ID A0A0M8WV54_9ACTN Unreviewed; 545 AA.
AC A0A0M8WV54;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Diacylglycerol kinase {ECO:0000313|EMBL:KOV93359.1};
GN ORFNames=ADL04_27720 {ECO:0000313|EMBL:KOV93359.1};
OS Streptomyces sp. NRRL B-3648.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOV93359.1, ECO:0000313|Proteomes:UP000037702};
RN [1] {ECO:0000313|EMBL:KOV93359.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOV93359.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOV93359.1}.
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DR EMBL; LGDZ01000205; KOV93359.1; -; Genomic_DNA.
DR RefSeq; WP_053710934.1; NZ_LGDZ01000205.1.
DR AlphaFoldDB; A0A0M8WV54; -.
DR PATRIC; fig|1519493.3.peg.5898; -.
DR Proteomes; UP000037702; 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:SF54; SPHINGOID LONG-CHAIN BASES KINASE 2, MITOCHONDRIAL; 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:KOV93359.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000037702};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..364
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 219..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 56778 MW; D151E5F83275DCFD CRC64;
MPRGIGWSVR WIAALTVCQA TFMVGLGLLI TGPARHLWPL TAEDRVNEAF VRLRTGTLTI
LSSVASQGGN TGTVIGVTLA SCLGLILIPR LPMWRQAVFL AVAVSLQSLV FLVITFAVDR
HRPEVHRLDG SLPTSSYTSG HTGAATAVYG GLALLALSRL RGPWRTVVAC LLCVLPLLVG
LARLYRGMHH PTDVMGGLVN GTLSLLIARR ALLTDGAVAA PPAPASPPTA GPSRPVAPGR
TAVIFNPTVT DEAGRDTLRR VLEHHGHTAP VFVETTAEDP GGGQTAGAVR DGATLVVVCG
GDGTLRAAAE SLAGTDVPLA LVPCGTGNLL ARNLGLPLAP ADALDAALRG TAHRVDLGRI
EGDGLPPTHF AAMAGAGLDA ATMRRANAND RAKAVLGWPT YVLAVLRELR TPRTGVSVRL
DGAPALRRTA RMVLVGNIGT VQGGVTLLPD ARADDGRLDL LILDPRGIGG WLSALWTLLR
GGTTASRKGG EGGAPVEFFS FRRAEFTFDT ELPRELDGDP VTAGRHLTAE VGPGALTVLL
PAREQ
//
