P32537POLG_HE701Genome polyproteinP1Capsid protein VP0VP4-VP2Capsid protein VP4P1AVirion protein 4Capsid protein VP2P1BVirion protein 2Capsid protein VP3P1CVirion protein 3Capsid protein VP1P1DVirion protein 1P2Protease 2AP2A3.4.22.29Picornain 2AProtein 2AProtein 2BP2BProtein 2CP2C3.6.1.15P3Protein 3ABProtein 3AP3AViral protein genome-linkedVPgProtein 3BP3BProtein 3CD3.4.22.28Protease 3C3.4.22.28Picornain 3CP3CRNA-directed RNA polymeraseRdRp2.7.7.483D polymerase3DpolProtein 3D3DHuman enterovirus 70 (strain J670/71)EV70EV-70VirusesRiboviriaOrthornaviraePisuviricotaPisoniviricetesPicornaviralesPicornaviridaeEnsavirinaeEnterovirusEnterovirus DHomo sapiensHumanThe complete nucleotide sequence of enterovirus type 70: relationships with other members of the picornaviridae.NUCLEOTIDE SEQUENCE [GENOMIC RNA]The HeLa cell receptor for enterovirus 70 is decay-accelerating factor (CD55).INTERACTION WITH HOST CD55Capsid protein VP1Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By similarity). Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells (By similarity). This attachment induces virion internalization (By similarity). Tyrosine kinases are probably involved in the entry process (By similarity). After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity).Capsid protein VP2Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).Capsid protein VP3Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).Capsid protein VP4Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity).Capsid protein VP0Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step (By similarity).Protease 2ACysteine protease that cleaves viral polyprotein and specific host proteins (By similarity). It is responsible for the autocatalytic cleavage between the P1 and P2 regions, which is the first cleavage occurring in the polyprotein (By similarity). Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation (By similarity). Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity). Counteracts stress granule formation probably by antagonizing its assembly or promoting its dissassembly (By similarity).Protein 2BPlays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.Protein 2CInduces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.Protein 3ABLocalizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity.Protein 3ALocalizes the viral replication complex to the surface of membranous vesicles (By similarity). It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (By similarity). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (By similarity).Viral protein genome-linkedActs as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (By similarity).Protein 3CDInvolved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity. Protein 3CD binds to the 5'UTR of the viral genome.RNA-directed RNA polymeraseReplicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated.Protease 3CMajor viral protease that mediates proteolytic processing of the polyprotein (By similarity). Cleaves host EIF5B, contributing to host translation shutoff (By similarity). Cleaves also host PABPC1, contributing to host translation shutoff (By similarity). Cleaves host NLRP1, triggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment (By similarity).Protein 2Ca ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphateProtease 2ASelective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.RNA-directed RNA polymerasea ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)Protease 3CSelective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.RNA-directed RNA polymeraseMg(2+)Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence of 3CDpro or 3CPro (By similarity).RNA-directed RNA