ID A0A1I8PG64_STOCA Unreviewed; 1705 AA.
AC A0A1I8PG64;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=106095625 {ECO:0000313|EnsemblMetazoa:SCAU007764-PE};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU007764-PE, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU007764-PE}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU007764-PE};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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_013118349.1; XM_013262895.1.
DR EnsemblMetazoa; SCAU007764-RE; SCAU007764-PE; SCAU007764.
DR GeneID; 106095625; -.
DR VEuPathDB; VectorBase:SCAU007764; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000095300; 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 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}; 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 1642..1705
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 470..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1705 AA; 190130 MW; 7ECD5E8BF00B3B89 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 IDRFSMHKQC QVAVLPLGTG NDLARVLGWG SSCDDDAHLP
QILERYETAS TKMLDRWSIM VFEKAVSVHP KMPKMSLSSE QEALLTGMVT AANENLRSIV
ETDDLPTLMS ATKTLCETID DLLERMCEHR KEDDQLTLKC DILRQKVNML LDALKEEETG
SHNGDDLLST INSIIAKSAP NSPILTASSS SLLNPNISIE KNEKDQLNLK ERRNSRSLRG
NEREALQSRA NSVKRAMYNV VEHSEPGRPK RYQRRLSVTP FEALKIPTTT SSDSTPCTSP
LPIIPPINII SPTMESSRLT CISPLPDTRR ESMDEHFFNT ISLPVPRQFA DSRRSSGVPE
VIQEQEENGN GHVETTYRRT RLSLSGGANI DDAGNRLSPG SEGASTPTER NFLTVPILTS
DHLVDPLSEF RPIEVFERNY YMSKQLDKDK EQEEGHQGKR VTISGEALVH TCDLQVPSIV
VSPKDACNVY TSDNITIIDT DGNTEQSSEE EFQGEPSDVL SAISNEECSV ASEIFDKQEP
PLTGYQLGDI LQNLDSNEFT HIDSPETSDE TENIPGESLM DDISSVLGHD ITYALQDNTI
TDDTTLMCSE RAAVPPPKPA RAKQTARRGS SPPRIPRLDR MDSDDNPQQF GFENIVFEID
NRCDDQKIRE PPRFCSLAQF VEGSDIARQS FKRPKKRSSL KQTKQTTSTL VSQQQHSLDE
VTVATTAITS SVHTLTTTSG HQSEDDLSTA TAIRIEVSDT TTSTSCLKSS PKKSIPGQDV
KRITFDDSCK KESFDDVTPH HPQISVVVRP PTPLRGDAIR PLNPDACSSL LAIRVPSEIR
RHSSHATSLT VREFDKDKDR RHSGFNPNYL SLDPEHNRFL NSSPAASRRI SCGSLFKPNE
ALPNLQNFKG SKASLFTGSS LFGFDHFGTG PEKEDKEKKD KTPTEENRKL PIINPIVKLP
NWPNLTGGGS GFISKCLLAN ADTLCAAVSP LMDPDETLLA GYHEKCVMNN YFGIGIDAKI
SLDFHNKREE HPEKCRSRAK NYIWYGVLGS KQLLQKTCKN LEQRVQLECD GQRIPLPSLQ
GIVILNIPSF MGGTNFWGNS KKDDIFLAPS FDDRILEVVA VFGSVQMAAS RLINLQHHRI
AQCQSVQINI LGDEEIPIQV DGEAWLQPPG MIRILHKNRV QMLCRNRNLE ASLKTWQEKQ
RQHSISIQRD HSSTASEHAT STDEVISERE CYVLLNFIEA VSSLIKWVKF LIISHPTLRH
DLYAVACRAQ DALESIHPQG KLLEGPSLRT NLVEVIDSSR QLYDDACTLL RDRGHSLILR
EDLESKLSAA LANMEMELKK CSVQKCVDGK LRAYFNVLAP NEEGDGRRKS RAFWTRLRSG
STAGQNQFKP PLTNTREAVS NWSVNEVVTW LETMQLSEYV DSFLRNDIRG KELLTLGRRD
LKDLGVIKVG HVKRILQAIK DMNDN
//
