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Database: UniProt
Entry: A0A069JNA6_9ACTN
LinkDB: A0A069JNA6_9ACTN
Original site: A0A069JNA6_9ACTN 
ID   A0A069JNA6_9ACTN        Unreviewed;       296 AA.
AC   A0A069JNA6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Sphingosine kinase {ECO:0000313|EMBL:KDQ66253.1};
GN   ORFNames=DT87_03155 {ECO:0000313|EMBL:KDQ66253.1};
OS   Streptomyces sp. NTK 937.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ66253.1, ECO:0000313|Proteomes:UP000027475};
RN   [1] {ECO:0000313|EMBL:KDQ66253.1, ECO:0000313|Proteomes:UP000027475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ66253.1,
RC   ECO:0000313|Proteomes:UP000027475};
RA   Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT   "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT   producer of the benzoxazol antibiotic caboxamycin.";
RL   Submitted (APR-2014) 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:KDQ66253.1}.
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DR   EMBL; JJOB01000001; KDQ66253.1; -; Genomic_DNA.
DR   RefSeq; WP_037875845.1; NZ_JJOB01000001.1.
DR   AlphaFoldDB; A0A069JNA6; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000027475; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.200.40; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR045540; YegS/DAGK_C.
DR   NCBIfam; TIGR00147; YegS/Rv2252/BmrU family lipid kinase; 1.
DR   PANTHER; PTHR12358:SF106; LIPID KINASE YEGS; 1.
DR   PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF19279; YegS_C; 1.
DR   SMART; SM00046; DAGKc; 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:KDQ66253.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..134
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   296 AA;  30451 MW;  14454BD6144AF378 CRC64;
     MTSEITLFVN PTAGRGRGAR AAQPAASALR DAGFSVRTVL GEDAADALRR AREAVAGGTG
     ALIAVGGDGM MSLALQAVAG TSTPLGAVAV GTGNDFARAL GLPVRDPAAA GRLCAEALKA
     GTVREIDLGR AGERWFGSVL ASGLDSRVND RGNRMRWIGG RFKYDVALLA ELAALRPFAY
     RVRLDGGPVR EIEATLIAVG NGTAYGGGMR ICADAVMDDG LFDVTVVGAC SRTTLLRVFP
     RVYKGTHLDH PAVSVHRVSS IELAAAGVTA YADGEPLGPL PLTATCVPRA VRVLTG
//
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