ID A0A8H7Z1G7_AJECA Unreviewed; 508 AA.
AC A0A8H7Z1G7;
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=Sphingosine kinase {ECO:0000313|EMBL:KAG5299369.1};
GN ORFNames=I7I52_09662 {ECO:0000313|EMBL:KAG5299369.1};
OS Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=5037 {ECO:0000313|EMBL:KAG5299369.1, ECO:0000313|Proteomes:UP000670092};
RN [1] {ECO:0000313|EMBL:KAG5299369.1, ECO:0000313|Proteomes:UP000670092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G184AR {ECO:0000313|EMBL:KAG5299369.1,
RC ECO:0000313|Proteomes:UP000670092};
RA Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT "Chromosome-level genome assembly of a human fungal pathogen reveals
RT clustering of transcriptionally co-regulated genes.";
RL Submitted (JAN-2021) 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:KAG5299369.1}.
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DR EMBL; JAEVHI010000002; KAG5299369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8H7Z1G7; -.
DR VEuPathDB; FungiDB:I7I52_09662; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000670092; 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:KAG5299369.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 139..278
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 508 AA; 55660 MW; 428C0765432EE0B8 CRC64;
MTIDTALDAG LSGDNGMASV TDGLLQSNSE NSATLPAGRN VFLTLTDDAL IVADKGIKSK
SQRRCCSFPT PGSASQSIPY FNILWAELSD DYITIKYADQ VTKKDVTLRS VQYSVNLENK
SKAKTWTQEL LDLAYGKAQR QKRIKVLINP FGGKGHAPKD YLRYVEPIFA AAKCQVDVES
TSHRGHAVDI VEKLDVNAYD VVVACSGDGI PYEIFNGLAK KPNASEALRK IAVAHIPCGS
GNAMSWNLNG TGRASLAAVS IVKGLRTPLD LVSITQGDKR TVSFLSQSFG IIAELDLGTE
NIRWMGSARF TYGFLVRLLG KTVYPCDLAI KVELDNKELI KDHYRAGSQR RSLDQLRDEE
SSDAVGLPPL RYGTVNDPLP EGWTLVPHDK LGNFYAGNMA YMAADTNFFP AALPNDGCMD
LITVNGDISR RTAIQMLMSV EDGAFFDMPE VNVRKVTGYR IIPRDRKEGY ISIDGEQVPF
EPFQAEVHKG LGTVLSRSGY KYETNGLK
//
