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Database: UniProt
Entry: A0A093FS18_TYTAL
LinkDB: A0A093FS18_TYTAL
Original site: A0A093FS18_TYTAL 
ID   A0A093FS18_TYTAL        Unreviewed;       613 AA.
AC   A0A093FS18;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=diacylglycerol kinase (ATP) {ECO:0000256|ARBA:ARBA00012133};
DE            EC=2.7.1.107 {ECO:0000256|ARBA:ARBA00012133};
DE   Flags: Fragment;
GN   ORFNames=N341_01178 {ECO:0000313|EMBL:KFV59470.1};
OS   Tyto alba (Barn owl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX   NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV59470.1, ECO:0000313|Proteomes:UP000054190};
RN   [1] {ECO:0000313|EMBL:KFV59470.1, ECO:0000313|Proteomes:UP000054190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV59470.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC         octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00023371};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC         Evidence={ECO:0000256|ARBA:ARBA00023371};
CC   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00005175}.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC       {ECO:0000256|ARBA:ARBA00009280}.
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DR   EMBL; KK400069; KFV59470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093FS18; -.
DR   UniPathway; UPA00230; -.
DR   Proteomes; UP000054190; Unassembled WGS sequence.
DR   GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
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   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:SF92; DIACYLGLYCEROL KINASE IOTA; 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   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; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFV59470.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..70
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REPEAT          542..574
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          570..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..584
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV59470.1"
FT   NON_TER         613
FT                   /evidence="ECO:0000313|EMBL:KFV59470.1"
SQ   SEQUENCE   613 AA;  69356 MW;  1A4357C4AA073D2F CRC64;
     VGWILSILDE LQLSPPPPVA VLPLGTGNDL ARTLNWGGGY TDEPVSKILC HVEDGTIVQL
     DRWNLQVERN PDLPQDELED GARKLPLSVF NNYFSLGFDA HVTLEFHESR EANPEKFNSR
     FRNKMFYAGA AFTDFLQRSS RDLSKHVKVV CDGTDLTPKI QELKFQCIVF LNIPRYCAGT
     MPWGNPGDHR DFEPQRHDDG YIEVIGFTMA SLAALQVGGH GERLHQCREV TLLTYKSIPM
     QVDGEPCRLA PSLIRISLRN QANMVQKSKR RTSMPLLNDP HSIPDRLRIR VNRINLQEYE
     GLHYDKEKLR EASIPLGIIV VRGDCDLETC RMYIDRLQED LQSVTSTTQR VHYQDQESSF
     PRVLSVQRLS PRWCFLDATS ADRFYRIDRS QEHLHFVTEI SQDEIFILDP ELVMSECLSL
     PSFLPRISDR WNPAVRKRML SDSGLGKISP HYEVPDKQKD ASQTHMLQSP VSSEDQALLQ
     AVIAGDLLKF IECCKKGANL LIQGPDHCSL LHHAAKTGQG EIVKYILEHG PSELLDMTDS
     ETGETALHKA ACQRHRAICQ LLVDAGASLR KTDSKGKTPR DRAQQAGDPD LASYLDSRQN
     YQMVSHEDLE TAV
//
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