ID A0A3S3PN14_9ACAR Unreviewed; 953 AA.
AC A0A3S3PN14;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
DE Flags: Fragment;
GN ORFNames=B4U79_02543 {ECO:0000313|EMBL:RWS13104.1}, B4U79_05767
GN {ECO:0000313|EMBL:RWS13103.1};
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:RWS13103.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS13103.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS13103.1};
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).
RN [2] {ECO:0000313|EMBL:RWS13103.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS13103.1};
RA Dong X.;
RT "Trombidioid mite genomics.";
RL Submitted (NOV-2018) 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Target cell membrane {ECO:0000256|ARBA:ARBA00004175}.
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:RWS13103.1}.
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DR EMBL; NCKU01001095; RWS13103.1; -; Genomic_DNA.
DR EMBL; NCKU01001094; RWS13104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3PN14; -.
DR STRING; 1965070.A0A3S3PN14; -.
DR Proteomes; UP000285301; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0044218; C:other organism cell membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; 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; cd20802; C1_DGK_typeIV_rpt1; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_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 PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF114; EYE-SPECIFIC DIACYLGLYCEROL KINASE; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Membrane {ECO:0000256|ARBA:ARBA00023298};
KW Neurotoxin {ECO:0000256|ARBA:ARBA00022699};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Presynaptic neurotoxin {ECO:0000256|ARBA:ARBA00023028};
KW Reference proteome {ECO:0000313|Proteomes:UP000285301};
KW Target cell membrane {ECO:0000256|ARBA:ARBA00022537};
KW Target membrane {ECO:0000256|ARBA:ARBA00023298};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128}.
FT DOMAIN 276..321
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REPEAT 864..886
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 899..931
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 203..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..218
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 953
FT /evidence="ECO:0000313|EMBL:RWS13103.1"
SQ SEQUENCE 953 AA; 106708 MW; 8C39AB1773BAF327 CRC64;
MVKSGLILFT RKCIMDNELT TKVLKRNFKK KAIQGEIKIS TENGETRTLR SAPDWGETAI
NGDHLWVSTS ASGDLCYVGE NECSKQGPRL CCPACKITAH TGCIGILIDK IKFHCKPTFK
DVGIRQYREQ TVMHHHWVHR RHQKGRCRQC VALSCSWCKV NFHNKETCFC MERLTETCNL
GIHSDLIIPP SWIVKLPRKG SFKSSIRRSP KNKRSSSKRR SKKEDSMPSD FSQHLPVHPI
LPLNSGSSSP PPDTKSPINV PGGQHRSFTI KPIPSPNSKP LLVFINPKSG GNQGSKLMQK
FQWLLNPRQV FDLTQGGPRP GYTDEPVSKI LLNIQDGEIV QLDRWDLKVF RNNDVPASEQ
VADTEGAKDV LPLNVVNNYF SIGVDAHIAL EFHEAREAHP ERFNSRLRNK MFYGQAGGKD
LLQRKWKDLC NYITLECDGV DLTQRLRDLK IHSLLFLNIP SYGGGTRPWG TNSPSFETPR
TDDGLIEVIG LTTYQLAGGH GSCIAQCRSA RIITSRTIPM QVDGEPCRLL PSLIELQLRN
QANMIAKSKS HSQITHIPLE REVTVEVRKL NLSDYETYHY DKEKLKEVSL QLGKLTINPD
LELDRVRAQI NEMVHGADHE EEEDIEINDG EAKQHHIESQ CALSADWCFV DCKRKFCALL
THAYGILFPI TLIACTAERF FRIDRAQEHL HYVVDICNDD LFILDPADDS AKDESSNVVP
NIIAENPTDS ANLTTSLITQ DNNKTIVLFK AEQVKDEMDT EGASDNKTSE MVVTEVSACG
ANNSVIGEDA NRNTTHDSSS DKNNGDGDDH NVQRNDQKAD PSLLRPVNTE KISTEIIDAA
REGDLQKIKN LLRQGYSVLA IDENGMTALH YAAKYGYEDI VQLLIQEEPS LIDIPDCDEG
QTALHKAAKY SKRKVCCILA AAGSSLSKLD NQGYTPKQLA IASKDEELAA YLQ
//
