT /note="Viral protein genome-linked"
FT /id="PRO_0000426175"
FT CHAIN 1557..2201
FT /note="Protein 3CD"
FT /id="PRO_0000426176"
FT CHAIN 1557..1739
FT /note="Protease 3C"
FT /id="PRO_0000426177"
FT CHAIN 1740..2201
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000426178"
FT TOPO_DOM 2..1511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1512..1527
FT /evidence="ECO:0000255"
FT TOPO_DOM 1528..2201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1221..1377
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1557..1735
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1966..2082
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ZN_FING 1385..1402
FT /note="C4-type; degenerate"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT REGION 566..582
FT /note="Amphipathic alpha-helix"
FT /evidence="ECO:0000255"
FT REGION 1117..1255
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1117..1189
FT /note="Membrane-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1138..1142
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1429..1436
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1440..1445
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT MOTIF 858..860
FT /note="Cell attachment site"
FT ACT_SITE 888
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 906
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 977
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 1596
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1627
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1703
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 923
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 925
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 983
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 985
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 1385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT BINDING 1397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT BINDING 1402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT BINDING 1972
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 1972
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 2068
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 2068
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 330..331
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 867..868
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1017..1018
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1116..1117
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1141
FT /note="Involved in the interaction with host RTN3"
FT /evidence="ECO:0000250|UniProtKB:Q66478"
FT SITE 1445..1446
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1534..1535
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1556..1557
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1739..1740
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT MOD_RES 1537
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 3..7
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1D4M"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 168..180
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1D4M"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:1D4M"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1D4M"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 288..299
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 308..324
FT /evidence="ECO:0007829|PDB:1D4M"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 394..398
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:1D4M"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:1D4M"
FT TURN 423..427
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 429..434
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 444..450
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 459..465
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 481..487
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 519..526
