##gff-version 3
P27707	UniProtKB	Chain	1	260	.	.	.	ID=PRO_0000175090;Note=Deoxycytidine kinase	
P27707	UniProtKB	Active site	127	127	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P27707	UniProtKB	Binding site	28	36	.	.	.	.	
P27707	UniProtKB	Binding site	53	53	.	.	.	.	
P27707	UniProtKB	Binding site	86	86	.	.	.	.	
P27707	UniProtKB	Binding site	97	97	.	.	.	.	
P27707	UniProtKB	Binding site	128	128	.	.	.	.	
P27707	UniProtKB	Binding site	133	133	.	.	.	.	
P27707	UniProtKB	Binding site	188	192	.	.	.	.	
P27707	UniProtKB	Binding site	197	197	.	.	.	.	
P27707	UniProtKB	Binding site	240	242	.	.	.	.	
P27707	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine%3B by CK1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20637175;Dbxref=PMID:20637175	
P27707	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine%3B by CK1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20637175;Dbxref=PMID:20637175	
P27707	UniProtKB	Modified residue	72	72	.	.	.	Note=Phosphothreonine%3B by CK1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20637175;Dbxref=PMID:20637175	
P27707	UniProtKB	Modified residue	74	74	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:20637175,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:20068231,PMID:20637175,PMID:23186163	
P27707	UniProtKB	Mutagenesis	74	74	.	.	.	Note=4.5-fold increase in Km. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20637175;Dbxref=PMID:20637175	
P27707	UniProtKB	Mutagenesis	100	100	.	.	.	Note=Strongly increased catalytic efficiency towards deoxycytidine%3B when associated with M-104 and A-133. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12808445;Dbxref=PMID:12808445	
P27707	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Strongly increased catalytic efficiency towards deoxythymidine%3B when associated with A-133. R->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12808445,ECO:0000269|PubMed:19159229,ECO:0000269|PubMed:20614893;Dbxref=PMID:12808445,PMID:19159229,PMID:20614893	
P27707	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Strongly increased catalytic efficiency towards deoxycytidine%3B when associated with V-100 and A-133. R->M;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12808445,ECO:0000269|PubMed:19159229,ECO:0000269|PubMed:20614893;Dbxref=PMID:12808445,PMID:19159229,PMID:20614893	
P27707	UniProtKB	Mutagenesis	133	133	.	.	.	Note=Strongly increased catalytic efficiency towards deoxycytidine%3B when associated with V-100 and M-104. Strongly increased catalytic efficiency towards deoxythymidine%3B when associated with L-104. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12808445,ECO:0000269|PubMed:19159229,ECO:0000269|PubMed:20614893;Dbxref=PMID:12808445,PMID:19159229,PMID:20614893	
P27707	UniProtKB	Sequence conflict	122	122	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P27707	UniProtKB	Beta strand	22	27	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	34	38	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Turn	39	41	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	42	44	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Beta strand	48	51	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	55	58	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Beta strand	61	63	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2A2Z	
P27707	UniProtKB	Helix	69	72	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2NO7	
P27707	UniProtKB	Helix	73	77	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ZI6	
P27707	UniProtKB	Helix	81	87	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	89	112	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	115	118	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Beta strand	119	121	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Beta strand	123	128	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	130	135	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	137	143	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	149	170	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Beta strand	173	179	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	182	192	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	195	197	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	202	216	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	226	230	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Beta strand	233	237	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z	
P27707	UniProtKB	Helix	242	258	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1P5Z