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Database: UniProt
Entry: C1AUR0_RHOOB
LinkDB: C1AUR0_RHOOB
Original site: C1AUR0_RHOOB 
ID   C1AUR0_RHOOB            Unreviewed;       304 AA.
AC   C1AUR0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   OrderedLocusNames=ROP_51530 {ECO:0000313|EMBL:BAH53400.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH53400.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH53400.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH53400.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; AP011115; BAH53400.1; -; Genomic_DNA.
DR   RefSeq; WP_015888906.1; NC_012522.1.
DR   AlphaFoldDB; C1AUR0; -.
DR   STRING; 632772.ROP_51530; -.
DR   KEGG; rop:ROP_51530; -.
DR   PATRIC; fig|632772.20.peg.5380; -.
DR   HOGENOM; CLU_045532_0_1_11; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
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; IPR005218; Diacylglycerol/lipid_kinase.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR045540; YegS/DAGK_C.
DR   NCBIfam; TIGR00147; YegS/Rv2252/BmrU family lipid kinase; 1.
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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..136
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   304 AA;  32072 MW;  B2E8D6F41FEFD5B1 CRC64;
     MSTQQVIEKV TVLVNPLAGH GHAPVAGRKG VARLRERGVA VTEIIGTDAD HARSLARRAI
     DDGTDALVVV GGDGAISIGL QAAALSGTPV GLIPAGTGND HAREFGIPVG DPVAAADVIA
     DGEVQESDLA RITLGDPAVV WAGTIVASGF DSLVTDRANR MSWPKGPMRY NLAMLAELTQ
     LKPLHYRIEL DDQAFEVDAT LVAVGNGRSY GGGMQICPNA DKTDGLLDVT VVDYGRRSRL
     VRLFPRVYKG THVDLPDVQT YRSRTVRLHC EGITAYADGD RVGPLPVTIE AVPAALRILS
     HTPA
//
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