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Database: UniProt
Entry: Q1D3C4_MYXXD
LinkDB: Q1D3C4_MYXXD
Original site: Q1D3C4_MYXXD 
ID   Q1D3C4_MYXXD            Unreviewed;       308 AA.
AC   Q1D3C4;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   OrderedLocusNames=MXAN_4683 {ECO:0000313|EMBL:ABF88943.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF88943.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF88943.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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DR   EMBL; CP000113; ABF88943.1; -; Genomic_DNA.
DR   RefSeq; WP_011554674.1; NC_008095.1.
DR   AlphaFoldDB; Q1D3C4; -.
DR   STRING; 246197.MXAN_4683; -.
DR   EnsemblBacteria; ABF88943; ABF88943; MXAN_4683.
DR   GeneID; 41361982; -.
DR   KEGG; mxa:MXAN_4683; -.
DR   eggNOG; COG1597; Bacteria.
DR   HOGENOM; CLU_045532_0_0_7; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000002402; 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   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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..135
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   308 AA;  32983 MW;  1F6604C053BC9756 CRC64;
     MKTFLVVNPR SANGQTGKRW AEISAQVGRA LGDFGHGFTQ GGMDAARITR QALLDGYECI
     VAVGGDGTLN EVTNGFFEDG KALNPNAALG LIPRGTGGDF RRTFGWDLEL ASSLERLRSG
     TTEPFDVGQL EFIDNAGQPA TRYFANIASF GVSAVVAQEV NQSSKALGGH LSFVWGTLKG
     LVKYSERQVR LSVDGGPEEV VSVTAVAVAN GRYFGSGMFV APDAVTHDGL FDVTIWSNYS
     LSDFVLKSKG VYNGSHVNWK GTRRLRCRTL RAEPVDGGDV FLDVDGETPG RLPCTMTLLP
     GAIRLKVL
//
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