##gff-version 3
Q7L2E3	UniProtKB	Chain	1	1194	.	.	.	ID=PRO_0000245538;Note=ATP-dependent RNA helicase DHX30	
Q7L2E3	UniProtKB	Domain	53	121	.	.	.	Note=DRBM	
Q7L2E3	UniProtKB	Domain	444	612	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
Q7L2E3	UniProtKB	Domain	654	827	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
Q7L2E3	UniProtKB	Region	1	27	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q7L2E3	UniProtKB	Region	150	199	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q7L2E3	UniProtKB	Motif	559	562	.	.	.	Note=DEAH box	
Q7L2E3	UniProtKB	Binding site	457	464	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
Q7L2E3	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q7L2E3	UniProtKB	Modified residue	226	226	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99PU8	
Q7L2E3	UniProtKB	Modified residue	380	380	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q7L2E3	UniProtKB	Alternative sequence	1	41	.	.	.	ID=VSP_022118;Note=In isoform 2. MFSLDSFRKDRAQHRQRQCKLPPPRLPPMCVNPTPGGTISR->MAAARRLMALAAGISPRLQPLGPRAAGRQGRSRGFSSSCAHPDHTKEAAEAESGMAPGGPGEGDGSLVN;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q7L2E3	UniProtKB	Alternative sequence	1	39	.	.	.	ID=VSP_036891;Note=In isoform 3. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:14702039,PMID:15489334	
Q7L2E3	UniProtKB	Alternative sequence	40	41	.	.	.	ID=VSP_036892;Note=In isoform 3. SR->MA;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:14702039,PMID:15489334	
Q7L2E3	UniProtKB	Natural variant	493	493	.	.	.	ID=VAR_080611;Note=In NEDMIAL%3B changed localization to stress granules%3B decreased RNA-binding%3B no effect on RNA-dependent ATPase activity%3B by inducing the formation of stress granules probably indirectly decreases global protein synthesis. R->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28327206,ECO:0000269|PubMed:29100085;Dbxref=dbSNP:rs1057519436,PMID:28327206,PMID:29100085	
Q7L2E3	UniProtKB	Natural variant	562	562	.	.	.	ID=VAR_080612;Note=In NEDMIAL%3B changed localization to stress granules%3B decreased RNA-dependent ATPase activity%3B by inducing the formation of stress granules probably indirectly decreases global protein synthesis. H->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28327206,ECO:0000269|PubMed:29100085;Dbxref=dbSNP:rs1060499733,PMID:28327206,PMID:29100085	
Q7L2E3	UniProtKB	Natural variant	781	781	.	.	.	ID=VAR_080613;Note=In NEDMIAL%3B changed localization to stress granules%3B decreased RNA-dependent ATPase activity%3B by inducing the formation of stress granules probably indirectly decreases global protein synthesis. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29100085;Dbxref=dbSNP:rs1553706775,PMID:29100085	
Q7L2E3	UniProtKB	Natural variant	782	782	.	.	.	ID=VAR_080614;Note=In NEDMIAL%3B changed localization to stress granules%3B decreased RNA-dependent ATPase activity%3B by inducing the formation of stress granules probably indirectly decreases global protein synthesis. R->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28327206,ECO:0000269|PubMed:29100085;Dbxref=dbSNP:rs753242774,PMID:28327206,PMID:29100085	
Q7L2E3	UniProtKB	Natural variant	785	785	.	.	.	ID=VAR_080615;Note=In NEDMIAL%3B changed localization to stress granules%3B decreased RNA-dependent ATPase activity%3B by inducing the formation of stress granules probably indirectly decreases global protein synthesis. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29100085;Dbxref=dbSNP:rs1085307451,PMID:29100085	
Q7L2E3	UniProtKB	Natural variant	785	785	.	.	.	ID=VAR_080616;Note=In NEDMIAL%3B changed localization to stress granules%3B decreased RNA-dependent ATPase activity%3B by inducing the formation of stress granules probably indirectly decreases global protein synthesis. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29100085;Dbxref=dbSNP:rs1553706799,PMID:29100085	
Q7L2E3	UniProtKB	Sequence conflict	557	557	.	.	.	Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q7L2E3	UniProtKB	Sequence conflict	1136	1136	.	.	.	Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q7L2E3	UniProtKB	Turn	47	49	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DB2	
Q7L2E3	UniProtKB	Helix	53	64	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DB2	
Q7L2E3	UniProtKB	Helix	67	73	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DB2	
Q7L2E3	UniProtKB	Beta strand	74	78	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DB2	
Q7L2E3	UniProtKB	Beta strand	81	91	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DB2	
Q7L2E3	UniProtKB	Beta strand	93	95	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DB2	
Q7L2E3	UniProtKB	Beta strand	97	105	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DB2	
Q7L2E3	UniProtKB	Helix	106	124	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DB2	
Q7L2E3	UniProtKB	Helix	136	144	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2DB2	
Q7L2E3	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18220336;Dbxref=PMID:18220336