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Database: UniProt
Entry: A0A4Z1JG88_9HELO
LinkDB: A0A4Z1JG88_9HELO
Original site: A0A4Z1JG88_9HELO 
ID   A0A4Z1JG88_9HELO        Unreviewed;       522 AA.
AC   A0A4Z1JG88;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=BOTNAR_0001g00370 {ECO:0000313|EMBL:TGO70362.1};
OS   Botryotinia narcissicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botryotinia.
OX   NCBI_TaxID=278944 {ECO:0000313|EMBL:TGO70362.1, ECO:0000313|Proteomes:UP000297452};
RN   [1] {ECO:0000313|EMBL:TGO70362.1, ECO:0000313|Proteomes:UP000297452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUCL2120 {ECO:0000313|EMBL:TGO70362.1,
RC   ECO:0000313|Proteomes:UP000297452};
RA   Valero-Jimenez C.A., Tapia P., Veloso J., Silva-Moreno E., Staats M.,
RA   Valdes J.H., Van Kan J.A.L.;
RT   "Comparative genomics of Botrytis spp.";
RL   Submitted (DEC-2017) 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:TGO70362.1}.
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DR   EMBL; PQXJ01000001; TGO70362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Z1JG88; -.
DR   STRING; 278944.A0A4Z1JG88; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000297452; 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:UP000297452};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          150..290
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..13
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  57013 MW;  D5609925A390E980 CRC64;
     MATSPTSCNS IPPSGQTASS GSAGQFDIDN TLFVSKDVSL SLSPESLIIK GAETAKKPEK
     GAKSAGARRS VTLDASAYSE PVGPSTLRAI PLRQILWAEI TETELIINYA KEISKTVLQP
     AVLKYVIEEE RDRVEAWVSR LKDRAYGKSQ QQKRVKVIIN PKSGKGQSEK IYAKDVAPIF
     DAAHLSIDVT VTKASREAIA VVEKLDIEAY DVIICCSGDG LPFEVFNGLG KRKDAKRALS
     KMAIAHIPCG SGNGLHCSLH GNIRSTSIAA LSIVKGIRTP LDLISVTQGE ERHLSFLSQA
     LGIVAEFDLG TEHLRWMGGT RFVYGFVMKS LQKKIFPCDI AVKVVTDDKE DIKRRYREAM
     EVGSTPEESL REISSSEGGL PELKCGNSSD PLPQGWEVEQ HDNLGSFYCG NMSWMGADVD
     YFPAALPNDG CMDMVTIDYS NLSRLQALQL MPAVESGKFF GLPYVNYRKV EAYRITPKNQ
     TDGYISIDGE RVPFGPFQAE VHRGLGTVLS VSGYRYETPG PK
//
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