POLG_CX16T
ID POLG_CX16T Reviewed; 2193 AA.
AC Q9QF31;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 161.
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 A16 (strain Tainan/5079/98).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Enterovirus; Enterovirus A.
OX NCBI_TaxID=231417;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11536241; DOI=10.1002/jmv.2038;
RA Yan J.-J., Su I.-J., Chen P.-F., Liu C.-C., Yu C.-K., Wang J.-R.;
RT "Complete genome analysis of enterovirus 71 isolated from an outbreak in
RT Taiwan and rapid identification of enterovirus 71 and coxsackievirus A16 by
RT RT-PCR.";
RL J. Med. Virol. 65:331-339(2001).
RN [2]
RP INTERACTION WITH HOST RTN3 (PROTEIN 2C).
RX PubMed=17182608; DOI=10.1074/jbc.m611145200;
RA Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H.,
RA Lin K.-H., Lai H.-C., Tang P., Horng J.-T.;
RT "Reticulon 3 binds the 2C protein of enterovirus 71 and is required for
RT viral replication.";
RL J. Biol. Chem. 282:5888-5898(2007).
RN [3]
RP INTERACTION WITH HOST IFIH1 (PROTEASE 3C), FUNCTION (PROTEASE 3C), AND
RP INTERACTION WITH HOST MAP3K7 (PROTEASE 3C).
RC STRAIN=CC024;
RX PubMed=28424289; DOI=10.1128/jvi.00546-17;
RA Rui Y., Su J., Wang H., Chang J., Wang S., Zheng W., Cai Y., Wei W.,
RA Gordy J.T., Markham R., Kong W., Zhang W., Yu X.F.;
RT "Disruption of MDA5-Mediated Innate Immune Responses by the 3C Proteins of
RT Coxsackievirus A16, Coxsackievirus A6, and Enterovirus D68.";
RL J. Virol. 91:0-0(2017).
RN [4] {ECO:0007744|PDB:4MG3}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 863-1007 IN COMPLEX WITH ZINC,
RP AND SUBUNIT (PROTEASE 2A).
RX PubMed=24026848; DOI=10.1007/s13238-013-3914-z;
RA Sun Y., Wang X., Yuan S., Dang M., Li X., Zhang X.C., Rao Z.;
RT "An open conformation determined by a structural switch for 2A protease
RT from coxsackievirus A16.";
RL Protein Cell 4:782-792(2013).
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. This attachment
CC induces virion internalization (By similarity). After binding to its
CC receptor, the capsid undergoes conformational changes (By similarity).
CC Capsid protein VP1 N-terminus (that contains an amphipathic alpha-
CC helix) and capsid protein VP4 are externalized (By similarity).
CC Together, they shape a pore in the host membrane through which viral
CC genome is translocated to host cell cytoplasm (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
CC capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC capsid protein and enclosing the viral positive strand RNA genome (By
CC similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
CC capsid is 300 Angstroms in diameter, composed of 60 copies of each
CC capsid protein and enclosing the viral positive strand RNA genome (By
CC similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
CC shell (By similarity). After binding to the host receptor, the capsid
CC undergoes conformational changes (By similarity). Capsid protein VP4 is
CC released, Capsid protein VP1 N-terminus is externalized, and together,
CC they shape a pore in the host membrane through which the viral genome
CC is translocated into the host cell cytoplasm (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which
CC is cleaved into capsid proteins VP4 and VP2 after maturation (By
CC similarity). Allows the capsid to remain inactive before the maturation
CC step (By similarity). {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protease 2A]: Cysteine protease that cleaves viral
CC polyprotein and specific host proteins (By similarity). It is
CC responsible for the autocatalytic cleavage between the P1 and P2
CC regions, which is the first cleavage occurring in the polyprotein (By
CC similarity). Cleaves also the host translation initiation factor
CC EIF4G1, in order to shut down the capped cellular mRNA translation (By
CC similarity). Inhibits the host nucleus-cytoplasm protein and RNA
CC trafficking by cleaving host members of the nuclear pores (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:P03301, 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 -!- FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA
CC replication and remains covalently bound to viral genomic RNA. VPg is
CC uridylylated prior to priming replication into VPg-pUpU (By
CC similarity). The oriI viral genomic sequence may act as a template for
CC this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by
CC the RNA-dependent RNA polymerase to replicate the viral genome (By
CC similarity). Following genome release from the infecting virion in the
CC cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By
CC similarity). During the late stage of the replication cycle, host TDP2
CC is excluded from sites of viral RNA synthesis and encapsidation,
CC allowing for the generation of progeny virions (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protein 3CD]: Involved in the viral replication complex and
CC viral polypeptide maturation. It exhibits protease activity with a
CC specificity and catalytic efficiency that is different from protease
CC 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the
CC 5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic
CC processing of the polyprotein (By similarity). Cleaves host EIF5B,
CC contributing to host translation shutoff (By similarity). Cleaves also
CC host PABPC1, contributing to host translation shutoff (By similarity).
