ID C8ZDM3_YEAS8 Unreviewed; 678 AA.
AC C8ZDM3;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=sphingosine kinase {ECO:0000256|ARBA:ARBA00044037};
DE EC=2.7.1.91 {ECO:0000256|ARBA:ARBA00044037};
GN ORFNames=EC1118_1L7_1090g {ECO:0000313|EMBL:CAY81489.1};
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680 {ECO:0000313|EMBL:CAY81489.1, ECO:0000313|Proteomes:UP000000286};
RN [1] {ECO:0000313|EMBL:CAY81489.1, ECO:0000313|Proteomes:UP000000286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse
RC {ECO:0000313|Proteomes:UP000000286};
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambot B.,
RA Legras J.L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
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; FN393080; CAY81489.1; -; Genomic_DNA.
DR AlphaFoldDB; C8ZDM3; -.
DR HOGENOM; CLU_013399_0_2_1; -.
DR Proteomes; UP000000286; Chromosome XII, Scaffold EC1118_1L7.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
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 PANTHER; PTHR12358:SF31; LD11247P-RELATED; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
FT DOMAIN 257..396
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..513
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 76544 MW; E77C59275471F3FB CRC64;
MTLKPSKRRK GRSRHSRKKQ ITSAILTEEG IMIKAKPSSP YTYANRMADK RSRSSIDNIS
RTSFQSNSDN NSIFETASLI SCVTCLSDTD TIDRSETSTT DTSKDDLSAN PKLHYPSVNG
QLPANTVIPY GRILDARYIE KEPLHYYDAN SSPSSPLSSS MSNISEKCDL DELESSQKKE
RKGNSLSRGS NSSSSLLTSR SPFTKLVEVI FARPRRHDVV PKRVSLYIDY KPHSSSHLKE
EDDLVEEILK RSYKNTRRNK SIFVIINPFG GKGKAKKLFM TKAKPLLLAS RCSIEVVYTK
YPGHAIEIAR EMDIDKYDTI ACASGDGIPH EVINGLYQRP DHVKAFNNIA ITEIPCGSGN
AMSVSCHWTN NPSYSTLCLI KSIETRIDLM CCSQPSYARE HPKLSFLSQT YGLIAETDIN
TEFIRWMGPA RFELGVAFNI IQKKKYPCEI YVKYAAKSKN ELKNHYLEHK NKGSLEFQHI
TMNKDNEDCD NYNYENEYET ENEDEDEDAD ADDEDSHLIS RDLADSSADQ IKEEDFKIKY
PLDEGIPSDW ERLDPNISNN LGIFYTGKMP YVAADTKFFP AALPSDGTMD MVITDARTSL
TRMAPILLGL DKGSHVLQPE VLHSKILAYK IIPKLGNGLF SVDGEKFPLE PLQVEIMPRL
CKTLLRNGRY VDTDFDSM
//
