ID A0A165FVD2_9APHY Unreviewed; 499 AA.
AC A0A165FVD2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=LAESUDRAFT_694967 {ECO:0000313|EMBL:KZT09459.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT09459.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT09459.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT09459.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV427611; KZT09459.1; -; Genomic_DNA.
DR RefSeq; XP_040767199.1; XM_040906222.1.
DR AlphaFoldDB; A0A165FVD2; -.
DR FunCoup; A0A165FVD2; 170.
DR STRING; 1314785.A0A165FVD2; -.
DR GeneID; 63823251; -.
DR InParanoid; A0A165FVD2; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000076871; 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 Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT DOMAIN 106..247
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 336..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 54505 MW; 09D74F25C62FF46F CRC64;
MTASPANLKL TIVGIENRTT TFTVEDGMLV VARPGEKKWP RIRTTLGHVL WAEVKGDSLE
VSFLARRKST SPLAVVRLTG TVQEAEADLA SAFTESLMDA AYAGVKRQRK LKVFVNPKSG
PGNGIVYYKK RIEPIFQAAR CAVDPTFTDY PGHAQELIKE LDLEQCDAVV VVSGDGLVHE
VINGFAQHRD PEGAFRVPIA PVACGSGNGL PLNLLGPQDG YDVCAGALNA IKGKPMHIDL
CSVTQKDKTV YSFMSQTVGL FADLDIGTEW LRFLGSTRFV VGFVIEVLKM KRCPVKLSIK
VADSDKKQMV QKLHGYHAKA RACTSPAEVP ISAEDTAADD DSTTAPSSAP PLSPTDPKAS
SPLSPPDSEG WSTFVRPLSY VYAGKGPYVS RDLMQFPVSI PDDGLVDIVA QEITTRKAMI
DAMDESEQGM QYWLDTQHYF RASAYRVEPY SPKGCFSVDG EEYPFEPFQV ECHRGMATVL
SPCGYYQAEF RLPDESKAS
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