ID A0A2Y9DY90_TRIMA Unreviewed; 911 AA.
AC A0A2Y9DY90;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
GN Name=LOC101343024 {ECO:0000313|RefSeq:XP_004383634.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004383634.1};
RN [1] {ECO:0000313|RefSeq:XP_004383634.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00023371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000256|ARBA:ARBA00023371};
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|RuleBase:RU361128};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00005175}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR RefSeq; XP_004383634.1; XM_004383577.1.
DR AlphaFoldDB; A0A2Y9DY90; -.
DR STRING; 127582.A0A2Y9DY90; -.
DR GeneID; 101343024; -.
DR KEGG; tmu:101343024; -.
DR InParanoid; A0A2Y9DY90; -.
DR OrthoDB; 4642163at2759; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000248480; Unplaced.
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:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
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; cd20803; C1_DGKtheta_typeV_rpt1; 1.
DR CDD; cd20804; C1_DGKtheta_typeV_rpt2; 1.
DR CDD; cd20854; C1_DGKtheta_typeV_rpt3; 1.
DR CDD; cd17111; RA1_DAGK-theta; 1.
DR CDD; cd01783; RA2_DAGK-theta; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
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 InterPro; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 3.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 3.
DR PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000248480};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 19..67
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 80..127
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 142..193
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 363..462
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 552..689
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 225..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|RefSeq:XP_004383634.1"
SQ SEQUENCE 911 AA; 99382 MW; 1E23BF03C6801AF2 CRC64;
GPGAERAGAR TPVPAAALGH SFRKVTLTKP TFCHLCSDFI WGLAGFLCDV CNFMSHEKCL
KHMKTPCACV APSLVRVPVA HCFGPRGLYK RRFCAVCRKG LEAPALRCEV CELHVHPDCV
PFACSDCRHC HQDGHQDHDT YHHHWREGNL SSGARCDVCR KTCGSSEVLA GLRCEWCSLQ
AHSVCYSALT PECTFGRLRS MILPPACVRL VSRNFSKMHC FRITENPTPE PGEGDDSMDG
SAAAGPGREV LASPESSKQT LRIYDGYDAM QRNHFRLITV PRLAKNEEVL EAALRAYYIS
EDPCDFELQA LPPSARSDDN GAQGKARTGG AAGDEGSRGP GSRDPAPREP APEAWVIRAL
PRTQEVLRIY PAWLKVGVAY VSIRVTPQST SRTVVLEVLP LLGRQAESPE SFQLVEVLMG
SRQVQRTVLA DEELLLDRLW DIRQASLRQM SQTRFYVAES QAVVPHVSLF VGGLPPGLAS
QEYGPLLQEA VGTKADVVTV SRVYPSQGAV VLDVACFAEA ERLYMLVKDT AVQGRPLTAL
VLPEVLHTKL PRDCCPLLVF VNPKSGGLKG RDLLCSFRKL LNPHQVFELT SGGPLPGFHV
FSRAPCFRVL VCGGDGTVGW VLGALEEIRH HLACPEPSVA ILPLGTGNDL GRVLRWGAGY
SGEDPFSVLV SVDEADAVLM DRWTILLDAQ EACGAENSVA DVEPPKIVQM NNYCGIGIDA
ELSLDFHQAR EEEPGKFTSR FHNKGVYVRV GLQKISHSRS LHREIRLQVE QQEVKLPSIE
GLIFINIPSW GSGADLWGSE SDARFEKPRI DDGLLEVVGV TGVVHMGQVQ GGLRSGIRIA
QGSYFRVTLL KATPVQVDGE PWVQAPGHMI ISAAGPKVHM LKKSKQKPRK AGGSPKEARV
DTPPAPDGDA K
//
