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Database: UniProt
Entry: A6EKB7_9SPHI
LinkDB: A6EKB7_9SPHI
Original site: A6EKB7_9SPHI 
ID   A6EKB7_9SPHI            Unreviewed;       296 AA.
AC   A6EKB7;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=PBAL39_05798 {ECO:0000313|EMBL:EDM34098.1};
OS   Pedobacter sp. BAL39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=391596 {ECO:0000313|EMBL:EDM34098.1, ECO:0000313|Proteomes:UP000003664};
RN   [1] {ECO:0000313|EMBL:EDM34098.1, ECO:0000313|Proteomes:UP000003664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL39 {ECO:0000313|EMBL:EDM34098.1,
RC   ECO:0000313|Proteomes:UP000003664};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:EDM34098.1}.
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DR   EMBL; ABCM01000030; EDM34098.1; -; Genomic_DNA.
DR   RefSeq; WP_008246402.1; NZ_ABCM01000030.1.
DR   AlphaFoldDB; A6EKB7; -.
DR   STRING; 391596.PBAL39_05798; -.
DR   eggNOG; COG1597; Bacteria.
DR   OrthoDB; 9786026at2; -.
DR   Proteomes; UP000003664; 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   4: Predicted;
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:UP000003664};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..131
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   296 AA;  32374 MW;  C997AFD3A62DA9CD CRC64;
     MSKSNILFII NPISGGKDKL KIPALIDAHL DRSKFNANYS FTEYVGHASE IAEEAASKNF
     DIIVAVGGDG TINEIASKVM QQHKILGVLP FGSGNGLSRF LKIPMNTAKA IRVINDLNVS
     VIDTATFNQK SFFNMAGMGF DAHISAVFAG NKSRGLSGYV KLGMKEMLNY KAQEYRIEID
     GKEYLRTAFV VSIANSSQYG NNAHIAPKAS ITDGLLDVCI IKSFPLYKIT LLAYHMLRGS
     TDQSSLVEII RGKDIRISRV ADDAIHIDGE PYFMGKEIEV SIVPLSLNII TPAYES
//
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