ID A0A0N0YI08_9ACTN Unreviewed; 584 AA.
AC A0A0N0YI08;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Diacylglycerol kinase {ECO:0000313|EMBL:KPC81908.1};
GN ORFNames=ADK82_14760 {ECO:0000313|EMBL:KPC81908.1};
OS Streptomyces sp. NRRL S-4.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519471 {ECO:0000313|EMBL:KPC81908.1, ECO:0000313|Proteomes:UP000037987};
RN [1] {ECO:0000313|Proteomes:UP000037987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-4 {ECO:0000313|Proteomes:UP000037987};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPC81908.1}.
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DR EMBL; LGKJ01000113; KPC81908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0YI08; -.
DR STRING; 1519471.ADK82_14760; -.
DR PATRIC; fig|1519471.3.peg.3064; -.
DR Proteomes; UP000037987; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR045540; YegS/DAGK_C.
DR PANTHER; PTHR12358:SF106; LIPID KINASE YEGS; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF01569; PAP2; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00014; acidPPc; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPC81908.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 277..405
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 60450 MW; 32C95F4E658C240C CRC64;
MPTDIPERRT VLPGGHVAAM PPPAEGRAPS ASGAERPRGT PEAAGGMGRA VGVIVSTAVC
QAALMVGLGL LITGPAARVR PLAAEDEITD ALERARTGTL DTVSLVVSEA GNTFTVVVGT
LLACLVLLLA PKLPRWRDAL FLAVAVSLQS LVFLVVTEAV DRTRPDVERL DASPPTSSYT
SGHTGAATAL YAGLAILVLH RTKGPWRRVV AALLLLLPLL VGVARAYRGM HHPTDIAGGM
LNGGLSLLIV GRALLAGPHV PGVAPAGTAV RGERAGPEPG RTAVVFNPTV TDETTCDGLR
RVLEDHGHHG PEFVPTTADD PGEGQTARAL REGATLVVVC GGDGTIRAAA EALAGTGTPL
AVVPCGTGNL LARNLGLPVR PAEALAVALR GVPHRIDLGR VEGDGMAPAH FTVMSGAGLD
AAMLESTGDR AKALLGWPAY VMAGLRELRA PRMRLTVGLD GARPLRRSAR MVLFANTGKV
QGGAALVPAA RPDDGLLDLM ILDPRGPAGW LGAITTLLRR RPEGGGGRAG GSRSVEYFTF
SRADVRFDEP QQREVDGDTV QPGRRLTAEV RPGALTVLMP VRGD
//
