ID A0A9P7JWC0_9AGAM Unreviewed; 481 AA.
AC A0A9P7JWC0;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE SubName: Full=ATP-NAD kinase-like domain-containing protein {ECO:0000313|EMBL:KAG2111604.1};
GN ORFNames=F5147DRAFT_92483 {ECO:0000313|EMBL:KAG2111604.1};
OS Suillus discolor.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX NCBI_TaxID=1912936 {ECO:0000313|EMBL:KAG2111604.1, ECO:0000313|Proteomes:UP000823399};
RN [1] {ECO:0000313|EMBL:KAG2111604.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FC423 {ECO:0000313|EMBL:KAG2111604.1};
RX PubMed=33355923;
RA Lofgren L.A., Nguyen N.H., Vilgalys R., Ruytinx J., Liao H.L., Branco S.,
RA Kuo A., LaButti K., Lipzen A., Andreopoulos W., Pangilinan J., Riley R.,
RA Hundley H., Na H., Barry K., Grigoriev I.V., Stajich J.E., Kennedy P.G.;
RT "Comparative genomics reveals dynamic genome evolution in host specialist
RT ectomycorrhizal fungi.";
RL New Phytol. 0:0-0(2020).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG2111604.1}.
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DR EMBL; JABBWM010000017; KAG2111604.1; -; Genomic_DNA.
DR RefSeq; XP_041294823.1; XM_041444473.1.
DR AlphaFoldDB; A0A9P7JWC0; -.
DR GeneID; 64706732; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000823399; 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:KAG2111604.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000823399};
KW Transferase {ECO:0000313|EMBL:KAG2111604.1}.
FT DOMAIN 113..253
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 322..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..338
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 53017 MW; F03189F8EA2F3000 CRC64;
MNQLLIDSRG VSTSLRFNEA SFFIEPTKLD GHNSSCCAGI YADREVKCTE VPLRNVIYTK
VTSGVIEVQY LVRKGKESRL NLATTTGAVQ NEDSTRVKKW CEALLLAAYQ GANPSKNLKV
LVNPHGGKGK ARASYVNKVE PIFLAAGCTL DVTYTTHGGH AIEIAREMKL GYDALVVVSG
DGLIHEVLNG IDQHEHRDQA FCIPIAPIPT GSGNGMSLNL LGLQDGLDVC AAALNVLKGQ
PLKTDLFSFT QGNRCRISFM SQTIGITADI DIETEHLRWM GDTRFIIGYI RAIIARKSCP
IELSMKVVEQ DKSRMMDVLH ARRAGESPSP SSVPSLLSAD KKPDSSSSSH EEWTQFKRPI
LWMYAGKGPF VSRDLMQFPV SLADDGLIDI SVQEITSRRA LLRAMDGAEE GRTYWINTNR
YFKASAYRAR PLAPKGMLVV DGEQVPFEEF QVDVLNGLGT FLAPYPHYAP EFLVRDIEGN
T
//
