ID A3LPP9_PICST Unreviewed; 521 AA.
AC A3LPP9;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 28-JAN-2026, entry version 86.
DE SubName: Full=Sphingosine kinase, involved in sphingolipid metabolism Lipid transport and metabolism {ECO:0000313|EMBL:ABN65078.2};
GN Name=SPH1 {ECO:0000313|EMBL:ABN65078.2};
GN ORFNames=PICST_54239 {ECO:0000313|EMBL:ABN65078.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN65078.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN65078.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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DR EMBL; CP000496; ABN65078.2; -; Genomic_DNA.
DR RefSeq; XP_001383107.2; XM_001383070.1.
DR AlphaFoldDB; A3LPP9; -.
DR FunCoup; A3LPP9; 625.
DR STRING; 322104.A3LPP9; -.
DR GeneID; 4837053; -.
DR KEGG; pic:PICST_54239; -.
DR eggNOG; KOG1116; Eukaryota.
DR HOGENOM; CLU_013399_0_1_1; -.
DR InParanoid; A3LPP9; -.
DR OMA; QAWSRRI; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
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:ABN65078.2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 134..277
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 521 AA; 58316 MW; 801CFAE57EE82F7F CRC64;
MTLHNNLSTE RLIYHQQDSI RATLQDFGIQ IDSQELLAIE DDSVDSTYSF CSWKSAPDNR
SRIPYRNILW VQPVIDETGQ VQEDDLEITY VKPKGKLSLE PVTLRISIQN YRALYNNLQE
LSNSILAKSY KNHIVKPSVL VIINPHGGQG KALKIYNTEI KPILKAARAK ITIQETSYHK
HGIDIGRELD ISKYDVIACC SGDGIPHEII NGFYERPDKG VSAFNKIAIT QLPCGSGNAL
SLSTHGSNDA SMATFHMLKA KRTKLDLMAV TQGVGPNEKI KLSFLTQCYG VIADADIGTE
HLRWMGAIRF DVGVLHGILA RRKFPCELYV DFLTNSKQEL SAHFDTYHQN SNSTAARIEH
HSQDDGELPL LNEERLQVKG PKLNHPPPES WTKISQNISD NVNILYVGKM PYISNDVQFF
PAALPNDGSM DMILTDTKTS VMETASILMS LDKGLHVHNE KVHHAKISSY RLIPKIPRNE
QHYISVDGES FPFEPLQVEV LPGVLTGLLQ GGNFVDTCFS R
//
