ID E3HDU0_ILYPC Unreviewed; 294 AA.
AC E3HDU0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Diacylglycerol kinase catalytic region {ECO:0000313|EMBL:ADO84276.1};
GN OrderedLocusNames=Ilyop_2517 {ECO:0000313|EMBL:ADO84276.1};
OS Ilyobacter polytropus (strain ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1).
OG Plasmid pILYOP01 {ECO:0000313|EMBL:ADO84276.1,
OG ECO:0000313|Proteomes:UP000006875}.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Ilyobacter.
OX NCBI_TaxID=572544 {ECO:0000313|EMBL:ADO84276.1, ECO:0000313|Proteomes:UP000006875};
RN [1] {ECO:0000313|EMBL:ADO84276.1, ECO:0000313|Proteomes:UP000006875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1
RC {ECO:0000313|Proteomes:UP000006875};
RC PLASMID=pILYOP01 {ECO:0000313|Proteomes:UP000006875};
RX PubMed=21304735; DOI=10.4056/sigs.1273360;
RA Sikorski J., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Yasawong M.,
RA Rohde M., Pukall R., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ilyobacter polytropus type strain (CuHbu1).";
RL Stand. Genomic Sci. 3:304-314(2010).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CP002282; ADO84276.1; -; Genomic_DNA.
DR RefSeq; WP_013388935.1; NC_014633.1.
DR AlphaFoldDB; E3HDU0; -.
DR KEGG; ipo:Ilyop_2517; -.
DR HOGENOM; CLU_045532_1_0_0; -.
DR OrthoDB; 142078at2; -.
DR Proteomes; UP000006875; Plasmid pILYOP01.
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, ECO:0000313|EMBL:ADO84276.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plasmid {ECO:0000313|EMBL:ADO84276.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006875};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..130
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 294 AA; 32745 MW; 84F5CD960C3890FB CRC64;
MKRARLIYNP YSGENYIVKH LDTIFKVYQK KGYTIDAFRI SYEANIEDAF KDIGGEYNHI
IIAGGDGTVN QIINIMKKTG IDLPVAILPT GTANDFATCL GMPKDISEAC QQILSSNVKL
IDLGKVNDTY FVNVASTGLF TDVSQKTNVN LKNTMGKLAY YFSGIIEIPN FKRLQITVES
KELKYTGHSL IIFAFNGKSA GNIDIAYKSQ LDDGLLDIVI VKAEIMTETL LSFFKFLKKE
HLENPKGVIH FKTNRLSLKC NESISTDLDG EKGPDFPLDI QCIKNGLKIL GYAN
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