##gff-version 3
A0QNG1	UniProtKB	Chain	1	625	.	.	.	ID=PRO_0000422953;Note=Serine/threonine-protein kinase PknB	
A0QNG1	UniProtKB	Topological domain	1	331	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
A0QNG1	UniProtKB	Transmembrane	332	352	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
A0QNG1	UniProtKB	Topological domain	353	625	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
A0QNG1	UniProtKB	Domain	11	274	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
A0QNG1	UniProtKB	Domain	355	421	.	.	.	Note=PASTA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00528	
A0QNG1	UniProtKB	Domain	422	489	.	.	.	Note=PASTA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00528	
A0QNG1	UniProtKB	Domain	490	556	.	.	.	Note=PASTA 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00528	
A0QNG1	UniProtKB	Domain	557	625	.	.	.	Note=PASTA 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00528	
A0QNG1	UniProtKB	Region	302	321	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A0QNG1	UniProtKB	Region	591	612	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A0QNG1	UniProtKB	Compositional bias	597	612	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A0QNG1	UniProtKB	Active site	138	138	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
A0QNG1	UniProtKB	Binding site	17	25	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
A0QNG1	UniProtKB	Binding site	40	40	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
A0QNG1	UniProtKB	Binding site	93	95	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
A0QNG1	UniProtKB	Binding site	140	143	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
A0QNG1	UniProtKB	Binding site	143	143	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
A0QNG1	UniProtKB	Binding site	156	156	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
A0QNG1	UniProtKB	Binding site	156	156	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
A0QNG1	UniProtKB	Modified residue	169	169	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
A0QNG1	UniProtKB	Modified residue	171	171	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
A0QNG1	UniProtKB	Modified residue	173	173	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
A0QNG1	UniProtKB	Modified residue	294	294	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
A0QNG1	UniProtKB	Modified residue	295	295	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
A0QNG1	UniProtKB	Modified residue	309	309	.	.	.	Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250