ID H0A0I8_9PROT Unreviewed; 310 AA.
AC H0A0I8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative lipid kinase {ECO:0000313|EMBL:EHM01010.1};
GN ORFNames=HMPREF9946_02327 {ECO:0000313|EMBL:EHM01010.1};
OS Acetobacteraceae bacterium AT-5844.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHM01010.1, ECO:0000313|Proteomes:UP000003292};
RN [1] {ECO:0000313|EMBL:EHM01010.1, ECO:0000313|Proteomes:UP000003292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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:EHM01010.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGEZ01000072; EHM01010.1; -; Genomic_DNA.
DR AlphaFoldDB; H0A0I8; -.
DR STRING; 1054213.HMPREF9946_02327; -.
DR PATRIC; fig|1054213.3.peg.2144; -.
DR eggNOG; COG1597; Bacteria.
DR HOGENOM; CLU_045532_5_1_5; -.
DR OrthoDB; 142078at2; -.
DR BioCyc; ABAC1054213:G1H32-2157-MONOMER; -.
DR Proteomes; UP000003292; 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: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, ECO:0000313|EMBL:EHM01010.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003292};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..137
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 310 AA; 33456 MW; 84B1ACBF70D7FE94 CRC64;
MQPSATRLCV IINKGGGSVG GRNPCAALEA IFARHGLQAD IHLCSGDELE DTARHALART
GPGKDYDGIL AGGGDGTINA VAGVLAHTGL PLGVLPLGTL NHFAKDLGLP LDLDGAVGVI
AAGHTRRVDV GEVNGQVFVN NSSLGLYATM VAERDRQRRR AGRGKWPAMV WACLRTALRF
PLRHLTVSAE GWTRRYKTPL IFIGNNAYEV SLPRPGTRAV LDDGRLCLFI ARPRRLLGLL
RVAVRAMFGR LKEERDFESY LISEVRITAH SAWLRVSVDG EVTPMRPPLR YRIHPGALVV
YAPPKAGSAL
//
