ID   CREA_NEOFI              Reviewed;         416 AA.
AC   A1DH89;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Probable DNA-binding protein creA;
DE   AltName: Full=Carbon catabolite repressor A;
GN   Name=creA; ORFNames=NFIA_087020;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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}.
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DR   EMBL; DS027696; EAW18746.1; -; Genomic_DNA.
DR   RefSeq; XP_001260643.1; XM_001260642.1.
DR   AlphaFoldDB; A1DH89; -.
DR   SMR; A1DH89; -.
DR   STRING; 36630.CADNFIAP00007056; -.
DR   EnsemblFungi; EAW18746; EAW18746; NFIA_087020.
DR   GeneID; 4587201; -.
DR   KEGG; nfi:NFIA_087020; -.
DR   VEuPathDB; FungiDB:NFIA_087020; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_036230_0_0_1; -.
DR   OMA; PKVAVHD; -.
DR   OrthoDB; 1617199at2759; -.
DR   Proteomes; UP000006702; 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..416
FT                   /note="Probable DNA-binding protein creA"
FT                   /id="PRO_0000395725"
FT   ZN_FING         66..88
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         94..118
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  44999 MW;  7063E4850EE2288B CRC64;
     MGFSDLLNPQ NPESTPSTPA NKSSAPSTPS TGQSNSNMTS VSLLPPLMKG ARPANEEPRQ
     DLPRPYKCPL CDRAFHRLEH QTRHIRTHTG EKPHACQFPG CTKRFSRSDE LTRHSRIHNN
     PNSRRNNKAQ HLAAAAAAAA ANQDNALASN AASMMPPPSK PITRSAPVSQ VGSPDISPPH
     SFSNYAGHMR SNLGPYARNS DRASSGMDIN LLATAASQVE RDEHYGFHNG PRGHHIFGSR
     HHNSNRLPSL SAYAISQNMS RSHSHDEDDM YSHRVKRSRP NSPNSTAPSS PTFSHDSLSP
     TPDHTPLATP AHSPRLRPLG TSELQLPSIR HLSLHHTPAL APMEPQPEGP NYYSPTQPHV
     GPSISDIMSK PDGTQRKLPV PQVPKVAVQD LLSPGFTSVS SSASNSVAGG DLADRF