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Database: UniProt
Entry: D9ZDR7_9ZZZZ
LinkDB: D9ZDR7_9ZZZZ
Original site: D9ZDR7_9ZZZZ 
ID   D9ZDR7_9ZZZZ            Unreviewed;       330 AA.
AC   D9ZDR7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
OS   uncultured organism.
OC   unclassified sequences; environmental samples.
OX   NCBI_TaxID=155900 {ECO:0000313|EMBL:ADD61471.1};
RN   [1] {ECO:0000313|EMBL:ADD61471.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20841432; DOI=10.1101/gr.108332.110;
RA   Tasse L., Bercovici J., Pizzut-Serin S., Robe P., Tap J., Klopp C.,
RA   Cantarel B.L., Coutinho P.M., Henrissat B., Leclerc M., Dore J., Monsan P.,
RA   Remaud-Simeon M., Potocki-Veronese G.;
RT   "Functional metagenomics to mine the human gut microbiome for dietary fiber
RT   catabolic enzymes.";
RL   Genome Res. 20:1605-1612(2010).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; GU942931; ADD61471.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9ZDR7; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        192..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..160
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   330 AA;  37589 MW;  5448E68CE2A12027 CRC64;
     MTATPLKRQI YKNVGPIERN GYMSVEPDKW GVIYNPKAGT RKVQKRWKEI KAYMDSKGVS
     YDYVQSEGFG SVERLAGILA NNGYRTIVVV GGDGALNDAI NGIMLSNAED KENIAIGIIP
     NGIGNDFAKY WEMSSEYKEA VDCIINNRRR KIDVGTCYYY DGQKHMTRYF LNAINIGLGA
     RIVKITDQCK RFWGVKFLSY FMAFISLIFE RKLYRMHLKI NGEHIRGRIM TVCIGSAWGY
     GQAPSAVPYN GWLDVSVIYR PELLQLFSGI WMLMEGRILN HKVVKPYRTQ KIKVLRAQNA
     SVDLDGRILD RHFPLDIGVL HEAITLIIPN
//
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