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Database: UniProt
Entry: A0A194VCV0_CYTMA
LinkDB: A0A194VCV0_CYTMA
Original site: A0A194VCV0_CYTMA 
ID   A0A194VCV0_CYTMA        Unreviewed;       551 AA.
AC   A0A194VCV0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   28-JAN-2026, entry version 29.
DE   SubName: Full=Sphingoid long chain base kinase 5 {ECO:0000313|EMBL:KUI61719.1};
GN   ORFNames=VP1G_08867 {ECO:0000313|EMBL:KUI61719.1};
OS   Cytospora mali (Apple Valsa canker fungus) (Valsa mali).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Cytosporaceae; Cytospora.
OX   NCBI_TaxID=578113 {ECO:0000313|EMBL:KUI61719.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN714785; KUI61719.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194VCV0; -.
DR   STRING; 694573.A0A194VCV0; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000078576; 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:TreeGrafter.
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:KUI61719.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078576};
KW   Transferase {ECO:0000313|EMBL:KUI61719.1}.
FT   DOMAIN          147..286
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          43..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..68
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  60514 MW;  A3D5653EB9936604 CRC64;
     MPQLSSAAPE VQADYPGPHY TIDLGRNVSL RIEDDSVFIQ DGKANKSNKK NNRTCGFGSS
     GSSQSPTTRS IPLYDILWAE LSEDRHTLTI DYAEELSKTR RGAAKLSFST VATSSSSEDD
     GQHLYSSPDN ITRWIDRLMN RSYGPASRQK RAYVLVNPHA GPGGAVKIWE EQVKPIFEAA
     RMPMTIHETT FSGEAVGLAE KMDIDAFDIV VPCSGDGLPH EVFNGLGRRP DARRALQKIA
     VAHIPCGSGN ALACNVFGTH RPSLAALAVV KGVATPMDLI SITQGDRRKL SFLSQALGII
     AEADLATEHL RWMGEHRFTY GVAMRILKKR VYPCDLYVKV DIDHKQGVRE HYRRERENSS
     VVELDKMTTS TGTRTHVGRD SSVADSEEAA GSEHGAGLPP LKYGTVNDKL PAGWEKIDAD
     NVGNFYCGNV AYMAPDVIFF NAAWINDGYM DLITVDGNVP TAKAPGLMLS VSNNSFFDNS
     LVTYRKVSAF RIIPKNQEDG YISIDGEKVP FEPFQAEVHQ GLGMVITKRG LMEAPGPRNW
     DKVSMSERLM A
//
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