##gff-version 3
Q28056	UniProtKB	Chain	1	754	.	.	.	ID=PRO_0000064705;Note=Aspartyl/asparaginyl beta-hydroxylase	
Q28056	UniProtKB	Topological domain	1	56	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q28056	UniProtKB	Transmembrane	57	77	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q28056	UniProtKB	Topological domain	78	754	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q28056	UniProtKB	Repeat	337	370	.	.	.	Note=TPR 1	
Q28056	UniProtKB	Repeat	378	411	.	.	.	Note=TPR 2	
Q28056	UniProtKB	Repeat	450	483	.	.	.	Note=TPR 3	
Q28056	UniProtKB	Repeat	485	517	.	.	.	Note=TPR 4	
Q28056	UniProtKB	Repeat	521	553	.	.	.	Note=TPR 5	
Q28056	UniProtKB	Region	1	48	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q28056	UniProtKB	Region	176	197	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q28056	UniProtKB	Region	247	326	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q28056	UniProtKB	Compositional bias	9	37	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q28056	UniProtKB	Compositional bias	257	288	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q28056	UniProtKB	Binding site	109	109	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Binding site	111	111	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Binding site	113	113	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Binding site	115	115	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Binding site	120	120	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Binding site	621	621	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Binding site	664	664	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Binding site	675	675	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Binding site	684	686	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Binding site	721	721	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Binding site	731	731	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797	
Q28056	UniProtKB	Glycosylation	96	96	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q28056	UniProtKB	Glycosylation	466	466	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q28056	UniProtKB	Glycosylation	702	702	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q28056	UniProtKB	Disulfide bond	637	644	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q12797