ID A0A511ZC56_9BACL Unreviewed; 222 AA.
AC A0A511ZC56;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Deoxycytidine kinase {ECO:0000313|EMBL:GEN85028.1};
GN Name=dck {ECO:0000313|EMBL:GEN85028.1};
GN ORFNames=SLU01_33400 {ECO:0000313|EMBL:GEN85028.1};
OS Sporosarcina luteola.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=582850 {ECO:0000313|EMBL:GEN85028.1, ECO:0000313|Proteomes:UP000321901};
RN [1] {ECO:0000313|EMBL:GEN85028.1, ECO:0000313|Proteomes:UP000321901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105378 {ECO:0000313|EMBL:GEN85028.1,
RC ECO:0000313|Proteomes:UP000321901};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Sporosarcina luteola NBRC 105378.";
RL Submitted (JUL-2019) 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:GEN85028.1}.
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DR EMBL; BJYL01000056; GEN85028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A511ZC56; -.
DR OrthoDB; 9776634at2; -.
DR Proteomes; UP000321901; 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:GEN85028.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000321901};
KW Transferase {ECO:0000313|EMBL:GEN85028.1}.
FT DOMAIN 15..214
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; 26149 MW; 0F20892F4CE43659 CRC64;
MNLREKYGIP KNAVITIAGT VGAGKSTMTH ALANALDFRT SLENVDENPY LDRFYDDFEK
WSFHLQIYFL AERFKEQKRI FEYGGGFIQD RSIYEDTGIF AKMHKDKGTM DPVDYDTYTK
LFDAMVMTPY FPHPDLLVYL DGPFETILER IQERGREMEQ QTPLSYWEEL HHRYVQWIDS
FNACPVLRID ITDYDLMKDP HEVETIVERI GNMLNLSAML KK
//