ID A0A1L9UQA6_ASPBC Unreviewed; 505 AA.
AC A0A1L9UQA6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN ORFNames=ASPBRDRAFT_121796 {ECO:0000313|EMBL:OJJ73842.1};
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ73842.1, ECO:0000313|Proteomes:UP000184499};
RN [1] {ECO:0000313|Proteomes:UP000184499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC {ECO:0000313|Proteomes:UP000184499};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR EMBL; KV878682; OJJ73842.1; -; Genomic_DNA.
DR RefSeq; XP_067481090.1; XM_067617460.1.
DR AlphaFoldDB; A0A1L9UQA6; -.
DR STRING; 767769.A0A1L9UQA6; -.
DR GeneID; 93569948; -.
DR VEuPathDB; FungiDB:ASPBRDRAFT_121796; -.
DR OMA; TMGNFYA; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000184499; 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 InterPro; IPR045540; YegS/DAGK_C.
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 Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000184499};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 136..275
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 343..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 54786 MW; 4BFE8F1A561E1518 CRC64;
MTTQNGPPRP SFNNADHPET RDQLLEHDAT LIVSNSVSLT LGGDSLLIVD ERSMRKTERG
CCGIAGKTAK PTHSIALYNV LDADLSPEGL TITYAEPASK EDVSVSALRY PFAPEEKAAV
ESWTNRLLDV AYGTAKRYKR LKVLVNPFGG QGHAVKLYSS YAAPVFAAAR CQVDVQETTH
GGHAVEIVEQ LDINAYDAII CCSGDGLPYE VFNGLAKKPN AGEALAKVAV AMVPCGSGNA
MAWNLCGTGS VSVAALAIVK GVRTPMDLVS ITQGKTRTLS FLSQSFGIIA ESDLGTDDIR
WMGAHRFTYG FLKRIMRRAV YPCDLAVKVV MDDKQAIKDH YSAYAQSQPP SRSSENTTER
PDGLPELVYG TVLDELPKDW EVIPGENLGN FYAGNMAIIS KDTNFFPASL PNDGLMDIVT
IDGTLSRLTT LKMMTAIPEG DFFDMPDVKI RKALAYRLVP HEKEGYISVD GESIPFEAFQ
VEIHKGLGTV LSRTGHLYEA EGPKP
//
