ID   A0A1M3F8G4_9CELL        Unreviewed;       373 AA.
AC   A0A1M3F8G4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Diacylglycerol kinase {ECO:0000313|EMBL:OJV80849.1};
GN   ORFNames=BGO37_15040 {ECO:0000313|EMBL:OJV80849.1};
OS   Cellulomonas sp. 73-92.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1895740 {ECO:0000313|EMBL:OJV80849.1, ECO:0000313|Proteomes:UP000184539};
RN   [1] {ECO:0000313|EMBL:OJV80849.1, ECO:0000313|Proteomes:UP000184539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-92 {ECO:0000313|EMBL:OJV80849.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJV80849.1}.
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DR   EMBL; MKTH01000013; OJV80849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3F8G4; -.
DR   STRING; 1895740.BGO37_15040; -.
DR   Proteomes; UP000184539; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR045540; YegS/DAGK_C.
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   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:OJV80849.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          53..183
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   373 AA;  39220 MW;  6BCD371FF3E453CD CRC64;
     MTWQAWVAVG AAVLAAVGIG IGIWVARRQR QLRTRLDIAG VPVVEEQPPG SGGPDTLVAV
     VVNPTKPGTP ALRELVTTTI AGRGWPEPLW LETTPDDPGV GQARQALEAG AHLVIAAGGD
     GTVRAVAEAL AHSAVPMGLL PQGTGNLLAR NLDLPIGNGP SALAIALDGL NRTIDVGRLT
     VDRWADAEPP EGAHDENVFL VIGGVGVDAA MVADADEQLK ARVGWIAYFV AAVRHLHGRR
     LRVKVKVDDR DWIEVRGRSL LVGNVGRLPG GITLLPDARI DDGWLDLAAL DARGGVAGWA
     QLLGEVMLQR IGVRNDLPAK IGRIDHVRAR QVTVQIVGGE QVQVDGESVG RAKQLSARVD
     PGALVVRVAP PRT
//