##gff-version 3
P20651	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Chain	2	525	.	.	.	ID=PRO_0000058827;Note=Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform	
P20651	UniProtKB	Region	1	23	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P20651	UniProtKB	Region	65	356	.	.	.	Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Region	357	379	.	.	.	Note=Calcineurin B binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Region	402	416	.	.	.	Note=Calmodulin-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Region	417	424	.	.	.	Note=Autoinhibitory segment;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Region	475	497	.	.	.	Note=Autoinhibitory domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Motif	316	320	.	.	.	Note=SAPNY motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08209	
P20651	UniProtKB	Active site	160	160	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q08209	
P20651	UniProtKB	Binding site	99	99	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Binding site	101	101	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Binding site	127	127	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Binding site	127	127	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Binding site	159	159	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Binding site	208	208	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Binding site	290	290	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16298	
P20651	UniProtKB	Modified residue	479	479	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P48453