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Database: UniProt
Entry: A0A317WAY8_9EURO
LinkDB: A0A317WAY8_9EURO
Original site: A0A317WAY8_9EURO 
ID   A0A317WAY8_9EURO        Unreviewed;       505 AA.
AC   A0A317WAY8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   28-JAN-2026, entry version 19.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=BO94DRAFT_625471 {ECO:0000313|EMBL:PWY83075.1};
OS   Aspergillus sclerotioniger CBS 115572.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY83075.1, ECO:0000313|Proteomes:UP000246702};
RN   [1] {ECO:0000313|EMBL:PWY83075.1, ECO:0000313|Proteomes:UP000246702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY83075.1,
RC   ECO:0000313|Proteomes:UP000246702};
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.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWY83075.1}.
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DR   EMBL; MSFK01000019; PWY83075.1; -; Genomic_DNA.
DR   RefSeq; XP_025465860.1; XM_025617289.1.
DR   AlphaFoldDB; A0A317WAY8; -.
DR   STRING; 1450535.A0A317WAY8; -.
DR   GeneID; 37119432; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000246702; 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   Reference proteome {ECO:0000313|Proteomes:UP000246702}.
FT   DOMAIN          136..275
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   505 AA;  54895 MW;  038CFEAF03D7F062 CRC64;
     MTTPNGPSRP SFNNADLPET RDQLLEHDAT LIVANSVSLT LGGDSLLIVD ERSMRKSERG
     CCGLANKTAK PTHSIGLYNI LDADLSPEGL TITYAESASK QDVRVTALRY PFAPEERAAV
     ESWTNRFLDV VYGSAKRYKK LKVLVNPFGG QGHAVKLYST YAAPVFAAAR CQVDVQETTH
     GGHAGEIVEQ LDINAYDAII CCSGDGLPYE VFNGLAKKPN AREALAKIAV ANIPCGSGNA
     MAWNLCGTGS VSVAALEIVK GVRTPIDLVS ITQGKSRTLS FLSQSFGIIA EADLGTDDIR
     WMGAHRFTYG FLKRIMHRAT YPCDLAIKVV MDDKQTIKNH YSAYAQSQPP SRPTEATARH
     PDGLPELVYG TVLDELPEDW EVIPAETLGN FYAGNMAIVS KDTNFFPASL PNDGLMDIVT
     IDGTLSRLTT LKMMTAIPEN AFFDMPDVKI RKALAYRLVP REKEGYISID GESVPFEAFQ
     AEIHKGLGTV LSKSGHLYEA EGPKP
//
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