CREA_ASPOR
ID CREA_ASPOR Reviewed; 429 AA.
AC Q9P889; Q2UEV4; Q9C408;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=DNA-binding protein creA;
DE AltName: Full=Carbon catabolite repressor A;
GN Name=creA; ORFNames=AO090026000464;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KCTC 6983;
RA Kim J.H., Kim S., Chae K.S.;
RT "Isolation and the nucleotide sequence of the creA gene for a carbon
RT catabolite repressor of Aspergillus oryzae.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TK3;
RA van den Broek P.;
RT "The creA gene from Aspergillus oryzae.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AJ272151; CAB89774.1; -; Genomic_DNA.
DR EMBL; AF322183; AAK11189.1; -; Genomic_DNA.
DR EMBL; AP007159; BAE59911.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9P889; -.
DR SMR; Q9P889; -.
DR STRING; 510516.Q9P889; -.
DR EnsemblFungi; BAE59911; BAE59911; AO090026000464.
DR VEuPathDB; FungiDB:AO090026000464; -.
DR HOGENOM; CLU_036230_0_0_1; -.
DR OMA; PKVAVHD; -.
DR Proteomes; UP000006564; Chromosome 3.
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..429
FT /note="DNA-binding protein creA"
FT /id="PRO_0000046872"
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..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..189
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 351..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..429
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 175..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 276
FT /note="S -> F (in Ref. 2; AAK11189)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="P -> S (in Ref. 2; AAK11189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 46211 MW; 2947C2B64BD8F39C CRC64;
MPPPASSVDF TNLLNPQNNE TGSAPSTPVD SSKAPSTPSS TQSNSTMASS VSLLPPLMKG
ARPATEEARQ DLPRPYKCPL CDRAFHRLEH QTRHIRTHTG EKPHACQFPG CTKRFSRSDE
LTRHSRIHNN PNSRRSNKAH LAAAAAAAAA GQENAMVNVT NAGSLMPPPT KPMTRSAPVS
QVGSPDVSPP HSFSNYAGHM RSNLGPYARN TERASSGMDI NLLATAASQV ERDEQHFGFH
AGPRNHHLFA SRHHTGRGLP SLSAYAISHS MSRSHSHEDE DGYTHRVKRS RPNSPNSTAP
SSPTFSHDSL SPTPDHTPLA TPAHSPRLRP LGSSELHLPS IRHLSLHHTP ALAPMEPQPE
GPNYYSPSQS HGPTISDIMS RPDGTQRKLP VPQVPKVAVQ DMLNPSAGFS SVSSSTNNSV
AGNDLAERF
