##gff-version 3 Q66765 UniProtKB Chain 1 2292 . . . ID=PRO_0000446100;Note=Genome polyprotein Q66765 UniProtKB Chain 1 67 . . . ID=PRO_0000423146;Note=Leader protein Q66765 UniProtKB Chain 68 393 . . . ID=PRO_0000423147;Note=Capsid protein VP0 Q66765 UniProtKB Chain 68 137 . . . ID=PRO_5000143569;Note=Capsid protein VP4 Q66765 UniProtKB Chain 138 393 . . . ID=PRO_5000143570;Note=Capsid protein VP2 Q66765 UniProtKB Chain 394 624 . . . ID=PRO_5000143571;Note=Capsid protein VP3 Q66765 UniProtKB Chain 625 901 . . . ID=PRO_5000143572;Note=Capsid protein VP1 Q66765 UniProtKB Chain 902 1044 . . . ID=PRO_5000143573;Note=Protein 2A Q66765 UniProtKB Chain 1045 1194 . . . ID=PRO_5000143574;Note=Protein 2B Q66765 UniProtKB Chain 1195 1519 . . . ID=PRO_5000143575;Note=Protein 2C Q66765 UniProtKB Chain 1520 1607 . . . ID=PRO_5000143576;Note=Protein 3A Q66765 UniProtKB Chain 1608 1627 . . . ID=PRO_0000423148;Note=VPg Q66765 UniProtKB Chain 1628 1832 . . . ID=PRO_5000143577;Note=Protease 3C Q66765 UniProtKB Chain 1833 2292 . . . ID=PRO_5000143578;Note=RNA-directed RNA polymerase Q66765 UniProtKB Domain 1281 1447 . . . Note=SF3 helicase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00551 Q66765 UniProtKB Domain 1630 1822 . . . Note=Peptidase C3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222 Q66765 UniProtKB Domain 2061 2179 . . . Note=RdRp catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00539 Q66765 UniProtKB Zinc finger 10 22 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Region 37 61 . . . Note=Acidic;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q66765 UniProtKB Region 1030 1036 . . . Note=Host EIF4E binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21145089;Dbxref=PMID:21145089 Q66765 UniProtKB Motif 995 1003 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21145089;Dbxref=PMID:21145089 Q66765 UniProtKB Active site 1673 1673 . . . Note=For protease 3C activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222 Q66765 UniProtKB Active site 1707 1707 . . . Note=For protease 3C activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222 Q66765 UniProtKB Active site 1786 1786 . . . Note=For protease 3C activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222 Q66765 UniProtKB Active site 2067 2067 . . . Note=For RdRp activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Active site 2165 2165 . . . Note=For RdRp activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 22 22 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 46 46 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 47 47 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 48 48 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 49 49 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 50 50 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 69 69 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 70 70 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 93 93 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 95 95 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 97 97 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 100 100 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12296 Q66765 UniProtKB Binding site 1313 1320 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00551 Q66765 UniProtKB Site 137 138 . . . Note=Cleavage;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q66765 UniProtKB Site 393 394 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03304 Q66765 UniProtKB Site 624 625 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03304 Q66765 UniProtKB Site 901 902 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03304 Q66765 UniProtKB Site 1044 1045 . . . Note=Cleavage%3B by ribosomal skip;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03304 Q66765 UniProtKB Site 1194 1195 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03304 Q66765 UniProtKB Site 1519 1520 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03304 Q66765 UniProtKB Site 1607 1608 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03304 Q66765 UniProtKB Site 1627 1628 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03304 Q66765 UniProtKB Site 1832 1833 . . . Note=Cleavage%3B by protease 3C;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03304 Q66765 UniProtKB Modified residue 41 41 . . . Note=Phosphotyrosine%3B by host SYK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24335301;Dbxref=PMID:24335301 Q66765 UniProtKB Modified residue 47 47 . . . Note=Phosphothreonine%3B by host CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24335301;Dbxref=PMID:24335301 Q66765 UniProtKB Modified residue 1610 1610 . . . Note=O-(5'-phospho-RNA)-tyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P03300 Q66765 UniProtKB Lipidation 68 68 . . . Note=N-myristoyl glycine%3B by host;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q66282 Q66765 UniProtKB Mutagenesis 19 19 . . . Note=Complete loss of inhibitory activity of nucleocytoplasmic transport. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16888036,ECO:0000269|PubMed:19073724;Dbxref=PMID:16888036,PMID:19073724 Q66765 UniProtKB Mutagenesis 35 35 . . . Note=25%25 loss of 2A-Leader interaction. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25210192;Dbxref=PMID:25210192 Q66765 UniProtKB Mutagenesis 37 37 . . . Note=30%25 loss of 2A-Leader interaction. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25210192;Dbxref=PMID:25210192 Q66765 UniProtKB Mutagenesis 40 40 . . . Note=20%25 loss of 2A-Leader interaction. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25210192;Dbxref=PMID:25210192 Q66765 UniProtKB Mutagenesis 41 41 . . . Note=No effect on the inhibitory activity of nucleocytoplasmic transport. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19073724;Dbxref=PMID:19073724 Q66765 UniProtKB Mutagenesis 47 47 . . . Note=No effect on the inhibitory activity of nucleocytoplasmic transport. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19073724;Dbxref=PMID:19073724 Q66765 UniProtKB Mutagenesis 993 994 . . . Note=5-10 fold decreased viral growth. YY->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21145089;Dbxref=PMID:21145089 Q66765 UniProtKB Mutagenesis 996 996 . . . Note=No effect on viral growth. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21145089;Dbxref=PMID:21145089 Q66765 UniProtKB Mutagenesis 998 998 . . . Note=5-10 fold decreased viral growth. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21145089;Dbxref=PMID:21145089 Q66765 UniProtKB Mutagenesis 1006 1006 . . . Note=No effect on viral growth. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21145089;Dbxref=PMID:21145089 Q66765 UniProtKB Mutagenesis 1035 1035 . . . Note=Complete loss of interaction with host EIF4E. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21145089;Dbxref=PMID:21145089