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CTNR_MONPU
ID   CTNR_MONPU              Reviewed;         576 AA.
AC   Q1ERI1;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Citrinin biosynthesis transcriptional activator ctnR;
GN   Name=ctnR {ECO:0000303|PubMed:17586673};
GN   Synonyms=ctnA {ECO:0000303|PubMed:17586673},
GN   orf2 {ECO:0000303|PubMed:17586673};
OS   Monascus purpureus (Red mold) (Monascus anka).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Monascus.
OX   NCBI_TaxID=5098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17586673; DOI=10.1128/aem.01979-06;
RA   Shimizu T., Kinoshita H., Nihira T.;
RT   "Identification and in vivo functional analysis by gene disruption of ctnA,
RT   an activator gene involved in citrinin biosynthesis in Monascus
RT   purpureus.";
RL   Appl. Environ. Microbiol. 73:5097-5103(2007).
RN   [2]
RP   FUNCTION.
RX   PubMed=19111642; DOI=10.1263/jbb.106.466;
RA   Sakai K., Kinoshita H., Shimizu T., Nihira T.;
RT   "Construction of a citrinin gene cluster expression system in heterologous
RT   Aspergillus oryzae.";
RL   J. Biosci. Bioeng. 106:466-472(2008).
CC   -!- FUNCTION: Transcription factor that regulates the expression of the
CC       gene cluster that mediates the biosynthesis of the mycotoxin citrinin,
CC       a hepato-nephrotoxic compound to humans due to inhibition of
CC       respiration complex III (PubMed:17586673, PubMed:19111642).
CC       {ECO:0000269|PubMed:17586673, ECO:0000269|PubMed:19111642}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Leads to a large decrease in the transcription of
CC       pksCT and ctnC, together with reduction of citrinin production to
CC       barely detectable level (PubMed:17586673).
CC       {ECO:0000269|PubMed:17586673}.
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DR   EMBL; AB243687; BAE95337.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1ERI1; -.
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   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00906; Fungal_trans; 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   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..576
FT                   /note="Citrinin biosynthesis transcriptional activator
FT                   ctnR"
FT                   /id="PRO_0000440324"
FT   DNA_BIND        29..56
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   576 AA;  65177 MW;  D74658680D5771CF CRC64;
     MLSHEMASTA HRQPSRPTTR QRQRTGRACE ECRRRKLRCD GQQPRCGVCV DSGVTCEVNS
     QRRPRGPKKG YLTALRNRVA MLETRLPAQH LVGPLSEFNP LSTPLTNDHH DGCSVSSASS
     RSDSNPPPTV SEPDMSLPNT TTSVSSAPSF ATCSKDIGGA EPITELVQAE LNQLYFDRVH
     PSIQILHQRR YLGWARNAAK KTSRRCLQYA VWTLASLLSA QFQHLQDSFY QETKRTLEFS
     YLSGDSNAPV DTEEIQAWIL IATYESMRTF HRSAWMSAGR AFRLVQLMRL HEIDSPTKPP
     VPEADLVETE EKRRVFWMAY FLDHLLSMRN NWPITLNEHV ICTRLPAPDM EFQSGQPVLG
     AFLSEAIMDV MPQTTSPFNE CVILATICGR SLFHAQQYSV RFVYGELAPN WTDQHQWLDN
     VLTNRLQILS QYYPSPTQIC DPMLSFAHIM GQASVIHLYK GMASVVWAVD DGAWVVEYQR
     RALSAAQEIV KLAKGLTEFN FFKVHPLMPI PLLLCAEFLY SNRGSDAAFN SLLQELLQIF
     RQLKNANDPS RSYIHLLELS CTTASMSLVR EHSNAP
 
 
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