ID A0A1S3K574_LINUN Unreviewed; 1094 AA.
AC A0A1S3K574;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=LOC106178934 {ECO:0000313|RefSeq:XP_013417788.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013417788.1};
RN [1] {ECO:0000313|RefSeq:XP_013417788.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013417788.1};
RG RefSeq;
RL Submitted (NOV-2023) 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|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 RefSeq; XP_013417788.1; XM_013562334.1.
DR AlphaFoldDB; A0A1S3K574; -.
DR EnsemblMetazoa; XM_013562334.1; XP_013417788.1; LOC106178934.
DR GeneID; 106178934; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000085678; 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; cd20802; C1_DGK_typeIV_rpt1; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 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; 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 InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF114; EYE-SPECIFIC DIACYLGLYCEROL KINASE; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00109; C1; 2.
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 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:UP000085678};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 385..519
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REPEAT 987..1010
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1023..1055
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 24..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 121048 MW; 915BC85949BE7AED CRC64;
MAMLCQRYNI CACHRTFTCQ TDTTTSQFTN RPHTDSSSGT GNSSSSDEDS EKETFPHTNG
LPVPEGDTNV MNTEDDNGKD FLTVVSLEVP VLKTHRSVSV DTGTAKGKTG YSPTSSPKEG
RRASFDVSYL KKSNSLSPTG SNESLKDVSA EGKRMAFRKA IARGGYGSHY LHPSHAENGY
HKYEPRSTVD WTENAIKGDH LWIETNASGD YCYIGEAECQ KAGPRKKCAA CKIVVHTGCM
THLERIHFGC KPTFREAGVR NYRDQTFVRH HWVHRRRQEG KCKQCGKSFQ NKFGFHSKEI
IAISCSWCKA AYHNKITCFM MQQLEEQCTL GSHAGIIIPP SWIIKIPKKG SFKSSIKKKR
RGSAKRRKSK EADSKPFIVK PIPSPHMKPL LVFINPKSGG NQGAKIMHKL YWLLNPRQVF
DLSRGGPRMG LELFKKVPNL RILACGGDGT AGWVLSALDT LGINPLPPVA ILPLGTGNDL
ARTLGWGGGY TDEPLSKILS AVEEGQVVEL DRWNLKVQNL AVSEPVDTLD EKEEKGEPTL
PLDVMNSYFS LGADAHVALE FHESREANPE KFNNRFKNKM FYAGAGGRDL LRRSWKDLAE
HVKVEGDGID LTSKIKEMRL HCLLFLNIPK YGAGTSPWGS SGSTFDPQRH DDGYLEVIGF
TTASLAALQV GGHGERIAQC KEVHLTTYKT IPMQVDGEPC RLLPSVIEIS LRNQANMIQK
PKRRGSVPIL NDPGLAIFSP PSAQRLRLQA SRISMADYEA LHYDKEKLKA ASIPLGIIVV
ENDSDLEVVR NRINHLQEDN LGVSNSAITQ KLSPNWCFLD STTAERFFRI DRSQEHLHYI
TDISSEDLYI LDPDLLVPSG LNPQDSPWQM VASREKGYEA AVTDVPDGAA EGKLDHLNLV
FSMPVTPPRS PGSEPGTPNS SAEERKSSFQ AVAPVTSDAS LTIPVAAKQT VTVPTDKMLI
DSSKRGDLVR IMELHRGGAN LLATDQYGMT ALHHASRFGH KEVVKFLIEN APPVILDIVD
LEKGQTALHK AAWYQRRTIC CMLVAAGASL TKKDYQGNTP RLQALKAEDM ELAAYLESQE
HFQLVVSEDH ETAV
//
