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Database: UniProt
Entry: A0A0Q8Q6F6_9ACTN
LinkDB: A0A0Q8Q6F6_9ACTN
Original site: A0A0Q8Q6F6_9ACTN 
ID   A0A0Q8Q6F6_9ACTN        Unreviewed;       308 AA.
AC   A0A0Q8Q6F6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Diacylglycerol kinase {ECO:0000313|EMBL:KRB78360.1};
GN   ORFNames=ASE01_03535 {ECO:0000313|EMBL:KRB78360.1};
OS   Nocardioides sp. Root190.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB78360.1, ECO:0000313|Proteomes:UP000050886};
RN   [1] {ECO:0000313|EMBL:KRB78360.1, ECO:0000313|Proteomes:UP000050886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root190 {ECO:0000313|EMBL:KRB78360.1,
RC   ECO:0000313|Proteomes:UP000050886};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB78360.1, ECO:0000313|Proteomes:UP000050886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root190 {ECO:0000313|EMBL:KRB78360.1,
RC   ECO:0000313|Proteomes:UP000050886};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRB78360.1}.
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DR   EMBL; LMIA01000007; KRB78360.1; -; Genomic_DNA.
DR   RefSeq; WP_056748907.1; NZ_LMIA01000007.1.
DR   AlphaFoldDB; A0A0Q8Q6F6; -.
DR   STRING; 1736488.ASE01_03535; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000050886; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRB78360.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050886};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..132
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   308 AA;  31221 MW;  5E4F183ABB6C8932 CRC64;
     MTAPSGRRFA FLVNPNSGGG AATKVVVPLA RALREAGAAV DVSYTTSPAE TPDLVATAVA
     AGAVVVSVGG DGMLSSVAGA VSERDGVLAV IPAGRGNDFA RMLEIPHDTA GQAALLLAGE
     ERRIDLLCAT RGDATTSVVA GSVYAGVDAR AAEIVDRSHW LPSRLQYPVA AVRALATYRP
     VHCVLEVDGV RSEHQAATVV VANSRYYGKG MAIAPDASVS DGLLDVIVIE AAGRLDLIRA
     LPKVYDGQHV ALDEVKVLTG HRVTLSGTYR GGGAVPVGAD GEALGALPGD PAAPLVVALV
     AGAVRILA
//
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