ID   CREA_ASPFN              Reviewed;         429 AA.
AC   B8NGC8;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Probable DNA-binding protein creA;
DE   AltName: Full=Carbon catabolite repressor A;
GN   Name=creA; ORFNames=AFLA_134680;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963478; EED50705.1; -; Genomic_DNA.
DR   RefSeq; XP_002379481.1; XM_002379440.1.
DR   AlphaFoldDB; B8NGC8; -.
DR   SMR; B8NGC8; -.
DR   STRING; 5059.CADAFLAP00007346; -.
DR   EnsemblFungi; EED50705; EED50705; AFLA_134680.
DR   VEuPathDB; FungiDB:AFLA_134680; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_036230_0_0_1; -.
DR   OMA; PKVAVHD; -.
DR   Proteomes; UP000001875; 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: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..429
FT                   /note="Probable DNA-binding protein creA"
FT                   /id="PRO_0000395721"
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..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..189
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          351..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..288
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  46211 MW;  2947C2B64BD8F39C CRC64;
     MPPPASSVDF TNLLNPQNNE TGSAPSTPVD SSKAPSTPSS TQSNSTMASS VSLLPPLMKG
     ARPATEEARQ DLPRPYKCPL CDRAFHRLEH QTRHIRTHTG EKPHACQFPG CTKRFSRSDE
     LTRHSRIHNN PNSRRSNKAH LAAAAAAAAA GQENAMVNVT NAGSLMPPPT KPMTRSAPVS
     QVGSPDVSPP HSFSNYAGHM RSNLGPYARN TERASSGMDI NLLATAASQV ERDEQHFGFH
     AGPRNHHLFA SRHHTGRGLP SLSAYAISHS MSRSHSHEDE DGYTHRVKRS RPNSPNSTAP
     SSPTFSHDSL SPTPDHTPLA TPAHSPRLRP LGSSELHLPS IRHLSLHHTP ALAPMEPQPE
     GPNYYSPSQS HGPTISDIMS RPDGTQRKLP VPQVPKVAVQ DMLNPSAGFS SVSSSTNNSV
     AGNDLAERF