ID A0A0V0YCV7_TRIPS Unreviewed; 863 AA.
AC A0A0V0YCV7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=Dgkb {ECO:0000313|EMBL:KRX97577.1};
GN ORFNames=T4E_2326 {ECO:0000313|EMBL:KRX97577.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX97577.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX97577.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX97577.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX97577.1}.
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DR EMBL; JYDU01000030; KRX97577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0YCV7; -.
DR Proteomes; UP000054815; 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:0005509; F:calcium ion binding; IEA:InterPro.
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; cd20799; C1_DGK_typeI_rpt1; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 1.10.238.110; Diacylglycerol kinase alpha; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR029477; DAG_kinase_typeI_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR038199; DGK_typeI_N_sf.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; PF14513; DAG_kinase_N; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000054815};
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 201..236
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 246..281
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 297..348
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 363..409
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 466..611
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 435..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 96900 MW; 593B593316862FE0 CRC64;
MTSSACGRSI FCGKHVKWRK LTPAEFEKLH GYLLYRTKEL KQVMVAFQDG GALAKYRRPN
ETVNFEGFKA LLDLYLETDV PFDLCLHLFR SFIKDRTKDE EVALQTTTQS NCKTNRGSLA
ASTISNAACT PSSRRSSFTL SENKLNIHDY IQRKCRNQEH DSRLFFLGLT NDQSETSTCQ
CSAVVRLKDI DCYFSLLENG TPEEKLEYTF HLYDADGNGY LDSNEIECII EQMMSVAEHL
AWDTVELKPI LRDMLLEIDY DADGTVSLEE WKRGGLTTVP LLVLLGIDSQ ALREDGTHMW
RLKHFNKPTY CNLCMKRLVS FSGKQGLCCT LCKYTVHERC AGGAANNCIS TYAKSKRETS
IMIHHWVDSN CSERCVRCKK HIKALEGKRC RWCKGEIHQR CLNDWDVKCN LGKLAHHIIP
PTSLVPLVLT ERRRSSSKSF KTGQNSSTNN GSLSSAMPSF EIDISPDTKP LLVLLNPKSG
GKQGTKLYRK LQYLLNPRQV FLLDNSGPLE GLKMFQNISN MNILCCGGDG TVKWVLDAMG
VEVIFYQINY GDNRPPVAVL PLGTGNDLSR CLNWGGGFAG KTGNDLIAFL KSIEKSRIVT
LDRWETNLIE NDDSEKGDAM PNNIITNYFS VGVCIFLLPI SIIIEQDASI AHRFHTMREK
YPEKFSSRMK NKLWYFEFAT FESLQATCKN LHEYVEIHCD GSPLNLDSGP PLEGIAFLNI
PSIYGGSNLW GRNASAAKSK RFWGIGSLGL RPSSENLTNS CNLLGNNQDM GDKKIEVVGI
QSVISMGQVK AGLRTSAKRL AQCSSAIIKT KKRFPMQIDG EPWVQQPCTI SIAHKNQVPM
LQANKKVHLH KSFGCINQAC SES
//
