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Database: UniProt
Entry: A0A1S2ZRY0_ERIEU
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Original site: A0A1S2ZRY0_ERIEU 
ID   A0A1S2ZRY0_ERIEU        Unreviewed;       211 AA.
AC   A0A1S2ZRY0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Deoxycytidine kinase {ECO:0000313|RefSeq:XP_007523624.1};
GN   Name=DCK {ECO:0000313|RefSeq:XP_007523624.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007523624.1};
RN   [1] {ECO:0000313|RefSeq:XP_007523624.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_007523624.1; XM_007523562.2.
DR   AlphaFoldDB; A0A1S2ZRY0; -.
DR   STRING; 9365.ENSEEUP00000010938; -.
DR   CTD; 1633; -.
DR   eggNOG; KOG4235; Eukaryota.
DR   InParanoid; A0A1S2ZRY0; -.
DR   OrthoDB; 315858at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019136; F:deoxynucleoside kinase activity; IEA:InterPro.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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; 2.
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; 2.
DR   PIRSF; PIRSF000705; DNK; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Kinase {ECO:0000313|RefSeq:XP_007523624.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Transferase {ECO:0000313|RefSeq:XP_007523624.1}.
FT   DOMAIN          24..134
FT                   /note="Deoxynucleoside kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01712"
FT   DOMAIN          135..208
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         139..143
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         191..193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
SQ   SEQUENCE   211 AA;  24498 MW;  C045F7193F4552F6 CRC64;
     MASPPKRSCP SPATNSEGTR IKKISIEGNI AAGKSTFVNI LKQVSEDWEV VPEPVARWCN
     VQSTQDEFEE LTTSQKSGGN VLQMMYEKPE RWSFTFQSYA CLSRIRAQLA SLNGKLKEAE
     KPVLFFERSV YSDRKCLNRI YLRGRNEEQG IPLEYLQRLH YKHESWLQHR TLKTNFDYLQ
     EVPILTLDVN EDFKDKHDSM VEKVKDFLST L
//
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