##gff-version 3
Q9IJX4	UniProtKB	Chain	1	1771	.	.	.	ID=PRO_0000398372;Note=Replicase polyprotein	
Q9IJX4	UniProtKB	Chain	1	166	.	.	.	ID=PRO_0000398374;Note=Protein 1A;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Chain	167	190	.	.	.	ID=PRO_0000398373;Note=Protein 2A;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Chain	191	328	.	.	.	ID=PRO_0000398375;Note=Protein 2B;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Chain	329	739	.	.	.	ID=PRO_0000398376;Note=Protein 2C;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Chain	909	1220	.	.	.	ID=PRO_0000398379;Note=3C-like protease;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Chain	1221	1771	.	.	.	ID=PRO_0000398380;Note=RNA-directed RNA polymerase 3D-POL;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Domain	482	656	.	.	.	Note=SF3 helicase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00551	
Q9IJX4	UniProtKB	Domain	954	1201	.	.	.	Note=Peptidase C3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222	
Q9IJX4	UniProtKB	Domain	1495	1634	.	.	.	Note=RdRp catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00539	
Q9IJX4	UniProtKB	Region	16	25	.	.	.	Note=BC-box;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30308158;Dbxref=PMID:30308158	
Q9IJX4	UniProtKB	Region	106	114	.	.	.	Note=Interaction with and inhibition of host AGO2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30308158;Dbxref=PMID:30308158	
Q9IJX4	UniProtKB	Region	919	942	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9IJX4	UniProtKB	Coiled coil	1	29	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Coiled coil	1385	1413	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Active site	1003	1003	.	.	.	Note=For picornain 3C-like protease activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222	
Q9IJX4	UniProtKB	Active site	1063	1063	.	.	.	Note=For picornain 3C-like protease activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222	
Q9IJX4	UniProtKB	Active site	1162	1162	.	.	.	Note=For picornain 3C-like protease activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01222	
Q9IJX4	UniProtKB	Binding site	510	517	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00551	
Q9IJX4	UniProtKB	Site	146	146	.	.	.	Note=Involved in the inhibition of host stress granules formation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28003491;Dbxref=PMID:28003491	
Q9IJX4	UniProtKB	Site	166	167	.	.	.	Note=Cleavage%3B by ribosomal skip;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Site	190	191	.	.	.	Note=Cleavage%3B by 3C-like protease;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Site	328	329	.	.	.	Note=Cleavage%3B by 3C-like protease;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Site	739	740	.	.	.	Note=Cleavage%3B by 3C-like protease;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Site	884	885	.	.	.	Note=Cleavage%3B by 3C-like protease;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Site	908	909	.	.	.	Note=Cleavage%3B by 3C-like protease;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Site	1220	1221	.	.	.	Note=Cleavage%3B by 3C-like protease;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9IJX4	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Reduced host AGO2 binding%2C loss of AGO2 inhibition and loss of RNA silencing inhibition. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30308158;Dbxref=PMID:30308158	
Q9IJX4	UniProtKB	Mutagenesis	114	114	.	.	.	Note=Reduced host AGO2 binding%2C loss of AGO2 inhibition and loss of RNA silencing inhibition. Loss of replication efficiency. F->A%2CD%2CG%2CN%2CP%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30308158;Dbxref=PMID:30308158	
Q9IJX4	UniProtKB	Mutagenesis	146	146	.	.	.	Note=Attenuated infection. Loss of inhibition of host stress granules formation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28003491;Dbxref=PMID:28003491	
Q9IJX4	UniProtKB	Helix	15	29	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C3R	
Q9IJX4	UniProtKB	Beta strand	37	43	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C3R	
Q9IJX4	UniProtKB	Turn	49	52	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C3R	
Q9IJX4	UniProtKB	Beta strand	55	61	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C3R	
Q9IJX4	UniProtKB	Helix	66	83	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C3R	
Q9IJX4	UniProtKB	Helix	90	103	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C3R	
Q9IJX4	UniProtKB	Turn	110	112	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C3R	
Q9IJX4	UniProtKB	Beta strand	117	121	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C3R	
Q9IJX4	UniProtKB	Helix	123	127	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C3R	
Q9IJX4	UniProtKB	Helix	130	136	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C3R	
Q9IJX4	UniProtKB	Helix	142	149	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C3R