ID A0A2U4B4V9_TURTR Unreviewed; 253 AA.
AC A0A2U4B4V9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Deoxycytidine kinase isoform X5 {ECO:0000313|RefSeq:XP_019788247.1};
GN Name=DCK {ECO:0000313|RefSeq:XP_019788247.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019788247.1};
RN [1] {ECO:0000313|RefSeq:XP_019788247.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019788247.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyadenosine + ATP = ADP + dAMP + H(+);
CC Xref=Rhea:RHEA:23452, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216;
CC EC=2.7.1.76; Evidence={ECO:0000256|ARBA:ARBA00036035};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a
CC ribonucleoside 5'-diphosphate + dCMP + H(+); Xref=Rhea:RHEA:20061,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:57566,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=2.7.1.74;
CC Evidence={ECO:0000256|ARBA:ARBA00036126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyguanosine + ATP = ADP + dGMP + H(+);
CC Xref=Rhea:RHEA:19201, ChEBI:CHEBI:15378, ChEBI:CHEBI:17172,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57673, ChEBI:CHEBI:456216;
CC EC=2.7.1.113; Evidence={ECO:0000256|ARBA:ARBA00036095};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DCK/DGK family.
CC {ECO:0000256|ARBA:ARBA00007420}.
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DR RefSeq; XP_019788247.1; XM_019932688.2.
DR AlphaFoldDB; A0A2U4B4V9; -.
DR GeneID; 101328143; -.
DR OrthoDB; 315858at2759; -.
DR Proteomes; UP000245320; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019136; F:deoxynucleoside kinase activity; IEA:InterPro.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01673; dNK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR002624; DCK/DGK.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10513:SF19; DEOXYCYTIDINE KINASE; 1.
DR PANTHER; PTHR10513; DEOXYNUCLEOSIDE KINASE; 1.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000705; DNK; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Kinase {ECO:0000313|RefSeq:XP_019788247.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Transferase {ECO:0000313|RefSeq:XP_019788247.1}.
FT DOMAIN 24..247
FT /note="Deoxynucleoside kinase"
FT /evidence="ECO:0000259|Pfam:PF01712"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 188..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 240..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
SQ SEQUENCE 253 AA; 29524 MW; 41C8EA21BEAAD885 CRC64;
MATPPKRSCP SPAASSEGTR IKKISIEGNI AAGKSTFVNI LKQVCEDWEV VPEPVARWCN
VQSTQDEFKE LTTSQKSGGN VLQMMYEKPE RWSFTFQSYA CLSRIRAQLA ALNGKLKDAE
KPVLFFERSV YSDRYIFASN LYESDCMNET EWTIYQDWHD WMNNQFGQSL ELDGIIYLRA
TPEKCLNRIY LRGRNEEQGI PLEYLEKLHY KHESWLLHRT VKTNFDYLQE VPILTLDVNE
DFKDKHDSLV EKQ
//
