ID   CREA_ASPNG              Reviewed;         427 AA.
AC   Q05620;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=DNA-binding protein creA;
DE   AltName: Full=Carbon catabolite repressor A;
GN   Name=creA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8359691; DOI=10.1016/0378-1119(93)90425-3;
RA   Drysdale M.R., Kolze S.E., Kelly J.M.;
RT   "The Aspergillus niger carbon catabolite repressor encoding gene, creA.";
RL   Gene 130:241-245(1993).
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; L03811; AAA32690.1; -; Genomic_DNA.
DR   PIR; JN0785; JN0785.
DR   AlphaFoldDB; Q05620; -.
DR   SMR; Q05620; -.
DR   STRING; 5061.CADANGAP00001839; -.
DR   VEuPathDB; FungiDB:An02g03830; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1020757; -.
DR   VEuPathDB; FungiDB:ATCC64974_62010; -.
DR   VEuPathDB; FungiDB:M747DRAFT_54685; -.
DR   eggNOG; KOG1721; Eukaryota.
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..427
FT                   /note="DNA-binding protein creA"
FT                   /id="PRO_0000046871"
FT   ZN_FING         76..98
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         104..128
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   427 AA;  46141 MW;  4CA3D3B7DD148456 CRC64;
     MPPPASSVDF SNLLNPQNNS TDSTPSTPVD SSKTPSTPSS TQSNSNMASS VSLLPPLMKG
     ARPATEEVRQ DLPRPYKCPL CDRAFHRLEH QTRHIRTHTG EKPHACQFPG CTKRFSRSDE
     LTRHSRIHNN PNSRRRNKAQ HLAAAAAAAA GQDNAMANTA SAMMPPPSKP MTRSAPVSQV
     GSPDISPPHS FSNYASHMRS NLGPYARKGD EASSGMELYL LATAASQVER DEHFDFHAGP
     RNHHLFSSRH HGSGRLPLLA AYAITHNMSR SHSPEDDDGY SHRVKRSRPN SPNSTAPSSP
     TFSHDSLSPT PDHTPLATPA HSPRLRPLGS SDLHLPSIRH LSLHHTPALA PMEPQPEGPN
     YYSPSQGHHG PSISDIMSKP DGTQRKLPVP QVPKVAVQDM LNPGSGFSSV HSSTANSVAG
     GDLAERF