ID A0A8H4MDY6_9EURO Unreviewed; 492 AA.
AC A0A8H4MDY6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=CNMCM6805_004632 {ECO:0000313|EMBL:KAF4240828.1};
OS Aspergillus fumigatiaffinis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=340414 {ECO:0000313|EMBL:KAF4240828.1, ECO:0000313|Proteomes:UP000653565};
RN [1] {ECO:0000313|EMBL:KAF4240828.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM6805 {ECO:0000313|EMBL:KAF4240828.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:KAF4240828.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM6805 {ECO:0000313|EMBL:KAF4240828.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) 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:KAF4240828.1}.
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DR EMBL; JAAAPX010000024; KAF4240828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8H4MDY6; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000653565; 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:UP000653565}.
FT DOMAIN 106..244
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 492 AA; 53844 MW; D498441CAB88668D CRC64;
MEITDSSSPA GIRLDLEGGG MLTIGTDHLE LHASPETQFI PLYNILWAKV SNNEITIDFV
QHTSKSLVEP RNLTFRLGSN NPDGPDGSFA ESFRRVLLAR AYREAKSRKC AYVLINPNSG
PGRAMRLWRN EVKPIFDAAR MELHVVVLGR GGEPAELAEK VDLRKYDTIL ACSGDGTVHE
IFNGLGNRPD ARHALASMPV SHIPCGSGNA FSCNLYGSHR ASFAALAIVK GIVAPIDLIS
VTYGESRILS FLSQTVGIIA ESDLDTEHLR WMGSARFQFG VIQRVFKRVC YPCDVALKVD
IEDKAGIKAH YRRHASSTRL TKATTDDSTK ASLAAECGLP KLKYGTVQDL VPEGWKLVSD
DGMGTFYAGN MAYMSPNVNL FSASNMTDGL VDVITIDGDL SPVTALRVMS QTDSPRFFDH
PYVKYRKVSA YRITPRNQDD GCISIDGERI PFGPFQAEVH QGLGRVISKS GKYEAEGPAN
WDNATIADRI PG
//