ID A0A147K3S8_9BACI Unreviewed; 222 AA.
AC A0A147K3S8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Deoxycytidine kinase {ECO:0000313|EMBL:KUP03900.1};
GN ORFNames=Q75_17320 {ECO:0000313|EMBL:KUP03900.1};
OS Bacillus coahuilensis p1.1.43.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP03900.1, ECO:0000313|Proteomes:UP000074108};
RN [1] {ECO:0000313|EMBL:KUP03900.1, ECO:0000313|Proteomes:UP000074108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA Olmedo-Alvarez G.;
RT "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT Phosphorus Acquisition Strategies and Their Regulation.";
RL Front. Microbiol. 7:58-58(2016).
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:KUP03900.1}.
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DR EMBL; LDYG01000059; KUP03900.1; -; Genomic_DNA.
DR RefSeq; WP_010169465.1; NZ_LDYG01000059.1.
DR AlphaFoldDB; A0A147K3S8; -.
DR STRING; 1150625.Q75_17320; -.
DR PATRIC; fig|1150625.3.peg.3639; -.
DR OrthoDB; 9776634at2; -.
DR Proteomes; UP000074108; 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: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:KUP03900.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000074108};
KW Transferase {ECO:0000313|EMBL:KUP03900.1}.
FT DOMAIN 15..212
FT /note="Deoxynucleoside kinase"
FT /evidence="ECO:0000259|Pfam:PF01712"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 150..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
SQ SEQUENCE 222 AA; 26143 MW; 501BA11AA8C6CCC6 CRC64;
MMLREKYAIP QNAVITIAGT VGVGKSTMTN GLADALGFRT SFEKVDSNPY LDKFYKDFQK
WSFHLQIYFL AERFKEQKRI FEYGGGFIQD RSIYEDTGIF ARMHHEKGNM SDVDYETYTS
LFDAMVMTPY FPHPDLLIYL EGSIDDIIDR IKVRGRPMEQ ETPLAYWEEM HYRYEKWINS
FNACPVLRLN IKEYDLVQDS GSIEPIIERI GYMIDQTRLL KK
//