##gff-version 3
Q62101	UniProtKB	Chain	1	918	.	.	.	ID=PRO_0000055715;Note=Serine/threonine-protein kinase D1	
Q62101	UniProtKB	Domain	428	547	.	.	.	Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145	
Q62101	UniProtKB	Domain	589	845	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q62101	UniProtKB	Zinc finger	144	194	.	.	.	Note=Phorbol-ester/DAG-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226	
Q62101	UniProtKB	Zinc finger	276	326	.	.	.	Note=Phorbol-ester/DAG-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226	
Q62101	UniProtKB	Region	338	362	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62101	UniProtKB	Region	379	410	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q62101	UniProtKB	Active site	712	712	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
Q62101	UniProtKB	Binding site	595	603	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q62101	UniProtKB	Binding site	618	618	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q62101	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15139	
Q62101	UniProtKB	Modified residue	203	203	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q62101	UniProtKB	Modified residue	206	206	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q62101	UniProtKB	Modified residue	217	217	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8BZ03	
Q62101	UniProtKB	Modified residue	221	221	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BZL6	
Q62101	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15139	
Q62101	UniProtKB	Modified residue	403	403	.	.	.	Note=Phosphoserine%3B by MAPK13;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15139	
Q62101	UniProtKB	Modified residue	407	407	.	.	.	Note=Phosphoserine%3B by MAPK13;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15139	
Q62101	UniProtKB	Modified residue	438	438	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15139	
Q62101	UniProtKB	Modified residue	454	454	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15139	
Q62101	UniProtKB	Modified residue	469	469	.	.	.	Note=Phosphotyrosine%3B by ABL;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BZL6	
Q62101	UniProtKB	Modified residue	508	508	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15139	
Q62101	UniProtKB	Modified residue	554	554	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8K1Y2	
Q62101	UniProtKB	Modified residue	744	744	.	.	.	Note=Phosphoserine%3B by PKC/PRKCD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11410586,ECO:0000269|PubMed:12407104;Dbxref=PMID:11410586,PMID:12407104	
Q62101	UniProtKB	Modified residue	748	748	.	.	.	Note=Phosphoserine%3B by autocatalysis and PKC/PRKCD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11410586,ECO:0000269|PubMed:12407104;Dbxref=PMID:11410586,PMID:12407104	
Q62101	UniProtKB	Modified residue	755	755	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9BZL6	
Q62101	UniProtKB	Modified residue	916	916	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10473617,ECO:0000269|PubMed:27184844;Dbxref=PMID:10473617,PMID:27184844	
Q62101	UniProtKB	Mutagenesis	744	744	.	.	.	Note=Loss of basal kinase activity and phorbol ester-stimulated kinase activity%3B when associated with A-748. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12407104;Dbxref=PMID:12407104	
Q62101	UniProtKB	Mutagenesis	744	744	.	.	.	Note=High basal kinase activity%2C loss of phorbol ester-stimulated kinase activity%3B when associated with D-748. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12407104;Dbxref=PMID:12407104	
Q62101	UniProtKB	Mutagenesis	748	748	.	.	.	Note=Loss of basal kinase activity and phorbol ester-stimulated kinase activity%3B when associated with A-744. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12407104;Dbxref=PMID:12407104	
Q62101	UniProtKB	Mutagenesis	748	748	.	.	.	Note=High basal kinase activity%2C loss of phorbol ester-stimulated kinase activity%3B when associated with D-744. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12407104;Dbxref=PMID:12407104	
Q62101	UniProtKB	Sequence conflict	683	683	.	.	.	Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305