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Database: UniProt
Entry: A0A1Q9JF30_9FIRM
LinkDB: A0A1Q9JF30_9FIRM
Original site: A0A1Q9JF30_9FIRM 
ID   A0A1Q9JF30_9FIRM        Unreviewed;       314 AA.
AC   A0A1Q9JF30;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=BHK98_01060 {ECO:0000313|EMBL:OLR54793.1};
OS   Hornefia porci.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis; Hornefia.
OX   NCBI_TaxID=2652292 {ECO:0000313|EMBL:OLR54793.1, ECO:0000313|Proteomes:UP000187404};
RN   [1] {ECO:0000313|EMBL:OLR54793.1, ECO:0000313|Proteomes:UP000187404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=68-3-10 {ECO:0000313|EMBL:OLR54793.1,
RC   ECO:0000313|Proteomes:UP000187404};
RX   PubMed=27613689;
RA   Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT   "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT   Transferases and Their Diversity in the Proximal Colon of Swine.";
RL   Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR54793.1}.
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DR   EMBL; MJIE01000001; OLR54793.1; -; Genomic_DNA.
DR   RefSeq; WP_075711812.1; NZ_MJIE01000001.1.
DR   AlphaFoldDB; A0A1Q9JF30; -.
DR   STRING; 1261640.BHK98_01060; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000187404; 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:SF106; LIPID KINASE YEGS; 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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187404};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..130
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   314 AA;  33991 MW;  1EA959607E71D28C CRC64;
     MKRALVIINP CAGTRQANRH FVQITDILCK AGYETVVATT AGRGDGTEIA RTRSRKFDLV
     VCIGGDGTFN EVVAGVLESG SKVPIGYIPA GSTNDFGASL GLSKNIIQAT KDIVMGVPVT
     LDIGSFNDRY FSYVASFGAF TATSYSVPQD LKNTLGHLAY ILEGIRDIPS IKPLKLRVRN
     EVGVYGGEYI FGAVCNSTSM GGIITLDKKL VDMNDGLFEV LLIRSPRNIF ELTQITMALT
     QGKYKECPMM SFFSSGNLHI EADPDMPWTL DGEYQPGSEE ISIRNNKSAI RIMVGRDNAA
     AQDVLRIAGN KGKL
//
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