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Database: UniProt
Entry: A0A0D1YCZ4_9EURO
LinkDB: A0A0D1YCZ4_9EURO
Original site: A0A0D1YCZ4_9EURO 
ID   A0A0D1YCZ4_9EURO        Unreviewed;       575 AA.
AC   A0A0D1YCZ4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, 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=PV08_08023 {ECO:0000313|EMBL:KIW12836.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW12836.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW12836.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW12836.1,
RC   ECO:0000313|Proteomes:UP000053328};
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 spinifera CBS89968.";
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; KN847497; KIW12836.1; -; Genomic_DNA.
DR   RefSeq; XP_016233052.1; XM_016382349.1.
DR   AlphaFoldDB; A0A0D1YCZ4; -.
DR   STRING; 91928.A0A0D1YCZ4; -.
DR   GeneID; 27335106; -.
DR   VEuPathDB; FungiDB:PV08_08023; -.
DR   HOGENOM; CLU_013399_0_1_1; -.
DR   OrthoDB; 374620at2759; -.
DR   Proteomes; UP000053328; 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:UP000053328}.
FT   DOMAIN          145..284
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   575 AA;  62253 MW;  38E186A4198AFBB8 CRC64;
     MAGDRHSQSD PFSDTAAIQD EREAIVESTL GVGRNATLTL GTDAVIVLDD GLRGNSGFDC
     FGLFKRTTNT HSIPYFNVLW AELVKGELTI QYAKPTSKSS SSSNNNNTPV RVAYINYTIE
     STTAVEERAL RWIERLLQRA YGKAQRKKRI KLLINPFGGA GKAAKIYAKA IEPIFAAARC
     ELDVERTTHT GHAVEICEKL DINAFDVVAS ASGDGLPHEC INGLARKSNA AEALRKVAVV
     QLPCGTGNAM SWNLTGTGEP STAALGIVKG IRTPMDLASV TQGSTRTLSF LSQSLGIVAE
     SDLGTENIRW MGDARFTYGF LVRLIGKTVY PIELAVKTEI EEKDDIRRHY AEHMAAARRR
     NQAGIALSRD DLDGPLDTST GLGLPPLKYG TVDDPLPGSD EGWTPMTSYP NMGNFYCGNM
     AMMAADAPFF SASLPCDGLL DLITIDGDIP RTTAVGLMLS VPKGTLFDQE CVRYRKVSAI
     RVVPKFGNMA KRSENEARQN KMGQLLDRMG VSGNGRNASR DGGYFSVDGE KLPFQPFQVE
     IHKGLGTVLS KNVGMYECMG PKGWEDVVVG TNGTV
//
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