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Database: UniProt
Entry: B5X8Q8_SALSA
LinkDB: B5X8Q8_SALSA
Original site: B5X8Q8_SALSA 
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
//
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