ID A0A177CZX7_9PLEO Unreviewed; 511 AA.
AC A0A177CZX7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE SubName: Full=Sphingoid long chain base kinase-like protein {ECO:0000313|EMBL:OAG13024.1};
GN ORFNames=CC84DRAFT_1160270 {ECO:0000313|EMBL:OAG13024.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG13024.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG13024.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG13024.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV441548; OAG13024.1; -; Genomic_DNA.
DR RefSeq; XP_018043389.1; XM_018177461.1.
DR AlphaFoldDB; A0A177CZX7; -.
DR FunCoup; A0A177CZX7; 593.
DR STRING; 1460663.A0A177CZX7; -.
DR GeneID; 28760947; -.
DR InParanoid; A0A177CZX7; -.
DR OrthoDB; 3853857at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR GO; GO:0001727; F:lipid kinase activity; IEA:UniProtKB-ARBA.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-ARBA.
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 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 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:OAG13024.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Transferase {ECO:0000313|EMBL:OAG13024.1}.
FT DOMAIN 141..280
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 55354 MW; 88C7E1281505C3C6 CRC64;
MAHGVGEDAI DPFRDPSMAG NTPNTPRADV PATLAVGRNA SLTLGTDALI VLDELLESKG
AGCCGMSLGG GNNKTTRSIP FYNVLWAETA DDGEVIIHYA HAVSKQVVRR QIISYKLEKP
DSDLAAAWVE RLLEKAYGAS QRQKRIKVLI NPFGGQGKAT QMYHKHIAPI LAAARCELDV
ESTTHNGHGV EIAQNLDIEK FDVVACCSGD GIPHEVWNGF GKREDAQRAL VKIAVAQLPC
GSGNALCLNH TGTDSPSLAA LAVVKGLRTP LGLASVTQGD RRLLSFLSQS AGIVAETDLA
TEHLRWMGSA RFTYGFLVRL LKKTVYPADI AIKVEHGNKE AVRAAYRAEA AKPPRTQDER
TLPAPGEPCA IPPLKYGTIN DPLPDGWELV PHDQLGNFYA GNLAYMSSDA NFFPAALPDD
GCLDLVRIKG TLPRTKSIAT LLAIEQHKFF DLPHVDYQKI SAYRIIPKNQ KEGYISVDGE
RIPFEPFQVE IHKGMGTVLS KNGHLFEAKG V
//
