ID T1JHM2_STRMM Unreviewed; 924 AA.
AC T1JHM2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Diacylglycerol kinase {ECO:0000256|RuleBase:RU361128};
DE Short=DAG kinase {ECO:0000256|RuleBase:RU361128};
DE EC=2.7.1.107 {ECO:0000256|RuleBase:RU361128};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR013353-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR013353-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:456216; EC=2.7.1.107;
CC Evidence={ECO:0000256|ARBA:ARBA00001383,
CC ECO:0000256|RuleBase:RU361128};
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR EMBL; JH429636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1JHM2; -.
DR STRING; 126957.T1JHM2; -.
DR EnsemblMetazoa; SMAR013353-RA; SMAR013353-PA; SMAR013353.
DR eggNOG; KOG0782; Eukaryota.
DR HOGENOM; CLU_003770_4_0_1; -.
DR OMA; NMIDNDK; -.
DR OrthoDB; 4642163at2759; -.
DR PhylomeDB; T1JHM2; -.
DR Proteomes; UP000014500; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd20802; C1_DGK_typeIV_rpt1; 1.
DR CDD; cd20855; C1_DGK_typeIV_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF114; EYE-SPECIFIC DIACYLGLYCEROL KINASE; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 249..383
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REPEAT 794..815
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..226
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 103521 MW; A310B9E220BB9C95 CRC64;
MQMATRGATS IGSKESNMRE TKFDEKKAIQ AEVLVATESG DQRSVRSAAI WNETAVNGDH
LWVSTSASGD FCYVNEVECS KQGPRLKCAA CKITAHTGCL SYVTEKFYCK PTFRDVGVRQ
YREHTIIHHH WVHRRNQKGK CKRCSKSFQS KLFSNKDIVA LSCSWCKAAY HNKESCFSMQ
TMEEQCTLGI HSNIIVPPSW IVKLPRKGSF KSSLRKSPKK RSSSKRKSKK EASDKEHQRF
FAIKPIPTPN AKPVIVFINP KSGGNQGSKL MQKFQWLLNP RQVFDLSQGG PQAGLELYKK
VPNLRILACG GDGTVGWILS VLDEIGFVPP PPVAVLPLGT GNDLARALGW GGGYTDEPVS
KILCNIEEGE TIQLDRWDLK VEKNSTNIDP SVCEDGKDNL PLSVINNYFS LGADAYIALE
FHEAREAHPE KFNSRLRNKM FYGQAGGKDL LQRKWKDLSE YVVLECDGKD ITPKLKELKV
HAILFLNIPS YGGGTHPWNS QNSGFEPQRT DDGLIEVIGL TTYQLPLLQA GGHGTCLAQC
KHARLVTTRT IPMQVDGEPC KLAPSVIELT HLNQVNMMAK AKQIGSRPNT QQPLERLRLQ
VSRITMSDYE NYHYDKERLR KASIPLGIIV VDQDTDLDHI RIHINRLQAD ISLSAHSNGW
SQKLSSDWCF LDSCTAERFF RIDRAQEHLH YVTDISCEEL YILDPDLLIS ERSSDALPSR
PAIDPEERIS EAASATLSKE NETIHRTEAQ SDDFLSSPQE KYSEDIIKAG RTGDLKLLKE
LHSMGFSLLS VDQFGMTSLH HAARHGFKDI VRYLIASAPP TILNMVDKDK QVFFILFTTA
LHTAAAYKRR TICCMLVAAG ASLTIVDNQC MTSRQQALKA EDKELAAYLE SKMLNNFLGL
DRNSDSAIMK VPKGQSLEGK YVHF
//
