ID A0A0U3MK16_9LACT Unreviewed; 317 AA.
AC A0A0U3MK16;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Transcription regulator {ECO:0000313|EMBL:ALV20863.1};
GN ORFNames=NY10_242 {ECO:0000313|EMBL:ALV20863.1};
OS Carnobacterium sp. CP1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV20863.1, ECO:0000313|Proteomes:UP000064734};
RN [1] {ECO:0000313|EMBL:ALV20863.1, ECO:0000313|Proteomes:UP000064734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP1 {ECO:0000313|EMBL:ALV20863.1,
RC ECO:0000313|Proteomes:UP000064734};
RA Chen J., Yang J., Zhu S., Zhang D., Xiong S.;
RT "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from
RT Amanda bay, East Antarctic.";
RL Submitted (FEB-2015) 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; CP010796; ALV20863.1; -; Genomic_DNA.
DR RefSeq; WP_058918256.1; NZ_CP010796.1.
DR AlphaFoldDB; A0A0U3MK16; -.
DR STRING; 1564681.NY10_242; -.
DR KEGG; carc:NY10_242; -.
DR PATRIC; fig|1564681.3.peg.240; -.
DR OrthoDB; 9786026at2; -.
DR Proteomes; UP000064734; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000064734};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..141
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 317 AA; 35296 MW; BC88D6B76539DFEF CRC64;
MTNQKHFHII VNELAGSGNG KLICATLVKL LTEKKLTFQL HKTQYAGHAI QLTTELAKKI
VTTSEINAPL LMIVGGDGTL HEAVRGLGEE YKDMPLAYIP AGSGNDFAKG LGISKKTHEA
LSQILQATSP KKIDVLRYQE KILQQEGYAI NNIGIGFDAA TVKYTNQSSA KVRLNKYKLG
SVAYLASVTT VLFKQKGFPI EVIADGKQRF FPKAFLVTVN NHPYFGGGIG ISPKASPYDQ
QVDLIVLQKS SVFKIIWLFL LMLNGGRHLQ HKDVHSFQAR HIQIRSTQLE DTQADGEFLG
HRSVHFYFSA TTRYFWF
//
