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Database: UniProt
Entry: A0A0F4G935_9PEZI
LinkDB: A0A0F4G935_9PEZI
Original site: A0A0F4G935_9PEZI 
ID   A0A0F4G935_9PEZI        Unreviewed;       538 AA.
AC   A0A0F4G935;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   28-JAN-2026, entry version 26.
DE   SubName: Full=Sphingosine kinase like protein {ECO:0000313|EMBL:KJX93876.1};
GN   ORFNames=TI39_contig4244g00021 {ECO:0000313|EMBL:KJX93876.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX93876.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJX93876.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJX93876.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KJX93876.1}.
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DR   EMBL; LAFY01004203; KJX93876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4G935; -.
DR   STRING; 1047168.A0A0F4G935; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000033647; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR   GO; GO:0001727; F:lipid kinase activity; IEA:TreeGrafter.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-ARBA.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IEA:TreeGrafter.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR055916; DUF7493.
DR   InterPro; IPR050187; Lipid_Phosphate_FormReg.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   PANTHER; PTHR12358:SF31; ACYLGLYCEROL KINASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF24321; DUF7493; 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:KJX93876.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033647};
KW   Transferase {ECO:0000313|EMBL:KJX93876.1}.
FT   DOMAIN          136..275
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   538 AA;  59140 MW;  9FF3E02C95BED6F3 CRC64;
     MHNHVHNPFD DPAGSDTSLE SNEAVLTVDR NATLTLATDA LIVLDEGLRH RRAASNCCGL
     LPQLSKTTRA IPFHNVLWAE LNDFDVNVHY TQSVGRKSKG CRVALITYNV TDKSTHAHAK
     RWVENLLARA YPPNTQRRKR IKVLINPFGG QGYAEKSWRK EIEPIFAAAS CVVDVERTQY
     RGHAVEIAQN LDIDAYDVVA CASGDGLPHE VFNGLAKHKT PKLALRKIAV VQLPCGTGNA
     MSLNLSGTDS ASLASLEIIK GTRTPLDLIA ITQGDKTYYS FLSQAVGIIA ESDLGTDNLR
     WMGSFRFTWG ILVRLLGKTI YPAEVSLVVD SDDKRVIKET YRQVAEEHEA ARAKHLRRAT
     YEDDLPQGDN AQLPELRFGT VTDPLPSNFA TQDIANLGNF YVGNMCYMSG DAPFFTATLP
     SDGKMDMVIA PGDMARMTAI RMLTTVEQGT LIDFPEISYS KVLAYRITPR MAPVPTERRL
     RSKVGRWLGG ASKQKEGLIS IDGEQVPFEP FQAEVVPKLG TVLSKSGAIY EIGGLAPL
//
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