ID A0A3S3PN27_9ACAR Unreviewed; 957 AA.
AC A0A3S3PN27;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=B4U79_08400 {ECO:0000313|EMBL:RWS13122.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS13122.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS13122.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS13122.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
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:RWS13122.1}.
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DR EMBL; NCKU01001086; RWS13122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3PN27; -.
DR STRING; 1965070.A0A3S3PN27; -.
DR Proteomes; UP000285301; 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:0003676; F:nucleic acid 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; 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; 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; 2.
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; 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:UP000285301};
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 96..144
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 162..213
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 284..333
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 367..462
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 553..691
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 108089 MW; 7511F78DC6CAFA1B CRC64;
MASSGGRASA KSSDNNPSPT TESVPEYDQF GHGHYFTKKT FHKPTYCHHC ADMLWGLIGQ
GCICEVCNFV VHDRCLKTVV SPCSTVASNV IKNPVPHCWT DVGHLKRKFC NVCRKRIEDS
SAVRCETCEY CVHLECQDFS VADCKECATY VPDQDLTKVV QYHHWREGNL PPNSKCHYCK
KTCWSAECLA GMRCEWCGWT AHAICYKNLS PECNFGVVQS IMLPPYCVSI PRTDVPLETI
IGVQNKRKTE SGSPRSASEE FSAQDQSRQK DIDEYPSPKD KDKDEEIIKV YDGNSSMRRR
TFRTITVSRS ATKEQIICAA LRAFHIHDDP RHYIITDFYD FMPVQSLLRR EGKRPAIFFR
FKPPNPNEGT IRVYPGRLNV NDTYRVIPVT NDTSVDDVMI AALNEFGLDA KDINRHRLVE
VSLDKGAVHE RTMDNQECPW EIIKNVARQK ENTRFYLQTK DEVYCSNVAV FVGNLPPNLN
QRQYEKILVD VLGKPYKYRQ VGPIYYEYGS LIITYDNADI AVKAFYMLRD ATYDDKNLLV
LLLPNIVAEM IPPGVRPLLV FVNVKSGGCQ GLELISSFRK LLNPYQVYDL ENGGPLPGLY
VFRHVKDYKI LVCGGDGTVG WVLQCLDNVG QDSECQSPPC AVVPLGTGND LARVLRWGSG
YTGGEDPLTV LKDVIDAEEI RLDRWTVVFH TDEAVKSEDK PGLPANSSGS TSEDNTAIYV
MNNYFGIGID ADLCLGFHNA REENPDKFNS RYSKIELVFH ILNTNFDYDK KRFHNKGVYV
KMGLRKMVSR KSWKDLHKEI RLEVDGKVVN LPPLEGIIIL NILSWGSGAN PWGPEKEDQF
SKPTHYDGML EIVGVTGIVH MGQIQSGLRS AIRIAQGGHI RIRINTEMPV QVDGEPWIQT
PGEVVVLKSA LKATMLRKTK MKRRNTEPVL TATEKSSIER SSIALQEKSS ISERPDE
//
