CREA_ASPAC
ID CREA_ASPAC Reviewed; 431 AA.
AC O94166;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=DNA-binding protein creA;
DE AltName: Full=Carbon catabolite repressor A;
GN Name=creA;
OS Aspergillus aculeatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5053;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Arai M., Kitawaki M., Takada G., Sumitani J., Kawaguchi T.;
RT "Cloning and sequence of the gene encoding CREA homologue from Aspergillus
RT aculeatus.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription regulator component of the regulatory network
CC controlling carbon source utilization through ubiquitination and
CC deubiquitination involving creA, creB, creC, creD and acrB. Represses
CC the transcription of the alcR, alcA and aldA genes by binding to a GC-
CC rich region in their promoter. Also plays a role in response to carbon
CC starvation and the control of extracellular proteases activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with creB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Deubiquitinated by creB, probably to control its
CC activity or amount (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the creA/MIG C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AB024314; BAA75519.1; -; Genomic_DNA.
DR AlphaFoldDB; O94166; -.
DR SMR; O94166; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_77778; -.
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 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; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..431
FT /note="DNA-binding protein creA"
FT /id="PRO_0000046870"
FT ZN_FING 79..101
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 107..131
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 46312 MW; C2812C4A48091DCE CRC64;
MPPPASSVDF SNLLNPQSNP TESTPSSPAT PVDSSKGPST PSSAQSTSSM ASSVSLLPPL
MKGSRPATEE VRQDLPRPYK CPLCDRAFHR LEHQTRHIRT HTGEKPHACQ FPGCTKRFSR
SDELTRHSRI HNNPNSRRSN KAQHLAAAAA AAAGQENAMP NNAGALMPPP SKPMTRSAPV
SQVGSPDISP PHSFSNYANH MRSNLGPYAR NTERASSGMD INLLATAASQ VERDDHFSFH
AGPRNHHLFS SSRHHGSGRL PSLSAYAITH NMSRSHSHEE DDSYSHRVKR SRPNSPNSTA
PSSPTFSHDL LSPTPDHTPL ATPAHSPRLR PLGSSDLHLP SIRHLSLHHT PALAPMEPQP
EGPSYYSPSQ SHGPSITDIM SKPDGTQRKL PVPQVPKVAV QDMLNPGSGF SSVTSSTANS
VAGGDLADRA F
