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Database: UniProt
Entry: A0AAF0IFB5_9EURO
LinkDB: A0AAF0IFB5_9EURO
Original site: A0AAF0IFB5_9EURO 
ID   A0AAF0IFB5_9EURO        Unreviewed;       462 AA.
AC   A0AAF0IFB5;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   SubName: Full=Sphinganine kinase lcb4 {ECO:0000313|EMBL:WEW55825.1};
DE            EC=2.7.1.91 {ECO:0000313|EMBL:WEW55825.1};
GN   Name=LCB4 {ECO:0000313|EMBL:WEW55825.1};
GN   ORFNames=PRK78_001258 {ECO:0000313|EMBL:WEW55825.1};
OS   Emydomyces testavorans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Nannizziopsiaceae; Emydomyces.
OX   NCBI_TaxID=2070801 {ECO:0000313|EMBL:WEW55825.1, ECO:0000313|Proteomes:UP001219355};
RN   [1] {ECO:0000313|EMBL:WEW55825.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=16-2883 {ECO:0000313|EMBL:WEW55825.1};
RA   Hoyer L.;
RT   "Emydomyces testavorans Genome Sequence.";
RL   Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP120627; WEW55825.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAF0IFB5; -.
DR   Proteomes; UP001219355; Chromosome 1.
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:0008481; F:sphingosine kinase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:WEW55825.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP001219355};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:WEW55825.1}.
FT   DOMAIN          95..234
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   462 AA;  50954 MW;  01DBE20C55C0C64B CRC64;
     MTLGSLLDCD RSPDGYSSSE EEQLQLPQTR RHTIPYFNVL WADISHEYLT IKYAEPTSGD
     DVSVASVYYA VNPEQKSKAE TWTEELLKLA YGDAQRKKRI KILINPFGGK GRAGKQYYKD
     VEPIFAAARC EVDVETTTHQ GHAVEIAQDI DISAYDVIAP ASGDGVIYEV FNGLGKRADA
     GDALAKLAVA HIPCGSGNAM SWNLYGTGSP SMAALSIVKG LRTPLDLVSI TQGDRRTLSF
     LSQSFGIVAE SDLGTDNIRW MGSARFTYGF LVRLFGKTVY PCDLAVKVEV GDKERIKDHY
     RAESKQRSGS VSEDEYRSVG LPPLRYGTVN DPLPDDWQLT THDKMGNFYA GNMGYMAPDA
     NFFPTALPND GLLDLITIRG DIPRLTALQM LMAVESGTLL DMPEVNIQKV SGYRIIPRER
     KEGYISIDGE KVPFEPFQAE VHKGLGMVIS KSGYKYENPG VQ
//
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