##gff-version 3
E3QKD2	UniProtKB	Chain	1	921	.	.	.	ID=PRO_0000412144;Note=Probable dipeptidyl-aminopeptidase B	
E3QKD2	UniProtKB	Topological domain	1	108	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
E3QKD2	UniProtKB	Transmembrane	109	129	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
E3QKD2	UniProtKB	Topological domain	130	921	.	.	.	Note=Vacuolar;Ontology_term=ECO:0000255;evidence=ECO:0000255	
E3QKD2	UniProtKB	Region	1	87	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
E3QKD2	UniProtKB	Compositional bias	13	34	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
E3QKD2	UniProtKB	Compositional bias	35	49	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
E3QKD2	UniProtKB	Active site	768	768	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
E3QKD2	UniProtKB	Active site	845	845	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
E3QKD2	UniProtKB	Active site	878	878	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
E3QKD2	UniProtKB	Glycosylation	131	131	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
E3QKD2	UniProtKB	Glycosylation	364	364	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
E3QKD2	UniProtKB	Glycosylation	577	577	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
E3QKD2	UniProtKB	Glycosylation	827	827	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255