ID   CREA_ASPCL              Reviewed;         425 AA.
AC   A1C6L9;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Probable DNA-binding protein creA;
DE   AltName: Full=Carbon catabolite repressor A;
GN   Name=creA; ORFNames=ACLA_070730;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027045; EAW14040.1; -; Genomic_DNA.
DR   RefSeq; XP_001275466.1; XM_001275465.1.
DR   AlphaFoldDB; A1C6L9; -.
DR   SMR; A1C6L9; -.
DR   STRING; 5057.CADACLAP00007012; -.
DR   EnsemblFungi; EAW14040; EAW14040; ACLA_070730.
DR   GeneID; 4708318; -.
DR   KEGG; act:ACLA_070730; -.
DR   VEuPathDB; FungiDB:ACLA_070730; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_036230_0_0_1; -.
DR   OMA; PKVAVHD; -.
DR   OrthoDB; 1617199at2759; -.
DR   Proteomes; UP000006701; 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; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..425
FT                   /note="Probable DNA-binding protein creA"
FT                   /id="PRO_0000395720"
FT   ZN_FING         75..97
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         103..127
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   425 AA;  45972 MW;  B53576055C150DAD CRC64;
     MPPSASSVGF SDLLNPQNPT ESAPSTPVNK SPASSAPSSA QSNSTMASSV SLLPPLMKGT
     RPANEEPRQD LPRPYKCPLC DRAFHRLEHQ TRHIRTHTGE KPHACQFPGC TKRFSRSDEL
     TRHSRIHNNP NSRRNNKAQH LAAAAAAAAN QDNVLVNNTG SMMPPPSKPI TRSAPVSQVG
     SPDISPPHSF TNYAGHMRSN LGPYARNNER ASSGMDINLL ATAASQVERD EHFGFHNGPR
     GLPLFSSRLH NSSRLPSLSA YAISQNMTRS HSHDEEDVYS HRVKRSRPNS PNSTAPSSPT
     FSHDSLSPTP DHTPLATPAH SPRLRPLGTS ELQLPSIRHL SLHHTPALAP MEPQPEGPNY
     YSPTQPHHGP SISDIMSKPD GTQRKLPVPQ VPKVAVQDML NPTGFVSVSS STSNSVAGGD
     LAERF