ID B5X8Q8_SALSA Unreviewed; 263 AA.
AC B5X8Q8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Deoxycytidine kinase {ECO:0000313|EMBL:ACI67228.1};
GN Name=DCK {ECO:0000313|EMBL:ACI67228.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI67228.1};
RN [1] {ECO:0000313|EMBL:ACI67228.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACI67228.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar full-length cDNAs.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADM16242.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ADM16242.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ADM16242.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ADM16242.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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 EMBL; BT047427; ACI67228.1; -; mRNA.
DR EMBL; BT125501; ADM16242.1; -; mRNA.
DR AlphaFoldDB; B5X8Q8; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019136; F:deoxynucleoside kinase activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Kinase {ECO:0000313|EMBL:ACI67228.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transferase {ECO:0000313|EMBL:ACI67228.1}.
FT DOMAIN 24..260
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 263 AA; 31051 MW; F22614C60FD3FD9D CRC64;
MSPTPPKRAG PSLLNDNMDK TKRISIEGNI AAGKSTFVRL LEEQSKDWEV VPEPIARWCN
VQTQHSEFEE LTVSQKNGGN VLQMMYEKPE RWAYTFQTYA FMSRVRAQMK STNGKLREAE
NPVQFFERSV YSDRYIFAAN LYESECLNET EWSIYQDWHG WLHEQFGKHI GLDGIIYLRA
APERCIERLH RRGREEEQGI PLEYLEKLHF KHESWLQHKT MCMEYKYLNN VPILTLDVNE
DFKVDKVKGE DMVEKVKEFL STL
//