ID A0A5N6ZD49_9EURO Unreviewed; 497 AA.
AC A0A5N6ZD49;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE SubName: Full=ATP-NAD kinase-like domain-containing protein {ECO:0000313|EMBL:KAE8355557.1};
GN ORFNames=BDV28DRAFT_162813 {ECO:0000313|EMBL:KAE8355557.1};
OS Aspergillus coremiiformis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=138285 {ECO:0000313|EMBL:KAE8355557.1, ECO:0000313|Proteomes:UP000327118};
RN [1] {ECO:0000313|Proteomes:UP000327118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 553.77 {ECO:0000313|Proteomes:UP000327118};
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; ML739050; KAE8355557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6ZD49; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000327118; 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:TreeGrafter.
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:KAE8355557.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000327118};
KW Transferase {ECO:0000313|EMBL:KAE8355557.1}.
FT DOMAIN 128..267
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 497 AA; 54200 MW; 6F2633D6C3AF9571 CRC64;
MTSFNYVDQS DSQHQLLQND LTLTVAQSVS LTIRGDSILI VDERPKSKDQ RACCGLLAKS
TKTTHSIELY NILDADLSPA GLTITYAQPI TKDSVSVAAL EYTVADKETP DAETWVSQLL
DLAYGEAQRY KRLKVLINPF GGKGAAAKSY HKHAAPVFAA ARCNVDVQET THQGHATEIM
EQIDVDAYDA IVCCSGDGLP YEVFNGLAKK SNAGEALAKL AVAMIPCGSG NAMAWNLCGT
GNVSVAALTI VKGLRTPMDL ISLTQGSTRT LSFLSQSFGV IAESDLGTDN IRWMGAHRFT
YGFLVRIMQR TVYPCDLAIK VDIDDKRAIK DHYNTYAHNP APCRSSEETA GQSKGLPELK
YGTVLDDLPK DWEIISGEEM GNFYAGKMAI MSKDTNFFPA SLPNDGLMDI ITINGTIPRT
TTLKMMTAIP ENDFFDMPDV KIRKASAYRL IPHQKEGYIS VDGESVPFEA FQAEVHKGLG
TVLSKSGHLY ETEGPRP
//
