ID K1X500_MARBU Unreviewed; 501 AA.
AC K1X500;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 28-JAN-2026, entry version 45.
DE SubName: Full=Putative sphingoid long chain base kinase {ECO:0000313|EMBL:EKD15738.1};
GN ORFNames=MBM_05749 {ECO:0000313|EMBL:EKD15738.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD15738.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD15738.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD15738.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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DR EMBL; JH921440; EKD15738.1; -; Genomic_DNA.
DR AlphaFoldDB; K1X500; -.
DR FunCoup; K1X500; 576.
DR STRING; 1072389.K1X500; -.
DR KEGG; mbe:MBM_05749; -.
DR eggNOG; KOG1116; Eukaryota.
DR HOGENOM; CLU_013399_0_1_1; -.
DR InParanoid; K1X500; -.
DR OMA; QAWSRRI; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR GO; GO:0001727; F:lipid kinase activity; IEA:TreeGrafter.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-ARBA.
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 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 SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EKD15738.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Transferase {ECO:0000313|EMBL:EKD15738.1}.
FT DOMAIN 121..260
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 501 AA; 54955 MW; 33BEBB96F1109A91 CRC64;
MTTTLMPSDN PFVDPATSFE DAAHGNSFVR EATLTLGKDV SLTLGTDSLI VLDSANTRAI
PFYNVLWAEL EASELALQYA SPVSETIVRA ATLKYAVGHQ MVEVVNQWVY KLLDRSYGES
QPRKRVKVLV NPHSGKGSAG KLYHRDAEPL LKAANCTIDM VMTKYKGEAV EISEQLNIEA
FDVVASVSGD GLPHEVFNGL GKRLDAKKAL SKIAVVNIPA GSGNAMSCNL NGTDSPSLAT
LAIIKGIPTP LDLISVTQGE TRTLSFLSQS IGIVAESDLA TEHLRFLGSQ RFTYGFLIRL
INKALYPCDI AVKVAIDDKQ EIREHYKKEQ NNREPVTERR GYKHLLDDDA SASSGAEEGL
PLLRYGTVND KLPEGWELVP YDKLGNFYCG NMAYMTADAN FFSSALPNDG YMDLVCINGD
ISRIQTIKML LAVETGKFFD MPAVWYRKVL GYRIIPKNQE DGFISVDGER IPFQPFQAEV
HKGLGTVLSK SGHMYEAPGP V
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