ID A0A395M4G2_9HYPO Unreviewed; 290 AA.
AC A0A395M4G2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Sphingosine kinase {ECO:0000313|EMBL:RFN40973.1};
DE Flags: Fragment;
GN ORFNames=FIE12Z_13012 {ECO:0000313|EMBL:RFN40973.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN40973.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN40973.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN40973.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFN40973.1}.
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DR EMBL; PXXK01000913; RFN40973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395M4G2; -.
DR STRING; 2594813.A0A395M4G2; -.
DR Proteomes; UP000265631; 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:RFN40973.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW Transferase {ECO:0000313|EMBL:RFN40973.1}.
FT DOMAIN 74..213
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFN40973.1"
FT NON_TER 290
FT /evidence="ECO:0000313|EMBL:RFN40973.1"
SQ SEQUENCE 290 AA; 31529 MW; 604855F0490DBA39 CRC64;
GASKDTGPFY SVLWAEVVDN HITIDYAIHA SKKLIKPGKW EFELAADDED EENSATPTET
FVKTLLSRAY GDAPPRKRAY VLVNPNSGPG KAVKQWENEV KPLLDAAKMQ LDVVILKRGG
EAVELAQNAD LSRYDTIMAC SGDGTPHEVF NGLAKRPDAA KALSTMAVSH IPCGSGNAFS
CNLYGSNHPS FAALAIIKGI VTPLDLVSVT SGNNRIISFL SQSLGLIAEC DLGTENMRWM
GSARFEVGVV QRMYKKKCYP FDLAVKVEIE EKEGVKAHYK HHASTTSLAQ
//
