DCK_CHICK
ID DCK_CHICK Reviewed; 257 AA.
AC Q5ZMF3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Deoxycytidine kinase {ECO:0000305|PubMed:27906638};
DE Short=GgdCK {ECO:0000303|PubMed:27906638};
DE EC=2.7.1.74 {ECO:0000269|PubMed:27906638};
DE AltName: Full=Deoxyadenosine kinase {ECO:0000305|PubMed:27906638};
DE EC=2.7.1.76 {ECO:0000269|PubMed:27906638};
DE AltName: Full=Deoxyguanosine kinase {ECO:0000305|PubMed:27906638};
DE EC=2.7.1.113 {ECO:0000269|PubMed:27906638};
GN Name=DCK {ECO:0000303|PubMed:27906638};
GN ORFNames=RCJMB04_2e2 {ECO:0000312|EMBL:CAG31090.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|EMBL:CAG31090.1};
RN [1] {ECO:0000312|EMBL:ACF41168.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gojkovic Z.;
RT "Mammals have lost vertebrate deoxyadenosine kinase.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CAG31090.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAG31090.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG31090.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
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 deoxycytidine,
CC deoxyguanosine and deoxyadenosine (PubMed:27906638). Displays highest
CC activity against deoxycytidine followed by deoxyadenosine and then
CC deoxyguanosine (PubMed:27906638). Shows only very minor activity
CC against deoxyuridine and deoxythymidine (PubMed:27906638).
CC {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'-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'-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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 uM for deoxycytidine {ECO:0000269|PubMed:27906638};
CC KM=93 uM for deoxyadenosine {ECO:0000269|PubMed:27906638};
CC KM=122 uM for deoxyguanosine {ECO:0000269|PubMed:27906638};
CC KM=7502 uM for deoxyuridine {ECO:0000269|PubMed:27906638};
CC KM=18546 uM for deoxythymidine {ECO:0000269|PubMed:27906638};
CC Vmax=0.1 umol/min/mg enzyme toward deoxycytidine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=8.1 umol/min/mg enzyme toward deoxyadenosine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=2.4 umol/min/mg enzyme toward deoxyguanosine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=2.1 umol/min/mg enzyme toward deoxyuridine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=2.1 umol/min/mg enzyme toward deoxythymidine
CC {ECO:0000269|PubMed:27906638};
CC Note=kcat is 0.05 sec(-1) with deoxycytodine as substrate. kcat is
CC 4.07 sec(-1) with deoxyadenosine as substrate. kcat is 1.23 sec(-1)
CC with deoxyguanosine as substrate. kcat is 1.05 sec(-1) with
CC deoxyuridine as substrate. kcat is 1.08 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 -!- TISSUE SPECIFICITY: Expressed at high levels in adult intestine,
CC spleen, thymus and testis with lower levels in skeletal muscle and eye.
CC In the embryo, expressed at higher levels until day 10 with lower
CC levels in later stages. {ECO:0000269|PubMed:27906638}.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; EU835757; ACF41168.1; -; mRNA.
DR EMBL; AJ719431; CAG31090.1; -; mRNA.
DR RefSeq; NP_001006451.1; NM_001006451.1.
DR AlphaFoldDB; Q5ZMF3; -.
DR SMR; Q5ZMF3; -.
DR PaxDb; Q5ZMF3; -.
DR GeneID; 422648; -.
DR KEGG; gga:422648; -.
DR CTD; 1633; -.
DR VEuPathDB; HostDB:geneid_422648; -.
DR eggNOG; KOG4235; Eukaryota.
DR HOGENOM; CLU_030466_1_1_1; -.
DR OrthoDB; 1505356at2759; -.
DR PhylomeDB; Q5ZMF3; -.
DR BRENDA; 2.7.1.74; 1306.
DR PRO; PR:Q5ZMF3; -.
DR Proteomes; UP000000539; Unplaced.
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..257
FT /note="Deoxycytidine kinase"
FT /id="PRO_0000449294"
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-1"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 182..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 234..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
SQ SEQUENCE 257 AA; 30373 MW; FBEB2F7B76D59D38 CRC64;
MATPPKRGRL EGRVKKIAVE GNIAAGKSTF VNILKQADEG WEVVPEPVAR WCNVQQNSEE
DCEELTTSQK SGGNVLQMMY EKPERWSFTF QMYACLSRIR AQLKSIDGKL REAENPVVFF
ERSVYSDRYI FAANLYESDC MNETEWTIYQ DWHDWMNKQF GQSLALDGII YLRATPEKCL
NRIYLRGRDE EQEIPIEYLE KLHYKHESWL QHKTLRTDFE YLQEIPILTL DVNEDFKGKK
DRYDHMTEKV KEFLSTL
