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Database: UniProt
Entry: A0A091JTL5_EGRGA
LinkDB: A0A091JTL5_EGRGA
Original site: A0A091JTL5_EGRGA 
ID   A0A091JTL5_EGRGA        Unreviewed;       228 AA.
AC   A0A091JTL5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Deoxycytidine kinase {ECO:0000313|EMBL:KFP14911.1};
DE   Flags: Fragment;
GN   ORFNames=Z169_04844 {ECO:0000313|EMBL:KFP14911.1};
OS   Egretta garzetta (Little egret).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX   NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP14911.1, ECO:0000313|Proteomes:UP000053119};
RN   [1] {ECO:0000313|EMBL:KFP14911.1, ECO:0000313|Proteomes:UP000053119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP14911.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KK501443; KFP14911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091JTL5; -.
DR   STRING; 188379.A0A091JTL5; -.
DR   Proteomes; UP000053119; Unassembled WGS sequence.
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: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; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Kinase {ECO:0000313|EMBL:KFP14911.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW   Transferase {ECO:0000313|EMBL:KFP14911.1}.
FT   DOMAIN          1..227
FT                   /note="Deoxynucleoside kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01712"
FT   ACT_SITE        98
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         159..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT   BINDING         211..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP14911.1"
FT   NON_TER         228
FT                   /evidence="ECO:0000313|EMBL:KFP14911.1"
SQ   SEQUENCE   228 AA;  27316 MW;  203485E54DD4CF85 CRC64;
     AAGKSTFVNL LKQADEEWEV VPEPVARWCN VQQNSEDDCE ELTSSQKGGR NVLRMMYEKP
     ERWSFTFQTY ACLSRIRAQL RSLDGKLREA ENPVVFFERS VYSDRYIFAA NLYESDCMNE
     TEWTIYQDWH DWMNKQFGPS LALDGIIYLR ATPEKCLNRI YLRGRDEEQE IPIEYLEKLH
     YKHESWLQHR TLRTDFEYLQ EIPILTLDVN EDFKGKKDRY DHMTEKVK
//
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