ID E1ZZZ7_CAMFO Unreviewed; 1570 AA.
AC E1ZZZ7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=EAG_11396 {ECO:0000313|EMBL:EFN73237.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN73237.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
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).
CC -!- FUNCTION: Phosphorylates diacylglycerol (DAG) to generate phosphatidic
CC acid (PA). {ECO:0000256|ARBA:ARBA00002064}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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; GL435531; EFN73237.1; -; Genomic_DNA.
DR STRING; 104421.E1ZZZ7; -.
DR EnsemblMetazoa; XM_011270263.3; XP_011268565.1; LOC105258764.
DR InParanoid; E1ZZZ7; -.
DR OMA; VEGNLAM; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd20800; C1_DGK_typeII_rpt1; 1.
DR CDD; cd20852; C1_DGK_typeII_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
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; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF34; DIACYLGLYCEROL KINASE ETA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 2.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 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:UP000000311};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 83..133
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 156..207
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 237..374
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT DOMAIN 1508..1570
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 542..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1570 AA; 174304 MW; C04F2109D4F37441 CRC64;
MSPTRRESQL KCRSNGEPVP DSRYGIARVG ARRGEPVVIT PLRSLVLCGE NRQDMEEWLN
TLRTVTENRP QGDPGTAELL GGNHQWYVTN HARPTYCNVC RDALHGVTSH GLSCEVCKYK
VHKRCSAKAI NNCKWTTLAS IGKDIIEDQD GNITMPHQWM EGNLPVSSKC FVCEKTCGSV
LRLQDWRCLW CRATVHTACR PAISIRCPLG PAKLSVVPPT ALHSIGSDEA WEAVRPTGCS
PLLVFVNSKS GDNQGVKFLR RFKQLLNPAQ VFDLIKGGPG PGLRLFRHFD PFRILVCSGD
GSVGWVLSEI DRLGMHKQCQ VGVLPLGTGN DLARVLGWGS SCDDDTHLPQ LLEKYEKAGT
KMLDRWSIMT FERSISLPCH KVTLHQPDPA IKSSVVHQYE DDVLAHITNI LQSDQESIVI
SSAKVLCETV KDFATHILEA SLNTGDQQLG EKCETLQQKL DLLLQTLSKE ENYLSDNAEE
IDIGTPNTET LNSNQEKGAL EKPEKEMTNL KKVRKRRCYM ERDAVMSRAN SLKRAIRKLV
EHTESAVDEQ NDPSDEKQSS KMPNITITSD NPSMNTTINQ TSDNISLMPT LESGSSLEIS
PCPSPTPNVA SLSPMPDLRR DSQPEELLTL PAPDGFADSR RNSENMPQGV FSFDSPAAQI
AGSQQEAQTS ASNDNFLSSE CTQIEPASDI PITVTKTTLD TSTPSDDATI QDTIVSPDTD
SLHSRNISPE HAQKLAKIKF EPRGSCTNSI ISTDSMVSDT LDSKSYTIRN SESEIGHIDS
DIFDSTKRSE SSEIGHIDSP DNSDMLSTET QHSESGLEDL SSLGQDVISA IMGEKYDSVR
EGLEIEEPRK SCGLAQFNEG NDIARQSFKT RSIKMDKEAM LNKYKTDGLT TCVRVSGTKS
IQPIETNIVS AKFDNIEKEK MSDLLSPVCC FTVSSDNTQA NEKCSINFPP QISVIIDPPS
PSLSIESHHK LNLDYNLDPH DKQYSSGGSM ERLSVELPES GFSPQATRRI SSGSLLKASE
VVSLAATARL GGSSMSLRHE RAKSVDKTED AKKLPIINPL VRLPMWPNVS GGAGLISQAL
LANADALCAA VSPLMDPDES LMEGYFERCV MNNYFGIGID AKISLDFHNK REEHPEKCRS
RAKNYMWYGV LGSKQWLQKT YKNLEQRVQL ECDGQRIPLP SLQGIVVLNI PSFMGGTNFW
GGTKEGDLFL APSFDDRILE VVAVFGSVQM AASRLINLQH HRIAQCQTIQ INILGEEGVP
IQVDGEAWVQ PPGIIRIIHK NRMQMLYRNR ALETSLRAWE EKQRNTLSAV TQSTSTLSSI
TSQSRTHLQI CSRPSHLIDE ELIILFSFIE AVTTLVKWVK LLIISHPSLE PDLYQVALRT
ANALEQVHPD GKILQGMSLR PMVTELVSSA RQLYEESCEL LRDKAHNLRL REDLENKLSM
SLATMEQELR KCIFDEAGTG LVYLQNTPAD DQGDKKNRHR GLFWLKFRRF AGNSGAAGHP
ARDQVTTWGV QEVCSWLENL QLGEYSDRFV SHDIRGRELL TLARRDLKEL GITKVGHVKR
ILQAINDLNN
//
