ID A0A1S3IQE0_LINUN Unreviewed; 346 AA.
AC A0A1S3IQE0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Diacylglycerol kinase beta {ECO:0000313|RefSeq:XP_013400440.1};
GN Name=LOC106166427 {ECO:0000313|RefSeq:XP_013400440.1};
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_013400440.1};
RN [1] {ECO:0000313|RefSeq:XP_013400440.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013400440.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013400440.1; XM_013544986.1.
DR AlphaFoldDB; A0A1S3IQE0; -.
DR STRING; 7574.A0A1S3IQE0; -.
DR EnsemblMetazoa; XM_013544986.1; XP_013400440.1; LOC106166427.
DR GeneID; 106166427; -.
DR KEGG; lak:106166427; -.
DR InParanoid; A0A1S3IQE0; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; 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; 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; 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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; PF13499; EF-hand_7; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_013400440.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 117..152
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 162..197
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 212..262
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 277..326
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 37..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 346
FT /evidence="ECO:0000313|RefSeq:XP_013400440.1"
SQ SEQUENCE 346 AA; 38639 MW; A3E91A0EF9631BFE CRC64;
MLVCLCDCSV FAFNKGSNSA SHHPAITVST PMLDKIHKSD DTTPDVSSHS RSSSKKSNHS
IHSLHLPDSN DPWIRQSTSS LLQGLGGKMK RQSIDVKSGN ILIKDLVCYL SLLEAGRPED
KLEFMFRLYD TDGNGLLDAT ELDCIVNQMM TVAEYLGWDV TELRPILKDM MVEIDYDNDG
TVSLEEWKRG GMTTIPLLVL LGLDTNVKDD GQHVWRLKHF NKPAYCNLCL NLLVGLGKQG
LSCTFCKYTV HERCVHRAPA SCITTYVKSK KTPQAMLHHW VEGNCPGKCD RCKKSIKTYN
GVTGLHCRWC QLNLHNKCAS QVKPDCDMGE FKDHILPPTS ICPAVL
//
