ID A0A2T3B388_AMORE Unreviewed; 513 AA.
AC A0A2T3B388;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=M430DRAFT_18286 {ECO:0000313|EMBL:PSS20108.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS20108.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS20108.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS20108.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(2018).
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DR EMBL; KZ679010; PSS20108.1; -; Genomic_DNA.
DR RefSeq; XP_024721378.1; XM_024863833.1.
DR AlphaFoldDB; A0A2T3B388; -.
DR FunCoup; A0A2T3B388; 602.
DR STRING; 857342.A0A2T3B388; -.
DR GeneID; 36571914; -.
DR InParanoid; A0A2T3B388; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000241818; 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 Reference proteome {ECO:0000313|Proteomes:UP000241818}.
FT DOMAIN 133..272
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 56019 MW; D05D6F099CCB81DD CRC64;
MATDNPFRDP ATSSDELGRD NSVTMDSTLA VGRDASLSLG TDSLVVLDEA FENGGIGCCG
LWPSGTANTR SVPFYNILWA ELQGDVLSID YAASLSKTTV RPATLKYPVE KPDLDRVNKW
LGKLLDRSYG EAQRRKRAKI LVNPYSGKGS AEKWYRRDVE PLLKAARCSI DMVKTRYRGE
AVEIAEKMDI DAFDTVVACS GDGLPHEVFN GLGKRADAKK ALSKMAVSHI PCGSGNAMSC
NVNGTNSASL ATLAIIKGIP TPLDLISITQ GETRTLSFLS QSVGIVAESD LATENLRWMG
SARFTYGFLV RLLGRTVYPC DLAVKVAIED KPSIKEHYGK EQDNDEPASE RRGYKTLLDD
DASASSGNED GLPALRYGTV NDKLPEGWEL IPYDKMGNFY CGNMAYMAAD TNFFQCALPN
DGYMDLVCIN GDISRLAAIQ MMLAVENGKF FDNPLVSYRK ILGYRIIPKN QKDGYISIDG
ERVPFQPFQA EVHKGLGTVL SRTGHMYAAP GPL
//