ID A0AAD4EIF1_9AGAM Unreviewed; 475 AA.
AC A0AAD4EIF1;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE SubName: Full=ATP-NAD kinase-like domain-containing protein {ECO:0000313|EMBL:KAG1905584.1};
GN ORFNames=F5891DRAFT_1182652 {ECO:0000313|EMBL:KAG1905584.1};
OS Suillus fuscotomentosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX NCBI_TaxID=1912939 {ECO:0000313|EMBL:KAG1905584.1, ECO:0000313|Proteomes:UP001195769};
RN [1] {ECO:0000313|EMBL:KAG1905584.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FC203 {ECO:0000313|EMBL:KAG1905584.1};
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:KAG1905584.1}.
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DR EMBL; JABBWK010000006; KAG1905584.1; -; Genomic_DNA.
DR RefSeq; XP_041231159.1; XM_041366199.1.
DR AlphaFoldDB; A0AAD4EIF1; -.
DR GeneID; 64660497; -.
DR Proteomes; UP001195769; 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:UniProtKB-ARBA.
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:KAG1905584.1};
KW Reference proteome {ECO:0000313|Proteomes:UP001195769};
KW Transferase {ECO:0000313|EMBL:KAG1905584.1}.
FT DOMAIN 113..247
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 316..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..332
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 52514 MW; A3ABB6F79BA2E934 CRC64;
MNHLLIDSRG LSTSLRFNEA SFFIEPTKPD GHNSSCCAGI YADREVKCTE VPLRNVIYAK
VTSGVIEVQY LVRKGKESRL ELAMTTGAVQ NEDSARVKKW CEALLLAAYQ GANPSKNLKV
LVNPYGGKGK ARASYVSKVE PIFLAAGYTT HGGHAIEIAR EMKLGYDALV IVSGDGLIHE
VLNGINQHEH RDQAFCIPIA PIPTGSGNGM SLNLLGLQDG LDVCAAALNV LKGQPLKTDL
FSFTQGNRRR ISFMSQTIGI TADIDIDTEH LRWMGDTRFI IGYIRAIIAR KSCPIELSMK
VVEQDKSRMM DVLHARRAGE SPSQSSVPSL FSADKKPDSP SSSHEEWTRF KRPILWMYAG
KGPFVSRDLM QFPVSLADDG LIDISIQEIT SRRALLRAMD GAEEGRTYWI NTNRYFKASA
YRARPLAPKG TLVVDGEQVP FEEFQVDVLN GLGTFLAPYP HYAPEFLVRD IEGNT
//
