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Database: UniProt
Entry: A0A0J8RQJ9_COCIT
LinkDB: A0A0J8RQJ9_COCIT
Original site: A0A0J8RQJ9_COCIT 
ID   A0A0J8RQJ9_COCIT        Unreviewed;       293 AA.
AC   A0A0J8RQJ9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=sphingosine kinase {ECO:0000256|ARBA:ARBA00044037};
DE            EC=2.7.1.91 {ECO:0000256|ARBA:ARBA00044037};
GN   ORFNames=CIHG_04042 {ECO:0000313|EMBL:KMU86254.1};
OS   Coccidioides immitis H538.4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU86254.1, ECO:0000313|Proteomes:UP000054563};
RN   [1] {ECO:0000313|Proteomes:UP000054563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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};
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DR   EMBL; DS016991; KMU86254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8RQJ9; -.
DR   STRING; 396776.A0A0J8RQJ9; -.
DR   VEuPathDB; FungiDB:CIHG_04042; -.
DR   eggNOG; KOG1116; Eukaryota.
DR   Proteomes; UP000054563; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   PANTHER; PTHR12358:SF31; LD11247P-RELATED; 1.
DR   PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KMU86254.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW   Transferase {ECO:0000313|EMBL:KMU86254.1}.
FT   DOMAIN          141..280
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   293 AA;  31796 MW;  8504E946EE9868CA CRC64;
     MTLSSLLDCD RSPDGYSSSE EEQLQRVDIG KDSVLAVGPK TLLILTAKSL VIADENAKKK
     DSRSCCSPYW CSGKLQRLSI PYFNVLWADV SHEYITIKYA ESTSNDDVSV ASVYYPVDPA
     HKSKTKQWLE ELMNAAYGKA QREKKVKVLI NPFGGKGRAQ KLYSREVEPV FAAAQCEVDV
     EITTHQGHAV EIAQNIDLQA YDVIAPASGD GVAYEVFNGL GKRADAGEAL RSLAVAHIPC
     GSGNAMSWNL YGTGSPSMAA LCIVKGLRTP LDLVSITQGD RRTLSFPSLM GLV
//
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