ID   A0A0Q0YK77_9CORY        Unreviewed;       309 AA.
AC   A0A0Q0YK77;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Diacylglycerol kinase {ECO:0000313|EMBL:KQB87248.1};
DE            EC=2.7.1.107 {ECO:0000313|EMBL:KQB87248.1};
GN   Name=dagK_1 {ECO:0000313|EMBL:KQB87248.1};
GN   ORFNames=Clow_00303 {ECO:0000313|EMBL:KQB87248.1};
OS   Corynebacterium lowii.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB87248.1, ECO:0000313|Proteomes:UP000050488};
RN   [1] {ECO:0000313|EMBL:KQB87248.1, ECO:0000313|Proteomes:UP000050488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML 130206 {ECO:0000313|EMBL:KQB87248.1,
RC   ECO:0000313|Proteomes:UP000050488};
RA   Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S.,
RA   Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H.,
RA   Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.;
RT   "Corynebacteirum lowii and Corynebacterium oculi species nova, derived from
RT   human clinical disease and and emended description of Corynebacterium
RT   mastiditis.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KQB87248.1}.
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DR   EMBL; LKEV01000001; KQB87248.1; -; Genomic_DNA.
DR   RefSeq; WP_055175267.1; NZ_LKEV01000001.1.
DR   AlphaFoldDB; A0A0Q0YK77; -.
DR   STRING; 1544413.Clow_00303; -.
DR   PATRIC; fig|1544413.3.peg.306; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000050488; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:KQB87248.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050488};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQB87248.1}.
FT   DOMAIN          10..141
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   309 AA;  33586 MW;  D43B9BA3BCD09E0D CRC64;
     MSDTYHMPKR DISRIALLTN PAAGKGKAVA ASEAAARAFY KYGVDVVRIS GSSPEASRNL
     AREMVQDDSI DALVACGGDG LISLALQEQA GSDTPLGIIP AGTGNDHARE YNIPRDTRRA
     VKTIVEGYTT RTDLGIMRTD DGQERYFGTI ACAGFDSLVT DRTNKIPWPS GQPRYMLAIL
     IEFANFHSIP TRITLDDGQP IEEEVTLCAI GNTKTYGGGM QVCPDADHYD GLFDITVLSK
     ISRSKAVLNV GKVFSGDFED VKEAKKYRAR KVRVEMPGIN SYADGDKYFP CPIECEIAPG
     AGYYIVPRP
//