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Database: UniProt
Entry: A0A0D2D3V4_9EURO
LinkDB: A0A0D2D3V4_9EURO
Original site: A0A0D2D3V4_9EURO 
ID   A0A0D2D3V4_9EURO        Unreviewed;       591 AA.
AC   A0A0D2D3V4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-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=PV06_10873 {ECO:0000313|EMBL:KIW36975.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW36975.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW36975.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW36975.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847347; KIW36975.1; -; Genomic_DNA.
DR   RefSeq; XP_016257191.1; XM_016412466.1.
DR   AlphaFoldDB; A0A0D2D3V4; -.
DR   STRING; 215243.A0A0D2D3V4; -.
DR   GeneID; 27362947; -.
DR   VEuPathDB; FungiDB:PV06_10873; -.
DR   HOGENOM; CLU_013399_0_1_1; -.
DR   OrthoDB; 374620at2759; -.
DR   Proteomes; UP000053342; 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:UP000053342}.
FT   DOMAIN          139..278
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          346..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  63960 MW;  E2058088876A6F8A CRC64;
     MAGDRRSESN PFSDNAAIQD EREAMVESTL SVGRNATLTL GTDAVIVLDD GLRGDSGFDC
     FGLFKRTTNT RSIPFFNVLW AELVKGELTI RYAKPSSKSA NAPVSVAYIN YTIESTTAVE
     EKALRWIDRL LDRAYGKAQR NKRIKLLINP FGGAGKAAKI YAKAIEPIFA AARCELDVER
     TTHSGHAVEI CADLDINAFD VVASASGDGL PHECVNGLAR KPNAAEALRK VAVVQLPCGT
     GNAMSWNLTG TAEPSAAALC IVKGIRTPMD LASVTQGNTR TLSFLSQSLG IVAESDLGTE
     NIRWMGDARF TFGFLVRLLG KTLYPIELAV KTEIENKEDI RRHYAEHRAR RRSQGSALSH
     DDLDGPLDTS TGLGLPPLKY GTVEDPLPEN EGWTPMAYYP NMGNFYCGNM AMMAADAPFF
     PASLPCDGLL DLITIDGDIK RTKAVDLLLS VPKGTFFDKE CVRYRKVSAI RVVPKFGNMV
     DQSDNEARQN KLGKVLDRMG VSGNGRNASR DGGYFSVDGE KLPFQPFQVE VHKGLATVLS
     KNVGMYECMG PRGWEDVPVS TTTTGHVSTS ASGTASGPGH DADDTDVRGQ L
//
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