polymeraseReplication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.Capsid protein VP0Interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers.Capsid protein VP1Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity). Interacts with capsid protein VP2, capsid protein VP3 and capsid protein VP4 following cleavage of capsid protein VP0 (By similarity).Capsid protein VP2Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid.Capsid protein VP3Interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity). Interacts with capsid protein VP4 in the mature capsid (By similarity). Interacts with protein 2C; this interaction may be important for virion morphogenesis (By similarity).Capsid protein VP4Interacts with capsid protein VP1 and capsid protein VP3.Protease 2AHomodimer.Protein 2CHomohexamer; forms a hexameric ring structure with 6-fold symmetry characteristic of AAA+ ATPases (By similarity). Interacts (via N-terminus) with host RTN3 (via reticulon domain); this interaction is important for viral replication (By similarity). Interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity).Protein 3ABInteracts with protein 3CD.Protein 3AHomodimer (By similarity). Interacts with host GBF1 (By similarity). Interacts (via GOLD domain) with host ACBD3 (via GOLD domain); this interaction allows the formation of a viral protein 3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will stimulate the recruitment of host PI4KB in order to synthesize PI4P at the viral RNA replication sites (By similarity).Viral protein genome-linkedInteracts with RNA-directed RNA polymerase.Protein 3CDInteracts with protein 3AB and with RNA-directed RNA polymerase.RNA-directed RNA polymeraseInteracts with Viral protein genome-linked and with protein 3CD.Capsid protein VP0VirionHost cytoplasmCapsid protein VP4VirionCapsid protein VP2VirionHost cytoplasmCapsid protein VP3VirionHost cytoplasmCapsid protein VP1VirionHost cytoplasmProtein 2BHost cytoplasmic vesicle membranePeripheral membrane proteinCytoplasmic sideProbably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.Protein 2CHost cytoplasmic vesicle membranePeripheral membrane proteinCytoplasmic sideProbably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.Protein 3AHost cytoplasmic vesicle membranePeripheral membrane proteinCytoplasmic sideProbably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.Protein 3ABHost cytoplasmic vesicle membranePeripheral membrane proteinCytoplasmic sideProbably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.Viral protein genome-linkedVirionHost cytoplasmProtease 3CHost cytoplasmProtein 3CDHost nucleusHost cytoplasmHost cytoplasmic vesicle membranePeripheral membrane proteinCytoplasmic sideProbably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.RNA-directed RNA polymeraseHost cytoplasmic vesicle membranePeripheral membrane proteinCytoplasmic sideProbably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.Protein 2CThe N-terminus has membrane-binding (By similarity). The N-terminus also displays RNA-binding properties (By similarity). The N-terminus is involved in oligomerization (By similarity). The central part contains an ATPase domain and a degenerate C4-type zinc-finger with only 3 cysteines (By similarity). The C-terminus is involved in RNA-binding (By similarity). The extreme C-terminus contains a region involved in oligomerization (By similarity).Genome polyproteinSpecific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.Capsid protein VP0Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion.Capsid protein VP0During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion.Capsid protein VP4Myristoylation is required during RNA encapsidation and