ID A0A1I8AW26_MELHA Unreviewed; 978 AA.
AC A0A1I8AW26;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 Meloidogyne hapla (Root-knot nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC Meloidogyne.
OX NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig0.frz3.gene34};
RN [1] {ECO:0000313|WBParaSite:MhA1_Contig0.frz3.gene34}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A1I8AW26; -.
DR WBParaSite; MhA1_Contig0.frz3.gene34; MhA1_Contig0.frz3.gene34; MhA1_Contig0.frz3.gene34.
DR OMA; GFHHARE; -.
DR Proteomes; UP000095281; 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:0046872; F:metal ion binding; 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; 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; -; 2.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_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 InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
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; 1.
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 PROSITE; PS50146; DAGK; 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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 45..96
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 109..157
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 175..226
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 570..708
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 259..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 109296 MW; 7B8FE8F12622A939 CRC64;
MSVQQAETST PVSFSSAEIG TTNAASTSSA INPIPNEQPP GDFGGHVFSS KKTFGKLTYC
HHCCDKIWGM LSQGYLCEVC NFVCHATCMR SIVTVCTGQM MQLIRNPVAH TWTDPQHIKR
HFCCVCRKRT DDTLSSECEV CSCYVHVDCQ DSALADCREA STYVPSLDRT TSKQFHHMRE
GNLARDAKCV VCKKGCYSAE CLSGFRCQWC NLSVHSTCYR QFRPQCDFGP LRKIVLPPNA
VTTPRAELPM DLLLNIHTTT TGVKNNSEGR KASSPSRPMG ADDKDERETR KGDRGERDPD
KEERDDDQLL LRIFDGNSSL RNKISRTAYV PKTASCEQIR DIAMRRFHIC DSNRESYYIT
QAPHELGDEE EPLEDPIPLR NVKKPEGKCA QVFLRYRDDP DKAIVRIHGG WLRIPCEYTD
ITVTVRMCVQ ECIQEVSLEK GVAERTVNPQ EEMLQLVRNL RKDSLRRSHV VRFYIQEKED
PHDHAIFVSN LPPSRSQRQY ERILLKLLSI NERPFCAIGP IYFEYGSLVI TFNTPKAASA
AVLRLQNAMY EDKKLVVLCL PNVQSHMIPP DVEPLLVLVN VKSGGCQGTE LISAFRRLLN
PFQVFDVLKG GPLVGLYVFR NIPKYRILAA GGDGTVGWVL QCLDIAKQDA ACFSPPCAVL
PLGTGNDLAR VLRWGGGYTG EESAVDILRD VIEAEEVRLD RWAVVFHEEE LPSTAALTQK
AQTEDAPMTN PEDQTSMIIM NNYFGIGIDA DVCMRFHTKR DANPEKFSSR LFNKTQYVKI
GLQKAFDRTC KDLWKRVELE VDGRPIELPP CEGIIVLNVL SWGSGANPWG TAKEEAGFQK
PTHYDGLLEV VGITDVSRLG LIQSKLAAGT RIAQGGSIKI TTKEMWSVQV DGEPHIQPPG
TITILKSALK AKMLKKAKKS RKSVAAAVRA VQSEGSPSND FEHPNSSHLE VELRSGHGKS
TPEEINSFDD DEEADSFL
//
