ID A0A2V1EFH0_9PLEO Unreviewed; 519 AA.
AC A0A2V1EFH0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=DM02DRAFT_578584 {ECO:0000313|EMBL:PVI08484.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI08484.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI08484.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI08484.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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DR EMBL; KZ805300; PVI08484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1EFH0; -.
DR STRING; 97972.A0A2V1EFH0; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000244855; 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:UP000244855}.
FT DOMAIN 151..290
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 56501 MW; 2E523BF6226B3560 CRC64;
MASTGQTNPF EDPSSKDAQV QEQGEIARGT SEPQEPVPHT ATTLAVGRNA SLTLGTESLV
VQDEELQQSG RVNCCGVSFA GKNKTTRSIP FYNILWAERS ENGDITIQYA HAVSKTVVRP
AIISYTLDKP ESSEVEAWIE SLLDRAYGTS QRRKRIKMLV NPFGGQGGAV KMYHKHIAPI
FAAAKCTLDM EKTQHNGHGT EIAQALDIDA FDVVACCSGD GIPHEVWNGL GKRADAARAL
AKLAVTQLPG GSGNALSLNL NGTVSPSLAA LAVVKGLRTP LDLISVTQGD RRILSFLSQA
VGIIAEADLG TEHLRWMGST RFTYGVIKRI LRQDVYPADI AIKVEHDNKT AIREVYRTEA
SKSPPRHNER EIPPADLGLP PLRYGSVQDP LPDSWTLVPH DHLGNFYAGN LAYMSADANF
FPASLPSDGC LDLVRMRGNL KRGAAIKALL AVAEHKFFDI EDVDYKKVTA YRIIPRNQKD
GYIDIDGERI PFEPFQAEVH QGLGTVLSKS GHLFEAEGV
//
