ID   CRE1_NEUCR              Reviewed;         430 AA.
AC   O59958; Q7RVF3;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=DNA-binding protein cre-1;
DE   AltName: Full=Carbon catabolite repressor;
GN   Name=cre-1; ORFNames=NCU08807;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=10361038; DOI=10.1006/fgbi.1999.1121;
RA   de la Serna I., Ng D., Tyler B.M.;
RT   "Carbon regulation of ribosomal genes in Neurospora crassa occurs by a
RT   mechanism which does not require Cre-1, the homologue of the Aspergillus
RT   carbon catabolite repressor, CreA.";
RL   Fungal Genet. Biol. 26:253-269(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the creA/MIG C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF055464; AAC13555.1; -; mRNA.
DR   EMBL; CM002239; EAA32758.1; -; Genomic_DNA.
DR   RefSeq; XP_961994.1; XM_956901.3.
DR   AlphaFoldDB; O59958; -.
DR   SMR; O59958; -.
DR   STRING; 5141.EFNCRP00000008726; -.
DR   EnsemblFungi; EAA32758; EAA32758; NCU08807.
DR   GeneID; 3878142; -.
DR   KEGG; ncr:NCU08807; -.
DR   VEuPathDB; FungiDB:NCU08807; -.
DR   HOGENOM; CLU_036230_0_0_1; -.
DR   InParanoid; O59958; -.
DR   OMA; PKVAVHD; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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   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; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..430
FT                   /note="DNA-binding protein cre-1"
FT                   /id="PRO_0000046877"
FT   ZN_FING         78..100
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         106..130
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..282
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        351
FT                   /note="A -> T (in Ref. 1; AAC13555)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        369
FT                   /note="A -> P (in Ref. 1; AAC13555)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   430 AA;  46898 MW;  FDC81F922BDC9195 CRC64;
     MQRVQSAVDF SNLLNPSEST AEKRDHSGSP RQQTAQPQQQ QQQPQPEADM ATVGLLRPNG
     PLPGAQATEP ANELPRPYKC PLCDKAFHRL EHQTRHIRTH TGEKPHACQF PGCSKKFSRS
     DELTRHSRIH SNPNSRRGNK GQQQQQHPLV HNHGLQPDMM PPPGPKAIRS APPTAMSSPN
     VSPPHSYSPY NFAPSGLNPY SHSRSSAGSQ SGPDISLLAR AAGQVERDGA AHHHFQPRFQ
     FYGNTLHAAT ASRNQLPGLQ AYHMSRSHSH EDHDDHYGQS YRHAKRSRPN SPNSTAPSSP
     TFSHDSLSPT PDHTPLATPA HSPRLRPHPG LELPPFRNLS LGQQHTTPAL APLEPALDGQ
     FSLPQTPPAA PRSSGMSLTD IISRPDGTQR KLPVPKVAVQ DLLGPADGFN PSVRNSSSTS
     LSGAEMMDRL