##gff-version 3
P45818	UniProtKB	Chain	1	564	.	.	.	ID=PRO_0000055063;Note=ATP-dependent RNA helicase ROK1	
P45818	UniProtKB	Domain	153	333	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
P45818	UniProtKB	Domain	344	506	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
P45818	UniProtKB	Region	1	45	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P45818	UniProtKB	Region	62	87	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P45818	UniProtKB	Region	512	564	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P45818	UniProtKB	Motif	122	150	.	.	.	Note=Q motif	
P45818	UniProtKB	Motif	280	283	.	.	.	Note=DEAD box	
P45818	UniProtKB	Compositional bias	31	45	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P45818	UniProtKB	Compositional bias	62	84	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P45818	UniProtKB	Binding site	166	173	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
P45818	UniProtKB	Mutagenesis	166	166	.	.	.	Note=No cell growth and 2-fold decrease in ATPase activity in vitro. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593	
P45818	UniProtKB	Mutagenesis	172	172	.	.	.	Note=Slow cell growth. K->G%2CR%2CS%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593	
P45818	UniProtKB	Mutagenesis	172	172	.	.	.	Note=No cell growth and drastic decrease in ATPase activity in vitro. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593	
P45818	UniProtKB	Mutagenesis	280	280	.	.	.	Note=Slow cell growth. D->A%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10373593;Dbxref=PMID:10373593