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Database: UniProt
Entry: A0A0J6XPK6_9ACTN
LinkDB: A0A0J6XPK6_9ACTN
Original site: A0A0J6XPK6_9ACTN 
ID   A0A0J6XPK6_9ACTN        Unreviewed;       301 AA.
AC   A0A0J6XPK6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Sphingosine kinase {ECO:0000313|EMBL:KMO97159.1};
GN   ORFNames=ACS04_14365 {ECO:0000313|EMBL:KMO97159.1};
OS   Streptomyces roseus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=66430 {ECO:0000313|EMBL:KMO97159.1, ECO:0000313|Proteomes:UP000035932};
RN   [1] {ECO:0000313|EMBL:KMO97159.1, ECO:0000313|Proteomes:UP000035932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31245 {ECO:0000313|EMBL:KMO97159.1,
RC   ECO:0000313|Proteomes:UP000035932};
RA   Cruz-Morales P., Martinez-Guerrero C., Morales-Escalante M.A.,
RA   Yanez-Guerra L.A., Kopp J.F., Feldmann J., Ramos-Aboites H.E.,
RA   Barona-Gomez F.;
RT   "Recapitulation of the evolution of biosynthetic gene clusters reveals
RT   hidden chemical diversity on bacterial genomes.";
RL   Submitted (JUN-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:KMO97159.1}.
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DR   EMBL; LFML01000053; KMO97159.1; -; Genomic_DNA.
DR   RefSeq; WP_048476966.1; NZ_LFML01000053.1.
DR   AlphaFoldDB; A0A0J6XPK6; -.
DR   STRING; 66430.ACS04_14365; -.
DR   PATRIC; fig|66430.4.peg.5305; -.
DR   OrthoDB; 142078at2; -.
DR   Proteomes; UP000035932; 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:KMO97159.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035932};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..135
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   301 AA;  30858 MW;  C963EF939C957D1F CRC64;
     MTAEITLFVN PTAGRGRGAH AAQPAASALR AAGFSVRTVL GADAADALAR LRTAVREGTG
     AVIAVGGDGV VSLALQALAG TLVPLGVVAA GTGNDFARAL GLPVREPARA GRLAAAALKE
     GRIREVDLGL LAGAPGRAEA WYGTVLCSGF DSRVNDRGNR MRLPAGRFKY DLAILAELAS
     FRPFPYRITL DDGPVIETEA TLVAVGNSSS YGGGMRICAD AVPDDGLFDV VIVGDCSRTT
     LLKVFPQVYK GTHLGHPKVA VHRAAKVTLE AAGITAYADG EPLGALPVTA RCVPGAVRLL
     V
//
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