DCK2_CHICK
ID DCK2_CHICK Reviewed; 265 AA.
AC Q5ZJM7; F6TYL4;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Deoxycytidine kinase 2 {ECO:0000305|PubMed:27906638};
DE Short=GgdCK2 {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=DCK2 {ECO:0000303|PubMed:27906638};
GN Synonyms=DAK {ECO:0000312|EMBL:ACF41169.1};
GN ORFNames=RCJMB04_17b6 {ECO:0000312|EMBL:CAG32066.1};
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:CAG32066.1};
RN [1] {ECO:0000312|EMBL:ACF41169.1}
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:CAG32066.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAG32066.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG32066.1};
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:0000312|Proteomes:UP000000539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [4] {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 deoxyadenosine,
CC deoxycytidine and deoxyguanosine (PubMed:27906638). Shows highest
CC activity against deoxyguanosine followed by deoxycytidine and then
CC deoxyadenosine (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'-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=19.8 uM for deoxyguanosine {ECO:0000269|PubMed:27906638};
CC KM=64 uM for deoxycytidine {ECO:0000269|PubMed:27906638};
CC KM=104 uM for deoxyadenosine {ECO:0000269|PubMed:27906638};
CC KM=20317 uM for deoxyuridine {ECO:0000269|PubMed:27906638};
CC KM=33613 uM for deoxythymidine {ECO:0000269|PubMed:27906638};
CC Vmax=1.3 umol/min/mg enzyme toward deoxyguanosine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=1.0 umol/min/mg enzyme toward deoxycytidine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=4.9 umol/min/mg enzyme toward deoxyadenosine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=1 umol/min/mg enzyme toward deoxyuridine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=0.5 umol/min/mg enzyme toward deoxythymidine
CC {ECO:0000269|PubMed:27906638};
CC Note=kcat is 0.67 sec(-1) with deoxyguanosine as substrate. kcat is
CC 0.52 sec(-1) with deoxycytidine as substrate. kcat is 2.56 sec(-1)
CC with deoxyadenosine as substrate. kcat is 0.53 sec(-1) with
CC deoxyuridine as substrate. kcat is 0.26 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; EU835758; ACF41169.1; -; mRNA.
DR EMBL; AJ720407; CAG32066.1; -; mRNA.
DR EMBL; AADN05000072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001072968.1; NM_001079500.1.
DR AlphaFoldDB; Q5ZJM7; -.
DR SMR; Q5ZJM7; -.
DR STRING; 9031.ENSGALP00000009571; -.
DR Ensembl; ENSGALT00000009585; ENSGALP00000009571; ENSGALG00000005961.
DR GeneID; 770922; -.
DR KEGG; gga:770922; -.
DR CTD; 770922; -.
DR VEuPathDB; HostDB:geneid_770922; -.
DR eggNOG; KOG4235; Eukaryota.
DR GeneTree; ENSGT00940000164917; -.
DR HOGENOM; CLU_030466_1_1_1; -.
DR InParanoid; Q5ZJM7; -.
DR OMA; KPTRWAY; -.
DR OrthoDB; 603679at2759; -.
DR PhylomeDB; Q5ZJM7; -.
DR TreeFam; TF324413; -.
DR PRO; PR:Q5ZJM7; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000005961; Expressed in granulocyte and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0019136; F:deoxynucleoside kinase activity; IBA:GO_Central.
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 2"
FT /id="PRO_0000449295"
FT ACT_SITE 130
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-1"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 191..195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 243..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
SQ SEQUENCE 265 AA; 31240 MW; 5DBE0E85E1131940 CRC64;
MSAPAKRRCR GPAADLDSSF QKRLRKISIE GNIAAGKSTL VRLLEKHSDE WEVIPEPIAK
WCNIQTSEDE CKELSTSQKS GGNLLQMLYD KPTRWAYTFQ TYACLSRVRA QLKPISAKLH
EAEHPVQFFE RSVYSDRYVF ASNLFESGNI NETEWAIYQD WHSWLLNQFQ SEIELDGIIY
LRTTPQKCME RLQKRGRKEE EGIDLEYLEN LHYKHETWLY EKTMRVDFEN LKEIPILVLD
VNEDFKNDKI KQEYLIDEIK SFLTS
