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Database: UniProt
Entry: A0A0A2W6A9_BEABA
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ID   A0A0A2W6A9_BEABA        Unreviewed;       299 AA.
AC   A0A0A2W6A9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Putative lipid kinase YegS-like protein {ECO:0000313|EMBL:KGQ13990.1};
GN   ORFNames=BBAD15_g68 {ECO:0000313|EMBL:KGQ13990.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ13990.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ13990.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ13990.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KGQ13990.1}.
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DR   EMBL; ANFO01000008; KGQ13990.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2W6A9; -.
DR   STRING; 1245745.A0A0A2W6A9; -.
DR   HOGENOM; CLU_045532_1_1_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.200.40; -; 1.
DR   HAMAP; MF_01377; YegS; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR022433; Lip_kinase_YegS.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR045540; YegS/DAGK_C.
DR   NCBIfam; TIGR03702; lip_kinase_YegS; 1.
DR   NCBIfam; TIGR00147; YegS/Rv2252/BmrU family lipid kinase; 1.
DR   PANTHER; PTHR12358:SF106; LIPID KINASE YEGS; 1.
DR   PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR   Pfam; PF00781; DAGK_cat; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGQ13990.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..132
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   299 AA;  32267 MW;  11E69B77B37679B4 CRC64;
     MERSPHSFLI LNGKGAGNPQ LREAVHTLRE EGYVLHIRVT WEKGDAERYI EEALSLGADT
     VVAGGGDGTI NEIATCLAKL SPDRRPALGI LPLGTANDFA TSAGIPEEFE KALRLALFGK
     AANIDLVQVN EEAFFINMAT GGFGTRITTE TPEKLKAALG GVSYFIHGLM RMDMLKPDRC
     DIRGEGFSWQ GDALVIGIGN GRQAGGGQQL CPEALINDGL LELRIFTGED LLPALLTTLT
     RPDENPNIIE GKSAWFEISA PHDITFNLDG EPLSGRQFRI EVHPNALACR LPPNCPLLG
//
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