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Database: UniProt
Entry: E2B307_HARSA
LinkDB: E2B307_HARSA
Original site: E2B307_HARSA 
ID   E2B307_HARSA            Unreviewed;      1070 AA.
AC   E2B307;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Diacylglycerol kinase delta {ECO:0000313|EMBL:EFN89976.1};
GN   ORFNames=EAI_15275 {ECO:0000313|EMBL:EFN89976.1};
OS   Harpegnathos saltator (Jerdon's jumping ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX   NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN   [1] {ECO:0000313|EMBL:EFN89976.1, ECO:0000313|Proteomes:UP000008237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN89976.1,
RC   ECO:0000313|Proteomes:UP000008237};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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DR   EMBL; GL445250; EFN89976.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2B307; -.
DR   STRING; 610380.E2B307; -.
DR   InParanoid; E2B307; -.
DR   OMA; SANRECN; -.
DR   Proteomes; UP000008237; Unassembled WGS sequence.
DR   GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd20800; C1_DGK_typeII_rpt1; 1.
DR   CDD; cd20852; C1_DGK_typeII_rpt2; 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; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR   PANTHER; PTHR11255:SF34; DIACYLGLYCEROL KINASE ETA; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00109; C1; 2.
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; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFN89976.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008237};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..13
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          29..79
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          102..153
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          183..320
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          489..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..754
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        755..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1070 AA;  117058 MW;  7D9E5C1024B2BD1B CRC64;
     MEEWLQALRT TTESRSQVDP GTAELLGGNH QWYATSHARP TYCNVCRDAL HGVTSHGLSC
     EVCKYKVHKR CSAKAINNCK WTTLASIGKD IIEDQDGNIT MPHQWMEGNL PVSSKCLVCE
     KTCGSVLRLQ DWRCLWCRAT VHTACRPAIS IRCPLGPAKL SVVPPTALHS IGSDEAWEAV
     RPTGCSPLLV FVNSKSGDNQ GVKFLRRFKQ LLNPAQVFDL IKGGPGPGLR LFRHFDPFRI
     LVCSGDGSVG WVLSEIDRLG MHKQCQVGVL PLGTGNDLAR VLGWGASCDD DTHLPQLLEK
     YEKAGTKMLD RWSVMTFERS ISLPCHKVTL HQPDPAIKLS VAHQYEDSVL AHITNILQSD
     QDNVVISSAK VLCETVKDFA THILEASLNT GDQQLGEKCE ILQQKLDLLL QTLSEEESYL
     SDNGEETDVG TVRTNTLSSD QEKGALEKPE KEMTNLKRVQ RRKCYMEKDA VMSRANSLKR
     AIRRLVEHTE TAVDEQNNPS DEKQGSKMPN ITVTSDISPI NSTGKKQQLD IPGFQTDQID
     NFNLMPTIDS ASSVDISPCP SPTPNVASLS PMPDLRRDSQ PEELLTLPAP DGFADSRRNS
     ENIMQGAFTF DEPAAQIAGG QSGMQAAVSD NLLTSEPTQV EASSDIPVTV TRTTLDTSTP
     SDDATMQDTI VSPDTDSLHS RNISPEPQAQ KLSQSKLEPR GSCTNSIVST DSIVSDTLDS
     RSCTIRNSES EIGHIDSDIF DSSKKSDSSE IGHIDSPDNS DMFSSETQHS ESVIDDLSSL
     GQDLISTILA ERYDSVRECL ESEEIEKPQK FCSLAQFVEG NDIARQSFKK GPKNMKTDRE
     VNIEGMLNKY KTDGLATCVR VTGNKSMHPV ETNVIPAPNR FPSVEKEKTS DLLSPVCCFT
     VSSDNTPANE KYATNFPPTI SVIIDPPSPS MSIESHQELN LDYKLDPHIK QYSGSSMERL
     SVELPESGFS PQATRRISSG SLLKASEVVS LAATTARLGG SSVSLRNERA KSMDKTEDVK
     KLPIINPLVR LPMWPNVSGG AGLISQALLA NADALCAAVS PLMDPDESLM
//
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