CYS3_NEUCR
ID CYS3_NEUCR Reviewed; 236 AA.
AC P22697; Q7RU61;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Regulatory protein cys-3;
GN Name=cys-3; ORFNames=B2A19.70, NCU21522;
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 [GENOMIC DNA].
RX PubMed=2524646; DOI=10.1128/mcb.9.3.1120-1127.1989;
RA Fu Y.-H., Paietta J.V., Mannix D.G., Marzluf G.A.;
RT "cys-3, the positive-acting sulfur regulatory gene of Neurospora crassa,
RT encodes a protein with a putative leucine zipper DNA-binding element.";
RL Mol. Cell. Biol. 9:1120-1127(1989).
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=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
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).
RN [4]
RP CHARACTERIZATION.
RX PubMed=2142156; DOI=10.1016/s0021-9258(19)38491-1;
RA Fu Y.-H., Marzluf G.A.;
RT "cys-3, the positive-acting sulfur regulatory gene of Neurospora crassa,
RT encodes a sequence-specific DNA-binding protein.";
RL J. Biol. Chem. 265:11942-11947(1990).
RN [5]
RP MUTAGENESIS.
RX PubMed=1831537; DOI=10.1128/mcb.11.9.4356-4362.1991;
RA Kanaan M.N., Marzluf G.A.;
RT "Mutational analysis of the DNA-binding domain of the CYS3 regulatory
RT protein of Neurospora crassa.";
RL Mol. Cell. Biol. 11:4356-4362(1991).
RN [6]
RP MUTAGENESIS.
RX PubMed=1532511; DOI=10.1021/bi00127a022;
RA Kanaan M.N., Fu Y.-H., Marzluf G.A.;
RT "The DNA-binding domain of the Cys-3 regulatory protein of Neurospora
RT crassa is bipartite.";
RL Biochemistry 31:3197-3203(1992).
CC -!- FUNCTION: Turns on the expression of structural genes which encode
CC sulfur-catabolic enzymes. Binds to sequence elements upstream of these
CC genes.
CC -!- SUBUNIT: Binds DNA as a dimer.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: By sulfur deprivation.
CC -!- SIMILARITY: Belongs to the bZIP family. GCN4 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA27579.2; Type=Erroneous gene model prediction; Note=The predicted gene NCU03536 has been split into 2 genes: NCU21521 and NCU21522.; Evidence={ECO:0000305};
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DR EMBL; M26008; AAA33585.1; -; Genomic_DNA.
DR EMBL; AL390092; CAB98237.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA27579.2; ALT_SEQ; Genomic_DNA.
DR PIR; A30225; A30225.
DR PIR; T51073; T51073.
DR AlphaFoldDB; P22697; -.
DR SMR; P22697; -.
DR STRING; 5141.EFNCRP00000002554; -.
DR EnsemblFungi; EAA27579; EAA27579; NCU03536.
DR HOGENOM; CLU_056562_0_0_1; -.
DR InParanoid; P22697; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..236
FT /note="Regulatory protein cys-3"
FT /id="PRO_0000076489"
FT DOMAIN 99..162
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 26..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..137
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 141..155
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 189..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 105
FT /note="K->Q: Loss of DNA-binding."
FT MUTAGEN 106
FT /note="R->Q: Loss of DNA-binding."
SQ SEQUENCE 236 AA; 25895 MW; 88AE35FEF57FEF6A CRC64;
MSSADFNFGD FTTTYTSPTI PAYPDTLGQL QPIQPNPQAA YPPVSQHHAS HHVQHPHQPG
YVLSNPPQLS GNKRKASDAM SVPPTPGARV MSFEEASRLA AEEDKRKRNT AASARFRIKK
KQREQALEKS AKEMSEKVTQ LEGRIQALET ENKWLKGLVT EKHGSKEDIL KLLREFSAHA
AKVSKDAAAA AADKAEAAAD KADAERAREE SSFCVSTSSP SSDESVDTDN KKRRKD
