ID   A0A165GAQ5_EXIGL        Unreviewed;       463 AA.
AC   A0A165GAQ5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=sphingosine kinase {ECO:0000256|ARBA:ARBA00044037};
DE            EC=2.7.1.91 {ECO:0000256|ARBA:ARBA00044037};
GN   ORFNames=EXIGLDRAFT_750735 {ECO:0000313|EMBL:KZV90236.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV90236.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV90236.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV90236.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KV426053; KZV90236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165GAQ5; -.
DR   STRING; 1314781.A0A165GAQ5; -.
DR   InParanoid; A0A165GAQ5; -.
DR   OrthoDB; 374620at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT   DOMAIN          97..237
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   463 AA;  50555 MW;  22F4B2835429B549 CRC64;
     MAESEAESEL KATVGGKPGA LRLSRKQSSL LVQAGGKKTE VPLSQVVWAE ANEGNVLVSA
     LVRKGNLALV NWHCECDAAA AKPWVEELMR AAYGDVKPRR RLKIIINPVG GPGRGRQIWE
     KRAKPVFDAA HAELDVTFTE RQGHAGDIAE SLPLDFDAVV TVSGDGLLHE VLNGFAKRPD
     ARKAMQIPVA PLPTGSGNGF ALSLIGLKDG LDPAAAALNV IKGQPMDLDL CSFTQAGKTY
     YSFMSQSMGL MADVDLGTEH LRWMGNARFM YGFLRGLVSL KECPVELSIK VSDTDKKKMV
     DTHRALRSKR VASASRPDLT DTNVEDLEDS SLPELRFADG PDHEWITFEK PVLYVYAGKM
     PYVSVDLLQF PVSHANDGLI DLVVQERTQR GDLVKAIGVA PKGGQYWIDS QHYFKVHAYR
     AKPLGPGYLS VDGEAYPWEE FQVEAHAGLA TTLSMLGHYA VDF
//