ID Q65PK6_BACLD Unreviewed; 213 AA.
AC Q65PK6; Q62ZZ6;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Deoxyadenosine/deoxycytidine kinase {ECO:0000313|EMBL:AAU21662.1};
GN Name=dck {ECO:0000313|EMBL:AAU21662.1};
GN OrderedLocusNames=BL02366 {ECO:0000313|EMBL:AAU21662.1};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU21662.1, ECO:0000313|Proteomes:UP000000606};
RN [1] {ECO:0000313|EMBL:AAU21662.1, ECO:0000313|Proteomes:UP000000606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC {ECO:0000313|Proteomes:UP000000606};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
CC -!- SIMILARITY: Belongs to the DCK/DGK family.
CC {ECO:0000256|ARBA:ARBA00007420}.
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DR EMBL; CP000002; AAU21662.1; -; Genomic_DNA.
DR RefSeq; WP_009330052.1; NC_006322.1.
DR AlphaFoldDB; Q65PK6; -.
DR STRING; 279010.BL02366; -.
DR GeneID; 66213687; -.
DR KEGG; bli:BL02366; -.
DR PATRIC; fig|279010.13.peg.18; -.
DR eggNOG; COG1428; Bacteria.
DR HOGENOM; CLU_030466_2_1_9; -.
DR Proteomes; UP000000606; Chromosome.
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:SF15; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 10, MITOCHONDRIAL; 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:AAU21662.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000606};
KW Transferase {ECO:0000313|EMBL:AAU21662.1}.
FT DOMAIN 12..211
FT /note="Deoxynucleoside kinase"
FT /evidence="ECO:0000259|Pfam:PF01712"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 147..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
SQ SEQUENCE 213 AA; 24860 MW; 223548C045247AFA CRC64;
MSVYDIPKDA IITVAGTVGV GKSTLTKELA KRLGFKTSLE EVVNNPYLEA FYQDFERWSF
HLQIFFLAER FKEQKYIYES GGGFVQDRSI YEDTGIFAKM HADKGTMSKV DYKTYTSLFE
AMVMTPYFPR PDVLVYLEGD LETILDRIQK RGREMELLTD RSYWEEMYTR YENWISGFNA
CPVVRVNIDE YDLFNNSASL DPIIEKISEA IQR
//
