ID A0A075ABV9_9TREM Unreviewed; 887 AA.
AC A0A075ABV9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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};
DE Flags: Fragment;
GN ORFNames=T265_14270 {ECO:0000313|EMBL:KER25134.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER25134.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER25134.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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 EMBL; KL596786; KER25134.1; -; Genomic_DNA.
DR RefSeq; XP_009171139.1; XM_009172875.1.
DR AlphaFoldDB; A0A075ABV9; -.
DR STRING; 6198.A0A075ABV9; -.
DR GeneID; 20328436; -.
DR KEGG; ovi:T265_14270; -.
DR CTD; 20328436; -.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000054324; 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: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; 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 PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF114; EYE-SPECIFIC DIACYLGLYCEROL KINASE; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00248; ANK; 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; PS50088; ANK_REPEAT; 1.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128}.
FT DOMAIN 78..212
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REPEAT 809..841
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 645..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KER25134.1"
SQ SEQUENCE 887 AA; 97494 MW; 16247CC459BC1646 CRC64;
RTSSLICPPI NDLEHTRSQI VTSVSRPDHL GQPSAEEIES LRVASLTDGR VSPSTGLSSL
ILAPNLPFVI KPNPLTAVKQ KPLLVFLNPR SGGNQGFSLL RKFQWLLNPR QVFDLSQGGP
RMGLELFARV PNLRVLACGG DGTVGWVLST IEELGLSPMP PVAVLPLGTG NDLARTLHWG
AGYADEPISK ILRSIEHGDI VALDRWHVDC EPRSDVAVTS TDNDAEDGAR NRVLSTTLPL
KIFNNYFSFG ADAATALEFH ESREANPEKF NSRLKNKMFY AGVGGHGDRI CQCRTVTLTT
DKVIPMQMDG EPCRLLPSKI EIRCSHQALV VQKPGRHSGT LSRDTSAYFG GQRTDQVRLN
IFVISLRDYE YISEDALALR GAAIFYGCVS VSPQESLSSV RKSIVQLIGS GAAEASAGNK
EESTPGFRLS DSWLFVDSTT AASRFFRIDS KREAAHFILD ICNMEELFLI DDGLEPRLID
RTPSGKISSD VHTADKQYTQ PVGERSVLET PGNLQGGEIS QMKLADTSLP TGETQQVEER
KLCTTTADVH QEPVDLERSS QETKVKEEML EQHLQIADTE DQTCANPSDK MKPLQNSTLI
ACDGQPENSV TGENPDAKSG IEVDDQLQTT VDELINQLIT TEAEPIITEP LTNGKDSENP
GNEITPYQTD ESRRLSIKKP NPAPRNDSLI SSVSGQPCVT ELVSTDSTRM EHKITRRKQH
PRRSGKECKP NLEGQSFQTR LDKAFLSAAR KGVSTNIEAV LDVGANPLAV DYRGRSALHL
AAKFGCEAAV RLLVKQAPPE LLEMREYEKN QTALHKAAAY RRRKICRILV EAGACPTSRD
ANGKRPRNIA LDADDQTLAH YLHNSELLFK IEHGKHELVC GKQEQGK
//
