ID A0A0N0P530_LEPSE Unreviewed; 972 AA.
AC A0A0N0P530;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=sphingosine kinase {ECO:0000256|ARBA:ARBA00044037};
DE EC=2.7.1.91 {ECO:0000256|ARBA:ARBA00044037};
GN ORFNames=ABL78_4948 {ECO:0000313|EMBL:KPI85986.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI85986.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI85986.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI85986.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
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};
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:KPI85986.1}.
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DR EMBL; LJSK01000155; KPI85986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0P530; -.
DR EnsemblProtists; KPI85986; KPI85986; ABL78_4948.
DR VEuPathDB; TriTrypDB:Lsey_0155_0070; -.
DR OMA; HDCEDYV; -.
DR OrthoDB; 374620at2759; -.
DR Proteomes; UP000038009; 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 SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 2.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPI85986.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 343..427
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..34
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 105964 MW; 8D6ED292E977E524 CRC64;
MPSQSAVATS SSLHKPPTAH RRRRQVPTAR PKPKSKLPKK PDGVPAVPTT AEPDSSTAAD
IASPPSLDCV ASTHVDPTMP VCSIDAGADA TRPSVQSGSR AGVKDSMRAD SSKFSPLRLM
QPGNESYGPA TPPPHRDPCR AGPAGGRTSA DMTAVVHAKG HTCKLTYSPT KDSLHIARTS
KSGNIRTVLN IPVHMIINIE TAAEKEDRQR ARQTNDEAVK LVFADSSGGA GLLCTHPTGT
TTCDAAPLVF AHSRVNTDIS ASGSCSYGGV LFQQNALTSP LGVCNWVTSP LATPATQIRC
YVHYVRQRNR ERLSIHTLEL LSHGPAEHMQ TVVNALVQRI YRKGPKHILI FISPKSGKGK
GEQSFDKHVR PLLHFSRHTY QTYITQRAHD CEDYVADLSH PMNANTVVAA VGGDGMVNEV
VNGLHRRKLA YVQWLRSITV DVLPCNLTED SSQRLSDGGS SNAWGLDPQA LATMSDGTSS
SAFPKAASSP DPQHANPTIA ATMTAAGALN RQPELEENKR CRCASPDYAA AVEAWRFAQR
LVEEGWDALM PLIATVPTGS ACGMAKSLDV LSIAQSAMAL VHLTTVHMDL LHMCFTPNKE
LKECQKKKLS LRKLTAAKED FSKYCKNYAA ELHERAEAET TAHQQQQSQE GEGREEGSSS
PISALSAADT KSPFLKDGSN VYTDEVNYAL KMPYFANRVA FMSLSFGTAN DIDHGSEPLR
WMGNTRFHVY GGYLILLGLR CYRGVLRYLP WRSKSGKTME KLHSRHTMPS TDDFPLCTMR
DDCPHCQDYT FTHCGQFSLA SSNVTEEKHT VNTPRSGRER AGARCRSSAA ATLAPYTDAE
LLDEDSVDFS DPNMPWVTIR GEFCTALICN VRDIAQDMLM APLSHLSDGA IDVVYCRIDP
CTGKGGRIEM VKFFMALESG KHVDLDFVNY VKARAVEMKV DEGILMSDGE LMPLSSVRIT
KLRSSIQVVR NE
//