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Database: UniProt
Entry: A0A8H5BXZ7_9AGAR
LinkDB: A0A8H5BXZ7_9AGAR
Original site: A0A8H5BXZ7_9AGAR 
ID   A0A8H5BXZ7_9AGAR        Unreviewed;       480 AA.
AC   A0A8H5BXZ7;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 18.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=D9619_005936 {ECO:0000313|EMBL:KAF5331066.1};
OS   Psilocybe cf. subviscida.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Psilocybe.
OX   NCBI_TaxID=2480587 {ECO:0000313|EMBL:KAF5331066.1, ECO:0000313|Proteomes:UP000567179};
RN   [1] {ECO:0000313|EMBL:KAF5331066.1, ECO:0000313|Proteomes:UP000567179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101986 {ECO:0000313|EMBL:KAF5331066.1,
RC   ECO:0000313|Proteomes:UP000567179};
RX   PubMed=32382073; DOI=10.1038/s41396-020-0667-6;
RA   Floudas D., Bentzer J., Ahren D., Johansson T., Persson P., Tunlid A.;
RT   "Uncovering the hidden diversity of litter-decomposition mechanisms in
RT   mushroom-forming fungi.";
RL   ISME J. 14:2046-2059(2020).
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:KAF5331066.1}.
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DR   EMBL; JAACJJ010000001; KAF5331066.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8H5BXZ7; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000567179; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000567179};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          106..246
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   480 AA;  52604 MW;  5A33AA8C9D887782 CRC64;
     MTTPKTITVH TIPMATVKLT LNDHSVSVHK TIPSKAVNHH DIAFRYILRA TFEESTRTLS
     LAYVHKKNKV LHLTTFEGTV EETETSNASE WAESVMKAVY DDAGIKRSRH LKVLVNPFSG
     TKRGTGAFTK QVKPMLDIAG CKLDVLYTTH RGHAKDVAKT LPLDFDAVIT VSGDGLIHEV
     MNGFAEHADP MRAFQIPVAP IPTGSGNGLS LNLLGLEEGF DIVAAALNII KGQPMPVDLF
     SVTQSGKRTI SFMSQALGLM ADLDLGTEHL RWMGDARFIY GLLRGLIKFK SCPVQLSFKL
     AENDKDKMAA EFAAKQKEIT DALPGSRTTI LPLPENIGQG LPPLQHIHED TDGWTTFDEP
     LLFVYAGKGP YVGRDYMAFP VSVADDGLID IIAMAKVNRG DILSSMDGAP KGDSFWHPHA
     HYVKAHAYRV KPLSQDGCLA VDGEAYPFEE YQVEVHKGLG NLLSLYGQYA GKFGPRPKKP
//
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