CC Binds and inhibits host IFIH1/MDA5, thereby inhibiting the type-I IFN
CC production and the establishment of the antiviral state
CC (PubMed:28424289). Cleaves host MAP3K7/TAK1, resulting in inhibition of
CC TRAF6-triggered NF-kappa-B induction (PubMed:28424289). Cleaves host
CC 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 ECO:0000269|PubMed:28424289}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- CATALYTIC ACTIVITY: [Protein 2C]:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000250|UniProtKB:P03300};
CC -!- CATALYTIC ACTIVITY: [Protease 2A]:
CC Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus
CC polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300};
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY: [Protease 3C]:
CC Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus
CC polyprotein. In other picornavirus reactions Glu may be substituted
CC for Gln, and Ser or Thr for Gly.; EC=3.4.22.28;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
CC -!- COFACTOR: [RNA-directed RNA polymerase]:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P03300};
CC Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal
CC center (By similarity). The magnesium ions are not prebound but only
CC present for catalysis (By similarity). Requires the presence of 3CDpro
CC or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300,
CC ECO:0000250|UniProtKB:P03313};
CC -!- ACTIVITY REGULATION: [RNA-directed RNA polymerase]: Replication or
CC transcription is subject to high level of random mutations by the
CC nucleotide analog ribavirin. {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 and
CC capsid protein VP3 to form heterotrimeric protomers.
CC {ECO:0000250|UniProtKB:P03300}.
CC -!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0, and
CC capsid protein VP3 to form heterotrimeric protomers (By similarity).
CC 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:0000269|PubMed:24026848}.
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 (PubMed:17182608).
CC Interacts with capsid protein VP3; this interaction may be important
CC for virion morphogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P03300, ECO:0000269|PubMed:17182608}.
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: [Protease 3C]: Interacts with host IFIH1/MDA5; this
CC interaction inhibits host IFIH1. {ECO:0000269|PubMed:28424289}.
CC -!- SUBUNIT: [Protein 3CD]: Protein 3CD: Interacts with protein 3AB and
CC with RNA-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}.
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DR EMBL; AF177911; AAD55085.1; -; Genomic_RNA.
DR PDB; 4MG3; X-ray; 1.80 A; A/B=863-1007.
DR PDB; 5C8C; X-ray; 2.50 A; A=566-862, B=1-323, C=324-565.
DR PDB; 6LHT; EM; 3.67 A; A/B/C/D/E=566-862.
DR PDBsum; 4MG3; -.
DR PDBsum; 5C8C; -.
DR PDBsum; 6LHT; -.
DR SMR; Q9QF31; -.
DR MEROPS; C03.020; -.
DR PRIDE; Q9QF31; -.
DR ABCD; Q9QF31; 3 sequenced antibodies.
DR BRENDA; 3.4.22.29; 12962.
DR Proteomes; UP000001439; 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:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0039554; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host MDA-5 activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd00205; rhv_like; 3.
DR Gene3D; 2.40.10.10; -; 4.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 6.10.20.20; -; 1.
DR InterPro; 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; 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 MDA5 by virus;
KW Inhibition of host mRNA nuclear export by virus;
KW Inhibition of host NF-kappa-B by virus;
KW Inhibition of host RLR pathway by virus; Ion channel; Ion transport;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Pore-mediated penetration of viral genome into host cell; Protease; Repeat;
KW 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..2193
FT /note="Genome polyprotein"
FT /id="PRO_0000426193"
FT CHAIN 2..862
FT /note="P1"
FT /id="PRO_0000426194"
FT CHAIN 2..323
FT /note="Capsid protein VP0"
FT /id="PRO_0000426195"
FT CHAIN 2..69
FT /note="Capsid protein VP4"
FT /id="PRO_0000426196"
FT CHAIN 70..323
FT /note="Capsid protein VP2"
FT /id="PRO_0000426197"
FT CHAIN 324..565
FT /note="Capsid protein VP3"
FT /id="PRO_0000426198"
FT CHAIN 566..862
FT /note="Capsid protein VP1"
FT /id="PRO_0000426199"
FT CHAIN 863..1440
FT /note="P2"
FT /id="PRO_0000426200"
FT CHAIN 863..1012
FT /note="Protease 2A"
FT /id="PRO_0000039529"
FT CHAIN 1013..1111
FT /note="Protein 2B"
FT /id="PRO_0000039530"
FT CHAIN 1112..1440
FT /note="Protein 2C"
FT /id="PRO_0000039531"
