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Database: UniProt
Entry: A4IK27_GEOTN
LinkDB: A4IK27_GEOTN
Original site: A4IK27_GEOTN 
ID   A4IK27_GEOTN            Unreviewed;       306 AA.
AC   A4IK27;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   OrderedLocusNames=GTNG_0297 {ECO:0000313|EMBL:ABO65681.1};
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO65681.1, ECO:0000313|Proteomes:UP000001578};
RN   [1] {ECO:0000313|EMBL:ABO65681.1, ECO:0000313|Proteomes:UP000001578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2 {ECO:0000313|EMBL:ABO65681.1,
RC   ECO:0000313|Proteomes:UP000001578};
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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}.
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DR   EMBL; CP000557; ABO65681.1; -; Genomic_DNA.
DR   RefSeq; WP_008881410.1; NC_009328.1.
DR   AlphaFoldDB; A4IK27; -.
DR   KEGG; gtn:GTNG_0297; -.
DR   eggNOG; COG1597; Bacteria.
DR   HOGENOM; CLU_045532_1_0_9; -.
DR   Proteomes; UP000001578; Chromosome.
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:SF115; DIACYLGLYCEROL KINASE; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..131
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   306 AA;  33464 MW;  38F4E1CE15A5B756 CRC64;
     MKRARVIYNP TSGRELFKRH LPDVLVRLEK AGYETSCHAT EGPGDATKAA RQAAEREFDL
     VVAAGGDGTI NEVVNGIANQ PYRPKLGVIP VGTTNDFARA IGVPRSIEGA CEVIATGEPV
     AIDIGSVTNE DQTRYFINIA GGGRLTELTY EVPSKLKTML GQLAYYLKGI EMLPSIKATE
     AQIEYDGKLF EGEIMMFLVS LTNSVGGFEK LAPDSSLNDG LFDFIIVKKT NLAEFIRLVT
     LAARGEHIND PHVIYTKANR VKVRSSMQLN LDGEFGGMLP GEFVNLYRHL EVFMPKEKAA
     QVRTGP
//
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