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Database: UniProt
Entry: A0A0A3ITV0_9BACI
LinkDB: A0A0A3ITV0_9BACI
Original site: A0A0A3ITV0_9BACI 
ID   A0A0A3ITV0_9BACI        Unreviewed;       222 AA.
AC   A0A0A3ITV0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Deoxycytidine kinase {ECO:0000313|EMBL:KGR88194.1};
GN   ORFNames=CD32_02105 {ECO:0000313|EMBL:KGR88194.1};
OS   Lysinibacillus odysseyi 34hs-1 = NBRC 100172.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1220589 {ECO:0000313|EMBL:KGR88194.1, ECO:0000313|Proteomes:UP000030437};
RN   [1] {ECO:0000313|EMBL:KGR88194.1, ECO:0000313|Proteomes:UP000030437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100172 {ECO:0000313|EMBL:KGR88194.1,
RC   ECO:0000313|Proteomes:UP000030437};
RA   Zhang F., Wang G., Zhang L.;
RT   "Draft genome sequence of Lysinibacillus odysseyi NBRC 100172.";
RL   Submitted (FEB-2014) 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:KGR88194.1}.
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DR   EMBL; JPVP01000042; KGR88194.1; -; Genomic_DNA.
DR   RefSeq; WP_036150705.1; NZ_JPVP01000042.1.
DR   AlphaFoldDB; A0A0A3ITV0; -.
DR   STRING; 1220589.CD32_02105; -.
DR   eggNOG; COG1428; Bacteria.
DR   OrthoDB; 9776634at2; -.
DR   Proteomes; UP000030437; 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:KGR88194.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030437};
KW   Transferase {ECO:0000313|EMBL:KGR88194.1}.
FT   DOMAIN          15..211
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;  26134 MW;  4A9A21DE8A0F78FF CRC64;
     MNLRDKYGIP ANAVITIAGT VGVGKSTMTK ALAEGLNFRT SFEKVDTNPY LDKFYDDFEK
     WSFHLQVYFL AERFKEQKRI FEYGGGFIQD RSIYEDTGIF AKMHYDKGTM SPTDYETYTN
     LFDAMVMTPY FPHPDLLVYL EGPIDHIIAR IQERGRAMEQ QTSNDYWYEM HERYENWINS
     FNSCPVLRLD INDYDLVKQP SQIEGIIERI GYMLEQTSHL RK
//
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