ID A0A2I2F1W7_ASPCN Unreviewed; 557 AA.
AC A0A2I2F1W7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE SubName: Full=Sphingosine kinase {ECO:0000313|EMBL:PLB34633.1};
GN ORFNames=BDW47DRAFT_72729 {ECO:0000313|EMBL:PLB34633.1};
OS Aspergillus candidus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=41067 {ECO:0000313|EMBL:PLB34633.1, ECO:0000313|Proteomes:UP000234585};
RN [1] {ECO:0000313|EMBL:PLB34633.1, ECO:0000313|Proteomes:UP000234585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102.13 {ECO:0000313|EMBL:PLB34633.1,
RC ECO:0000313|Proteomes:UP000234585};
RG DOE Joint Genome Institute;
RA Haridas S., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Mondo S., Lyhne E.K.,
RA Kogle M.E., Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C.,
RA Chiniquy J., Barry K., LaButti K., Simmons B.A., Magnuson J.K.,
RA Mortensen U.H., Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ559175; PLB34633.1; -; Genomic_DNA.
DR RefSeq; XP_024668645.1; XM_024819699.1.
DR AlphaFoldDB; A0A2I2F1W7; -.
DR STRING; 41067.A0A2I2F1W7; -.
DR GeneID; 36526859; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000234585; 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, ECO:0000313|EMBL:PLB34633.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000234585};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..557
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014117071"
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 191..330
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 53..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 60691 MW; 1A12BA1197843D43 CRC64;
MSFFFLLLLP PPLSSLSPLF LLSLLLFLFV STPLLFFLWR ALYDALFPSR RTMTSPSPNG
ASRPPLTHPD QPDSQQHLLA HDASLTVAQS VSLTLAGDSL IVLDERPSRQ ADRTCCGLLP
LSAPQETHSI ALFNILDADL TPTDLTITYA APQPKSEISV ATLHYPVAQK EKAQIEKWVA
KLLDLAYGAA QRHRRLKVLI NPFGGQGGAR KLYHKYAESV FAATGCRLDV QETTHRGHAT
EIAENIDVDA YDAIVCCSGD GLPYEVFNGL AKKPNAREAL AKVAVAMLPC GSGNAMSWNL
YGTGSVSVAA LTIAKGVQTP IDLVSLTQGQ TRTLSFLSQS FGIVAESDLG TDDIRWMGAH
RFTYGFLVRL MRRTIYPCDL AMKVVLDDKK AIKDHYEEYA GRPAPGRPDE VPAGGLPELQ
YGTVQDELPS DWEVIPGETM GNFYAGNMAI MSKDTSFFPA AVPQDGLMDV VTIDGTVSRS
TSIKMMTSIP EGTFFDMPDV HVRKVAAYRL IPRETEGYIS VDGESVPFEG IQAEVHQGLG
TVLSKSGHLY ETDGPRP
//
