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Database: UniProt
Entry: A0A1V6QK33_9EURO
LinkDB: A0A1V6QK33_9EURO
Original site: A0A1V6QK33_9EURO 
ID   A0A1V6QK33_9EURO        Unreviewed;       489 AA.
AC   A0A1V6QK33;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   28-JAN-2026, entry version 28.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=PENANT_c002G02764 {ECO:0000313|EMBL:OQD89565.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD89565.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQD89565.1}.
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DR   EMBL; MDYN01000002; OQD89565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QK33; -.
DR   STRING; 416450.A0A1V6QK33; -.
DR   Proteomes; UP000191672; 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:UP000191672};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          118..257
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
SQ   SEQUENCE   489 AA;  52922 MW;  B6D23F2CE9E75386 CRC64;
     MSTTDTAQDA HDSTLKVDSV SLTLGTDSLL IIDDRPARPN RRCCGLLKSS SQTTHAISLY
     NVLGAEVTAS NIVIAYAQPA GKDDVAVATV QYPIAEKEKK AVEAWVVKLV DQAYGKAMRG
     KKLKVLINPF GGKGAAASLY QRYAAPVFAA AKCQVDLQST EHRGHAIDIA ENLDVDAYDA
     VVCCSGDGLP YEVFNGLGKR PDARTALVKT AVALLPCGSG NGMTWNAFGT GSVSIAALAI
     VKGLRTPLDL VSISQKDSRT LSFLSQSFGI VAESDLATEN IRWMGAQRFT YGFLVRLMRQ
     TIWPCDLTVK VDIGDKEAIK EHYATWSTRP EESDVDTKRL EAAAQSPTLP ELKYGTIADD
     VPSDWQVVPG ETMGNFYAGN MAIVSKDTNM FPATLPNDGL MDVITIDGRV SRGTAITMMN
     EIPSGRFFDM PELNIRKASA FRLVPHQKEG YISIDGERVP FEAFQAEVHQ GLGTILTKSG
     RLYEAEGPR
//
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