##gff-version 3
Q1LZ53	UniProtKB	Chain	1	908	.	.	.	ID=PRO_0000313030;Note=DNA (cytosine-5)-methyltransferase 3A	
Q1LZ53	UniProtKB	Domain	257	315	.	.	.	Note=PWWP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00162	
Q1LZ53	UniProtKB	Domain	478	610	.	.	.	Note=ADD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00865	
Q1LZ53	UniProtKB	Domain	630	908	.	.	.	Note=SAM-dependent MTase C5-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01016	
Q1LZ53	UniProtKB	Zinc finger	489	519	.	.	.	Note=GATA-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00865	
Q1LZ53	UniProtKB	Zinc finger	530	586	.	.	.	Note=PHD-type%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00865	
Q1LZ53	UniProtKB	Region	1	183	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q1LZ53	UniProtKB	Region	195	399	.	.	.	Note=Interaction with DNMT1 and DNMT3B;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q1LZ53	UniProtKB	Region	226	281	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q1LZ53	UniProtKB	Region	443	462	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q1LZ53	UniProtKB	Region	490	582	.	.	.	Note=Interaction with the PRC2/EED-EZH2 complex;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q1LZ53	UniProtKB	Compositional bias	12	41	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q1LZ53	UniProtKB	Compositional bias	63	82	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q1LZ53	UniProtKB	Compositional bias	226	240	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q1LZ53	UniProtKB	Active site	706	706	.	.	.	Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01016,ECO:0000255|PROSITE-ProRule:PRU10018	
Q1LZ53	UniProtKB	Binding site	637	641	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6K1	
Q1LZ53	UniProtKB	Binding site	660	660	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6K1	
Q1LZ53	UniProtKB	Binding site	682	684	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6K1	
Q1LZ53	UniProtKB	Binding site	887	889	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6K1	
Q1LZ53	UniProtKB	Modified residue	102	102	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
Q1LZ53	UniProtKB	Modified residue	120	120	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
Q1LZ53	UniProtKB	Modified residue	167	167	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88508	
Q1LZ53	UniProtKB	Modified residue	239	239	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
Q1LZ53	UniProtKB	Modified residue	251	251	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
Q1LZ53	UniProtKB	Modified residue	257	257	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6K1	
Q1LZ53	UniProtKB	Modified residue	386	386	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88508	
Q1LZ53	UniProtKB	Modified residue	389	389	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88508	
Q1LZ53	UniProtKB	Modified residue	706	706	.	.	.	Note=S-methylcysteine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88508	
Q1LZ53	UniProtKB	Cross-link	158	158	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y6K1	
Q1LZ53	UniProtKB	Alternative sequence	1	219	.	.	.	ID=VSP_029986;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15203217;Dbxref=PMID:15203217