POLG_HRV3
ID POLG_HRV3 Reviewed; 2178 AA.
AC Q82081; A5GZD4; A7KC14;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 4.
DT 03-AUG-2022, entry version 145.
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 Human rhinovirus 3 (HRV-3).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Enterovirus.
OX NCBI_TaxID=44130;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17477878; DOI=10.1186/1743-422x-4-40;
RA Kistler A.L., Webster D.R., Rouskin S., Magrini V., Credle J.J.,
RA Schnurr D.P., Boushey H.A., Mardis E.R., Li H., DeRisi J.L.;
RT "Genome-wide diversity and selective pressure in the human rhinovirus.";
RL Virol. J. 4:40-40(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Tapparel C., Junier T., Gerlach D., Cordey S., Van Belle S., Perrin L.,
RA Zdobnov E.M., Kaiser L.;
RT "New complete genome sequences of human rhinoviruses shed light on their
RT phylogeny and genomic features.";
RL BMC Genomics 8:224-224(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-855, AND X-RAY CRYSTALLOGRAPHY (3.0
RP ANGSTROMS).
RX PubMed=8939746; DOI=10.1016/s0969-2126(96)00128-1;
RA Zhao R., Pevear D.C., Kremer M.J., Giranda V.L., Kofron J.A., Kuhn R.J.,
RA Rossmann M.G.;
RT "Human rhinovirus 3 at 3.0-A resolution.";
RL Structure 4:1205-1220(1996).
RN [4]
RP REVIEW.
RX PubMed=23227049; DOI=10.1155/2012/826301;
RA Fuchs R., Blaas D.;
RT "Productive entry pathways of human rhinoviruses.";
RL Adv. Virol. 2012:826301-826301(2012).
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 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=1rhi";
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DR EMBL; DQ473485; ABF51179.1; -; Genomic_RNA.
DR EMBL; EF173422; ABO69378.1; -; Genomic_RNA.
DR EMBL; U60874; AAB05616.1; -; Genomic_RNA.
DR PDB; 1RHI; X-ray; 3.00 A; 1=568-855, 2=70-331, 3=332-567, 4=2-69.
DR PDBsum; 1RHI; -.
DR SMR; Q82081; -.
DR MEROPS; C03.013; -.
DR MEROPS; C03.020; -.
DR MEROPS; N08.001; -.
DR PRIDE; Q82081; -.
DR EvolutionaryTrace; Q82081; -.
DR Proteomes; UP000013737; Genome.
DR Proteomes; UP000165566; 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; 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 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..2178
FT /note="Genome polyprotein"
FT /id="PRO_0000426521"
FT CHAIN 2..855
FT /note="P1"
FT /id="PRO_0000426522"
FT CHAIN 2..331
FT /note="Capsid protein VP0"
FT /id="PRO_0000426523"
FT CHAIN 2..69
FT /note="Capsid protein VP4"
FT /id="PRO_0000426524"
FT CHAIN 70..331
FT /note="Capsid protein VP2"
FT /id="PRO_0000426525"
FT CHAIN 332..561
FT /note="Capsid protein VP3"
FT /id="PRO_0000426526"
FT CHAIN 562..855
FT /note="Capsid protein VP1"
FT /id="PRO_0000426527"
FT CHAIN 856..1428
FT /note="P2"
FT /id="PRO_0000426528"
FT CHAIN 856..1001
FT /note="Protease 2A"
FT /id="PRO_0000423099"
FT CHAIN 1002..1098
FT /note="Protein 2B"
FT /id="PRO_0000423100"
FT CHAIN 1099..1428
FT /note="Protein 2C"
FT /id="PRO_0000426529"
FT CHAIN 1429..2178
FT /note="P3"
FT /id="PRO_0000426530"
FT CHAIN 1429..1536
FT /note="Protein 3AB"
FT /id="PRO_0000426531"
FT CHAIN 1429..1513
FT /note="Protein 3A"
FT /id="PRO_0000423102"
FT CHAIN 1514..1536
FT /note="Viral protein genome-linked"
FT /id="PRO_0000426532"
FT CHAIN 1537..2178
FT /note="Protein 3CD"
FT /id="PRO_0000426533"
FT CHAIN 1537..1718
FT /note="Protease 3C"
FT /id="PRO_0000426534"
FT CHAIN 1719..2178
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000426535"
FT TOPO_DOM 2..1490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1491..1506
FT /evidence="ECO:0000255"
