ID A0A0N4WK15_HAEPC Unreviewed; 496 AA.
AC A0A0N4WK15;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Trichostrongyloidea; Haemonchidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001138801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001138801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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; A0A0N4WK15; -.
DR WBParaSite; HPLM_0001138801-mRNA-1; HPLM_0001138801-mRNA-1; HPLM_0001138801.
DR OMA; DECIMIL; -.
DR Proteomes; UP000038042; Unplaced.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
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; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU361128};
KW Kinase {ECO:0000256|RuleBase:RU361128};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU361128};
KW Transferase {ECO:0000256|RuleBase:RU361128}.
FT DOMAIN 1..114
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 496 AA; 55517 MW; 5D7A43F2F42F8DBF CRC64;
LCWLLNPRQV FDITSLKGPK FGLEIYRKLV TQLRILVCGG DGTVGWVLQT LDSLNWPAYP
PMAIMPLGTG NDLSRCMGWG GTFSDEPLSQ LLQAIFHETT VTHLDRWRIH VSPNETCAMD
TSDELSDAVQ SSLPLTVMNN YFSIGADAHV ALQFHHSRSA NPQMLNSRLK NRIAYGGLGT
IDLFKRTWKD LSEYIYLECD GIDITPRIKE LKLHCILFHN ITYYAGGTTP WGSEVTADSV
KPSCCDGRIE VLGFTTATLA ALQMGGKGER LAQCSQVSVT TYKAIPMQLG LLNRIRNLGV
RSCFQVPMLK REKKIACTPN LIRRNTKADK KDSQVQSTSL IVHLPVIVVG RHDYDTYKDV
IDRLKETAFE IGVINLESES DLDVARALIQ KLLDDHPCLP YEPSKEWRFL DYVTNAEEGT
FRVSRGQERV QSVSDICNPD ECLLILDDAF PSITSRSTAI GNELVDGAQP PRTLMQRRIS
ETLRIVLSSE AQETHL
//