##gff-version 3
P33609	UniProtKB	Chain	1	1465	.	.	.	ID=PRO_0000046429;Note=DNA polymerase alpha catalytic subunit	
P33609	UniProtKB	Zinc finger	1287	1317	.	.	.	Note=CysA-type	
P33609	UniProtKB	Region	20	39	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P33609	UniProtKB	Region	105	135	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P33609	UniProtKB	Region	261	297	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P33609	UniProtKB	Region	654	719	.	.	.	Note=DNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P33609	UniProtKB	Region	1249	1380	.	.	.	Note=DNA-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P33609	UniProtKB	Motif	1352	1378	.	.	.	Note=CysB motif	
P33609	UniProtKB	Compositional bias	110	134	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P33609	UniProtKB	Compositional bias	265	297	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P33609	UniProtKB	Binding site	1287	1287	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09884	
P33609	UniProtKB	Binding site	1290	1290	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09884	
P33609	UniProtKB	Binding site	1314	1314	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09884	
P33609	UniProtKB	Binding site	1319	1319	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09884	
P33609	UniProtKB	Binding site	1352	1352	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09884	
P33609	UniProtKB	Binding site	1357	1357	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09884	
P33609	UniProtKB	Binding site	1375	1375	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09884	
P33609	UniProtKB	Binding site	1378	1378	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09884	
P33609	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09884	
P33609	UniProtKB	Modified residue	192	192	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09884	
P33609	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P33609	UniProtKB	Modified residue	230	230	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337	
P33609	UniProtKB	Modified residue	974	974	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337	
P33609	UniProtKB	Natural variant	1180	1180	.	.	.	Note=In temperature-sensitive FT20 cell line%3B defective activity. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8125989;Dbxref=PMID:8125989	
P33609	UniProtKB	Mutagenesis	1008	1008	.	.	.	Note=Results in loss of primer extension catalytic activity but retains ability to bind to the primase complex. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8253737;Dbxref=PMID:8253737