##gff-version 3
P38712	UniProtKB	Chain	1	501	.	.	.	ID=PRO_0000055064;Note=ATP-dependent rRNA helicase RRP3	
P38712	UniProtKB	Domain	112	284	.	.	.	Note=Helicase ATP-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
P38712	UniProtKB	Domain	307	461	.	.	.	Note=Helicase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00542	
P38712	UniProtKB	Region	36	79	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38712	UniProtKB	Region	480	501	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38712	UniProtKB	Coiled coil	3	44	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P38712	UniProtKB	Motif	81	109	.	.	.	Note=Q motif;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P38712	UniProtKB	Motif	231	234	.	.	.	Note=DEAD box;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P38712	UniProtKB	Compositional bias	36	61	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38712	UniProtKB	Compositional bias	63	79	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38712	UniProtKB	Compositional bias	485	501	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38712	UniProtKB	Binding site	125	132	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00541	
P38712	UniProtKB	Modified residue	43	43	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
P38712	UniProtKB	Modified residue	45	45	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
P38712	UniProtKB	Modified residue	47	47	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
P38712	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Leads to defects in A1 and A2 processing. K->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16449634;Dbxref=PMID:16449634	
P38712	UniProtKB	Mutagenesis	231	231	.	.	.	Note=Leads to defects in A1 and A2 processing. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16449634;Dbxref=PMID:16449634	
P38712	UniProtKB	Mutagenesis	263	263	.	.	.	Note=Leads to defects in A1 and A2 processing. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16449634;Dbxref=PMID:16449634