CREA_BOTFU
ID CREA_BOTFU Reviewed; 435 AA.
AC O94130;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=DNA-binding protein creA;
DE AltName: Full=Carbon catabolite repressor;
GN Name=creA;
OS Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=40559;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SAS56;
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; Y16625; CAA76329.1; -; Genomic_DNA.
DR AlphaFoldDB; O94130; -.
DR SMR; O94130; -.
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 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..435
FT /note="DNA-binding protein creA"
FT /id="PRO_0000046873"
FT ZN_FING 73..95
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 101..125
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 114..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 47525 MW; BA9CE268A9CD474E CRC64;
MQRASSAVDF NSLLNPPQSA QELEHQAARQ KLAIIQQQQQ HQREAEMAAM SMMAPTMVGG
HHGDDRQDLP RPYKCPLCEK AFHRLEHQTR HIRTHTGEKP HACMFPGCTK RFSRSDELTR
HSRIHNNPNS RRSNKAQQAP QMGVAMHSES MATMMPPPNK NITRSAPASA LGSPNVSPPH
SYSSYSSNYL SSLNPHGRSL GGSPSNGQAP LTDINMLATA ATQVERESST TATHYSQHTQ
PRHQPYYSHS SHNSRNHLPS LQAYAMTRAH SHEEDDHYAH RHAKRSRPNS PMSTAPSSPT
FSHDSLSPTP DHTPLATPAH SPRLRPFGGG YDLPGIRNLS LHHTPALAPM EPQHLDGQYH
TTATPTPPTT SAPRTGLTIS DIMSRTDGST RKLPVPQAPV AVQDLSSPGE IGFNTSGQSS
TTGSVAGNDL ADRMI