ID E0VZ55_PEDHC Unreviewed; 830 AA.
AC E0VZ55;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=8234988 {ECO:0000313|EnsemblMetazoa:PHUM524980-PA};
GN ORFNames=Phum_PHUM524980 {ECO:0000313|EMBL:EEB18661.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB18661.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB18661.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB18661.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB18661.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM524980-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM524980-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 EMBL; AAZO01006372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAZO01006373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235849; EEB18661.1; -; Genomic_DNA.
DR RefSeq; XP_002431399.1; XM_002431354.1.
DR AlphaFoldDB; E0VZ55; -.
DR STRING; 121224.E0VZ55; -.
DR EnsemblMetazoa; PHUM524980-RA; PHUM524980-PA; PHUM524980.
DR GeneID; 8234988; -.
DR KEGG; phu:Phum_PHUM524980; -.
DR CTD; 8234988; -.
DR VEuPathDB; VectorBase:PHUM524980; -.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_003770_1_0_1; -.
DR InParanoid; E0VZ55; -.
DR OMA; QTHKSFP; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000009046; 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; cd20851; C1_DGK_typeI_like_rpt2; 1.
DR CDD; cd20845; C1_DGKbeta_rpt1; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 1.10.238.110; Diacylglycerol kinase alpha; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR047471; C1_DGKbeta-like_rpt1.
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; 1.
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; 1.
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:UP000009046};
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 189..224
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 284..334
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 349..398
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 464..598
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 121..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 92310 MW; B44C41EF2EFEF9D9 CRC64;
MNTYLDVNTP EDLVQHLFLS FVLLSSTTAC AAITPYTTTT KGAVGAPGSV PNVATCVVDF
GRDLEFHRPL GSLFSGFTEK LQSLGYHKSE IEGRTRTGSV GAAVHPMLTV THNSYSCHEV
LEKKSTDSSP SHSPISRNSS KKSSNSALVV NNDKREDGKI IQEPPVDINT LRVSLKDIAC
YLSLLEGGRP EDKLEFMFRL YDTDGNGVLD TNEMDCIVNQ MMNVAEYLGW DVTELKPILQ
DMMIEIDYDA DGTVSLEEWT RGGMTTIPLL VLLGLDSNVK EDGNHLWRLK HFSKPAYCNL
CLNMLVGLGK KGLCCVFCKY TVHERCVQRA PANCIATYSK SKKTPHLMAH HWVEGNCHGK
CSRCRKTVKS YNGITGLHCR WCQLTLHNRC ASQVPPGCTL GENRPHIIPP TAICPVVLDR
QRSISKDQQR KSIHRSESQT PVSDTSSNSI ALGQPMSFQI NPMEGTKPLV VFINPKSGGR
QGARILRKFQ YLLNPRQVYN LAKGGPLQGL QLFKDVKDFR VLCCGGDGTV GWVLETMDKV
QFECQPPVGV IPLGTGNDLA RCLRWGGGYE GEAISKLLKK IEKASIVMLD RWQIDVTEDP
SVDPKEIGDP IPYNIINNYF SVGVDAAICV KFHLEREKCP EKFNSRMKNK LWYFEFATSE
TFAASCKNLH EDLEIICDGV SLDLAKGQSL QGIALLNIPY THGGSNLWGD NNSKKRSFNK
KLSTTSFTSV DLSLAYQDIG DGLIEVIGLE SSLHMGQVRT GLRASGRRLA QCSHIVIKTK
KRFPMQIDGE PWMQNPSTIR ITHKNQAPML MAPQPEKKKG IFSFFKKWHN
//
