CHEC_CHAGB
ID CHEC_CHAGB Reviewed; 409 AA.
AC Q2HEW6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Chaetoglobosin A biosynthesis cluster protein C {ECO:0000303|PubMed:33622536};
GN Name=cheC {ECO:0000303|PubMed:33622536}; ORFNames=CHGG_01238;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
RN [2]
RP FUNCTION.
RX PubMed=23611317; DOI=10.1021/ja402828w;
RA Ishiuchi K., Nakazawa T., Yagishita F., Mino T., Noguchi H., Hotta K.,
RA Watanabe K.;
RT "Combinatorial generation of complexity by redox enzymes in the
RT chaetoglobosin A biosynthesis.";
RL J. Am. Chem. Soc. 135:7371-7377(2013).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=33622536; DOI=10.1016/j.funbio.2020.10.010;
RA Cheng M., Zhao S., Liu H., Liu Y., Lin C., Song J., Thawai C.,
RA Charoensettasilp S., Yang Q.;
RT "Functional analysis of a chaetoglobosin A biosynthetic regulator in
RT Chaetomium globosum.";
RL Fungal Biol. 125:201-210(2021).
CC -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC chaetoglobosin A which has a unique inhibitory activity against actin
CC polymerization in mammalian cells (PubMed:23611317, PubMed:33622536).
CC Chaetoglobosin A and its intermediates are involved in the
CC morphological differentiation of C.globosum (PubMed:33622536). The
CC first step of the pathway is the synthesis of prochaetoglobosin I via
CC condensation of one acetyl-CoA, 8 malonyl-CoA, and a L-tryptophan
CC molecule by the PKS-NRPS hybrid synthetase cheA, followed by reduction
CC of backbone double bond to install desired geometry by the enoyl
CC reductase cheB (PubMed:23611317). Further multiple oxidation steps
CC performed by the cytochrome P450 monooxygenases cheE and cheG, as well
CC as by the FAD-linked oxidoreductase cheF, lead to the formation of
CC chaetoglobosin A (PubMed:23611317). Depending on the order of action of
CC these reductases, distinct intermediates can be identified
CC (PubMed:23611317). Within the pathway, the cytochrome P450
CC monooxygenase cheE catalyzes a stereospecific epoxidation on
CC prochaetoglobosin I, cytoglobosin D, and chaetoglobosin J intermediates
CC (PubMed:23611317). The FAD-linked oxidoreductase cheF performs
CC dehydrogenation of the C-20 hydroxyl groups in the 20-
CC dihyrochaetoglobosin A and cytoglobosin D intermediates
CC (PubMed:23611317). Finally, the cytochrome P450 monooxygenase cheG can
CC catalyze the stereospecific dihydroxylation of prochaetoglobosin I and
CC prochaetoglobosin IV at C-19 and C-20, respectively (PubMed:23611317).
CC The Diels-Alderase cheD may play a role in the post-PKS-NRPS
CC biosynthetic steps catalyzing Diels-Alder cyclization (Probable).
CC {ECO:0000269|PubMed:23611317, ECO:0000269|PubMed:33622536,
CC ECO:0000305|PubMed:33622536}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00583}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor cheR that binds directly to an asymmetric direct
CC repeat present in the promoter. {ECO:0000269|PubMed:33622536}.
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DR EMBL; CH408029; EAQ93003.1; -; Genomic_DNA.
DR RefSeq; XP_001220459.1; XM_001220458.1.
DR AlphaFoldDB; Q2HEW6; -.
DR SMR; Q2HEW6; -.
DR EnsemblFungi; EAQ93003; EAQ93003; CHGG_01238.
DR GeneID; 4387644; -.
DR eggNOG; KOG3105; Eukaryota.
DR HOGENOM; CLU_013929_4_1_1; -.
DR InParanoid; Q2HEW6; -.
DR OMA; CKVGESA; -.
DR OrthoDB; 1343623at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR InterPro; IPR007889; HTH_Psq.
DR Pfam; PF05225; HTH_psq; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51253; HTH_CENPB; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..409
FT /note="Chaetoglobosin A biosynthesis cluster protein C"
FT /id="PRO_0000452798"
FT DOMAIN 51..120
FT /note="HTH CENPB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00583"
FT DNA_BIND 84..113
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00583"
FT REGION 243..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 409 AA; 46085 MW; B4FE1B5DDA001E57 CRC64;
MRSPPREARL RMAVEAIGKN KNLSIRAAAR QYNVPEATIR HRCTGRSARR DLPANSRKLT
DLEERTIVQY ILELDARAFP PRLRGVEDMA NHLLRERDAP PVGKLWAHNF VKRQPQLRTR
RTRRYDYQRA KCEDPKVIGE WFTLVQDAKA KYGIVDDDVY NFDETGLMMG IIFAGQAYGR
LIDELMRAHI NHITKLEFLC AFREAFFASM TEKNIQGGFS GAGIVPFDPE RVLSKLDVKL
HTPTHPDSRP GTAQPWASKT PYNAQETRSQ SDFIKTRISS YQNSSPASVL VAVDQLTKGA
TAVMHQVALL QSEVSSLRKA NEPLSKRRKA KRTRIQLGGP LTVQDAQDPL DQRDVGKGAL
QETQPDSSGA GGARAKVRRC NSCCKVGESA SLAYMRRSLI IYVRSYNDF
