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Database: UniProt
Entry: A0A436ZVZ8_9PEZI
LinkDB: A0A436ZVZ8_9PEZI
Original site: A0A436ZVZ8_9PEZI 
ID   A0A436ZVZ8_ARTFL        Unreviewed;       495 AA.
AC   A0A436ZVZ8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JAN-2026, entry version 19.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=DFL_007426 {ECO:0000313|EMBL:RVD83022.1};
OS   Arthrobotrys flagrans (Nematode-trapping fungus) (Trichothecium flagrans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Arthrobotrys.
OX   NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD83022.1, ECO:0000313|Proteomes:UP000283090};
RN   [1] {ECO:0000313|EMBL:RVD83022.1, ECO:0000313|Proteomes:UP000283090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD83022.1,
RC   ECO:0000313|Proteomes:UP000283090};
RA   Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT   "Intercellular communication is required for trap formation in the
RT   nematode-trapping fungus Duddingtonia flagrans.";
RL   Submitted (JAN-2019) 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:RVD83022.1}.
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DR   EMBL; SAEB01000009; RVD83022.1; -; Genomic_DNA.
DR   RefSeq; XP_067488566.1; XM_067637007.1.
DR   AlphaFoldDB; A0A436ZVZ8; -.
DR   STRING; 97331.A0A436ZVZ8; -.
DR   GeneID; 93589737; -.
DR   VEuPathDB; FungiDB:DFL_007426; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000283090; 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:UniProtKB-ARBA.
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:UP000283090}.
FT   DOMAIN          133..272
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   495 AA;  54308 MW;  716BFB7C5A208B7E CRC64;
     MSSEHQGLVT STSHDGVGIS PEDALLLDTH SLVIREDRVT IADKRKSSKR DASCCGIAGT
     GRPSDELVTL HNILWARVYI SEDKSAVQIT SAKEVSSRLV KPTTISIPID DNDLEKADRW
     VERLLEKAYE GSQQAKRFKV LINPHGGPGT AEKIYKTEIE PIFTAASCHI DVECTQYSQH
     AIKIAQELDI EAYDAVVCIS GDGVPHEVFN GLAKRPDARK ALNKIAVCQL PGGSGNGMCW
     SFTGTDSPSL AAVALVKGKR TPFDLISVTQ GDRRILSFLS QSVGLTAELD LGTENMRWMG
     NTRFTVGFLQ RVVTERIYPS EIHVKLAIES KEEIRRNAST VRLPPDGEHE GEGLPPLQYG
     TVNDPVPDDW VAESHPKMGN FYCGNMICMS KDIHFFPAAK PNDGHMDLAT MDGDVGRLKA
     VSVMLGAETG KHFDIPELNY RKVLAYRFTP KSQKDGYISI DGEKVVFAPF QAEIHHGLGV
     SLSLRPNVYE GPILV
//
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