ID A0A371DVW8_9APHY Unreviewed; 488 AA.
AC A0A371DVW8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=OH76DRAFT_1395809 {ECO:0000313|EMBL:RDX56689.1};
OS Lentinus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Lentinus.
OX NCBI_TaxID=2498619 {ECO:0000313|EMBL:RDX56689.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX56689.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX56689.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ857380; RDX56689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371DVW8; -.
DR STRING; 139420.A0A371DVW8; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000256964; 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:UP000256964}.
FT DOMAIN 101..242
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 318..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..343
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 52987 MW; 907B24EF4653CD46 CRC64;
MSTRELALGS GVNASRFTLT DTELVVERAA DKKWPKVKTS LRNVLWAELK GDAFEVSLLA
KKKPKSPLSL LHVTGSVGDA DKESAASFTE ALMSAAYAGL PRQRRLKVFV NPKSGPGKAV
AQYRKKIEPI FNAAKCKVDV TFTTRGKHAQ EIVEKLPLDG FDAIVVMSGD GLVHEVINGY
AAHAEPAKAF RIPISPIPTG SGNGLAINLL GLEESKDVAV AALNAIKGRP MAMDIFSMTQ
GDKRYMSFMS QALGLMADID LGTEHLRFMG GTRFVVGFIY EVIKNKQVSA KVSIKIAEQD
KRKMVQDLQA ARAQARSTIA SADASDPATL TTDGESSTTG TGLPELKHTG AARVNDDGWV
TFDKPFTFLY AGQGPYVSTD LMQFPVSQPN DGLIDVVLQL QSDRGTMLKA IDGAEHGNPF
WMDAQHYYKA HAFRVEPHFT KGYLSIDGES YPVAPFEIEV HKGLGSLLSM YGCFQAEFNL
PPEQPAKK
//
