ID   CREA_GIBFU              Reviewed;         420 AA.
AC   O94131;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=DNA-binding protein creA;
DE   AltName: Full=Carbon catabolite repressor;
GN   Name=CREA;
OS   Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium
OS   fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=5127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=m567;
RX   PubMed=10689158; DOI=10.1111/j.1574-6968.2000.tb08982.x;
RA   Tudzynski B., Liu S., Kelly J.M.;
RT   "Carbon catabolite repression in plant pathogenic fungi: isolation and
RT   characterization of the Gibberella fujikuroi and Botrytis cinerea creA
RT   genes.";
RL   FEMS Microbiol. Lett. 184:9-15(2000).
CC   -!- FUNCTION: Involved in carbon catabolite repression. Represses the
CC       transcription of a number of genes by binding to a GC-rich region in
CC       their promoter (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the creA/MIG C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; Y16626; CAA76330.1; -; Genomic_DNA.
DR   AlphaFoldDB; O94131; -.
DR   EnsemblFungi; CCT64031; CCT64031; FFUJ_04790.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_036230_0_0_1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0061987; P:negative regulation of transcription from RNA polymerase II promoter by glucose; IEA:EnsemblFungi.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..420
FT                   /note="DNA-binding protein creA"
FT                   /id="PRO_0000046876"
FT   ZN_FING         64..86
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         92..116
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   420 AA;  45892 MW;  106CDD10A1DBB4DC CRC64;
     MQRAQSAVDF SNLLNPTVPA DKESEKPHQG DVEMATAAVT VIKPNGPLPG VQNSENSNEL
     PRPYKCPLCD KAFHRLEHQT RHIRTHTGEK PHACQFPGCS KKFSRSDELT RHSRIHNNPN
     SRRGNKAAQA HQQQQHQMHQ QQGLPPHMMP DGMMAPPPAP KTIRSAPGSA LASPNVSPPH
     SYSTFALPVS AVHYNRGGDI SMLAKAATQV ERETLTAPPH HSNNHRHHPY FGHGMHSSRG
     HLPTLSSYHM GRSHSNEDPS DDHYSGAMRH AKRSRPNSPN STAPSSPTFS HDSLSPTPDH
     TPIATPAHSP RLRPFSTGYE LPSLRNLSLQ HNTTPALAPM EPHLEQNQFQ QGSAPTTQPR
     PTGMSLTDII SRPDGSQRKL PVPQVPKVAV QDLLSDNGFS HSGRSSGTSS LAGGDLMDRM