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 536..546
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 551..555
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 612..615
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 632..636
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 640..650
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 654..657
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 658..662
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 665..668
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 669..675
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 678..695
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 709..715
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 728..731
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 733..735
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 737..741
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 756..762
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 766..769
FT /evidence="ECO:0007829|PDB:1D4M"
FT TURN 770..772
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 773..777
FT /evidence="ECO:0007829|PDB:1D4M"
FT HELIX 778..781
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 786..793
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 800..818
FT /evidence="ECO:0007829|PDB:1D4M"
FT STRAND 843..845
FT /evidence="ECO:0007829|PDB:1D4M"
SQ SEQUENCE 2201 AA; 246535 MW; CCEA86F9E80F385F CRC64;
MGAQVSTQKT GAHETSLSAA GNSIIHYTNI NYYKDAASNS ANRQDFTQDP SKFTEPVKDV
MIKSLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV VVGYGRWPTY LRDDEATAED
QPTQPDVATC RFYTLDSIKW EKGSVGWWWK FPEALSDMGL FGQNMQYHYL GRAGYTIHLQ
CNASKFHQGC LLVVCVPEAE MGGAVVGQAF SATAMANGDK AYEFTSATQS DQTKVQTAIH
NAGMGVGVGN LTIYPHQWIN LRTNNSATIV MPYINSVPMD NMFRHYNFTL MVIPFVKLDY
ADTASTYVPI TVTVAPMCAE YNGLRLAQAQ GLPTMNTPGS TQFLTSDDFQ SPCALPQFDV
TPSMNIPGEV KNLMEIAEVD SVVPVNNVQD TTDQMEMFRI PVTINAPLQQ QVFGLRLQPG
LDSVFKHTLL GEILNYYAHW SGSMKLTFVF CGSAMATGKF LIAYSPPGAN PPKTRKDAML
GTHIIWDIGL QSSCVLCVPW ISQTHYRLVQ QDEYTSAGYV TCWYQTGMIV PPGTPNSSSI
MCFASACNDF SVRMLRDTPF ISQDNKLQGD VEEAIERARC TVADTMRTGP SNSASVPALT
AVETGHTSQV TPSDTMQTRH VKNYHSRSES TVENFLGRSA CVYMEEYKTT DKHVNKKFVA
WPINTKQMVQ MRRKLEMFTY LRFDMEVTFV ITSRQDPGTT LAQDMPVLTR QIMYVPPGGP
IPAKVDDYAW QTSTNPSIFW TEGNAPARMS IPFISIGNAY SNFYDGWSNF DQRGSYGYNT
LNNLGHIYVR HVSGSSPHPI TSTIRVYFKP KHTRAWVPRP PRLCQYKKAF SVDFTPTPIT
DTRKDINTVT TVAQSRRRGD MSTLNTHGAF GQQSGAVYVG NYRVINRHLA THTDWQNCVW
EDYNRDLLVS TTTAHGCDVI ARCQCTTGVY FCASKNKHYP VSFEGPGLVE VQESEYYPKR
YQSHVLLAAG FSEPGDCGGI LRCEHGVIGI VTMGGEGVVG FADVRDLLWL EDDAMEQGVK
DYVEQLGNAF GSGFTNQICE QVNLLKESLV GQDSILEKSL KALVKIISAL VIVVRNHDDL
ITVTAILALI GCTSSPWRWL KQKVSQYYGI PMAERQNDSW LKKFTEMTNA CKRMEWIAIK
IQKFIEWLKV KILPEVREKH EFLNRLKQLP LLESQIATIE QSAPSQSDQE QLFSNVQYFA
HYCRKYAPLY AAEAKRVFSL EKKMSNYIQF KSKCRIEPVC LLLHGSPGAG KSVATNLIGR
SLAEKLNSSV YSLPPDPDHF DGYKQQAVVI MDDLCQNPDG KDVSLFCQMV SSVDFVPPMA
ALEEKGILFT SPFVLASTNA GSINAPTVSD SRALARRFHF DMNIEVISMY SQNGKINMPM
SVKTCDEECC PVNFKKCCPL VCGKAIQFID RRTQVRYSLD MLVTEMFREY NHRHSVGATL
EALFQGPPIY REIKISVAPE TPPPPVIADL LKSVDSEDVR EYCKEKGWLI PEVNSTLQIE
KYVSRAFICL QAITTFVSVA GIIYIIYKLF AGFQGAYTGI PNQKPKVPTL RQAKVQGPAF
EFAVAMMKRN SSTVKTEYGE FTMLGIYDRW AVLPRHAKPG PTILMNDQEV GVMDAKELVD
KDGTNLELTL LKLNRNEKFR DIRGFLAKEE MEVNEAVLAI NTSKFPNMYI PVGQVTDYGF
LNLGGTPTKR MLMYNFPTRA GQCGGVLMST GKVLGIHVGG NGHQGFSAAL LKHYFNDEQG
EIEFIESSKD AGFPIINTPS KTKLEPSVFH QVFEGVKEPA VLRNGDPRLK ANFEEAIFSK
YIGNVNTHVD EYMLEAVDHY AGQLATLDIS TEPMKLEDAV YGTEGLEALD LTTSAGYPYV
ALGIKKRDIL SKKTRDLTKL KECMDKYGLN LPMITYVKDQ LRSAEKVAKG KSRLIEASSL
NDSVAMRQTF GNLYKTFHLN PGIVTGSAVG CDPDLFWSKI PVMLNGHLIA FDYSGYDASL
SPVWFACLKL LLEKLGYSHK ETNYIDYLCN SHHLYRDKHY FVRGGMPSGC SGTSIFNSMI
NNIIIRTLML KVYKGIDLDQ FRMIAYGDDV IASYPWPIDA SLLAEAGKDY GLIMTPADKG
ECFNEVTWTN VTFLKRYFRA DEQYPFLVHP VMPMKDIHES IRWTKDPKNT QDHVRSLCLL
AWHNGEHEYE EFIRKIRSVP VGRCLTLPAF STLRRKWLDS F
