##gff-version 3
Q80ZH1	UniProtKB	Chain	1	1111	.	.	.	ID=PRO_0000357050;Note=Histone deacetylase 5	
Q80ZH1	UniProtKB	Region	40	63	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q80ZH1	UniProtKB	Region	107	136	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q80ZH1	UniProtKB	Region	187	272	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q80ZH1	UniProtKB	Region	474	495	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q80ZH1	UniProtKB	Region	527	611	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q80ZH1	UniProtKB	Region	645	666	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q80ZH1	UniProtKB	Region	671	1017	.	.	.	Note=Histone deacetylase	
Q80ZH1	UniProtKB	Region	1086	1111	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q80ZH1	UniProtKB	Motif	1070	1109	.	.	.	Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q80ZH1	UniProtKB	Compositional bias	240	272	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q80ZH1	UniProtKB	Compositional bias	572	606	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q80ZH1	UniProtKB	Active site	822	822	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q80ZH1	UniProtKB	Binding site	685	685	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q80ZH1	UniProtKB	Binding site	687	687	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q80ZH1	UniProtKB	Binding site	693	693	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q80ZH1	UniProtKB	Binding site	770	770	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q80ZH1	UniProtKB	Modified residue	250	250	.	.	.	Note=Phosphoserine%3B by AMPK%2C CaMK1%2C SIK1 and PKD/PRKD1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UQL6	
Q80ZH1	UniProtKB	Modified residue	283	283	.	.	.	Note=Phosphothreonine%3B by PKC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UQL6	
Q80ZH1	UniProtKB	Modified residue	489	489	.	.	.	Note=Phosphoserine%3B by AMPK%2C CaMK1%2C SIK1 and PKD/PRKD1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UQL6	
Q80ZH1	UniProtKB	Modified residue	524	524	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UQL6	
Q80ZH1	UniProtKB	Modified residue	600	600	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UQL6	
Q80ZH1	UniProtKB	Modified residue	650	650	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UQL6	
Q80ZH1	UniProtKB	Modified residue	1097	1097	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UQL6	
Q80ZH1	UniProtKB	Cross-link	35	35	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UQL6