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Database: UniProt
Entry: A0A0F7TWF5_PENBI
LinkDB: A0A0F7TWF5_PENBI
Original site: A0A0F7TWF5_PENBI 
ID   A0A0F7TWF5_PENBI        Unreviewed;       465 AA.
AC   A0A0F7TWF5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   28-JAN-2026, entry version 30.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=PMG11_09569 {ECO:0000313|EMBL:CEJ61023.1};
OS   Penicillium brasilianum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=104259 {ECO:0000313|EMBL:CEJ61023.1, 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; CDHK01000009; CEJ61023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7TWF5; -.
DR   STRING; 104259.A0A0F7TWF5; -.
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          109..249
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   465 AA;  52233 MW;  50A03FD4C96C5838 CRC64;
     MEMKDVTDQA ICQTTLYVES ATLELDEGRL TIRQSQKQFA RQQSIQVQYL HVLWAHATTE
     QLTIHFAAER HKVLNAATRV FQLLDQDTSS SRVQAWIQLL LDRAYGASKP RKHLKIYLNP
     VSGKGSAVKL YHRYAEPLFE GARCHVELHE TCYSGHASWS VREDRDIDSW DAIVCCSGDG
     LPYEVINGIA QRDDAGYILR NVPIVQLPGG SGNAMCVNMF KTTSFSHAAL YTIKGIRQPI
     DLMSVTQGDK RYISFLSQNI GLLAECDLDT ENMRFLGGQR FAVGFLQRLF NPPVYGCDLA
     VYNPASEHLT DPCAGRLGSQ FDVEGRHGLP DLQFGSVNDS LPESWKWEHH PTLSVFFAGQ
     FPFVDAKSKV FPDANHDDGL VDIIIMDSRI GARKLLQLFK RVPEGNHLAM REVHHRKVSA
     YRVVPARTRG AFSIDGERSS FQTFQVEVHP QLGMTLVAPT GVEER
//
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