POLG_BOVEV
ID POLG_BOVEV Reviewed; 2175 AA.
AC P12915;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
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 Bovine enterovirus (strain VG-5-27) (BEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Enterovirus.
OX NCBI_TaxID=12065;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2828511; DOI=10.1099/0022-1317-69-2-253;
RA Earle J.A.P., Skuce R.A., Fleming C.S., Hoey E.M., Martin S.J.;
RT "The complete nucleotide sequence of a bovine enterovirus.";
RL J. Gen. Virol. 69:253-263(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-840.
RX PubMed=7773791; DOI=10.1038/nsb0395-224;
RA Smyth M., Tate J., Hoey E.M., Lyons C., Martin S.J., Stuart D.;
RT "Implications for viral uncoating from the structure of bovine
RT enterovirus.";
RL Nat. Struct. Biol. 2:224-231(1995).
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). {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: [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
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=1bev";
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; D00214; BAA24003.1; ALT_SEQ; Genomic_RNA.
DR PIR; A29824; GNNYBE.
DR RefSeq; NP_045756.1; NC_001859.1.
DR PDB; 1BEV; X-ray; 3.00 A; 1=560-840, 2=70-317, 3=318-559, 4=2-69.
DR PDBsum; 1BEV; -.
DR SMR; P12915; -.
DR DrugBank; DB08231; Myristic acid.
DR MEROPS; C03.014; -.
DR MEROPS; C03.020; -.
DR MEROPS; N08.001; -.
DR GeneID; 1493914; -.
DR KEGG; vg:1493914; -.
DR EvolutionaryTrace; P12915; -.
DR Proteomes; UP000006566; 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; -; 2.
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; IPR004004; Helic/Pol/Pept_Calicivir-typ.
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 PRINTS; PR00918; CALICVIRUSNS.
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..2175
FT /note="Genome polyprotein"
FT /id="PRO_0000426107"
FT CHAIN 2..840
FT /note="P1"
FT /id="PRO_0000426108"
FT CHAIN 2..317
FT /note="Capsid protein VP0"
FT /id="PRO_0000426109"
FT CHAIN 2..69
FT /note="Capsid protein VP4"
FT /id="PRO_0000426110"
FT CHAIN 70..317
FT /note="Capsid protein VP2"
FT /id="PRO_0000426111"
FT CHAIN 318..559
FT /note="Capsid protein VP3"
FT /id="PRO_0000426112"
FT CHAIN 560..840
FT /note="Capsid protein VP1"
FT /id="PRO_0000426113"
FT CHAIN 841..1419
FT /note="P2"
FT /id="PRO_0000426114"
FT CHAIN 841..990
FT /note="Protease 2A"
FT /id="PRO_0000039463"
FT CHAIN 991..1089
FT /note="Protein 2B"
FT /id="PRO_0000039464"
FT CHAIN 1090..1419
FT /note="Protein 2C"
FT /id="PRO_0000039465"
FT CHAIN 1420..2175
FT /note="P3"
FT /id="PRO_0000426115"
FT CHAIN 1420..1531
FT /note="Protein 3AB"
FT /id="PRO_0000426116"
FT CHAIN 1420..1508
FT /note="Protein 3A"
FT /id="PRO_0000039466"
FT CHAIN 1509..1531
FT /note="Viral protein genome-linked"
FT /id="PRO_0000426117"
FT CHAIN 1532..2175
FT /note="Protein 3CD"
FT /id="PRO_0000426118"
FT CHAIN 1532..1714
FT /note="Protease 3C"
FT /id="PRO_0000426119"
FT CHAIN 1715..2175
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000426120"
FT TOPO_DOM 2..1485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1486..1501
FT /evidence="ECO:0000255"
FT TOPO_DOM 1502..2175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1194..1352
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1532..1710
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1941..2056
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ZN_FING 1359..1375
FT /note="C4-type; degenerate"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT REGION 557..574
FT /note="Amphipathic alpha-helix"
FT /evidence="ECO:0000255"
FT REGION 560..581
FT /note="Amphipathic alpha-helix"
FT /evidence="ECO:0000255"
FT REGION 1090..1228
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1090..1162
FT /note="Membrane-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1111..1115
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1403..1410
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1414..1419
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 861
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 879
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 950
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 1571
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1602
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1678
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 896
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 898
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 956
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 958
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 1359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT BINDING 1370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT BINDING 1375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT BINDING 1947
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 1947
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 2042
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 2042
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 317..318
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 840..841
