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Database: UniProt
Entry: A0A318ZKV0_9EURO
LinkDB: A0A318ZKV0_9EURO
Original site: A0A318ZKV0_9EURO 
ID   A0A318ZKV0_9EURO        Unreviewed;       504 AA.
AC   A0A318ZKV0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=BP01DRAFT_416628 {ECO:0000313|EMBL:PYH44410.1};
OS   Aspergillus saccharolyticus JOP 1030-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH44410.1, ECO:0000313|Proteomes:UP000248349};
RN   [1] {ECO:0000313|EMBL:PYH44410.1, ECO:0000313|Proteomes:UP000248349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH44410.1,
RC   ECO:0000313|Proteomes:UP000248349};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ821237; PYH44410.1; -; Genomic_DNA.
DR   RefSeq; XP_025430392.1; XM_025579209.1.
DR   AlphaFoldDB; A0A318ZKV0; -.
DR   STRING; 1450539.A0A318ZKV0; -.
DR   GeneID; 37080438; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000248349; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000248349}.
FT   DOMAIN          135..274
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   504 AA;  54285 MW;  D7F073620509EAAF CRC64;
     MASTADSSRP SFSPADASDQ LLQHDATLAV GDSVTLTLGG DSLLVVDERS GRKSERGCCS
     VRKKDAATRI SRTISLYNVL DADLSPTGLT ITYAEPTQQD EVAVAALQYS IGEEEKGAAE
     SWMKKLLDVA YGSAQRNKRL KVLVNPFGGQ GHAAKLYSTH AAPILASARC QIDVQETTHR
     GHATEIVQQL DIDAYDAIVC CSGDGLPYEV FNGLARKPNA REALAKVAVA LLPGGSGNAM
     SWNLYGTGSV SVAALAIVKG LRTPLDLVSI TQGDTRTLSF LSQSFGIIAE SDLGTDDIRW
     MGAHRFTYGF LKRLMHMTVY PCDLAIKVVM DDKQAIKNHY SSYAQSQPPG RPAKLTADQT
     GGLPDLVYGT VQDELPKDWE VIPAETLGNF YAGNMAIMSK DTNFFPASVP NDGLMDIVTI
     DGTIGRLRSL KMMTEIPEGG FFDMPEVNIR KALAYRLVPR EKEGFISVDG ESVPFEAFQG
     EIHKGLGTVL SKSGHLYEAA GPRP
//
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