ID V2WIC4_MONRO Unreviewed; 482 AA.
AC V2WIC4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=sphingosine kinase {ECO:0000256|ARBA:ARBA00044037};
DE EC=2.7.1.91 {ECO:0000256|ARBA:ARBA00044037};
DE Flags: Fragment;
GN ORFNames=Moror_16723 {ECO:0000313|EMBL:ESK81332.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK81332.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK81332.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK81332.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK81332.1}.
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DR EMBL; AWSO01002540; ESK81332.1; -; Genomic_DNA.
DR RefSeq; XP_007859363.1; XM_007861172.1.
DR AlphaFoldDB; V2WIC4; -.
DR STRING; 1381753.V2WIC4; -.
DR KEGG; mrr:Moror_16723; -.
DR HOGENOM; CLU_013399_0_1_1; -.
DR OrthoDB; 374620at2759; -.
DR Proteomes; UP000017559; 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, ECO:0000313|EMBL:ESK81332.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 115..256
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ESK81332.1"
SQ SEQUENCE 482 AA; 53111 MW; C4513382E11B64DA CRC64;
SLSTKLQEPR LLHFSLLDKA MAVEVDVQGK TRSYSAEDSH LVIIVGKRLQ RIPLYDVVSA
DFNREVKSLE LGYVTRRKKS GPLLFIRVKG QVKGSEDEAA EFSTTLLEKA YEGVKRNRRL
KVLINPNGGV GKAVPLFKLS VEPVLRAAGC SLDIVHTKGH GDAFDIAKNL PLDEFDALLT
VSGDGLIHEV LNGFGKHPKP KKALAIPVAP VPAGSGNGLS LNLLGIEDGF DPVAAALNAV
KGKPMSIDIF SITQNGETSL SFMSQALGLM ADLDLGTEHL RWMGDTRFFY GFLRGLIKFK
SCALELSYKI AEEDKNTMFN TLKARREGTR PNYTPPAEDL GDVALPKPRY SSTDNDGWTT
FDKPSLFIYA GQGPYVGRDF MAFPVSLPDD GLIDIFVQAK STRGDAIAMM DEAPRGGIYW
NENCHYIKAH AYRIRPLSKR GSLSVDGERY PFEEFQVEVI PKLATLLSPY GCYAAEFKRQ
ES
//
