ID Q9RU35_DEIRA Unreviewed; 318 AA.
AC Q9RU35;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN OrderedLocusNames=DR_1560 {ECO:0000313|EMBL:AAF11121.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF11121.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF11121.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; AE000513; AAF11121.1; -; Genomic_DNA.
DR PIR; B75382; B75382.
DR RefSeq; NP_295283.1; NC_001263.1.
DR AlphaFoldDB; Q9RU35; -.
DR STRING; 243230.DR_1560; -.
DR PaxDb; 243230-DR_1560; -.
DR EnsemblBacteria; AAF11121; AAF11121; DR_1560.
DR KEGG; dra:DR_1560; -.
DR PATRIC; fig|243230.17.peg.1761; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_0_1_0; -.
DR InParanoid; Q9RU35; -.
DR OrthoDB; 9786026at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR PANTHER; PTHR12358:SF106; LIPID KINASE YEGS; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002524};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..146
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 318 AA; 33135 MW; 455DC6193E4DE6DF CRC64;
MPFSALLYAG WTVTTASSAL PFAVVLNAQA GRGLAGREWP RLRGELEARG IAYQLVAAQS
GAGALAEVQA LPPGQPVLAA GGDGTVGALL PALVGTGRPL ALVPLGSGND FAGMLGLKPG
QFAGALGRLS EPPRQVDALE AEVVRGDHAG LKKPLLNGLG TGFDAQVTHA YLRAPRQLPG
FWRYAWGAAA SLGRLPLAEL TLRVDGETLY QGQSALAAVM NGTRYGGGFR ISPASAARDG
LLNAVCSGPL SRLQLIELMA RVLPGRHLGH PRVHHGTGRV MELHWSQPMF LHLDGDLYGQ
AEQVRARVLP GAVTLLNG
//
