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Database: UniProt
Entry: A0A2B7WL83_9EURO
LinkDB: A0A2B7WL83_9EURO
Original site: A0A2B7WL83_9EURO 
ID   A0A2B7WL83_9EURO        Unreviewed;       495 AA.
AC   A0A2B7WL83;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   28-JAN-2026, entry version 30.
DE   SubName: Full=Sphingosine kinase {ECO:0000313|EMBL:PGH00134.1};
GN   ORFNames=GX51_05947 {ECO:0000313|EMBL:PGH00134.1};
OS   Blastomyces parvus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH00134.1, ECO:0000313|Proteomes:UP000224080};
RN   [1] {ECO:0000313|EMBL:PGH00134.1, ECO:0000313|Proteomes:UP000224080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH130 {ECO:0000313|EMBL:PGH00134.1,
RC   ECO:0000313|Proteomes:UP000224080};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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:PGH00134.1}.
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DR   EMBL; PDNC01000090; PGH00134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7WL83; -.
DR   STRING; 2060905.A0A2B7WL83; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000224080; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0001727; F:lipid kinase activity; IEA:TreeGrafter.
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   InterPro; IPR045540; YegS/DAGK_C.
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   Pfam; PF19279; YegS_C; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PGH00134.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224080};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          126..265
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   495 AA;  54283 MW;  0E43474E2396C3E9 CRC64;
     MTVGTTVLEA GPSGNKGTKS AVEDVRHPSS ESSATLDVGK NALLTLAADA VIVAESSGAR
     TTLSIPYANI LWAEVSHDYI TIKYAHQVTK TDVTLRSVLY PVTLEQKSKA ETWTEKLLDS
     AYGKAQRQKR IKVLINPFGG KGRAAKSYYK HVEPIFTAAK CQVDVELTNY RGHAVEIVEK
     LDIDAYDVVA ACSGDGIPYE VFNGLAKKPN ASEALRKIAV ANVPCGSGNA MSWNLNGTGS
     ASLAALWIIK GLRTPLDLVS ITQGDKRTLS FLSQSFGIVA ELDLGTDHIR WMGQARFTYG
     YLVRLFGKIV YPCDLAVKVE LDNKEQIKDH YRAGSERKSF DQLRDEESSN CVGLPPLRYG
     TVNDPLPEGW TLVPHDKLGN FYAGNMAYMA ADSNFFPTAL PNDGCMDLIT INGDISRKTA
     IQMFMTLDSG ALFDMPEVNV RKVTAYRIIP RDRKDGYISI DGERVPFEPF QAEVHRGLGT
     VLSKSGYRYE TNGLK
//
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