ID A0A1I8MFZ0_MUSDO Unreviewed; 1712 AA.
AC A0A1I8MFZ0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=101892971 {ECO:0000313|EnsemblMetazoa:MDOA004499-PC};
GN Synonyms=LOC101892971 {ECO:0000313|RefSeq:XP_019892753.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA004499-PC};
RN [1] {ECO:0000313|EnsemblMetazoa:MDOA004499-PC}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA004499-PC};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_019892753.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_019892753.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_019892753.1; XM_020037194.1.
DR STRING; 7370.A0A1I8MFZ0; -.
DR EnsemblMetazoa; MDOA004499-RC; MDOA004499-PC; MDOA004499.
DR GeneID; 101892971; -.
DR KEGG; mde:101892971; -.
DR VEuPathDB; VectorBase:MDOA004499; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; Unplaced.
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 CDD; cd09507; SAM_DGK-delta-eta; 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; PF00536; SAM_1; 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; 1.
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:UP000694905};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 33..83
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 106..157
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 188..324
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT DOMAIN 1649..1712
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 452..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1712 AA; 191032 MW; F85E81F127A69B16 CRC64;
MEDWLGSLKS ASIPPRSRGD SFFIEQHDIF ANHHHWYATS HARPTYCNVC RDALSGVTSH
GLSCEVCKCK VHKRCAAKAI ANCKWTTLAT VGKDIIEDQN GSIVMPHQWM EGNLPVSATC
AVCKKTCGSV LRLQDWRCLW CRTTVHVACR PHVAIACPLG PAKLSVVPPT CVHSIGNDDS
WDVASPKGNF SPLLVFVNSK SGDNQGVKFL RRFKQLLNPA QVFDLISTGP GLGLRLFRHF
EMFRILVCSG DGSVGWVLSE IDRFNMHKQC QVAVLPLGTG NDLARVLGWG SSCDDDAHLP
QILERYETAS TKMLDRWSIM VFEKAIAVQP KMPKMSLSSE QEALLTGMIT SANENLRSIV
ETDDLPTLMS ATKTLCETID DLLERMCENR KEDDQLTVKC DILRQKVNML LDALKEEENG
SHSGDEFLAT INNIIAKSAP NSPILSASSS NLLNPNISME KNEKDQLNLK ERRNSRSLRG
SEREALQSRA NSVKRAMYNV VEHSEPGRPK RYQRRLSVTP FEALKIPTTT SSDSTPCTSP
LPIIPPINVI SPTMESSRLT CISPLPDTRR ESMDEHFFNT ISLPVPRQFA DSRRSSGVPE
VIEEQEENTN GEITYRRTRL SLSGGANIDD AGNRLSPGSE GASTPGERNF LTVPILTNEH
MVDPLSEFRP IEVFERNYYM SKQLHKDKET EQPSDKVAGE ALVHTCDLQV PSIVVSQKDA
CNVYTSDNIT IIDTDGNTEQ SSEEEFQGEP SDVLSAISNE ECSVASEIFD GKEPTIPGYQ
LGDILQNLDS NEFTHIDSPE TSDETENIPG ESLMDDISSV LGHDITYALQ DNTITDDTTL
MCSERSMIPP PKPARAKQVA ADNKVNPSPP RMPSLARMDS DDNPQQFGFE NIVFEIDNRC
DDQKIREPPR YCSLAQFVEG SDIARQSFKR PKKRSSLKQN NKTNTSKLVS QQQLSLDETN
IAITTAAAIN NNSVNTLTTT SGHQQSEDDL STATAIRIEV SDTTTVTSTS CLKTSPKKSI
PGQDVKRITF DDSCKKESFD DVTPHHPQIS VVVRPPTPLR GDAIRPLNPD TCSSLLALRL
PSEIRRHSSH ATSLTVREFD KDKDRRHSGF NPNYLSLDPE HNRFLNSSPA ASRRISCGSL
FKPNEALPNL QNLKGSKTSL FTGSSIFGFD HFGATPEKEE KDKKEKDKTP SEENRKLPII
NPIVKLPNWP NLTGGGSGFI SKCLLANADT LCAAVSPLMD PDETLLAGYH EKCVMNNYFG
IGIDAKISLD FHNKREEHPE KCRSRAKNYM WYGVLGSKQL LQKTCKNLEQ RVQLECDGQR
IPLPSLQGIV ILNIPSFMGG TNFWGNSKKD DIFLAPSFDD RILEVVAVFG SVQMAASRLI
NLQHHRIAQC QSVQINILGD EEIPIQVDGE AWLQPPGMIR ILHKNRVQML CRNRHLEASL
KTWQEKQRQH SISIQRDHSS TASEHATSTD EVISERECYV LLNFIEAVSS LIKWVKFLII
SHPTLRHDLY SVACRAQDAL ESIHPQGKLL EGPSLRTKLV EVIDSSRQLY DDACNLLRDR
GHSLILREDL ESKLSAALAN MEMELKKCSV QKCVDGKLRA YFNVLAPNEE GDGRRKSRAF
WTRLRSGSTA GQNQFKAPLT NTREAVSNWS VNEVVTWLET MQLSEYVDSF LRNDIRGKEL
LTLGRRDLKD LGVIKVGHVK RILQAIKDMN EN
//
