ID A0A0G2ID50_9EURO Unreviewed; 494 AA.
AC A0A0G2ID50;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=sphingosine kinase {ECO:0000256|ARBA:ARBA00044037};
DE EC=2.7.1.91 {ECO:0000256|ARBA:ARBA00044037};
GN ORFNames=EMCG_01037 {ECO:0000313|EMBL:KKZ68587.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ68587.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(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:KKZ68587.1}.
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DR EMBL; LCZI01000091; KKZ68587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2ID50; -.
DR VEuPathDB; FungiDB:EMCG_01037; -.
DR Proteomes; UP000034164; 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, ECO:0000313|EMBL:KKZ68587.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 125..264
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 54428 MW; 545B9EA7B6232E77 CRC64;
MTFGTRFEAG PSRSKGTPSS LEDLFHPNPE SSATLSVGKN AFLTLASDAV VVVGKYQPGI
ARSIPYYNIL WAEVSHDYIT IKYADQVTKT DVTLSSVHYL VNLEHKSKAE TWTEKLLDSA
YGKAQRQKRI KILVNPFGGK GRAAKQYYKH VEPIFAAAKC QIDAESTNYR GHAVDIVEKI
DVDAYDVIAA CSGDGIPYEI FNGLAKKPNA GEALRKIAVA HIPCGSGNAM SWNLNGTGSA
SLAALRIVKG LRTPLDLVSI TQGDKRTLSF LSQSFGIVAE TDLGTDHIRW MGQARFTYGF
LVRLFGKTVY PCDLAVKVEL DNKEQIKDHY RAGSERKSFD QLRDEGLSDT VGLPPLRYGT
VNDPLPEDWT LVPHDKLGNL YAGNMAYMTA DANFFPTALP NDGCMDLITI DGDISRRTAV
QMLMAVDNGT LFDMPEVNVR KVTGYRVIPR DRKEGYISID GEQVSFEPFQ AEVHRGLGTV
LSKSGYRYET NGLK
//
