CREA_ASPNC
ID CREA_ASPNC Reviewed; 427 AA.
AC A2QCJ9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Probable DNA-binding protein creA;
DE AltName: Full=Carbon catabolite repressor A;
GN Name=creA; ORFNames=An02g03830;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270005; CAL00597.1; -; Genomic_DNA.
DR RefSeq; XP_001399519.1; XM_001399482.2.
DR AlphaFoldDB; A2QCJ9; -.
DR SMR; A2QCJ9; -.
DR PaxDb; A2QCJ9; -.
DR PRIDE; A2QCJ9; -.
DR EnsemblFungi; CAL00597; CAL00597; An02g03830.
DR GeneID; 4978870; -.
DR KEGG; ang:ANI_1_524024; -.
DR VEuPathDB; FungiDB:An02g03830; -.
DR HOGENOM; CLU_036230_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 4R.
DR GO; GO:0005634; C:nucleus; IGI:AspGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:AspGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043609; P:regulation of carbon utilization; IMP:AspGD.
DR GO; GO:0010468; P:regulation of gene expression; IMP:AspGD.
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..427
FT /note="Probable DNA-binding protein creA"
FT /id="PRO_0000395724"
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..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..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..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..427
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 269..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 404..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 46016 MW; 50BF25D48CC0D1E6 CRC64;
MPPPASSVDF SNLLNPQNNS TDSTPSTPVD SSKTPSTPSS TQSNSNMASS VSLLPPLMKG
ARPATEEVRQ DLPRPYKCPL CDRAFHRLEH QTRHIRTHTG EKPHACQFPG CTKRFSRSDE
LTRHSRIHNN PNSRRSNKAQ HLAAAAAAAA GQDNAMANTA SAMMPPPSKP MTRSAPVSQV
GSPDISPPHS FSNYASHMRS NLGPYARKGE RASSGMDINL LATAASQVER DEHFSFHAGP
RNHHLFSSRH HGSGRLPSLS AYAITHNMSR SHSHEDDDGY SHRVKRSRPN SPNSTAPSSP
TFSHDSLSPT PDHTPLATPA HSPRLRPLGS SDLHLPSIRH LSLHHTPALA PMEPQPEGPN
YYSPSQGHHG PSISDIMSKP DGTQRKLPVP QVPKVAVQDM LNPGSGFSSV TSSTANSVAG
GDLAERF
