ID A0A5N6DZA5_ASPPA Unreviewed; 502 AA.
AC A0A5N6DZA5;
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:KAB8210566.1};
GN ORFNames=BDV34DRAFT_154401 {ECO:0000313|EMBL:KAB8210566.1};
OS Aspergillus parasiticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5067 {ECO:0000313|EMBL:KAB8210566.1, ECO:0000313|Proteomes:UP000326532};
RN [1] {ECO:0000313|EMBL:KAB8210566.1, ECO:0000313|Proteomes:UP000326532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117618 {ECO:0000313|EMBL:KAB8210566.1,
RC ECO:0000313|Proteomes:UP000326532};
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; ML734942; KAB8210566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6DZA5; -.
DR VEuPathDB; FungiDB:BDV34DRAFT_154401; -.
DR OMA; TMGNFYA; -.
DR Proteomes; UP000326532; 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:KAB8210566.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000326532};
KW Transferase {ECO:0000313|EMBL:KAB8210566.1}.
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; 54265 MW; E16F25A0B1F8C007 CRC64;
MTSPSNGPSS NHADQPDSQR LLQHDSTLTV AQSVSLSIGG DSLLVVDERP KSKDQRACCG
LLAKSSKTTH SIGLYNILDA DLSPAGLTIT YAQAATKDSI SVAALEYPIS EKEKANAQTW
VSQLLDLAYG EAQRYKRLKV LINPFGGKGA ASKSYHKHAA PVFAAARCVV DVQQTTHRGH
ATEIVEQIDI DAYDAIVCCS GDGLPYEVFN GLGKKPNAGE ALAKVAVAMV PCGSGNAMAW
NLCGTGNVSV AALAIVKGLR TPMDLVSLTQ GNTRTLSFLS QSFGVIAESD LGTDNIRWMG
AHRFTYGFLV RIMQRTVYPC DLAIKVEIDD KRAIKDHYNT YAHNPAPRRS PEETAGQSKG
LPELRYGTVQ DDLPKDWEVI PGEEMGNFYA GKMAIVSKDT NFFPASVPND GLMDIVTING
TIPRTTTLKM MTAIPENEFF DMPDVKIRKA AAYRLVPRQK EGYISVDGES IPFEALQAEV
HKGLGTVLSK SGHLYEAEGP RP
//
