##gff-version 3
P38859	UniProtKB	Chain	1	1522	.	.	.	ID=PRO_0000080711;Note=DNA replication ATP-dependent helicase/nuclease DNA2	
P38859	UniProtKB	Region	1	29	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38859	UniProtKB	Region	77	119	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38859	UniProtKB	Region	140	160	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38859	UniProtKB	Region	239	270	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38859	UniProtKB	Region	283	330	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38859	UniProtKB	Region	450	900	.	.	.	Note=Nuclease activity	
P38859	UniProtKB	Region	901	1522	.	.	.	Note=Helicase activity	
P38859	UniProtKB	Compositional bias	1	18	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38859	UniProtKB	Compositional bias	77	104	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38859	UniProtKB	Compositional bias	105	119	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38859	UniProtKB	Compositional bias	246	264	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38859	UniProtKB	Compositional bias	286	308	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38859	UniProtKB	Compositional bias	309	325	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P38859	UniProtKB	Binding site	519	519	.	.	.	.	
P38859	UniProtKB	Binding site	768	768	.	.	.	.	
P38859	UniProtKB	Binding site	771	771	.	.	.	.	
P38859	UniProtKB	Binding site	777	777	.	.	.	.	
P38859	UniProtKB	Binding site	1074	1081	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P38859	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
P38859	UniProtKB	Modified residue	17	17	.	.	.	Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
P38859	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
P38859	UniProtKB	Modified residue	962	962	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18407956;Dbxref=PMID:18407956	
P38859	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Abolishes phosphorylation by CDK1%2C leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with A-17 and A-237. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
P38859	UniProtKB	Mutagenesis	17	17	.	.	.	Note=Abolishes phosphorylation by CDK1%2C leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with A-4 and A-237. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
P38859	UniProtKB	Mutagenesis	17	17	.	.	.	Note=Mimics phosphorylation%3B restores nuclear localization and recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with D-237. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
P38859	UniProtKB	Mutagenesis	237	237	.	.	.	Note=Abolishes phosphorylation by CDK1%2C leading to a poor recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with A-4 and A-17. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
P38859	UniProtKB	Mutagenesis	237	237	.	.	.	Note=Mimics phosphorylation%3B restores nuclear localization and recruitment at double-strand. break (DSB) sites following DNA damage%3B when associated with D-17. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21841787;Dbxref=PMID:21841787	
P38859	UniProtKB	Mutagenesis	504	504	.	.	.	Note=In dna2-1%3B temperature-sensitive mutant unable to grow at 37 degrees Celsius%2C probably due to abolition of iron-sulfur-binding. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504	
P38859	UniProtKB	Mutagenesis	519	519	.	.	.	Note=Abolishes iron-sulfur-binding%3B when associated with A-768%3B A-771 and A-777. Impaired nuclease and ATPase activities%3B when associated with A-768. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504	
P38859	UniProtKB	Mutagenesis	675	675	.	.	.	Note=Nuclease dead mutant. No helicase activity when the 5'-end of the substrate is blocked. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20929864;Dbxref=PMID:20929864	
P38859	UniProtKB	Mutagenesis	677	677	.	.	.	Note=Nuclease dead mutant. No helicase activity when the 5'-end of the substrate is blocked. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20929864;Dbxref=PMID:20929864	
P38859	UniProtKB	Mutagenesis	768	768	.	.	.	Note=Abolishes iron-sulfur-binding%3B when associated with A-519%3B A-771 and A-777. Impaired nuclease and ATPase activities%3B when associated with A-519. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504	
P38859	UniProtKB	Mutagenesis	771	771	.	.	.	Note=Abolishes iron-sulfur-binding%3B when associated with A-519%3B A-768 and A-777. Impaired nuclease and ATPase activities%3B when associated with A-777. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504	
P38859	UniProtKB	Mutagenesis	777	777	.	.	.	Note=Abolishes iron-sulfur-binding%3B when associated with A-519%3B A-768 and A-771. Impaired nuclease and ATPase activities%3B when associated with A-771. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22684504;Dbxref=PMID:22684504	
P38859	UniProtKB	Helix	212	215	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5HOG