DCK2_XENLA
ID DCK2_XENLA Reviewed; 264 AA.
AC Q6DD33; A0A1L8GXD1;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Deoxycytidine kinase 2 {ECO:0000305|PubMed:27906638};
DE Short=XldCK2 {ECO:0000303|PubMed:27906638};
DE EC=2.7.1.74 {ECO:0000269|PubMed:27906638};
DE AltName: Full=Deoxyadenosine kinase 2 {ECO:0000305|PubMed:27906638};
DE EC=2.7.1.76 {ECO:0000269|PubMed:27906638};
DE AltName: Full=Deoxyguanosine kinase 2 {ECO:0000305|PubMed:27906638};
DE EC=2.7.1.113 {ECO:0000269|PubMed:27906638};
GN Name=dck.2 {ECO:0000312|Xenbase:XB-GENE-5727756};
GN Synonyms=dck {ECO:0000312|Xenbase:XB-GENE-5727756};
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|EMBL:AAH77796.1};
RN [1] {ECO:0000312|EMBL:AAO64435.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Knecht W., Sandrini M.P.B., Piskur J.;
RT "Xenopus laevis deoxyribonucleoside kinases.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {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 [3] {ECO:0000312|EMBL:AAH77796.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH77796.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {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 deoxyguanosine followed by deadenosine and then deoxycytidine
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'-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 -!- 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for deoxyguanosine {ECO:0000269|PubMed:27906638};
CC KM=300 uM for deoxyadenosine {ECO:0000269|PubMed:27906638};
CC KM=505 uM for deoxycytidine {ECO:0000269|PubMed:27906638};
CC KM=20132 uM for deoxyuridine {ECO:0000269|PubMed:27906638};
CC KM=33152 uM for deoxythymidine {ECO:0000269|PubMed:27906638};
CC Vmax=2.4 umol/min/mg enzyme toward deoxyguanosine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=9.3 umol/min/mg enzyme toward deoxyadenosine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=0.8 umol/min/mg enzyme toward deoxycytidine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=0.7 umol/min/mg enzyme toward deoxyuridine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=0.3 umol/min/mg enzyme toward deoxythymidine
CC {ECO:0000269|PubMed:27906638};
CC Note=kcat is 1.26 sec(-1) with deoxyguanosine as substrate. kcat is
CC 4.87 sec(-1) with deoxyadenosine as substrate. kcat is 0.42 sec(-1)
CC with deoxycytidine as substrate. kcat is 0.36 sec(-1) with
CC deoxyuridine as substrate. kcat is 0.14 sec(-1) with deoxythymidine
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=OCT88483.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY192985; AAO64435.1; -; mRNA.
DR EMBL; CM004470; OCT88483.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC077796; AAH77796.1; -; mRNA.
DR RefSeq; NP_001086938.1; NM_001093469.1.
DR AlphaFoldDB; Q6DD33; -.
DR SMR; Q6DD33; -.
DR STRING; 8355.A0A1L8GXD1; -.
DR DNASU; 446773; -.
DR GeneID; 446773; -.
DR KEGG; xla:446773; -.
DR CTD; 446773; -.
DR Xenbase; XB-GENE-5727756; dck.2.L.
DR OrthoDB; 1505356at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 446773; Expressed in blastula and 15 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..264
FT /note="Deoxycytidine kinase 2"
FT /id="PRO_0000449297"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-1"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 189..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 241..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
SQ SEQUENCE 264 AA; 31174 MW; EBA1A71F56A82154 CRC64;
MATPPKRMCH SPVFNNSFEK RVKKLSIEGN IAAGKSTFVR ILEKASDEWE VVPEPIAKWC
NVQTTENENE ELSTSQKSGG NLLQMLYDKP TRWAYTFQTY ACLSRVRAQL KTPSPKLLEA
EHPVQFFERS VYSDRYIFAS SLFEFQNINE TEWAIYQDWH TWFLNQFESD IDLDGIIYLR
ATPEKCMDRL HTRGREEEQG IQLEYLESLH YKHESWLYDR TMSVDFENLQ HMPVMVLDVN
EDFKYDKIKQ EALLDKVKEF LASL
