ID T0M6A3_COLGC Unreviewed; 579 AA.
AC T0M6A3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 28-JAN-2026, entry version 42.
DE SubName: Full=Diacylglycerol kinase catalytic domain-containing protein {ECO:0000313|EMBL:EQB56405.1};
GN ORFNames=CGLO_03573 {ECO:0000313|EMBL:EQB56405.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB56405.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB56405.1}.
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DR EMBL; AMYD01000735; EQB56405.1; -; Genomic_DNA.
DR AlphaFoldDB; T0M6A3; -.
DR STRING; 1237896.T0M6A3; -.
DR eggNOG; KOG1116; Eukaryota.
DR HOGENOM; CLU_013399_0_1_1; -.
DR OMA; TIWTLYR; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000015530; 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:EQB56405.1};
KW Transferase {ECO:0000313|EMBL:EQB56405.1}.
FT DOMAIN 141..280
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 62485 MW; EFAB4C9F8A2BE079 CRC64;
MANNQSSPQT VPESISESSQ SYGKPASRGG LPDVIKVDGV KSLVLDSENL VLNDPTAKKT
SRTCSFASFG APAAPPTSTI PLYNVLWVEL AGQTLTIDYA KYVGKHRVQA AQWIFNVADA
DTPDVKTWAD NLLTRAYGPA KRCKRAKVLV NPHAGPGGAQ KKWDVDCEPL FKAARMPIDV
VKTERQGQAV DIAQAIDVDA FDTIVTCSGD GLAHEVFNGL GSRPDAFHAL QTIAVSHIPC
GSGNAMSCNL YGTYRPSLAA LAIIKGVETP FDLVSITQGD RRLLSFLSQA LGVVAESDLG
TEHLRWMGGA RFTVGFLQRI FQKKCYPCDL AVKVEIEDKH GVKEHYRQKM SNASATNLGE
GPNAAPVESG SSPDAHQGLP PLRYGTINDA LPEGWESISS DTMGNFYCGN MAYMAADANF
FAAACANDGL MDLVCVDGDV SVGSQLSMLL SVENGQFFDN PLVSYKKITA YRITPRNQKD
GYISIDGEKV PFEPFQAEIH QGLGKVISKR GGYEAAGPTN WDKITIGAVA PIDVTARAVA
WVAQAVRRQL HAFINGIVAC LTFSSYFFKI TFDGQQWLR
//
