ID F0RD81_CELLC Unreviewed; 206 AA.
AC F0RD81;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Deoxyadenosine kinase {ECO:0000313|EMBL:ADY29782.1};
DE EC=2.7.1.76 {ECO:0000313|EMBL:ADY29782.1};
GN OrderedLocusNames=Celly_1960 {ECO:0000313|EMBL:ADY29782.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY29782.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY29782.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
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DR EMBL; CP002534; ADY29782.1; -; Genomic_DNA.
DR RefSeq; WP_013621527.1; NC_015167.1.
DR AlphaFoldDB; F0RD81; -.
DR STRING; 867900.Celly_1960; -.
DR KEGG; cly:Celly_1960; -.
DR eggNOG; COG1428; Bacteria.
DR HOGENOM; CLU_030466_2_1_10; -.
DR OrthoDB; 9776634at2; -.
DR Proteomes; UP000007487; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004136; F:deoxyadenosine kinase activity; IEA:UniProtKB-EC.
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:SF49; DEOXYADENOSINE 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 4: Predicted;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Kinase {ECO:0000313|EMBL:ADY29782.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000007487};
KW Transferase {ECO:0000313|EMBL:ADY29782.1}.
FT DOMAIN 3..199
FT /note="Deoxynucleoside kinase"
FT /evidence="ECO:0000259|Pfam:PF01712"
FT ACT_SITE 78
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT BINDING 7..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 180..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
SQ SEQUENCE 206 AA; 24182 MW; 5B646FEEFE84FB3F CRC64;
MHIAVAGNIG AGKTTLTRLL AKHFNWQPNF EDVVDNPYLD DFYNQMERWS FNLQIYFLNS
RFRQILQIRE SGKDIIQDRT IYEDAFIFAP NLHAMGLLTN RDFENYTSLF ELMESLVQPP
DLLIYLRSSI PNLVNQIHKR GREYENTISI DYLSRLNERY EAWIHGYDKG NLLIIDVDNL
NFVDDPEDLG FVINKIDAEI NGLFQP
//
