##gff-version 3 Q5XXP3 UniProtKB Chain 1 261 . . . ID=PRO_0000226225;Note=Capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Chain 262 748 . . . ID=PRO_0000226226;Note=Precursor of protein E3/E2;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Chain 262 325 . . . ID=PRO_0000226227;Note=Assembly protein E3;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Chain 326 748 . . . ID=PRO_0000226228;Note=Spike glycoprotein E2;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Chain 749 809 . . . ID=PRO_0000226229;Note=6K protein;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Chain 810 1248 . . . ID=PRO_0000226230;Note=Spike glycoprotein E1;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Topological domain 1 692 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Transmembrane 693 713 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Topological domain 714 748 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Topological domain 749 763 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Transmembrane 764 784 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Topological domain 785 795 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Transmembrane 796 816 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Topological domain 817 1224 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Transmembrane 1225 1245 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Topological domain 1246 1248 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Domain 113 261 . . . Note=Peptidase S3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01027 Q5XXP3 UniProtKB Region 14 104 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5XXP3 UniProtKB Region 36 68 . . . Note=Host transcription inhibition;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09592 Q5XXP3 UniProtKB Region 84 114 . . . Note=Binding to the viral RNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27284 Q5XXP3 UniProtKB Region 99 113 . . . Note=Ribosome-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27284 Q5XXP3 UniProtKB Region 183 193 . . . Note=Dimerization of the capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0DOK1 Q5XXP3 UniProtKB Region 219 223 . . . Note=Dimerization of the capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0DOK1 Q5XXP3 UniProtKB Region 262 274 . . . Note=Functions as an uncleaved signal peptide for the precursor of protein E3/E2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03315 Q5XXP3 UniProtKB Region 721 741 . . . Note=Transient transmembrane before p62-6K protein processing;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Region 893 910 . . . Note=E1 fusion peptide loop;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8JUX5 Q5XXP3 UniProtKB Motif 61 99 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09592 Q5XXP3 UniProtKB Motif 144 154 . . . Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09592 Q5XXP3 UniProtKB Compositional bias 73 87 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5XXP3 UniProtKB Compositional bias 88 102 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5XXP3 UniProtKB Active site 139 139 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01027 Q5XXP3 UniProtKB Active site 161 161 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01027 Q5XXP3 UniProtKB Active site 213 213 . . . Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01027 Q5XXP3 UniProtKB Site 187 187 . . . Note=Involved in dimerization of the capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86925 Q5XXP3 UniProtKB Site 220 220 . . . Note=Involved in dimerization of the capsid protein;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q86925 Q5XXP3 UniProtKB Site 261 262 . . . Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03315 Q5XXP3 UniProtKB Site 325 326 . . . Note=Cleavage%3B by host furin;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Site 748 749 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Site 809 810 . . . Note=Cleavage%3B by host signal peptidase;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Lipidation 721 721 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Lipidation 741 741 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Lipidation 742 742 . . . Note=S-palmitoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Lipidation 1242 1242 . . . Note=S-stearoyl cysteine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Glycosylation 273 273 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Glycosylation 588 588 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Glycosylation 670 670 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Glycosylation 950 950 . . . Note=N-linked (GlcNAc...) asparagine%3B by host;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q5XXP3 UniProtKB Disulfide bond 113 128 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Disulfide bond 858 923 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Disulfide bond 871 903 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Disulfide bond 872 905 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Disulfide bond 877 887 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Disulfide bond 1068 1080 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Disulfide bond 1110 1185 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Disulfide bond 1115 1189 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5XXP3 UniProtKB Disulfide bond 1137 1179 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250