CREA_EMENI
ID CREA_EMENI Reviewed; 416 AA.
AC Q01981; C8V211; Q5AZT5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=DNA-binding protein creA;
DE AltName: Full=Carbon catabolite repressor A;
GN Name=creA; ORFNames=AN6195;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1922072; DOI=10.1128/mcb.11.11.5701-5709.1991;
RA Dowzer C.E.A., Kelly J.M.;
RT "Analysis of the creA gene, a regulator of carbon catabolite repression in
RT Aspergillus nidulans.";
RL Mol. Cell. Biol. 11:5701-5709(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP CHARACTERIZATION.
RX PubMed=8076597; DOI=10.1002/j.1460-2075.1994.tb06718.x;
RA Mathieu M., Felenbok B.;
RT "The Aspergillus nidulans CREA protein mediates glucose repression of the
RT ethanol regulon at various levels through competition with the ALCR-
RT specific transactivator.";
RL EMBO J. 13:4022-4027(1994).
RN [5]
RP FUNCTION.
RX PubMed=11442830; DOI=10.1046/j.1365-2958.2001.02474.x;
RA Lockington R.A., Kelly J.M.;
RT "Carbon catabolite repression in Aspergillus nidulans involves
RT deubiquitination.";
RL Mol. Microbiol. 40:1311-1321(2001).
RN [6]
RP FUNCTION.
RX PubMed=18512059; DOI=10.1007/s00294-008-0198-6;
RA Katz M.E., Bernardo S.M., Cheetham B.F.;
RT "The interaction of induction, repression and starvation in the regulation
RT of extracellular proteases in Aspergillus nidulans: evidence for a role for
RT CreA in the response to carbon starvation.";
RL Curr. Genet. 54:47-55(2008).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18063396; DOI=10.1016/j.fgb.2007.10.016;
RA Roy P., Lockington R.A., Kelly J.M.;
RT "CreA-mediated repression in Aspergillus nidulans does not require
RT transcriptional auto-regulation, regulated intracellular localisation or
RT degradation of CreA.";
RL Fungal Genet. Biol. 45:657-670(2008).
RN [8]
RP UBIQUITINATION, INTERACTION WITH CREB, AND DEUBIQUITINATION BY CREB.
RA Kamlangdee N.;
RT "Identifying target proteins of the CreB deubiquitination enzyme in the
RT fungus Aspergillus nidulans.";
RL Thesis (2008), University of Adelaide, Australia.
RN [9]
RP INDUCTION.
RX PubMed=25043916; DOI=10.1186/1471-2164-15-613;
RA Martins I., Hartmann D.O., Alves P.C., Martins C., Garcia H.,
RA Leclercq C.C., Ferreira R., He J., Renaut J., Becker J.D.,
RA Silva Pereira C.;
RT "Elucidating how the saprophytic fungus Aspergillus nidulans uses the plant
RT polyester suberin as carbon source.";
RL BMC Genomics 15:613-613(2014).
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.
CC {ECO:0000269|PubMed:11442830, ECO:0000269|PubMed:18063396,
CC ECO:0000269|PubMed:18512059}.
CC -!- SUBUNIT: Interacts with creB. {ECO:0000269|Ref.8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18063396}.
CC -!- INDUCTION: Induced during growth on suberin.
CC {ECO:0000269|PubMed:25043916}.
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; AY219921; AAR02858.1; -; Genomic_DNA.
DR EMBL; AACD01000105; EAA57981.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF69992.1; -; Genomic_DNA.
DR PIR; A41694; A41694.
DR RefSeq; XP_663799.1; XM_658707.1.
DR AlphaFoldDB; Q01981; -.
DR SMR; Q01981; -.
DR STRING; 162425.CADANIAP00006813; -.
DR EnsemblFungi; CBF69992; CBF69992; ANIA_06195.
DR EnsemblFungi; EAA57981; EAA57981; AN6195.2.
DR GeneID; 2870784; -.
DR KEGG; ani:AN6195.2; -.
DR VEuPathDB; FungiDB:AN6195; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_036230_0_0_1; -.
DR InParanoid; Q01981; -.
DR OMA; PKVAVHD; -.
DR OrthoDB; 1617199at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IDA:AspGD.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000433; P:carbon catabolite repression of transcription from RNA polymerase II promoter by glucose; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IMP:AspGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IMP:AspGD.
DR GO; GO:0043609; P:regulation of carbon utilization; 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 1: Evidence at protein level;
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="DNA-binding protein creA"
FT /id="PRO_0000046875"
FT ZN_FING 64..86
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 92..116
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..368
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 163..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 44729 MW; 487EC100A228145E CRC64;
MPQPGSSVDF SNLLNPQNNT AIPAEVSNAT ASATMASGAS LLPPMVKGAR PAAEEARQDL
PRPYKCPLCE RAFHRLEHQT RHIRTHTGEK PHACQFPGCS KRFSRSDELT RHSRIHNNPN
SRRGNKAQHL AAAAAAAAAN QDGSAMANNA GSMMPPPSKP ITRSAPVSQV GSPDISPPHS
FSNYANHMRS NLSPYSRTSE RASSGMDINL LATAASQVER DESFGFRSGQ RSHHMYGPRH
GSRGLPSLSA YAISHSMSRS HSHEDEDSYA SHRVKRSRPN SPNSTAPSSP TFSHDSLSPT
PDHTPLATPA HSPRLKPLSP SELHLPSIRH LSLHHTPALA PMEPQAEGPN YYNPNQPHVG
PSISDIMSRP EGAQRKLPIP QVPKVAVQDM LNPSGFTSVS SSTANSVAGG DLAERF
