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Database: UniProt
Entry: A0A2J6PKK7_9HELO
LinkDB: A0A2J6PKK7_9HELO
Original site: A0A2J6PKK7_9HELO 
ID   A0A2J6PKK7_9HELO        Unreviewed;       517 AA.
AC   A0A2J6PKK7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   SubName: Full=Sphingoid long chain base kinase-like protein {ECO:0000313|EMBL:PMD14547.1};
GN   ORFNames=NA56DRAFT_682427 {ECO:0000313|EMBL:PMD14547.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD14547.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD14547.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD14547.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ613521; PMD14547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6PKK7; -.
DR   STRING; 1745343.A0A2J6PKK7; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000235672; 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:PMD14547.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235672};
KW   Transferase {ECO:0000313|EMBL:PMD14547.1}.
FT   DOMAIN          135..274
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   517 AA;  56978 MW;  A3AE91055A6340FC CRC64;
     MTTASMATDN PFVDPTSFED GRGSLAADTL ALGRSISLTL GTDALIVLDE EFEKRDRSNC
     CGLWPGTAAN TRAIPFYNIL WAELKDSELT INYASPNSKT SVRAATLKYP IEYQMVELVN
     LFTKRLLDRA YGESQQRKRA KVLVNPHSGK GSAEKWYFRD IEPLLKAAQI TIDMAKTRHK
     GEAVDIAEKM DIDAFDIIAS CSGDGLPHEV FNGLGKRPDA KKALSKIAVV HIPCGSGNAM
     SCNLNGTDSP SLATLAIIKG IPTPLDLISI TQGNTRTLSF LSQSVGIVAE ADLATEHLRW
     MGSQRFTYGF LVRLIRKALY PCDIAVKVAI DDKSSIREHY KREQKNHEPA SERRGYKFLL
     DDDASASTGS GNDDGLPPLR YGTVNDKLPE GWELAPYDKL GNFYCGNMAY MASDANFFSP
     ALPNDGYMDL VCINGDISRL EAMQMMFAVE NNKLFDNPGV WYRKILGYRI IPKNQEDGYI
     SIDGERVPFA PFQAEIHKGL GTVLSKTGHM YEAPGPV
//
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