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CGHD_CHAGB
ID   CGHD_CHAGB              Reviewed;         484 AA.
AC   Q2HBN3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Transcription factor cghD {ECO:0000303|PubMed:26360642};
DE   AltName: Full=Sch210972 biosynthesis cluster protein D {ECO:0000303|PubMed:26360642};
GN   Name=cghD {ECO:0000303|PubMed:26360642}; ORFNames=CHGG_02371;
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=26360642; DOI=10.1002/cbic.201500386;
RA   Sato M., Yagishita F., Mino T., Uchiyama N., Patel A., Chooi Y.H., Goda Y.,
RA   Xu W., Noguchi H., Yamamoto T., Hotta K., Houk K.N., Tang Y., Watanabe K.;
RT   "Involvement of lipocalin-like CghA in decalin-forming stereoselective
RT   intramolecular [4+2] cycloaddition.";
RL   ChemBioChem 16:2294-2298(2015).
CC   -!- FUNCTION: Transcription factor that regulates the expression of the
CC       gene cluster that mediates the biosynthesis of the tetramic acid
CC       Sch210972, a potential anti-HIV fungal natural product that contains a
CC       decalin core. {ECO:0000305|PubMed:26360642}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
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DR   EMBL; CH408030; EAQ90436.1; -; Genomic_DNA.
DR   RefSeq; XP_001228887.1; XM_001228886.1.
DR   EnsemblFungi; EAQ90436; EAQ90436; CHGG_02371.
DR   GeneID; 4388356; -.
DR   eggNOG; ENOG502S7PT; Eukaryota.
DR   HOGENOM; CLU_578946_0_0_1; -.
DR   InParanoid; Q2HBN3; -.
DR   OMA; LEEGPWH; -.
DR   OrthoDB; 1576792at2759; -.
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   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   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; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..484
FT                   /note="Transcription factor cghD"
FT                   /id="PRO_0000453349"
FT   DNA_BIND        21..54
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          59..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   484 AA;  50375 MW;  E0663CCC25AD3C41 CRC64;
     MFQTESHPAG GSPLQSIRSS CDRCRLQKLK CTVQSMESDG RMVCERCVRA KVPCAFGRRR
     RASRPSDTKK QGDSSTRRST APRTTNPEPT VLTPPLSTTS STSEQTLGGA TPSPTLATSS
     ALEAPLETLA ECEPDTTAPT YSYHHHHHDS YQLGEGPPTP FPNPATTGGG SGSSMMDWDW
     LEQDFHANEL YCLDPELLAS APASTSTSTG SPTAHHRALP DGGSGSSTMS MGGGADTPFS
     TTASVAGRRL PALIAEMQQR LEALENGAWL HDGAQSFDHY PIGAVLRLSQ EFGALAGQVL
     GMAATYGGGG GVPPSDVAGL QMMAAVGGGG GLYELGRGGL AEGGSSTATV LLVLGGYVFL
     VRLYGLVLGH FHAHLNRIPS GSLGGHMHST PAPTTSPTLQ LGELPSGGAM PDVSRIHAAL
     GMLLAALHSV EEQLGQGGEV AREMVVSILT QGSGLEPAKL QDGFGDLGEK VRSVKELLRE
     KMGL
 
 
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