##gff-version 3
Q62167	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10859333;Dbxref=PMID:10859333	
Q62167	UniProtKB	Chain	2	662	.	.	.	ID=PRO_0000055010;Note=ATP-dependent RNA helicase DDX3X	
Q62167	UniProtKB	Domain	211	403	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
Q62167	UniProtKB	Domain	414	575	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
Q62167	UniProtKB	Region	2	139	.	.	.	Note=Required for TBK1 and IKBKE-dependent IFNB1 activation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Region	19	144	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62167	UniProtKB	Region	38	44	.	.	.	Note=Interaction with EIF4E;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Region	100	662	.	.	.	Note=Interaction with GSK3B;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Region	100	110	.	.	.	Note=Interaction with IKBKE;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Region	139	172	.	.	.	Note=Interaction with CHUK;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Region	250	259	.	.	.	Note=Involved in stimulation of ATPase activity by DNA and RNA%2C nucleic acid binding and unwinding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Region	536	661	.	.	.	Note=Interaction with NXF1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Region	601	633	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62167	UniProtKB	Motif	12	21	.	.	.	Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Motif	180	208	.	.	.	Note=Q motif	
Q62167	UniProtKB	Motif	347	350	.	.	.	Note=DEAD box	
Q62167	UniProtKB	Compositional bias	19	34	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62167	UniProtKB	Compositional bias	55	69	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62167	UniProtKB	Compositional bias	91	142	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62167	UniProtKB	Compositional bias	603	626	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62167	UniProtKB	Binding site	200	207	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
Q62167	UniProtKB	Binding site	224	231	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
Q62167	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10859333;Dbxref=PMID:10859333	
Q62167	UniProtKB	Modified residue	55	55	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337	
Q62167	UniProtKB	Modified residue	82	82	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Modified residue	90	90	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Modified residue	101	101	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
Q62167	UniProtKB	Modified residue	104	104	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:15592455;Dbxref=PMID:15592455	
Q62167	UniProtKB	Modified residue	110	110	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
Q62167	UniProtKB	Modified residue	118	118	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Modified residue	131	131	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17242355;Dbxref=PMID:17242355	
Q62167	UniProtKB	Modified residue	183	183	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Modified residue	456	456	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q62095	
Q62167	UniProtKB	Modified residue	592	592	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Modified residue	594	594	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Modified residue	605	605	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Modified residue	612	612	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Modified residue	617	617	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571	
Q62167	UniProtKB	Modified residue	632	632	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
Q62167	UniProtKB	Cross-link	215	215	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O00571