formation of the mature virus particle.Viral protein genome-linkedVPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication.Belongs to the picornaviruses polyprotein family.Activation of host autophagy by virusATP-bindingAutocatalytic cleavageCapsid proteinCovalent protein-RNA linkageDNA replicationEukaryotic host gene expression shutoff by virusEukaryotic host translation shutoff by virusHelicaseHost cytoplasmHost cytoplasmic vesicleHost gene expression shutoff by virusHost membraneHost mRNA suppression by virusHost nucleusHost-virus interactionHydrolaseInhibition of host innate immune response by virusInhibition of host mRNA nuclear export by virusInhibition of host RIG-I by virusInhibition of host RLR pathway by virusIon channelIon transportLipoproteinMagnesiumMembraneMetal-bindingMyristateNucleotide-bindingNucleotidyltransferasePhosphoproteinPore-mediated penetration of viral genome into host cellProteaseRepeatRNA-bindingRNA-directed RNA polymeraseT=pseudo3 icosahedral capsid proteinThiol proteaseTransferaseTransportViral attachment to host cellViral immunoevasionViral ion channelViral penetration into host cytoplasmViral RNA replicationVirionVirus endocytosis by hostVirus entry into host cellZincZinc-fingerZn(2+)structuralZn(2+)structuralZn(2+)structuralZn(2+)structuralATPZn(2+)Zn(2+)Zn(2+)Mg(2+)catalytic; for RdRp activityMg(2+)catalytic; for RdRp activityMg(2+)catalytic; for RdRp activityMg(2+)catalytic; for RdRp activityMGAQVSRQQTGTHENANVATGGSSITYNQINFYKDSYAASASKQDFSQDPSKFTEPVAEALKAGAPVLKSPSAEACGYSDRVLQLKLGNSSIVTQEAANICCAYGEWPTYLPDNEAVAIDKPTQPETSTDRFYTLKSKKWESNSTGWWWKLPDALNQIGMFGQNVQYHYLYRSGFLCHVQCNATKFHQGTLLIVAIPEHQIGKKGTGTSASFAEVMKGAEGGVFEQPYLLDDGTSLACALVYPHQWINLRTNNSATIVLPWMNSAPMDFALRHNNWTLAVIPVCPLAGGTGNTNTYVPITISIAPMCAEYNGLRNAITQGVPTCLLPGSNQFLTTDDHSSAPAFPDFSPTPEMHIPGQVHSMLEIVQIESMMEINNVNDASGVERLRVQISAQSDMDQLLFNIPLDIQLEGPLRNTLLGNISRYYTHWSGSLEMTFMFCGSFMTTGKLIICYTPPGGSSPTDRMQAMLATHVVWDFGLQSSITIIIPWISGSHYRMFNTDAKAINANVGYVTCFMQTNLVAPVGAADQCYIVGMVAAKKDFNLRLMRDSPDIGQSAILPEQAATTQIGEIVKTVANTVESEIKAELGVIPSLNAVETGATSNTEPEEAIQTRTVINMHGTAECLVENFLGRSALVCMRSFEYKNHSTSTSSIQKNFFIWTLNTRELVQIRRKMELFTYLRFDTEITIVPTLRLFSSSNVSFSGLPNLTLQAMYVPTGARKPSSQDSFEWQSACNPSVFFKINDPPARLTIPFMSINSAYANFYDGFAGFEKKATVLYGINPANTMGNLCLRVVNSYQPVQYTLTVRVYMKPKHIKAWAPRAPRTMPYTNILNNNYAGRSAAPNAPTAIVSHRSTIKTMPNDINLTTAGPGYGGAFVGSYKIINYHLATDEEKERSVYVDWQSDVLVTTVAAHGKHQIARCRCNTGVYYCKHKNRSYPVCFEGPGIQWINESDYYPARYQTNTLLAMGPCQPGDCGGLLVCSHGVIGLVTAGGEGIVAFTDIRNLLWLEDDAMEQGITDYIQNLGSAFGTGFTETISEKAKEIQNMLVGEDSLLEKLLKALIKIVSAMVIVIRNSEDLVTVTATLALLGCNDSPWAFLKQKVCSYLGIPYTIRQSDSWLKKFTEACNALRGLDWLAQKIDKFINWLKTKILPEAREKHEFVQKLKQLPVIESQINTIEHSCPNSEXQQALFNNVQYYSHYCKKYAPLYALEAKRVSALERKINNYIQFKSKSRIEPVCLIIHGSPGTGKSVASNLIARAITEKLGGDSYSLPPDPKYFDGYKQQTVVLMDDLMQNPDGNDIAMFCQMVSTVDFIPPMASLEEKGTLYTSPFLIATTNAGSIHAPTVSDSKALARRFKFDMEIESMESYKDGVRLDMFKAVELCNPEKCRPTNYKKCCPLICGKAIQFRDKRTNVRYSVDMLVTEMIKEYRIRNSTQDKLEALFQGPPTFKEIKISVTPETPAPDAINDLLRSIDSQEVRDYCQKKGWIVMHPPTELVVDKHISRAFIALQAITTFVSIAGVVYVIYKLFAGIQGPYTGLPNQKPKVPTLRTAKVQGPSLDFAQAIMRKNTVIARTSKGEFTMLGIYDRIAVVPTHASVEEEIYINDVPVKVKDAYALRDINDVNLEITVVELDRNEKFRDIRGFLPKYEDDYNDAILSVNTSKFPNMYIPVGQTLNYGFLNLGGTPTHRILMYNFPTRAGQCGGVVTTTGKVIGIHVGGNGAQGFAAMLLQNYFTEKQGEIVSIEKTGVFINAPAKTKLEPSVFHEVFEGVKEPAVLHSKDKRLKVDFEEAIFSKYVGNKTMLMDEYMEEAVDHYVGCLEPLDISTEPIKLEEAMYGMDGLEALDLTTSAGYPYLLQGKKKRDIFNRQTRDTTEMTKMLDKYGVDLPFVTFVKDELRSREKVEKGKSRLIEASSLNDSVAMRVAFGNLYATFHKNPGVATGSAVGCDPDLFWSKIPVXLDGKIFAFDYTGYDASLSPVWFACLKKTLVKLGYTHQTAFVDYLCHSVHLYKDRKYIVNGGMPSGSSGTSIFNTMINNIIIRTLLLKVYKGIDLDQFKMIAYGDDVIASYPHEIDPGLLAKAGKEYGLIMTPADKSSGFTETTWENVTFLKRYFRADEQYPFLIHPVMPMKEIHESIRWTKDPRNTQDHVRSLCLLAWHNGEETYNEFCRKIRTVPVGRALALPVYSSLRRKWLDSF
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