ID A0A5N6EM41_9EURO Unreviewed; 502 AA.
AC A0A5N6EM41;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE SubName: Full=ATP-NAD kinase-like domain-containing protein {ECO:0000313|EMBL:KAB8218682.1};
GN ORFNames=BDV33DRAFT_175186 {ECO:0000313|EMBL:KAB8218682.1};
OS Aspergillus novoparasiticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=986946 {ECO:0000313|EMBL:KAB8218682.1, ECO:0000313|Proteomes:UP000326799};
RN [1] {ECO:0000313|EMBL:KAB8218682.1, ECO:0000313|Proteomes:UP000326799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 126849 {ECO:0000313|EMBL:KAB8218682.1,
RC ECO:0000313|Proteomes:UP000326799};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Petersen T.I., 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 Pangilinan J., Riley R., Salamov A., Simmons B.A., Magnuson J.K.,
RA Henrissat B., Mortensen U.H., Larsen T.O., De vries R.P., Grigoriev I.V.,
RA Machida M., Baker S.E., Andersen M.R.;
RT "Fungal friends and foes A comparative genomics study of 23 Aspergillus
RT species from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; ML733447; KAB8218682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6EM41; -.
DR Proteomes; UP000326799; 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:KAB8218682.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000326799};
KW Transferase {ECO:0000313|EMBL:KAB8218682.1}.
FT DOMAIN 133..272
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 341..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 54284 MW; AA2DD25376CB2C85 CRC64;
MTSPSNGPSS NHADQPDSQR LLQHDSTLTV AQSVSLSIGG DSLLVVDERP KSKDQRACCG
LLAKSSKTTH SIGLYNILDA DLSPAGLTIT YAQAATKDSI SVAALEYPIS EKEKANAQTW
VSQLLDLAYG EAQRYKRLKV LINPFGGKGA ASKSYHKHAA PVFAAARCVV DVQQTTRQGH
ATEIVEQIDI DAYDAIVCCS GDGLPYEVFN GLGKKPNAGE ALAKVAVAMI PCGSGNAMAW
NLCGTGNVSV AALAIVKGLR TPMDLVSLTQ GNTRTLSFLS QSFGVIAESD LGTDNIRWMG
AHRFTYGFLV RIMQRTVYPC DLAIKVEIDD KRAIKDHYNT YAHNPAPRRS PEETAGQSKG
LPELRYGTVQ DDLPKDWEVI PGEEMGNFYA GKMAIVSKDT NFFPASVPND GLMDIVTING
TIPRTTTLKM MTAIPENEFF DMPDVKIRKA AAYRLIPRQK EGYISVDGES IPFEALQAEV
HKGLGTVLSK SGHLYEAEGP RP
//
