##gff-version 3
Q866Y3	UniProtKB	Signal peptide	1	31	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q866Y3	UniProtKB	Chain	32	598	.	.	.	ID=PRO_0000023922;Note=N-acetylmuramoyl-L-alanine amidase	
Q866Y3	UniProtKB	Domain	428	554	.	.	.	Note=N-acetylmuramoyl-L-alanine amidase;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q866Y3	UniProtKB	Region	172	194	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q866Y3	UniProtKB	Region	212	233	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q866Y3	UniProtKB	Compositional bias	172	191	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q866Y3	UniProtKB	Binding site	432	432	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8INK6	
Q866Y3	UniProtKB	Binding site	544	544	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8INK6	
Q866Y3	UniProtKB	Binding site	552	552	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8INK6	
Q866Y3	UniProtKB	Site	469	469	.	.	.	Note=Important for catalytic activity%3B essential for amidase activity and zinc hydrate coordination;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00806	
Q866Y3	UniProtKB	Modified residue	261	261	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96PD5	
Q866Y3	UniProtKB	Glycosylation	353	353	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q866Y3	UniProtKB	Glycosylation	507	507	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q866Y3	UniProtKB	Disulfide bond	441	447	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96PD5	
Q866Y3	UniProtKB	Alternative sequence	1	346	.	.	.	ID=VSP_009082;Note=In isoform A. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.1	
Q866Y3	UniProtKB	Alternative sequence	347	356	.	.	.	ID=VSP_009083;Note=In isoform A. ALTLTPNLTQ->MDCFCSRSQE;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.1