ID A0A094ZYR0_SCHHA Unreviewed; 1148 AA.
AC A0A094ZYR0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=MS3_08570 {ECO:0000313|EMBL:KGB40110.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB40110.1};
RN [1] {ECO:0000313|EMBL:KGB40110.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(2012).
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|RuleBase:RU361128};
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR EMBL; KL251371; KGB40110.1; -; Genomic_DNA.
DR RefSeq; XP_012799868.1; XM_012944414.1.
DR AlphaFoldDB; A0A094ZYR0; -.
DR STRING; 6185.A0A094ZYR0; -.
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; cd20803; C1_DGKtheta_typeV_rpt1; 1.
DR CDD; cd20804; C1_DGKtheta_typeV_rpt2; 1.
DR CDD; cd20854; C1_DGKtheta_typeV_rpt3; 1.
DR CDD; cd17111; RA1_DAGK-theta; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
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; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00788; RA; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 3.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 3.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
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 85..135
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 148..196
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 282..333
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 520..598
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 663..801
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 127816 MW; B22BADE17F3C2752 CRC64;
MECESSKVVS LQETLKLNPS TSIESESTLN DQTQSVSKHE EQKDKGKDFG GQCDSTKANP
SSFTPNSGII SSLQTSCSPT NTIQGHSFIR RTLHKPAYCH HCGEVIWGLL GSGFQCEICN
LLAHERCQTV VSSPCTSVAP LHIKSPVSHC WSDVGHFKRK FCNVCRKRLE DSLSVRCEVC
EYYCHVDCQD YSINDCKQGA TCSPGKPVVR YSSVGVGMGV WASRLSSACI PFTVPSKHMS
SATDQLTCNL HFSTSTKLFI NELLFCSLLH FIPKKQCSPR QTHHWREGNL PTNSKCFICR
KTCWSSECLT GYRCQWCGRT SHAGCIEKVD DECDFGPLRD IMLPSFCVSL PRMNIPIEHV
IGVTKRPRGR AISADWSSSG ESKEDSWQDT RSPRETIDRA SSDEYLCVFD GVGALKRRSC
RSFSFSKSMS TYSAVKRFLK TFHLAGTPDY YNVYEVNEHD GTENKLNYHV NLRSQLRFDL
KQPSILIRSK EPEESTITIK VYAGDLRLLL APHVPPYEEV TINSETTASK VVAMALNNFG
CGHMSPDDCY LSSVCVDRTV SEQLLNKDDR PMLLLDQLRE ESARISQFTR FELRFVEDPP
IGPSVSLFVG NLKENLSQRL YERVLLDKLG EKCRWDSIEE SIFMNKPITA LLLPTIHPQN
LPKGIQPLLV FVNLKSGGCQ GVDLIVAFRR LLNPFQVFNL DYGGPLPGLY CFRHLASYKI
LVCGGDGTVG WTLSCLDIVG QDAACNAPPI APLPLGTGND LSRVLRWGSG YSSADDPLTI
LKDVVAAEEV KLDRWTLIVR PEEDFKDETK LALELQTNAS NTNEDNSIMI IMNNYFGIGI
DADLSLDFHN ARSENPSKFN SRIHNKGVYF KIGLRKMINR TICKDLHKQI VVIADGKIVI
LPPIEGLVVL NILSWGGGAN PWNVEKHDDE FVKPTHYDGL LEIVGISGVV HMGQIYSGLG
TGIRLAQAAH ANMLRKVKRP KRRPGTEDYG LNQLSSTTDQ QYQNSIQQYS TTRLHDFSSS
SDYSSLNVIQ NIKEDLQLPI NKLNMDPFIS DTPTYSKPII NLTSKPIYNK VNTPTNTVQS
STVSAVHSND NDNTAVYHQG SLTNTLNQLS LGSNIRSQEV LSSSSSVNLP SSLLRICSYT
TLSGDDSV
//
