ID B6QR21_TALMQ Unreviewed; 504 AA.
AC B6QR21;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 28-JAN-2026, entry version 64.
DE SubName: Full=Sphingosine kinase (SphK), putative {ECO:0000313|EMBL:EEA20423.1};
GN ORFNames=PMAA_042660 {ECO:0000313|EMBL:EEA20423.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA20423.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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DR EMBL; DS995904; EEA20423.1; -; Genomic_DNA.
DR AlphaFoldDB; B6QR21; -.
DR STRING; 441960.B6QR21; -.
DR VEuPathDB; FungiDB:PMAA_042660; -.
DR HOGENOM; CLU_013399_0_1_1; -.
DR OrthoDB; 3853857at2759; -.
DR PhylomeDB; B6QR21; -.
DR Proteomes; UP000001294; 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:EEA20423.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 134..273
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 504 AA; 55003 MW; 1420AA6DA0F18736 CRC64;
MSVDEIPVDA SSAKMTASDI GEVRPDLSLE VENNVTLTLQ SDALFINDPK TKKDVRYCGL
QVVTSTASQS IPFYDILSAQ ISDSALILKY AKPVVKDDYA PSTVTYALDI SQTTPAKVEA
WVEQLLKSAY GQAQRNRRLR VLINPHGGKG YAKDLYNEYA APMFEAAGCK VDLEMTKYAG
HATDIAEKMD IDAYDAILCC SGDGLPYEVL NGFAKRSNAA EALAKVAVAM IPCGSGNAMA
WNLFGTNSVS LSALSVIKGL RTHMDLVSLT QTGTRTLSFL SQSYGIVAES DLGTNHLRWM
GAARFTYGFL TRLLRQATYP CDIAFKLETD SKQTMKERYL EYKKQKPSLR PVGGSEEVIG
QGLPTLKYGT VDDEVPSDWH KISTDTLSNF YAGNMAIMTA DANIFPATVP NDGLIDVVMI
DGAIGRLRAL SMMTAVENGG FFDYPEVEVR KVHAYRLTPR GSNDGYISVD GERIPWQPFQ
VEVHPGLGTV LSKSGHLYEA QGPI
//
