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Database: UniProt
Entry: A0A195D3Y9_9HYME
LinkDB: A0A195D3Y9_9HYME
Original site: A0A195D3Y9_9HYME 
ID   A0A195D3Y9_9HYME        Unreviewed;       593 AA.
AC   A0A195D3Y9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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   ORFNames=ALC62_01440 {ECO:0000313|EMBL:KYN07620.1};
OS   Cyphomyrmex costatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Cyphomyrmex.
OX   NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN07620.1, ECO:0000313|Proteomes:UP000078542};
RN   [1] {ECO:0000313|EMBL:KYN07620.1, ECO:0000313|Proteomes:UP000078542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS0001 {ECO:0000313|EMBL:KYN07620.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN07620.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Cyphomyrmex costatus WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ976881; KYN07620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A195D3Y9; -.
DR   STRING; 456900.A0A195D3Y9; -.
DR   Proteomes; UP000078542; 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; cd20851; C1_DGK_typeI_like_rpt2; 1.
DR   CDD; cd20845; C1_DGKbeta_rpt1; 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; IPR047471; C1_DGKbeta-like_rpt1.
DR   InterPro; IPR037607; DGK.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR   PANTHER; PTHR11255:SF48; DIACYLGLYCEROL KINASE 1; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078542};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          43..93
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          108..157
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          226..360
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          469..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  66526 MW;  B209A08E7FA4D231 CRC64;
     MMIEIDYDAD GTVSLEEWKR GGLTTIPLLV LLGLDSHVKE DGNHLWRLKH FSKPAYCNLC
     LNMLVGLGKK GLCCVFCKYT VHERCVQRAP ASCIATYVKS KKTPQTMAHH WVEGNCHGKC
     SKCRKTIKSY NGITGLRCRW CQLTLHNKCA SQVRAECTLG DHAIHILPPT AICPVVLERQ
     RSLSRDNKRG SKHCQDSSSV SSGVFLSCSS GSNQQPAMSF QITPPENTTP LLVFINPKSG
     GRQGERMLRK FQYVLNPRQV HNLAIGGPMQ GLQMFKDVEN FNVICCGGDG TVGWVLETMD
     RVQFEKQPAV GVIPLGTGND LARCLRWGGG YEGEAVHKVL KKIEKATQVM MDRWQIEVDQ
     KDEKKPNQDS IPYNIINNYF SVGVDAAICV KFHMEREKNP EKFNSRMKNK LWYFEYATTE
     QFAASCKNLH EDLEIICDGT PLDLAHGPSL QGVALLNIPF THGGSNLWGE HHPRHRLGKR
     KKRPDKELST SSFNSVDLTA AIQDIGDNLI EVIGLENCLH MGQVKTGLRH SGRRLAQCSS
     VTIITSKRFP MQIDGEPWMQ GPCTIRITHK NQVPMLMAPP PDKSKGFFRF LKR
//
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