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Database: UniProt
Entry: A0A0G0BY53_9BACT
LinkDB: A0A0G0BY53_9BACT
Original site: A0A0G0BY53_9BACT 
ID   A0A0G0BY53_9BACT        Unreviewed;       240 AA.
AC   A0A0G0BY53;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Deoxynucleoside kinase {ECO:0000313|EMBL:KKP36062.1};
GN   ORFNames=UR26_C0001G0106 {ECO:0000313|EMBL:KKP36062.1};
OS   candidate division TM6 bacterium GW2011_GWF2_32_72.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619079 {ECO:0000313|EMBL:KKP36062.1, ECO:0000313|Proteomes:UP000034766};
RN   [1] {ECO:0000313|EMBL:KKP36062.1, ECO:0000313|Proteomes:UP000034766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKP36062.1}.
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DR   EMBL; LBON01000001; KKP36062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0BY53; -.
DR   STRING; 1619079.UR26_C0001G0106; -.
DR   Proteomes; UP000034766; Unassembled WGS sequence.
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; DEOXYNUCLEOSIDE KINASE; 1.
DR   PANTHER; PTHR10513:SF35; THYMIDINE KINASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01712; dNK; 1.
DR   PIRSF; PIRSF000705; DNK; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KKP36062.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..214
FT                   /note="Deoxynucleoside kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01712"
FT   ACT_SITE        85
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT   BINDING         6..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT   BINDING         144..148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT   BINDING         194..196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
SQ   SEQUENCE   240 AA;  28159 MW;  D930EA52D4112B8A CRC64;
     MYIIEGNIGA GKSTFLNLIK IFLPQYSVHQ EPVDTWHKKK EGQSLLESFY TTPKRWAYTL
     ETLSLINRVK EHLAIQEMPG ISIAERSVYS GNYCFAKNGY LNQFLDPIEW FAYNEWFNFM
     VPGKCKTPTG FIYLQVSPEK SYERVLKRNR SSENGLTLEY LKEINKRHEE FLIQKYNVLP
     ELQNIPVLIL NVNENFDKHT LKLQEHLNKV EKFIEETQVQ KLTNLNNLKT SGIFNKSLDI
//
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