FT TOPO_DOM 1507..2178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1204..1360
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1537..1714
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1946..2059
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ZN_FING 1368..1385
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..584
FT /note="Amphipathic alpha-helix"
FT /evidence="ECO:0000255"
FT REGION 1100..1238
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1100..1172
FT /note="Membrane-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1121..1125
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1412..1419
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1423..1428
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 875
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 893
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 964
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 1576
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1607
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1682
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 910
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 912
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 970
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 972
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 1368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT BINDING 1951
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 1951
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 2045
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 2045
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 331..332
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 855..856
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1001..1002
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1098..1099
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1124
FT /note="Involved in the interaction with host RTN3"
FT /evidence="ECO:0000250|UniProtKB:Q66478"
FT SITE 1428..1429
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1513..1514
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1536..1537
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1718..1719
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT MOD_RES 1516
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 VARIANT 87
FT /note="L -> M"
FT VARIANT 98
FT /note="A -> R"
FT VARIANT 260
FT /note="L -> M"
FT VARIANT 475
FT /note="E -> K"
FT VARIANT 523
FT /note="Q -> L"
FT VARIANT 846
FT /note="I -> V"
FT VARIANT 1349
FT /note="M -> L"
FT VARIANT 1389
FT /note="I -> V"
FT VARIANT 1703
FT /note="R -> Q"
FT VARIANT 1925
FT /note="E -> G"
FT VARIANT 1978
FT /note="Q -> H"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1RHI"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 168..180
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1RHI"
FT TURN 238..244
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:1RHI"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 286..298
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 307..323
FT /evidence="ECO:0007829|PDB:1RHI"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:1RHI"
FT TURN 374..379
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 427..432
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 473..476
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 517..524
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 536..544
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 549..553
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 630..632
