ID B3RJ69_TRIAD Unreviewed; 536 AA.
AC B3RJ69;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=sphingosine kinase {ECO:0000256|ARBA:ARBA00044037};
DE EC=2.7.1.91 {ECO:0000256|ARBA:ARBA00044037};
GN ORFNames=TRIADDRAFT_51430 {ECO:0000313|EMBL:EDV29279.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV29279.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV29279.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV29279.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:51496, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:76941, ChEBI:CHEBI:84410, ChEBI:CHEBI:456216;
CC EC=2.7.1.91; Evidence={ECO:0000256|ARBA:ARBA00043822};
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DR EMBL; DS985241; EDV29279.1; -; Genomic_DNA.
DR RefSeq; XP_002108481.1; XM_002108445.1.
DR AlphaFoldDB; B3RJ69; -.
DR STRING; 10228.B3RJ69; -.
DR EnsemblMetazoa; TriadT51430; TriadP51430; TriadG51430.
DR GeneID; 6748896; -.
DR KEGG; tad:TRIADDRAFT_51430; -.
DR CTD; 6748896; -.
DR eggNOG; KOG1116; Eukaryota.
DR HOGENOM; CLU_013399_1_1_1; -.
DR InParanoid; B3RJ69; -.
DR OMA; TMGNFYA; -.
DR OrthoDB; 374620at2759; -.
DR PhylomeDB; B3RJ69; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR PANTHER; PTHR12358:SF31; LD11247P-RELATED; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 155..297
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 536 AA; 59576 MW; 05DEAA3997F61921 CRC64;
MEEIRISNKS TTLISQIIMQ DTLQLIWPRN KLRPCHVVLT QNQMCIKVSD SGPPASLLGD
DGVIQLKDVI GCKVSRGTST KRRDRGGYLT LFWYPMRKKK IGSACKRISI PVYLRVAQSK
EVEDNIKIAD QWHAAIICAL RGIKYQPDLG SKSCPAPRKL LVFINPCSGS GKASKIFNGK
SKDILNEADI LCEVVTTERV GHAKDYIINA NLSKWDGILV VSGDGLIYEV INGLNERQDW
DTVRHMPIGI LPAGSGNALY ASIMKFSGEP NDIVSATFII AKYSTRPLDL MHLQSKKNNF
LAFLSIGWGM IADIDIKSEK FHFLGSNRFT VEAVSMIAKR KVYRGKISYL PCDKEPEETR
ESQWTNNGNV SERSAVMDET FNFHNDDDMN VTQLDANHQQ SAILTVGDDS NPIPSLDKPL
PNQWKVIDQD FITVVIGNLP YLSTDFLFAP PSRLDDGKAY IVAVSDKVNR KGLTKILLST
KNGQYIESPD VQLIPCKAFR LVPETEGGYL TVDGEVVDYG PIQGTVEKGG LQVFCL
//
