ID C5FHJ2_ARTOC Unreviewed; 487 AA.
AC C5FHJ2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 28-JAN-2026, entry version 67.
DE SubName: Full=Sphingoid long chain base kinase 4 {ECO:0000313|EMBL:EEQ28732.1};
GN ORFNames=MCYG_01551 {ECO:0000313|EMBL:EEQ28732.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ28732.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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DR EMBL; DS995702; EEQ28732.1; -; Genomic_DNA.
DR RefSeq; XP_002848617.1; XM_002848571.1.
DR AlphaFoldDB; C5FHJ2; -.
DR STRING; 554155.C5FHJ2; -.
DR GeneID; 9230755; -.
DR VEuPathDB; FungiDB:MCYG_01551; -.
DR eggNOG; KOG1116; Eukaryota.
DR HOGENOM; CLU_013399_0_1_1; -.
DR OMA; TMGNFYA; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000002035; 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:EEQ28732.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 119..258
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 53128 MW; C45D34FC009546E7 CRC64;
MTFSRFFPGS ADSDRGQDAE MQAPRDGTAV LPVGVNATLT LAAESLVVQG VARTTRSIPY
FNILWADISD NHLNIKYANP RNKHDVGLAT ICYSVERTQL SKAETWVSTL LDLSYGEAQK
KKRIKVLVNP FGGKGNASKI YNKEVEPIFE AAKCVIDTQK TEYSGHAVDI AEKLDVDAWD
VIAACSGDGV IFEIFNGLGK KENAGEALAK LAVAHIPCGS GNAMSRNLNG TAGPSMAALC
IIKGLRTPLD LVSISHGQRR TLSFLSQAFG IIADSDLGTD NLRWMGPARF TFGFLVRLFG
NTVYPCDVAL KVEIDDKKHI KEHYNAIVQN KSNTEPREEV PASGGLPPLK YGLATDPIPD
DWMRISHDKL GNFYSGKMAF MAQDANFFPA SLPNDGFLDV IMIRGDISRL TAIQMLGALD
DGELFDLPDV HALKISAFRI TPRNQEDGYI SIDGEQIPYE PFQAEVHRGL GTVISRSGYK
YETGKGS
//
