ID   CREA_ASPFC              Reviewed;         424 AA.
AC   B0XSK6;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Probable DNA-binding protein creA;
DE   AltName: Full=Carbon catabolite repressor A;
GN   Name=creA; ORFNames=AFUB_027530;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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; DS499595; EDP54692.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XSK6; -.
DR   SMR; B0XSK6; -.
DR   EnsemblFungi; EDP54692; EDP54692; AFUB_027530.
DR   VEuPathDB; FungiDB:AFUB_027530; -.
DR   HOGENOM; CLU_036230_0_0_1; -.
DR   PhylomeDB; B0XSK6; -.
DR   Proteomes; UP000001699; 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..424
FT                   /note="Probable DNA-binding protein creA"
FT                   /id="PRO_0000395723"
FT   ZN_FING         74..96
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         102..126
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          115..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..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          403..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..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   424 AA;  45812 MW;  1ED4E63CF0E570FD CRC64;
     MPPPASSMGF SDLLNPQNPE STPSTPASKS SAPSTPSTEQ SNSNMASSVS LLPPLMKGAR
     PANEEPRQDL PRPYKCPLCD RAFHRLEHQT RHIRTHTGEK PHACQFPGCT KRFSRSDELT
     RHSRIHNNPN SRRNNKAQHL AAAAAAAAAN QDNALASNAA SMMPPPSKPI TRSAPVSQVG
     SPDISPPHSF SNYAGHMRSN LGSYARNSDR ASSGMDINLL ATAASQVERD EHYGFHNGPR
     GHHIFGSRHH NNNRLPSLSA YAISQNMSRS YSHDEDDMYS HRVKRSRPNS PNSTAPSSPT
     FSHDSLSPTP DHTPLATPAH SPRLRPLGTS ELQLPSIRHL SLHHTPALAP MEPQPEGPNY
     YSPTQPHVGP SISDIMSKPD GTQRKLPVPQ VPKVAVQDLL SPGFTSVSSS ASNSVAGGDL
     ADRF