ID A0A0K0FEM6_STRVS Unreviewed; 1044 AA.
AC A0A0K0FEM6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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};
OS Strongyloides venezuelensis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_0731100.1};
RN [1] {ECO:0000313|Proteomes:UP000035680}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A, De Silva N.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SVE_0731100.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0K0FEM6; -.
DR STRING; 75913.A0A0K0FEM6; -.
DR WBParaSite; SVE_0731100.1; SVE_0731100.1; SVE_0731100.
DR Proteomes; UP000035680; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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; -; 3.
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; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_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; 2.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00314; RA; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 3.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50200; RA; 2.
DR PROSITE; PS50102; RRM; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000035680};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 84..134
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 147..195
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 213..264
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 343..431
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 433..531
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 535..608
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 621..759
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 977..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 117387 MW; 636E6C9D2B09E96D CRC64;
MIFDFCISRT TKSGTLSFKK KILSQHQYHY HQQQQSETLT EVSGIEYNSK HQKISSICCG
GMAAEGHNVD ATLLSSTTIT KDHGHFFVKK TFGKPMYCHH CCDKIWGMIS QGYACEVCNF
VCHDKCLKTI VSYCSGVALQ LIKNPVAHTW TEPGVIKKHF CSVCRKKTDD SLSKECEVCE
YYVHVECQDL AVSDCREAAT YIPSIDQSAQ KQLHHMREGN LPKDSKCYVC KKSCYSFECL
TGMRCEWCSQ TVHATCYRMM SPECDFGPLR KIMLPPNCLT IPRTELPMEQ LLNIHSNVNG
DGTITGSIND QNTNLKVDKK SSNHLNDDNN NGCDEKERDD YEILRIFDGN YSLRTQVYRT
ISVPKVAAVE QIRDIALRKF NIYDTSDNYF LTQVPTEPGG EEELLEDPVP LRNVKRPEGR
RAQLFLRHKD DPEKAIVKIY GGWLRISITF TEIYVNRETL VQDVLSEALT SFGLDKNSWN
KYNLIEVSLE RGVVERTANP QENMLQLVRN LKKDSLRRFH VVRFYIQEKE DPHDHAVFVG
NLPVSLAQRQ YERILLKLLG AKEKPFTAIG PIYFEYGSLV ITFNTPKAAT AAVQKLQNAV
YEDKKLIVLC LPNIQQHMIP SDVEPLLVLV NTKSGGCQGN ELITAFRRQL NPFQVFDVLK
GGPLVGLYVF RNIPKYRILA CGGDGTIGWV LQCLDIVKQE AACFSPPCGI VPLGTGNDLA
RVLRWGGGYT GEENPLDILK DVIEAEEVRL DRWAVVFHEE EKQPANPGRE GEIIPEREQT
MTNPEDQTSM IIMNNYFGIG IDADVCLKFH NKRDANPEKF QSRLFNKTQY VKIGLQKALF
ERSCKDLWKR IELEVDGKMI ELPNIEGIVI LNLLSWGSGA NPWGTAKEEG VFQKPTHYDG
LLEVVGIPDV SRLGLIQSKL AAGIRIAQGG SIRITTHEEW PVQVDGEPHI QPPGTITILK
SALKAKMLKK AKKSRRFNAA STLSSSNQQQ LRQAQSEGSP GSFGGCGVVT SHLGVDVQLS
HGKSTPDDLQ TAGTGEEEEE DAFL
//
