ID A0A0F4Z7B1_9PEZI Unreviewed; 501 AA.
AC A0A0F4Z7B1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=sphingosine kinase {ECO:0000256|ARBA:ARBA00044037};
DE EC=2.7.1.91 {ECO:0000256|ARBA:ARBA00044037};
GN ORFNames=TD95_001374 {ECO:0000313|EMBL:KKA26392.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA26392.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA26392.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA26392.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:51496, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:76941, ChEBI:CHEBI:84410, ChEBI:CHEBI:456216;
CC EC=2.7.1.91; Evidence={ECO:0000256|ARBA:ARBA00043822};
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:KKA26392.1}.
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DR EMBL; LAEV01002193; KKA26392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4Z7B1; -.
DR OrthoDB; 374620at2759; -.
DR Proteomes; UP000033483; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR PANTHER; PTHR12358:SF31; LD11247P-RELATED; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 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:UP000033483};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 105..244
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 323..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 54844 MW; BB566BBC15E88F1A CRC64;
MTANELSEPA ADIPALETPL KLSGKRTLAL QEHQLVFEEP SSIEIPFYNV LWVEAKDNTL
TLDYVERQNN DLVVRKLTGE VSDVATEALT AWADTVMDRA YKKAKRNKRA LVLVNPASGP
GGAVKRWSTK SKPIFEAARM SMDIIVTTHG GQAIEICEKM DINNFDIVVG CAGDGMPYEI
FNGLGKRADA SHALAKISVA HIPCGSGNGM SCNLYGSHKP SVAALGIVKG VSTPLDLVSV
TQGETRLLSF MSQNVGIIAE CDLATENLRW MGDNRFVVGF LQRVMSGSKY PCDIAAKVEI
DEVKGIKEHY HREQSQVDLN VSSAMKQQGA DADGESSADT QNQQNKGLPP LKYGTTTDPL
PEDWEVVKSD KLGCLYVGNM AYMDRTNNFF SAACTNDGLL DMITVDADIG TMAWIKLMDY
VEKGKLLDHD LVRYKKVSAF RVTPRDQQDG YISIDGERIP FGPFQCEVHR GLGRVISKNG
TFEGPGPGSW DKVSMAERLH A
//
