##gff-version 3
Q5PQT2	UniProtKB	Chain	1	1194	.	.	.	ID=PRO_0000304808;Note=Myotubularin-related protein 3	
Q5PQT2	UniProtKB	Domain	151	572	.	.	.	Note=Myotubularin phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00669	
Q5PQT2	UniProtKB	Zinc finger	1115	1175	.	.	.	Note=FYVE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
Q5PQT2	UniProtKB	Region	583	609	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q5PQT2	UniProtKB	Region	693	731	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q5PQT2	UniProtKB	Region	852	871	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q5PQT2	UniProtKB	Region	876	897	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q5PQT2	UniProtKB	Region	932	971	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q5PQT2	UniProtKB	Region	988	1017	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q5PQT2	UniProtKB	Coiled coil	1025	1058	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q5PQT2	UniProtKB	Compositional bias	693	721	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q5PQT2	UniProtKB	Compositional bias	988	1006	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q5PQT2	UniProtKB	Active site	409	409	.	.	.	Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10044	
Q5PQT2	UniProtKB	Binding site	322	325	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q5PQT2	UniProtKB	Binding site	347	348	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q5PQT2	UniProtKB	Binding site	409	415	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q5PQT2	UniProtKB	Binding site	455	455	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q5PQT2	UniProtKB	Binding site	1121	1121	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
Q5PQT2	UniProtKB	Binding site	1124	1124	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
Q5PQT2	UniProtKB	Binding site	1137	1137	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
Q5PQT2	UniProtKB	Binding site	1140	1140	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
Q5PQT2	UniProtKB	Binding site	1145	1145	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
Q5PQT2	UniProtKB	Binding site	1148	1148	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
Q5PQT2	UniProtKB	Binding site	1167	1167	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
Q5PQT2	UniProtKB	Binding site	1170	1170	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091	
Q5PQT2	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13615	
Q5PQT2	UniProtKB	Modified residue	609	609	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
Q5PQT2	UniProtKB	Modified residue	629	629	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13615	
Q5PQT2	UniProtKB	Modified residue	643	643	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13615	
Q5PQT2	UniProtKB	Modified residue	647	647	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13615	
Q5PQT2	UniProtKB	Modified residue	725	725	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13615	
Q5PQT2	UniProtKB	Modified residue	904	904	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13615	
Q5PQT2	UniProtKB	Modified residue	1060	1060	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8K296