ID A0A395NEV9_TRIAR Unreviewed; 527 AA.
AC A0A395NEV9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Sphingosine kinase {ECO:0000313|EMBL:RFU74303.1};
GN ORFNames=TARUN_7930 {ECO:0000313|EMBL:RFU74303.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU74303.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU74303.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU74303.1,
RC ECO:0000313|Proteomes:UP000266272};
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:RFU74303.1}.
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DR EMBL; PXOA01000550; RFU74303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395NEV9; -.
DR STRING; 490622.A0A395NEV9; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000266272; 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:RFU74303.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000266272};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 153..292
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 527 AA; 56796 MW; EE8532DBA977FAEB CRC64;
MQDAVPLADM ENGAKRMGAS EAIGLRLGLG GNKTLTIGEK DLVLFDPDGK NHKKSSNGKA
SSGKQLLEDL SCFNCLPSRS ADGKGKHTIP LYNILWAELR GDALVVDYAA PRKSSLKLQK
WTFAIPTQDA EAGGPSPESF VSALVSAAYG EAKPRKRAYV LINPNSGPGG ALGKWKKHVK
PLFEAARMEL EVVNLSRGGE ATELTEKADI EKYDTIMALS GDGTPFEIFN GLGRRPDAAK
ALAKIAVSHI PCGSGNAFSL NCNGSNNDAV AALAVVKGVV MPLDLVSVTQ GDRRTLSFLS
QTVGIIAESD LGTENLRWMG STRFEVGLVT RVLKKKCYPF DLSVKVEIEG KEMIKQHYKK
YAVDPSLLNV DAEAETGGAE GLPKLKYGTV QDEIPSDWET ASHDNVGTFY VGNMAYMSSD
ANFFSAAVPT DGLMDMVMIR ADISPVAVTK AFLSVETGKF FDNPNVTYKK VSAYRITPRN
QESGYISIDG ERIPFEPFQA EIHRGLGRVI SKRGVYEAAG PAGWEKA
//
