ID A0A5N7B304_9EURO Unreviewed; 497 AA.
AC A0A5N7B304;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=ATP-NAD kinase-like domain-containing protein {ECO:0000313|EMBL:KAE8376325.1};
GN ORFNames=BDV26DRAFT_240900 {ECO:0000313|EMBL:KAE8376325.1};
OS Aspergillus bertholletiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1226010 {ECO:0000313|EMBL:KAE8376325.1, ECO:0000313|Proteomes:UP000326198};
RN [1] {ECO:0000313|EMBL:KAE8376325.1, ECO:0000313|Proteomes:UP000326198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29228 {ECO:0000313|EMBL:KAE8376325.1,
RC ECO:0000313|Proteomes:UP000326198};
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 studyof 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; ML736243; KAE8376325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N7B304; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000326198; 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:KAE8376325.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000326198};
KW Transferase {ECO:0000313|EMBL:KAE8376325.1}.
FT DOMAIN 128..267
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 335..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 54130 MW; D8C6F4E6C9FC5C63 CRC64;
MTSSSNHADQ PDSQQLLQYD STLIVAQSVS LTIGGDSLLV VDERPKSKDQ RACCGLLPRS
TKTTHSIALY NILDADLSPA GLTITYAQAA TKDSISATAL EYPITEKEKE NARKWVSQLL
DLAYGEAQRY KRLKVLINPF GGKGSASKNY HKHAAPVFAA ARCVLDVQET THQGHATEIA
EQIDIDAYDA IVCCSGDGLP YEVFNGLGKK PNAGEALAKM AVTMLPCGSG NAMAWNLCGT
GNASVAALAI IKGLRTPIDL VSLTQGNTRL LSFLSQSFGV IAESDLGTDN IRWMGAHRFT
YGFLVRIMQR TVYPCDLAIK VEIDDKRAIK NHYNTYANNP APRRSPEETG EQSNGLPELK
YGTVQDDLPK DWEVIPGEEM GNFYAGKMAI VSKDTNFFPA SVPNDGLMDI VTIKGTIPRT
TTLKMMTAIP ENEFFDMPDV KIRKAAAYRL VPRQKEGFIS VDGESIPFEA FQAEVHKGLG
TVLSKSGHLY EAEGPRP
//
