ID   A0A2A8S6L7_9BACI        Unreviewed;       212 AA.
AC   A0A2A8S6L7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Deoxynucleoside kinase {ECO:0000313|EMBL:PEZ02559.1};
GN   ORFNames=CN326_19925 {ECO:0000313|EMBL:PEZ02559.1};
OS   Bacillus sp. AFS018417.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033491 {ECO:0000313|EMBL:PEZ02559.1, ECO:0000313|Proteomes:UP000220085};
RN   [1] {ECO:0000313|EMBL:PEZ02559.1, ECO:0000313|Proteomes:UP000220085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS018417 {ECO:0000313|EMBL:PEZ02559.1,
RC   ECO:0000313|Proteomes:UP000220085};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DCK/DGK family.
CC       {ECO:0000256|ARBA:ARBA00007420}.
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:PEZ02559.1}.
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DR   EMBL; NTTM01000054; PEZ02559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A8S6L7; -.
DR   OrthoDB; 9776634at2; -.
DR   Proteomes; UP000220085; 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:SF46; DEOXYGUANOSINE 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:PEZ02559.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220085};
KW   Transferase {ECO:0000313|EMBL:PEZ02559.1}.
FT   DOMAIN          7..204
FT                   /note="Deoxynucleoside kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01712"
FT   ACT_SITE        86
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT   BINDING         11..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT   BINDING         138..142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
SQ   SEQUENCE   212 AA;  24682 MW;  8CABC2E43D88DBA6 CRC64;
     MTGVPFITVE GPIGVGKTSL AKAISTHMQL HLLKEIVDEN PFLGKFYEDI QEWSFQTEMF
     FLCNRYKQLE DIDTKYLKQH IPVVADYHIF KNLIFASRTL QGSQYEKYMQ IYRILTQDMP
     VPNVIVYITA SLETLQKRIA MRGREFEKNM DPNYLLQLIE DYEAAMEAFK QDHPSIPVLK
     FNGDNMDFVK NESDLNVILS ALQNTLTKEI NQ
//