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 990..991
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1089..1090
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1114
FT /note="Involved in the interaction with host RTN3"
FT /evidence="ECO:0000250|UniProtKB:Q66478"
FT SITE 1419..1420
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1508..1509
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1531..1532
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1714..1715
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT MOD_RES 1511
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 33..35
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1BEV"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 168..180
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 187..197
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1BEV"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:1BEV"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1BEV"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 273..289
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 294..309
FT /evidence="ECO:0007829|PDB:1BEV"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 397..402
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 415..420
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 479..484
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:1BEV"
FT TURN 499..502
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 503..506
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 510..517
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 527..537
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 542..546
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 610..613
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 630..634
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:1BEV"
FT TURN 647..649
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 662..668
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 671..685
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 699..705
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 718..721
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 727..731
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 737..741
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 746..752
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 756..759
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 765..767
FT /evidence="ECO:0007829|PDB:1BEV"
FT HELIX 772..774
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 778..785
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 792..807
FT /evidence="ECO:0007829|PDB:1BEV"
FT STRAND 818..820
FT /evidence="ECO:0007829|PDB:1BEV"
SQ SEQUENCE 2175 AA; 242504 MW; 44FCADE8704E48FD CRC64;
MGAQLSRNTA GSHTTGTYAT GGSTINYNNI NYYSHAASAA QNKQDFTQDP SKFTQPIADV
IKETAVPLKS PSAEACGYSD RVAQLTLGNS TITTQEAANI CVAYGCWPAK LSDTDATSVD
KPTEPGVSAD AFYTLRSKPW QADSKGWYWK LPDALNNTGM FGQNAQFHYI YRGGWAVHVQ
CNATKFHQGT LLVLAIPEHQ IATQEQPAFD RTMPGSEGGT FQEPFWLEDG TSLGNSLIYP
HQWINLRTNN SATLILPYVN AIPMDSAIRH SNWTLAIIPV APLKYAAETT PLVPITVTIA
PMETEYNGLR RAIASNQGLP TKPGPGSYQF MTTDEDCSPC ILPDFQPTLE IFIPGKVNNL
LEIAQVESIL EANNREGVEG VERYVIPVSV QDALDAQIYA LRLELGGSGP LSSSLLGTLA
KHYTQWSGSV EITCMFTGTF MTTGKVLLAY TPPGGDMPRN REEAMLGTHV VWDFGLQSSI
TLVIPWISAS HFRGVSNDDV LNYQYYAAGH VTIWYQTNMV IPPGFPNTAG IIMMIAAQPN
FSFRIQKDRE DMTQTAILQN DPGKMLKDAI DKQVAGALVA GTTTSTHSVA TDSTPALQAA
ETGATSTARD ESMIETRTIV PTHGIHETSV ESFFGRSSLV GMPLLATGTS ITNWRIDFRE
FVQLRAKMSW FTYMRFDVEF TIIATSSTGQ NVTTEQHTTY QVMYVPPGAP VPSNQDSFQW
QSGCNPSVFA DTDGPPAQFS VPFMSSANAY STVYDGYARF MDTDPDRYGI LPSNFLGFMY
FRTLEDAAHQ VRFRICAKIK HTSCWIPRAP RQAPYKKRYN LVFSGDSDRI CSNRASLTSY
GPFGQQQGAA YVGSYKILNR HLATYADWEN EVWQSYQRDL LVTRVDAHGC DTIARCNCRS
GIYYCKSTAK HYPIVVTPPS IYKIEANDYY PERMQTHILL GIGFAEPGDC GGLLRCEHGV
MGILTVGGGD HVGFADVRDL LWIEDDAMEQ GITDYVQQLG NAFGAGFTAE IANYTNQLRD
MLMGSDSVVE KIIRSLVRLV SALVIVVRNH QDLITVGATL ALLGCEGSPW KWLKRKVCQI
LGINMAERQS DNWMKKFTEM CNAFRGLDWI AAKISKFIDW LKQKILPELK ERAEFVKKLK
QLPLLEAQVN TLEHSSASQE RQEQLFGNVQ YLAHHCRKNA PLYAAEAKRV YHLEKRVLGA
MQFKTKNRIE PVCALIHGSP GTGQSLATMI VGRKLAEYEG SDVYSLPPDP DHFDGYQQQA
VVVMDDLLQN PDGKDMTLFC QMVSTAPFTV PMAALEDKGK LFTSKFVLAS TNAGQVTPPT
VADYKALQRR FFFDCDIEVQ KEYKRDGVTL DVAKATETCE DCSPANFKKC MPLICGKALQ
LKSRKGDGMR YSLDTLISEL RRESNRRYNI GNVLEALFQG PVCYKPLRIE VHEEEPAPSA
ISDLLQAVDS EEVREYCRSK GWIVEERVTE LKLERNVNRA LAVIQSVSLI AAVAGTIYIV
YRLFSGMQGP YSGIGTNYAT KKPVVRQVQT QGPLFDFGVS LLKKNIRTVK TGAGEFTALG
VYDTVVVLPR HAMPGKTIEM NGKDIEVLDA YDLNDKTDTS LELTIVKLKM NEKFRDIRAM
VPDQITDYNE AVVVVNTSYY PQLFTCVGRV KDYGFLNLAG RPTHRVLMYE FPTKAGQCGG
VVISMGKIVG VHVGGNGAQG FAASLLRRYF TAEQGQIEYI EKSKDAGYPV INAPTQTKLE
PSVFFDVFPG VKEPAVLHKK DKRLETNFEE ALFSKYIGNV QRDMPEELLI AIDHYSEQLK
MLNIDPRPIS MEDAIYGTEG LEALDLGTSA SYPYVAMGIK KRDILNKETR DVTKMQECID
KYGLNLPMVT YVKDELRAPD KIRKGKSRLI EASSLNDSVA MRCYFGNLYK VFHTNPGTIS
GCAVGCDPET FWSKIPVMMD GELFGFDYTA YDASLSPMWF HALAEVLRRI GFVECKHFID
QLCCSHHLYM DKHYYVVGGM PSGCSGTSIF NSMINNLIIR TLVLTVYKNI DLDDLKIIAY
GDDVLASYPY EIDASLLAEA GKSFGLIMTP PDKSAEFVKL TWDNVTFLKR KFVRDARYPF
LVHPVMDMSN IHESIRWTKD PRHTEDHVRS LCLLAWHCGE EEYNEFVTKI RSVPVGRALH
LPSFKALERK WYDSF
