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Database: UniProt
Entry: A0A0A0DJG2_9STRE
LinkDB: A0A0A0DJG2_9STRE
Original site: A0A0A0DJG2_9STRE 
ID   A0A0A0DJG2_9STRE        Unreviewed;       316 AA.
AC   A0A0A0DJG2;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Transcription regulator, contains diacylglycerol kinase catalytic domain {ECO:0000313|EMBL:KGM37998.1};
GN   ORFNames=SSIN_0208 {ECO:0000313|EMBL:KGM37998.1};
OS   Streptococcus sinensis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=176090 {ECO:0000313|EMBL:KGM37998.1, ECO:0000313|Proteomes:UP000030019};
RN   [1] {ECO:0000313|EMBL:KGM37998.1, ECO:0000313|Proteomes:UP000030019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKU4 {ECO:0000313|EMBL:KGM37998.1,
RC   ECO:0000313|Proteomes:UP000030019};
RA   Teng J.L., Huang Y., Tse H., Lau S.K., Woo P.C.;
RL   Submitted (JUN-2014) 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}.
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:KGM37998.1}.
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DR   EMBL; JPEN01000022; KGM37998.1; -; Genomic_DNA.
DR   RefSeq; WP_037614736.1; NZ_JPEN01000022.1.
DR   AlphaFoldDB; A0A0A0DJG2; -.
DR   STRING; 176090.SSIN_0208; -.
DR   PATRIC; fig|176090.4.peg.208; -.
DR   eggNOG; COG1597; Bacteria.
DR   Proteomes; UP000030019; 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:SF115; DIACYLGLYCEROL KINASE; 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:KGM37998.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..138
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   316 AA;  34557 MW;  1AA900BB8EEC2EBD CRC64;
     MKNKIKKARL IYNPTSGQEI IKKNIAEVLD VLEDVGYETS AYQTTPEPFS AQREAERAAK
     AGFDLVIAAG GDGTINEVVN GVASLDVRPK LAFIPTGTTN DYARALKIPM GDPVAAARII
     EKNQTIQMDI GRAYGSKYFI NIAAAGTLTE LTYSVPSEVK SRLGYLAYVA EGAKMLPRSK
     SRKVRIEHDH GVFEGKVSLV FVALTNSIGG FEKLAPDTKF DDGNFTLIVV KTAKLFDMLS
     LIIQAINGGQ HVTDAKVEYL KTSKLKLEVL DKKAPFMLNL DGEYGGDTPV ELEVLHNHLE
     FFANIDEIDE NALSIE
//
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