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 634..637
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 642..651
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 660..663
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 665..669
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 673..676
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 677..683
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 686..702
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 714..720
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 733..736
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 742..746
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 749..755
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 760..766
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 770..774
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:1RHI"
FT HELIX 784..786
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 790..795
FT /evidence="ECO:0007829|PDB:1RHI"
FT STRAND 804..822
FT /evidence="ECO:0007829|PDB:1RHI"
SQ SEQUENCE 2178 AA; 242794 MW; 0DFED5280AF25CCF CRC64;
MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASSS SAGQSFSMDP SKFTEPVKDL
MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA IVCYAEWPEY LSDNDASDVN
KTSKPDISVC RFYTLDSKTW KATSKGWCWK LPDALKDMGV FGQNMFYHSL GRTGYTIHVQ
CNATKFHSGC LLVVVIPEHQ LASHEGGTVS VKYKYTHPGD RGIDLDTVEV AGGPTSDAIY
NMDGTLLGNL LIFPHQFINL RTNNTATIVV PYINSVPIDS MTRHNNVSLM VVPIAPLNAP
TGSSPTLPVT VTIAPMCTEF TGIRSRSIVP QGLPTTTLPG SGQFLTTDDR QSPSALPSYE
PTPRIHIPGK VRNLLEIIQV GTLIPMNNTG TNDNVTNYLI PLHADRQNEQ IFGTKLYIGD
GVFKTTLLGE IAQYYTHWSG SLRISLMYTG PALSSAKIIL AYTPPGTRGP EDRKEAMLGT
HVVWDIGLQS TIVMTIPWTS GVQFRYTDPD TYTSAGYLSC WYQTSLILPP QTSGQVYLLS
FISACPDFKL RLMKDTQTIS QTDALTEGLS DELEEVIVEK TKQTLASVSS GPKHTQSVPA
LTANETGATL PTRPSDNVET RTTYMHFNGS ETDVESFLGR AACVHVTEIK NKNAAGLDNH
RKEGLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT ASQPEASSYS SNLTVQAMYV
PPGAPNPKEW DDYTWQSASN PSVFFKVGET SRFSVPFVGI ASAYNCFYDG YSHDDPDTPY
GITVLNHMGS MAFRVVNEHD VHTTIVKIRV YHRAKHVEAW IPRAPRALPY VSIGRTNYPR
DSKTIIKKRT NIKTYGLGPR FGGVFTSNVK IINYHLMTPD DHLNLVAPYP NRDLAVVATG
AHGAETIPHC NCTSGVYYSR YYRKFYPIIC ERPTNIWIEG SSYYPSRYQA GVMKGVGPAE
PGDCGGILRC IHGPIGLLTA GGGGYVCFAD IRQLDFIADE QGLGDYITSL GRAFGTGFTD
QISAKVCELQ DVAKDFLTTK VLSKVVKMIS ALVIICRNHD DLVTVTATLA LLGCDGSPWR
FLKMYISKHF QVPYIERQAN DGWFRKFNDA CNAAKGLEWI ANKISKLIEW IKNKVLPQAR
EKLEFCSKLK QLDILERQIA SIHDSNPTQE KREQLFNNVL WLEQMSQKFS PLYASEAKRI
RDLKNKITNY MQFKSKQRTE PVCVLIHGTP GSGKSLTTSI VGRALAEHFN SSVYSLPPDP
KHFDGYQQQE VVIMDDLNQN PDGQDISMFC QMVSSVDFLP PMASLDNKGM LFTSNFVLAS
TNSNTLSPPT ILNPEALIRR FGFDLDICMH STYTKNGKLN AAMATSLCKD CHQPSNFKKC
CPLVCGKAIS LVDRVSNVRF SIDQLVTAII NDYKNKVKIT DSLEVLFQGP VYKDLEIDIC
NTPPPECISD LLKSVDSEEV REYCKKKKWI IPQISTNIER AVNQASMIIN TILMFVSTLG
IVYVIYKLFA QTQGPYSGNP VHNKLKPPTL KPVVVQGPNT EFALSLLRKN ILTITTEKGE
FTSLGIHDRI CVLPTHAQPG DNVLVNGQKI QIKDKYKLVD PDNTNLELTI IELDRNEKFR
DIRGFISEDL EGLDATLVVH SNGFTNTILD VGPITMAGLI NLSNTPTTRM IRYDYPTKTG
QCGGVLCTTG KIFGIHVGGN GRRGFSAQLK KQYFVEKQGL IVSKQKVRDI GLNPINTPTK
TKLHPSVFYN VFPGSKQPAV LNDNDPRLEV KLAESLFSKY KGNVQMEPTE NMLIAVDHYA
GQLMSLDIST KELTLKEALY GVDGLEPIDV TTSAGYPYVS LGIKKRDILN KETQDVEKMK
FYLDKYGIDL PLVTYIKDEL RSVDKVRLGK SRLIEASSLN DSVNMRMKLG NLYKAFHQNP
GIITESAVGC DPDVFWSVIP CLMDGHLMAF DYSNFDASLS PVWFECLEKV LNKLGFKQPS
LIQSICNTHH IFRDEIYRVE GGMPSGCSGT SIFNSMINNI IIRTLILDAY KGIDLDSLRI
LAYGDDLIVS YPFELDSNIL AAIGKNYGLT ITPPDKSDAF TKITWENITF LKRYFRPDPQ
FPFLIHPVMP MQDIYESIRW TRDPRNTQDH VRSLCMLAWH SGEKDYNDFI TKIRTTDIGK
CLNLPEYSVL RRRWLDLF
