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Database: UniProt
Entry: A0A0F7VFY8_PENBI
LinkDB: A0A0F7VFY8_PENBI
Original site: A0A0F7VFY8_PENBI 
ID   A0A0F7VFY8_PENBI        Unreviewed;       501 AA.
AC   A0A0F7VFY8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   28-JAN-2026, entry version 33.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=PMG11_03554 {ECO:0000313|EMBL:CEO58855.1};
OS   Penicillium brasilianum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=104259 {ECO:0000313|EMBL:CEO58855.1, ECO:0000313|Proteomes:UP000042958};
RN   [1] {ECO:0000313|Proteomes:UP000042958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG11 {ECO:0000313|Proteomes:UP000042958};
RX   PubMed=26337871; DOI=10.1128/genomea.00724-15;
RA   Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Brakhage A.A.,
RA   Valiante V.;
RT   "Draft genome sequence of the fungus Penicillium brasilianum MG11.";
RL   Genome Announc. 3:0-0(2015).
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DR   EMBL; CDHK01000003; CEO58855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7VFY8; -.
DR   STRING; 104259.A0A0F7VFY8; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000042958; 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:UP000042958};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          128..267
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   501 AA;  54966 MW;  526523D11D2D7940 CRC64;
     MSSSDLATEH PEAQLEHDST LVLDKAVSLT LSSDSLLILD DRPHRKSTRG CCGLCKSKAN
     TKTTHAISLY NVLDAEINPS SLVITYAQHS SKDDVSVTAL HYPVGEKEKP AVEAWMNKLL
     DLAYGTAQRR KRLKVLINPF GGKGNAASLY QKYSAPIFAA ARCQVDVQST EYRGHAIEIA
     EHLDIDAYDA IICCSGDGLP YEVFNGLGKR PNGREALAKV AVALLPCGSG NGLTWNCQGT
     GSNSIAALCI VKGLRTPLDL VSVTQQNTRT LSFLSQSFGI VAECDLGTDH IRWMGAQRFT
     YGFLVRLLQR TIWPCDLAIK VEMDDKQAIK EHYAAWRAKE EEDDPLADQN RLAAAKQSPA
     LPELQFGTVK DELPKEWEVI PGETMGNFYA GNMAIMSKDT NFFPASLPND GLMDIVTIDG
     TVSRGTSLKM MTEIETGGFF NMPDVKIRKA IAYRLVPHQK EGYISIDGER VPFEAFQCEI
     HQGLGTVLAK STRVYEADGP R
//
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