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Database: UniProt
Entry: A0A143BM13_9BACT
LinkDB: A0A143BM13_9BACT
Original site: A0A143BM13_9BACT 
ID   A0A143BM13_9BACT        Unreviewed;       291 AA.
AC   A0A143BM13;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=GEMMAAP_13490 {ECO:0000313|EMBL:AMW05550.1};
OS   Gemmatimonas phototrophica.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1379270 {ECO:0000313|EMBL:AMW05550.1, ECO:0000313|Proteomes:UP000076404};
RN   [1] {ECO:0000313|EMBL:AMW05550.1, ECO:0000313|Proteomes:UP000076404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP64 {ECO:0000313|EMBL:AMW05550.1,
RC   ECO:0000313|Proteomes:UP000076404};
RX   PubMed=24821787; DOI=10.1073/pnas.1400295111;
RA   Zeng Y., Feng F., Medova H., Dean J., Koblizek M.;
RT   "Functional type 2 photosynthetic reaction centers found in the rare
RT   bacterial phylum Gemmatimonadetes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:7795-7800(2014).
RN   [2] {ECO:0000313|EMBL:AMW05550.1, ECO:0000313|Proteomes:UP000076404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP64 {ECO:0000313|EMBL:AMW05550.1,
RC   ECO:0000313|Proteomes:UP000076404};
RX   PubMed=26636755; DOI=10.1111/1758-2229.12363;
RA   Zeng Y., Baumbach J., Barbosa E.G., Azevedo V., Zhang C., Koblizek M.;
RT   "Metagenomic evidence for the presence of phototrophic Gemmatimonadetes
RT   bacteria in diverse environments.";
RL   Environ. Microbiol. Rep. 8:139-149(2016).
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DR   EMBL; CP011454; AMW05550.1; -; Genomic_DNA.
DR   RefSeq; WP_026848755.1; NZ_CP011454.1.
DR   AlphaFoldDB; A0A143BM13; -.
DR   STRING; 1379270.GEMMAAP_13490; -.
DR   GeneID; 78445138; -.
DR   KEGG; gph:GEMMAAP_13490; -.
DR   eggNOG; COG1597; Bacteria.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000076404; Chromosome.
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   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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076404};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..129
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   291 AA;  30525 MW;  675A0488E1391EBA CRC64;
     MIALLVNPVA GRGDARRRAE AVEAALRTTG ALQRYETQSR GDERRCAREA CAAGATVLAV
     VGGDGSVHHA ARGLLDVGAP IPLAIFAAGT GNDFVKSLQT PAHDAVAMAA AVARGQTQAV
     DVGVIDSVPF LNAAGLGFDV EVLERMQHPL WFTGTAAYVV TAVRALFGYT GFTVQHPDTS
     PPASDHRLMT VFANGRVFGG TFQIAPTASL TDGRLDVVNI ASLAPLARPA VFWRATRGTH
     LQHPAVHHSQ TVATTITSPT PLPFEADGEL YRASNTTIQI AVRPAALRVI V
//
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