FT CHAIN 1441..2193
FT /note="P3"
FT /id="PRO_0000426201"
FT CHAIN 1441..1548
FT /note="Protein 3AB"
FT /id="PRO_0000426202"
FT CHAIN 1441..1526
FT /note="Protein 3A"
FT /id="PRO_0000039532"
FT CHAIN 1527..1548
FT /note="Viral protein genome-linked"
FT /id="PRO_0000426203"
FT CHAIN 1549..2193
FT /note="Protein 3CD"
FT /id="PRO_0000426204"
FT CHAIN 1549..1731
FT /note="Protease 3C"
FT /id="PRO_0000426205"
FT CHAIN 1732..2193
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000426206"
FT TOPO_DOM 2..1503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 1504..1519
FT /evidence="ECO:0000255"
FT TOPO_DOM 1520..2193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1216..1374
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1549..1727
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1958..2074
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ZN_FING 1381..1397
FT /note="C4-type; degenerate"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..588
FT /note="Amphipathic alpha-helix"
FT /evidence="ECO:0000255"
FT REGION 1112..1250
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1112..1184
FT /note="Membrane-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1133..1137
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1424..1431
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT REGION 1435..1440
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 883
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 901
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 972
FT /note="For protease 2A activity"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT ACT_SITE 1588
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1619
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1695
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 918
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:24026848"
FT BINDING 920
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:24026848"
FT BINDING 978
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:24026848"
FT BINDING 980
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:24026848"
FT BINDING 1240..1247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT BINDING 1381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B9VUU3"
FT BINDING 1392
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 1964
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 1964
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 2060
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 2060
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 323..324
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 862..863
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1012..1013
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1111..1112
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1136
FT /note="Involved in the interaction with host RTN3"
FT /evidence="ECO:0000250|UniProtKB:Q66478"
FT SITE 1440..1441
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1526..1527
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1548..1549
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT SITE 1731..1732
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03301"
FT MOD_RES 1529
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 TURN 19..22
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5C8C"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5C8C"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 168..180
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:5C8C"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:5C8C"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:5C8C"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:5C8C"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 281..292
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 301..317
FT /evidence="ECO:0007829|PDB:5C8C"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 388..392
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 423..428
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 438..444
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 453..459
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 475..481
FT /evidence="ECO:0007829|PDB:5C8C"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 508..512
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 516..523
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 533..543
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 625..628
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 641..643
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 645..649
