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Database: UniProt
Entry: A0A074YBX0_AURPU
LinkDB: A0A074YBX0_AURPU
Original site: A0A074YBX0_AURPU 
ID   A0A074YBX0_AURPU        Unreviewed;       515 AA.
AC   A0A074YBX0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=sphingosine kinase {ECO:0000256|ARBA:ARBA00044037};
DE            EC=2.7.1.91 {ECO:0000256|ARBA:ARBA00044037};
GN   ORFNames=M438DRAFT_397077 {ECO:0000313|EMBL:KEQ84361.1};
OS   Aureobasidium pullulans EXF-150.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ84361.1, ECO:0000313|Proteomes:UP000030706};
RN   [1] {ECO:0000313|EMBL:KEQ84361.1, ECO:0000313|Proteomes:UP000030706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ84361.1,
RC   ECO:0000313|Proteomes:UP000030706};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584982; KEQ84361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074YBX0; -.
DR   STRING; 1043002.A0A074YBX0; -.
DR   HOGENOM; CLU_013399_0_1_1; -.
DR   OrthoDB; 374620at2759; -.
DR   Proteomes; UP000030706; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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   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   Kinase {ECO:0000313|EMBL:KEQ84361.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW   Transferase {ECO:0000313|EMBL:KEQ84361.1}.
FT   DOMAIN          136..275
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   515 AA;  56116 MW;  A1394314874B091A CRC64;
     MSERSLPVDN PFVDPSIHET PSALQGEATL FVAEDASLTL GADSLIILDD RFVHREAANC
     CGLLPTRSKT THSIPHYNIL DASLDDLELT IQHALPTSKT SCRPSTISYT LIDKSSINAA
     KSWLAKLLDL AYGNSQRNKR IKVLVNPFGG QGAARKLYAS EVEPLLRAAG CEIDAQETTH
     SGHAVEIARQ LNVDAYDVVA CASGDGLPHE VFNGLAQQQK PRRALRKVAV VQLPCGSGNA
     MSINLNGTNS PSFAALAIVK GLRTPLDLMA VTQGEKMYWS FLSQAVGIIA DCDLGTENMR
     WMGSARFTVG ILTRLLGKTV YPAELAVKVD IDDKQAIKAA YSHVRSQRED VSGRREWEAH
     QDLDGDKHDS LPALQYGSVL QDVPSDWEKA SLPTLGNFYC GNMAYMSPDT PFFAAALPSD
     NHIDMVNVDG AIPRLKALDM ILAVEQNKMF DMDVVNYRKV SAYRISPKLR PGQKVGYISI
     DGEKVPFEPF QVEIVGGLGT VLSRNGAVYE FEGPK
//
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