ID A0A1I3YA32_9BACL Unreviewed; 299 AA.
AC A0A1I3YA32;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Lipid kinase, YegS/Rv2252/BmrU family {ECO:0000313|EMBL:SFK28724.1};
GN ORFNames=SAMN05518846_11134 {ECO:0000313|EMBL:SFK28724.1};
OS Brevibacillus centrosporus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54910 {ECO:0000313|EMBL:SFK28724.1, ECO:0000313|Proteomes:UP000198915};
RN [1] {ECO:0000313|Proteomes:UP000198915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK042 {ECO:0000313|Proteomes:UP000198915};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC {ECO:0000256|ARBA:ARBA00005983}.
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DR EMBL; FORT01000011; SFK28724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3YA32; -.
DR STRING; 1884381.SAMN05518846_11134; -.
DR Proteomes; UP000198915; Unassembled WGS sequence.
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:SF54; SPHINGOID LONG-CHAIN BASES KINASE 2, MITOCHONDRIAL; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFK28724.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000198915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..131
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 299 AA; 32443 MW; 6C585B563DC1B25F CRC64;
MIGFVVNPAA GNGKGEKVWN SLESILRQQG VVYRVRRTSS EGEAETLAIE LIEKEEVKMI
VAVGGDGTVS EVVNGIYEAG KECTLGHVPA GSGNDFARGH GLPKDPAQAI ERILSKTREK
CIDLLKINGR VAVNSVGAGF DGQVAKTTNE AGYKKWLNRL RLGKLAYIWS VIRVLCTYCP
CDVTLLIDGQ VHQMKRIWLI AIANIPNYGG GMLICPQALP DDGVAEICVV QNVTRLGLLF
AFPRIFTGAH VDHPNVVFLR GRQITIESEQ PLLVHADGEM AAQTPIYVEI EAGKLRICG
//