CREA_COCCA
ID CREA_COCCA Reviewed; 430 AA.
AC Q9HFS2;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=DNA-binding protein creA;
DE AltName: Full=Carbon catabolite repressor;
GN Name=CREA;
OS Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=5017;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12825351; DOI=10.1080/1042517031000073727;
RA Tonukari N.J., Scott-Craig J.S., Walton J.D.;
RT "Isolation of the carbon catabolite repressor (CREA) gene from the plant-
RT pathogenic fungus Cochliobolus carbonum.";
RL DNA Seq. 14:103-107(2003).
CC -!- FUNCTION: Involved in carbon catabolite repression. Represses the
CC transcription of a number of genes by binding to a GC-rich region in
CC their promoter (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the creA/MIG C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF306571; AAG29826.1; -; mRNA.
DR AlphaFoldDB; Q9HFS2; -.
DR SMR; Q9HFS2; -.
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 Pfam; PF00096; zf-C2H2; 2.
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 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..430
FT /note="DNA-binding protein creA"
FT /id="PRO_0000046874"
FT ZN_FING 68..90
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 96..120
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..284
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 401..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 46333 MW; 54F0F399F5B299DF CRC64;
MQSNSASTGF ANLLNPETAS QNQQQQQQQP TSTPTASMAA ATVSLMAPLL QNAPQQTEEP
RQDLPRPYKC PLCDKAFHRL EHQTRHIRTH TGEKPHACTF PGCTKRFSRS DELTRHSRIH
NNPNSRRGKG QQHAAATQAA VAAVQAGLME PGSNLAHMMP PPSKPISRSA PGSQLGSPNV
SPPHSFSNYS PGMSNDLAAY HQGGLSNSSS PSGLARPMDL LADAASRLEQ RPGHISHSSR
HHLTSGYHPY ANRLPGLSQY AYSSQPMSRS HSHEDDDPYS HRMTKKSRPG SPSSTAPPSP
TFSHDSCSPT PDHTPLATPA HSPRLRPHGF SDLQLPHLRH LSLNQNFVPA LAPMEPSTER
EQPYVPSQSS GLRIGDIISK PEGAQRKLPV PQVPKVAVQD LLNGPSNSGF SSGNNSATAS
LAGEDLSNRN