##gff-version 3
Q66431	UniProtKB	Chain	1	4036	.	.	.	ID=PRO_0000222026;Note=RNA-directed RNA polymerase L	
Q66431	UniProtKB	Domain	29	158	.	.	.	Note=OTU;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00139	
Q66431	UniProtKB	Domain	2424	2639	.	.	.	Note=RdRp catalytic;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00539	
Q66431	UniProtKB	Region	1	28	.	.	.	Note=Essential for the vOTU enzymatic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6GWS6	
Q66431	UniProtKB	Region	624	805	.	.	.	Note=Endonuclease;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6GWS6	
Q66431	UniProtKB	Region	779	879	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q66431	UniProtKB	Region	2800	2833	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q66431	UniProtKB	Region	4008	4036	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q66431	UniProtKB	Compositional bias	793	812	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q66431	UniProtKB	Compositional bias	828	846	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q66431	UniProtKB	Compositional bias	847	870	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q66431	UniProtKB	Compositional bias	4016	4036	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q66431	UniProtKB	Active site	40	40	.	.	.	Note=For ubiquitin thioesterase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6TQR6	
Q66431	UniProtKB	Active site	151	151	.	.	.	Note=For ubiquitin thioesterase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6TQR6	
Q66431	UniProtKB	Active site	153	153	.	.	.	Note=For ubiquitin thioesterase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6TQR6	
Q66431	UniProtKB	Active site	733	733	.	.	.	Note=For endonuclease activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:I0DF35	
Q66431	UniProtKB	Binding site	631	631	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6GWS6	
Q66431	UniProtKB	Binding site	692	692	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6GWS6	
Q66431	UniProtKB	Binding site	692	692	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6GWS6	
Q66431	UniProtKB	Binding site	717	717	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6GWS6	
Q66431	UniProtKB	Binding site	2606	2606	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:I0DF35	
Q66431	UniProtKB	Mutagenesis	10	10	.	.	.	Note=75%25 loss of debubiquitination activity and 60%25 loss of deISGylation activity. E->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23345508;Dbxref=PMID:23345508	
Q66431	UniProtKB	Mutagenesis	101	101	.	.	.	Note=More than 90%25 loss of deISGylation and debubiquitination activities. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23345508;Dbxref=PMID:23345508	
Q66431	UniProtKB	Mutagenesis	128	128	.	.	.	Note=110%25 increase in debubiquitination activity and almost 2%2C000%25 increase in deISGylation activity. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23345508;Dbxref=PMID:23345508	
Q66431	UniProtKB	Helix	3	6	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Beta strand	10	13	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Beta strand	16	19	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Helix	25	28	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Beta strand	29	32	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Beta strand	36	38	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Helix	40	49	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Beta strand	50	52	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Turn	55	57	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Helix	58	72	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Helix	73	75	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Helix	77	80	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Helix	86	93	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Helix	102	111	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Beta strand	116	121	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Beta strand	125	135	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Beta strand	141	146	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Beta strand	148	150	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD	
Q66431	UniProtKB	Beta strand	152	157	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HXD