DCK1_XENLA
ID DCK1_XENLA Reviewed; 265 AA.
AC A0A1L8HV70; Q5XHI7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Deoxycytidine kinase 1 {ECO:0000305|PubMed:27906638};
DE Short=XldCK {ECO:0000303|PubMed:27906638};
DE EC=2.7.1.74 {ECO:0000269|PubMed:27906638};
DE AltName: Full=Deoxyadenosine kinase 1 {ECO:0000305|PubMed:27906638};
DE EC=2.7.1.76 {ECO:0000269|PubMed:27906638};
DE AltName: Full=Deoxyguanosine kinase 1 {ECO:0000305|PubMed:27906638};
DE EC=2.7.1.113 {ECO:0000269|PubMed:27906638};
GN Name=dck.1.L {ECO:0000312|Xenbase:XB-GENE-17335585};
GN Synonyms=dck {ECO:0000312|Xenbase:XB-GENE-17335585};
GN ORFNames=XELAEV_18005792mg {ECO:0000312|EMBL:OCU00010.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|Proteomes:UP000186698};
RN [1] {ECO:0000312|Proteomes:UP000186698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J {ECO:0000312|Proteomes:UP000186698};
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [2] {ECO:0000312|EMBL:AAH84070.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH84070.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27906638; DOI=10.1080/15257770.2016.1143557;
RA Mutahir Z., Christiansen L.S., Clausen A.R., Berchtold M.W., Gojkovic Z.,
RA Munch-Petersen B., Knecht W., Piskur J.;
RT "Gene duplications and losses among vertebrate deoxyribonucleoside kinases
RT of the non-TK1 Family.";
RL Nucleosides Nucleotides Nucleic Acids 35:677-690(2016).
CC -!- FUNCTION: Phosphorylates the deoxyribonucleosides deoxyadenosine,
CC deoxycytidine and deoxyguanosine with highest activity against
CC deoxycytidine followed by deadenosine and deoxyguanosine
CC (PubMed:27906638). Shows only very minor activity against deoxyuridine
CC and deoxythymidine (PubMed:27906638). {ECO:0000269|PubMed:27906638}.
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:0000269|PubMed:27906638};
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:0000269|PubMed:27906638};
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:0000269|PubMed:27906638};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 uM for deoxycytidine {ECO:0000269|PubMed:27906638};
CC KM=527 uM for deoxyguanosine {ECO:0000269|PubMed:27906638};
CC KM=533 uM for deoxyadenosine {ECO:0000269|PubMed:27906638};
CC KM=12457 uM for deoxythymidine {ECO:0000269|PubMed:27906638};
CC KM=15081 uM for deoxyuridine {ECO:0000269|PubMed:27906638};
CC Vmax=0.1 umol/min/mg enzyme toward deoxycytidine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=6.6 umol/min/mg enzyme toward deoxyguanosine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=5.2 umol/min/mg enzyme toward deoxyadenosine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=0.6 umol/min/mg enzyme toward deoxythymidine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=2.5 umol/min/mg enzyme toward deoxyuridine
CC {ECO:0000269|PubMed:27906638};
CC Note=kcat is 0.09 sec(-1) with deoxycytodine as substrate. kcat is
CC 3.40 sec(-1) with deoxyguanosine as substrate. kcat is 2.73 sec(-1)
CC with deoxyadenosine as substrate. kcat is 0.29 sec(-1) with
CC deoxythymidine as substrate. kcat is 1.27 sec(-1) with deoxyuridine
CC as substrate. {ECO:0000269|PubMed:27906638};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P27707}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27707}.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; CM004466; OCU00010.1; -; Genomic_DNA.
DR EMBL; BC084070; AAH84070.1; -; mRNA.
DR RefSeq; NP_001088163.1; NM_001094694.1.
DR AlphaFoldDB; A0A1L8HV70; -.
DR SMR; A0A1L8HV70; -.
DR STRING; 8355.A0A1L8HV70; -.
DR GeneID; 494987; -.
DR KEGG; xla:494987; -.
DR CTD; 494987; -.
DR Xenbase; XB-GENE-17335585; dck.1.L.
DR OMA; HECWLQH; -.
DR OrthoDB; 1505356at2759; -.
DR BRENDA; 2.7.1.74; 6725.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 494987; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004136; F:deoxyadenosine kinase activity; IDA:UniProtKB.
DR GO; GO:0004137; F:deoxycytidine kinase activity; IDA:UniProtKB.
DR GO; GO:0004138; F:deoxyguanosine kinase activity; IDA:UniProtKB.
DR GO; GO:0009157; P:deoxyribonucleoside monophosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01673; dNK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002624; DCK/DGK.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000705; DNK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..265
FT /note="Deoxycytidine kinase 1"
FT /id="PRO_0000449296"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-1"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 190..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 242..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
FT CONFLICT 23..24
FT /note="Missing (in Ref. 2; AAH84070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 265 AA; 31112 MW; 8AAE9EB5738616D3 CRC64;
MATPPKRICI DVPASPSGNK CKVKRISIEG NIAAGKSTFV NILKKANEEW DVVPEPIARW
CNIQSCKDEF EELTTSQKSG GNLLQMMYEK PERWSFTFQS YACLSRIRAQ LKALGGKLKE
AENPVLFFER SVYSDRYIFA SNLYEAECMN ETEWTVYQDW HDWMNSQFGA DLELDGIIYL
RAIPEKCLNR VYTRGREEEQ GIPMEYLEKL HYKHETWLHH RTLRTDFEYL QEIPILTLDV
NEDFRDNKQK QESLIEKVKE FLSTL