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 653..660
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 662..667
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 669..675
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 682..688
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 691..705
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 715..721
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 734..737
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 739..741
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 743..747
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 753..757
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 762..768
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 781..786
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 791..793
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 797..806
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 812..828
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 838..841
FT /evidence="ECO:0007829|PDB:5C8C"
FT HELIX 846..848
FT /evidence="ECO:0007829|PDB:5C8C"
FT STRAND 869..881
FT /evidence="ECO:0007829|PDB:4MG3"
FT HELIX 882..884
FT /evidence="ECO:0007829|PDB:4MG3"
FT HELIX 887..891
FT /evidence="ECO:0007829|PDB:4MG3"
FT STRAND 893..897
FT /evidence="ECO:0007829|PDB:4MG3"
FT HELIX 898..900
FT /evidence="ECO:0007829|PDB:4MG3"
FT STRAND 902..912
FT /evidence="ECO:0007829|PDB:4MG3"
FT STRAND 922..927
FT /evidence="ECO:0007829|PDB:4MG3"
FT TURN 928..931
FT /evidence="ECO:0007829|PDB:4MG3"
FT STRAND 932..937
FT /evidence="ECO:0007829|PDB:4MG3"
FT STRAND 942..946
FT /evidence="ECO:0007829|PDB:4MG3"
FT STRAND 950..952
FT /evidence="ECO:0007829|PDB:4MG3"
FT STRAND 954..965
FT /evidence="ECO:0007829|PDB:4MG3"
FT HELIX 969..971
FT /evidence="ECO:0007829|PDB:4MG3"
FT STRAND 975..978
FT /evidence="ECO:0007829|PDB:4MG3"
FT STRAND 981..990
FT /evidence="ECO:0007829|PDB:4MG3"
FT STRAND 993..998
FT /evidence="ECO:0007829|PDB:4MG3"
FT HELIX 1003..1005
FT /evidence="ECO:0007829|PDB:4MG3"
SQ SEQUENCE 2193 AA; 243184 MW; 927839DB58F61E7F CRC64;
MGSQVSTQRS GSHENSNSAS EGSTINYTTI NYYKDAYAAS AGRQDMSQDP KKFTDPVMDV
IHEMAPPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI VIAYGEWPEY CPDTDATAVD
KPTRPDVSVN RFFTLDTKSW AKDSKGWYWK FPDVLTEVGV FGQNAQFHYL YRSGFCVHVQ
CNASKFHQGA LLVAVLPEYV LGTIAGGTGN ENSHPPYATT QPGQVGAVLT HPYVLDAGIP
LSQLTVCPHQ WINLRTNNCA TIIVPYMNTV PFDSALNHCN FGLLVVPVVP LDFNAGATSE
IPITVTIAPM CAEFAGLRQA VKQGIPTELK PGTNQFLTTD DGVSAPILPG FHPTPPIHIP
GEVHNLLEIC RVETILEVNN LKTNETTPMQ RLCFPVSVQS KTGELCAAFR ADPGRDGPWQ
STILGQLCRY YTQWSGSLEV TFMFAGSFMA TGKMLIAYTP PGGNVPADRI TAMLGTHVIW
DFGLQSSVTL VVPWISNTHY RAHARAGYFD YYTTGIITIW YQTNYVVPIG APTTAYIVAL
AAAQDNFTMK LCKDTEDIEQ TANIQGDPIA DMIDQTVNNQ VNRSLTALQV LPTAADTEAS
SHRLGTGVVP ALQAAETGAS SNASDKNLIE TRCVLNHHST QETAIGNFFS RAGLVSIITM
PTTGTQNTDG YVNWDIDLMG YAQLRRKCEL FTYMRFDAEF TFVVAKPNGE LVPQLLQYMY
VPPGAPKPTS RDSFAWQTAT NPSVFVKMTD PPAQVSVPFM SPASAYQWFY DGYPTFGEHL
QANDLDYGQC PNNMMGTFSI RTVGTEKSPH SITLRVYMRI KHVRAWIPRP LRNQPYLFKT
NPNYKGNDIK CTSTSRDKIT TLGKFGQQSG AIYVGNYRVV NRHLATHNDW ANLVWEDSSR
DLLVSSTTAQ GCDTIARCNC QTGVYYCSSK RKHYPVSFTK PSLIFVEASE YYPARYQSHL
MLAVGHSEPG DCGGILRCQH GVVGIVSTGG NGLVGFADVR DLLWLDEEAM EQGVSDYIKG
LGDAFGVGFT DAVSREVEAL KNHLIGSEGA VEKILKNLVK LISALVIVVR SDYDMVTLTA
TLALIGCHGS PWAWIKAKTA SILGIPIVQK QSASWLKKFN DMANAAKGLE WISSKISKFI
DWLKEKIIPA AKEKVEFLNN LKQLPLLENQ ISNLEQSAAS QEDLEAMFGN VSYLAHFCRK
FQPLYATEAK RVYALEKRMN NYMQFKSKHR IEPVCLIIRG SPGTGKSLAT GIIARAIADK
YHSSVYSLPP DPDHFDGYKQ QVVTVMDDLC QNPDGKDMSL FCQMVSTVDF IPPMASLEEK
GVSFTSKFVI ASTNASNIVV PTVSDSDAIR RRFYMDCDIE VTDSYKTDLG RLDAGRAAKL
CTENNTANFK RCSPLVCGKA IQLRDRKSKV RYSIDTVVSE LIREYNNRSA IGNTIEALFQ
GPLKFKPIRI SLEEKPAPDA ISDLLASVDS EEVRQYCREQ GWIIPETPTN VERHLNRAVL
VMQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPKQALKKP VLRTATVQGP SLDFALSLLR
RNIRQVQTDQ GHFTMLGVRD RLAILPRHSQ PGKTIWVEHK LINVLDAVEL VDEQGVNLEL
TLVTLDTNEK FRDVTKFIPE TITGASDATL VINTEHMPSM FVPVGDVVQY GFLNLSGKPT
HRTMMYNFPT KAGQCGGVVT SVGKIIGIHI GGNGRQGFCA GLKRGYFASE QGEIQWMKPN
KETGRLNING PTRTKLEPSV FHDVFEGNKE PAVLTSKDPR LEVDFEQALF SKYVGNTLHE
PDEYVTQAAL HYANQLKQLD ININKMSMEE ACYGTEYLEA IDLHTSAGYP YSALGVKKRD
ILDPITRDTT KMKFYMDKYG LDLPYSTYVK DELRSLDKIK KGKSRLIEAS SLNDSVYLRM
TFGHLYETFH ANPGTVTGSA VGCNPDVFWS KLPILLPGSL FAFDYSGYDA SLSPVWFRAL
EVVLREIGYS EEAVSLIEGI NHTHHVYRNK TYCVLGGMPS GCSGTSIFNS MINNIIIRTL
LIKTFKGIDL DELNMVAYGD DVLASYPFPI DCSELAKTGK EYGLTMTPAD KSPCFNEVTW
ENATFLKRGF LPDHQFPFLI HPTMPMREIH ESIRWTKDAR NTQDHVRSLC LLAWHNGKEE
YEKFVSTIRS VPIGKALAIP NFENLRRNWL ELF
