CALC_PENDC
ID CALC_PENDC Reviewed; 426 AA.
AC A0A1V6PAU0;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Transcriptional regulator calC {ECO:0000303|PubMed:30598828};
DE AltName: Full=Calbistrin biosynthesis cluster protein C {ECO:0000303|PubMed:30598828};
GN Name=calC {ECO:0000303|PubMed:30598828}; ORFNames=PENDEC_c013G06298;
OS Penicillium decumbens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11843;
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).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=8436557; DOI=10.7164/antibiotics.46.34;
RA Jackson M., Karwowski J.P., Humphrey P.E., Kohl W.L., Barlow G.J.,
RA Tanaka S.K.;
RT "Calbistrins, novel antifungal agents produced by Penicillium restrictum.
RT I. Production, taxonomy of the producing organism and biological
RT activity.";
RL J. Antibiot. 46:34-38(1993).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=24287995; DOI=10.3390/molecules181214629;
RA Bladt T.T., Duerr C., Knudsen P.B., Kildgaard S., Frisvad J.C.,
RA Gotfredsen C.H., Seiffert M., Larsen T.O.;
RT "Bio-activity and dereplication-based discovery of ophiobolins and other
RT fungal secondary metabolites targeting leukemia cells.";
RL Molecules 18:14629-14650(2013).
RN [4]
RP IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=30598828; DOI=10.1186/s40694-018-0063-4;
RA Grijseels S., Pohl C., Nielsen J.C., Wasil Z., Nygaard Y., Nielsen J.,
RA Frisvad J.C., Nielsen K.F., Workman M., Larsen T.O., Driessen A.J.M.,
RA Frandsen R.J.N.;
RT "Identification of the decumbenone biosynthetic gene cluster in Penicillium
RT decumbens and the importance for production of calbistrin.";
RL Fungal Biol. Biotechnol. 5:18-18(2018).
CC -!- FUNCTION: Transcription activator that specifically regulates the
CC expression of the gene cluster that mediates the biosynthesis of
CC calbistrins and related compounds such as decumbenones. Calbistrin A is
CC a secondary metabolite with an interesting structure that was recently
CC found to have bioactivity against leukemia cells. It consists of two
CC polyketides linked by an ester bond: a bicyclic decalin containing
CC polyketide and a linear 12 carbon dioic acid structure.
CC {ECO:0000269|PubMed:30598828}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- INDUCTION: Expression is induced in complex medium (Czapek yeast
CC autolysate medium) supporting calbistrin production.
CC {ECO:0000269|PubMed:30598828}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of calbistrin and of the
CC related metabolites decumbenones, whereas production of unrelated
CC compounds, such as andrastin C, remains unaffected (PubMed:30598828).
CC Results in a significant down-regulation of the expression of the
CC calbistrin biosynthesis cluster genes calA, calB and calF
CC (PubMed:30598828). {ECO:0000269|PubMed:30598828}.
CC -!- BIOTECHNOLOGY: Calbistrin A has been reported to possess a number of
CC interesting bioactivities including antifungal active against Candida
CC albicans and cytotoxic toward both healthy and leukemic human cells.
CC {ECO:0000269|PubMed:24287995, ECO:0000269|PubMed:8436557}.
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DR EMBL; MDYL01000013; OQD73953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PAU0; -.
DR OMA; AQKLRCH; -.
DR OrthoDB; 1576792at2759; -.
DR Proteomes; UP000191522; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..426
FT /note="Transcriptional regulator calC"
FT /id="PRO_0000446471"
FT DNA_BIND 13..44
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 46..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 46697 MW; 37D71BB7CF7D07AC CRC64;
MSEPQAPKKR AACDRCRTQK LRCLRVPDHP TDSCIRCARS RMECITSSSK RPGRPRNPNN
ARPQQSDPGP ATCAETNPPL PAVDIPVQSL GTVDDWFNFG SLETDYEICS VPWDSVDSGF
PMEGVTAAHS ISSLSTPPPL VPSTTPTFLN TLATDTSVDE QFENEKCAQN EAEMLQPFGD
NIDHGLHLSL LQRELSKQLF ALNSMPWDMT KVMRITCLHD AEASASQVDS KYNSLAKIAK
TSAEFAQLLC SIQTPIAGDG GSNVSKNASP LSSIHPRLSM ADLLTILSCY MLTLSIYDSI
FSRFTEQASH NPGAVNVVLQ SAPKLYLGGI AVPPRLEMLS HLLCCLTSRQ LRPIEMLLGL
PDEYCIAWKR NGGSKEKQSG LFSGQSGQLL FSTLMRVETE RAGEEKGGLG VIESLKETIR
RIYEFD
