ID A0A8H6AW45_9HELO Unreviewed; 522 AA.
AC A0A8H6AW45;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Putative sphingosine kinase protein {ECO:0000313|EMBL:KAF5874510.1};
GN ORFNames=Bfra_004520 {ECO:0000313|EMBL:KAF5874510.1};
OS Botrytis fragariae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1964551 {ECO:0000313|EMBL:KAF5874510.1, ECO:0000313|Proteomes:UP000531561};
RN [1] {ECO:0000313|EMBL:KAF5874510.1, ECO:0000313|Proteomes:UP000531561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BVB16 {ECO:0000313|EMBL:KAF5874510.1,
RC ECO:0000313|Proteomes:UP000531561};
RX PubMed=32648525;
RA Wu Y., Saski C.A., Schnabel G., Xiao S., Hu M.;
RT "A high-quality genome resource of Botrytis fragariae, a new and rapidly
RT spreading fungal pathogen causing strawberry gray mold in the U.S.A.";
RL Phytopathology 0:0-0(2020).
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:KAF5874510.1}.
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DR EMBL; JABFCT010000007; KAF5874510.1; -; Genomic_DNA.
DR RefSeq; XP_037193456.1; XM_037334922.1.
DR AlphaFoldDB; A0A8H6AW45; -.
DR GeneID; 59258614; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000531561; 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, ECO:0000313|EMBL:KAF5874510.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000531561};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 150..290
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 57098 MW; 9FE21FBE619DBFEA CRC64;
MATSPTSSNS IPPPGHTASS GSAGQFDIDN TLFVSKDVSL SLSPESLIIK GAETAKKPEK
GAKSAGARRS VTLDASAYSE PVGASTLRAI PLRQILWAEI TETELIINHA KEISKTVLQP
AVLKYAIEEE RDRVEAWVSR LKDRAYGKSQ QQKRVKVIIN PKSGKGQSEK IYAKDVAPIF
DAAHLSIDVT VTKASREATD IVEKLDIEAY DVIICCSGDG LPFEVFNGLG KRKDAKRALS
KMAIAHIPCG SGNGLHCSLH GNIRSTSIAA LSIVKGIRTP LDLISVTQGE ERHLSFLSQA
LGIVAEFDLG TEHLRWMGGT RFVYGFVMKS LQKKIFPCDI AVKVVTDDKE DIKRRYRDAM
DIGTTSEELL RENGSLEGGL PELKYGNSSD PLPQGWEVEQ HDNLGSFYCG NMSWMGADVD
YFPAALPNDG CMDMVTIDYS NLSRLQALQL MPAVENGKFF SLPYVNYRKV EAYRITPKNQ
SDGYISIDGE RVPFGPFQAE VHRGLGTVLS VSGYRYETPG PK
//
