##gff-version 3
Q5RDH5	UniProtKB	Chain	1	554	.	.	.	ID=PRO_0000085592;Note=5'-AMP-activated protein kinase catalytic subunit alpha-1	
Q5RDH5	UniProtKB	Domain	22	274	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q5RDH5	UniProtKB	Region	297	376	.	.	.	Note=AIS;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13131	
Q5RDH5	UniProtKB	Region	480	531	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q5RDH5	UniProtKB	Active site	145	145	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
Q5RDH5	UniProtKB	Binding site	28	36	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q5RDH5	UniProtKB	Binding site	51	51	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q5RDH5	UniProtKB	Modified residue	27	27	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13131	
Q5RDH5	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphothreonine%3B by LKB1 and CaMKK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5EG47	
Q5RDH5	UniProtKB	Modified residue	264	264	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P54645	
Q5RDH5	UniProtKB	Modified residue	350	350	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13131	
Q5RDH5	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13131	
Q5RDH5	UniProtKB	Modified residue	355	355	.	.	.	Note=Phosphoserine%3B by ULK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P54645	
Q5RDH5	UniProtKB	Modified residue	363	363	.	.	.	Note=Phosphothreonine%3B by ULK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P54645	
Q5RDH5	UniProtKB	Modified residue	377	377	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13131	
Q5RDH5	UniProtKB	Modified residue	392	392	.	.	.	Note=Phosphoserine%3B by ULK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P54645	
Q5RDH5	UniProtKB	Modified residue	462	462	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13131	
Q5RDH5	UniProtKB	Modified residue	481	481	.	.	.	Note=Phosphoserine%3B by ULK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P54645	
Q5RDH5	UniProtKB	Modified residue	483	483	.	.	.	Note=Phosphothreonine%3B by ULK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P54645	
Q5RDH5	UniProtKB	Modified residue	485	485	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13131	
Q5RDH5	UniProtKB	Modified residue	491	491	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13131	
Q5RDH5	UniProtKB	Modified residue	503	503	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13131	
Q5RDH5	UniProtKB	Modified residue	519	519	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13131	
Q5RDH5	UniProtKB	Modified residue	522	522	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13131	
Q5RDH5	UniProtKB	Non-terminal residue	1	1	.	.	.	.