ID A0A5N6TT91_ASPAV Unreviewed; 506 AA.
AC A0A5N6TT91;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE SubName: Full=ATP-NAD kinase-like domain-containing protein {ECO:0000313|EMBL:KAE8149281.1};
GN ORFNames=BDV25DRAFT_156616 {ECO:0000313|EMBL:KAE8149281.1};
OS Aspergillus avenaceus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=36643 {ECO:0000313|EMBL:KAE8149281.1, ECO:0000313|Proteomes:UP000325780};
RN [1] {ECO:0000313|EMBL:KAE8149281.1, ECO:0000313|Proteomes:UP000325780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 18842 {ECO:0000313|EMBL:KAE8149281.1,
RC ECO:0000313|Proteomes:UP000325780};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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; ML742128; KAE8149281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6TT91; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000325780; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001727; F:lipid kinase activity; IEA:TreeGrafter.
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:KAE8149281.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000325780};
KW Transferase {ECO:0000313|EMBL:KAE8149281.1}.
FT DOMAIN 137..276
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 506 AA; 54785 MW; 2C29EB8A07A39417 CRC64;
MTSFSNGDAR PSLSHADQLD SQHQLLQHDS TLTVAQSVSL TIGGDSLLVV DERPRSTDQR
ACCGLIAKST KTTHAIGLYN ILDADLSSTG LTITYAEPVP KDSVTVTALE YPIAEEEKAH
AQAWVSQLSM LAYGEAQPYK RLKVLINPFG GKGTASKIYH KHAAPVFAAA RCKVDVQETT
HQGHATEIVE EIDIDAYDAI ICCSGDGLPY EVFNGLAKKP NAGEALAKIA VAMIPCGSGN
AMAWNLCGTG DASVAALTIV KGLRTPMDLV SLTQGKNRML SFLSQSFGVI AESDLGTDNI
RWMGAHRFTY GFLVRIMHRT VYPCDLAMKV ELDDKQVIKE HYNTYAHNPA PTRSPEETAG
QSKGLPQLKY GTVLDELPKD WEVIPGEVMG NFYAGKMAIV SKDTNFFPGS VPNDGLMDVV
TIDGTIPRTT SLKMMTAIPE GGFFDMPDVN IRKASAYRLI PRQKEGYISV DGESIPFEAF
QAEVHKGLGT VLSKSGHLYE AEGPRP
//
