ID D2VLL2_NAEGR Unreviewed; 560 AA.
AC D2VLL2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=sphingosine kinase {ECO:0000256|ARBA:ARBA00044037};
DE EC=2.7.1.91 {ECO:0000256|ARBA:ARBA00044037};
GN ORFNames=NAEGRDRAFT_69820 {ECO:0000313|EMBL:EFC42329.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC42329.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC42329.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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; GG738880; EFC42329.1; -; Genomic_DNA.
DR RefSeq; XP_002675073.1; XM_002675027.1.
DR AlphaFoldDB; D2VLL2; -.
DR STRING; 5762.D2VLL2; -.
DR EnsemblProtists; EFC42329; EFC42329; NAEGRDRAFT_69820.
DR GeneID; 8851893; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_69820; -.
DR eggNOG; KOG1116; Eukaryota.
DR InParanoid; D2VLL2; -.
DR OMA; TIWTLYR; -.
DR OrthoDB; 374620at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IEA:UniProt.
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; 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:UP000006671};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 166..312
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 560 AA; 63346 MW; 3A6AD66F1B24E43D CRC64;
MTQQAAEEEI TLVVNDNDSG VVAVEDQQHS EQQKQLTAID NYSLNNNDQN LIGFKPITLD
SNLRYRNKKF KAELNGDFLI LRNLEGKKSN DNLVPLLTIE MESIFAVHKK TDQPLVFVVF
TFRAKDCKKI VYEFEALGNE ECAEWVDSIR SNAFKTNLIM SGSKSFGNRR VLLFINPFSG
KKTGTKIFEK QIKPMLDVAH LSYDAIITER ADHAFEFCST SDKILEYTDI CGMGGDGIIY
EIINGIGKRK DWKNVFDRVR IGHIPGGTSN ALAVFSGSQV KSGKPAVPEM AAFIIARGFH
QPMDLLSCFQ EANKRYISFL SITWSAIADV DIGTENMRWL GAARNTVGAI KQIMNKKAYR
GKLKYVQQSQ ELKRVKSLKN IRENEQRYSS YTESSIEFLQ GKENEKGQLS CPLLEQYFHE
EFKKLAPEYC SEKEPNITED STNSHLEVKE IEDRFCMFLA ANISHISFDF IASPMAHHHD
GYIDLVYVKD DISRGDFLNI FLAAEKGDHI FEKCVDLSKV KAFMLTPIDT GSFVVVDGEA
VDYSPILVEV HPSCCKLLTL
//
