ID A0A2G7FY91_9EURO Unreviewed; 464 AA.
AC A0A2G7FY91;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=AARAC_007328 {ECO:0000313|EMBL:PIG85558.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG85558.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG85558.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG85558.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-2017) 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:PIG85558.1}.
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DR EMBL; NEXV01000314; PIG85558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G7FY91; -.
DR STRING; 656916.A0A2G7FY91; -.
DR Proteomes; UP000231358; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000231358};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 104..244
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 464 AA; 52037 MW; 223E240D7AF02F0A CRC64;
MEPLSQTAPE VRFAQIELSE EGLTIRQGQT CFAQQKLRQV QYLHVLWAQA TAEHLAIYYV
EERRKTLRVV KAVFQLVNNG FPSPSFQLQA WVRSLLDRAY GKSKLRARLK VYLNPFSGKG
SAVQLYRRYA EPIFAAAQCS VDLRETCHAG HAGQMVREDP EIDSWDAIVC CSGDGLPYEV
INGIALRGDA GHVLRKTPII QLPGGSGNAL CVNMFKTTSV SHAALYTLKG IRQPIDLMSV
TQGDRRYLSF LSQSIGLLAE CDLDTEDMRF LGGKRFAFGF FQRLFKPPLY DCDIAVQHPA
LHQPTESHSI GVIDQATGRR KEGLPNLQFG SVSDSLSESW GLEHHPDLSL FFAGQFPFMD
AKSKVFPDAR PNDGLVDIIL VDRGIGARKF LQLFRKIFRG NHLAMREVHH RKVSAYRVTP
ARTCGAMSVD GERSDFQPFQ VEVHPQLGMT LIKPPGIMEH HCNR
//
