CRF1_YARLI
ID CRF1_YARLI Reviewed; 411 AA.
AC P45815;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Copper resistance protein CRF1;
DE AltName: Full=YlCRF1;
GN Name=CRF1; OrderedLocusNames=YALI0B08206g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX PubMed=12114501; DOI=10.1074/jbc.m201091200;
RA Garcia S., Prado-Gonzalez M., Degano R., Dominguez A.;
RT "A copper-responsive transcription factor, CRF1, mediates copper and
RT cadmium resistance in Yarrowia lipolytica.";
RL J. Biol. Chem. 277:37359-37368(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Transcriptional regulator involved in resistance to high
CC copper concentration. {ECO:0000269|PubMed:12114501}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12114501}.
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DR EMBL; Z23265; CAA80803.1; -; Genomic_DNA.
DR EMBL; CR382128; CAG82873.1; -; Genomic_DNA.
DR RefSeq; XP_500631.1; XM_500631.1.
DR AlphaFoldDB; P45815; -.
DR SMR; P45815; -.
DR STRING; 4952.CAG82873; -.
DR EnsemblFungi; CAG82873; CAG82873; YALI0_B08206g.
DR GeneID; 2907407; -.
DR KEGG; yli:YALI0B08206g; -.
DR VEuPathDB; FungiDB:YALI0_B08206g; -.
DR HOGENOM; CLU_669403_0_0_1; -.
DR InParanoid; P45815; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.90.430.10; -; 1.
DR InterPro; IPR001083; Cu_fist_DNA-bd_dom.
DR InterPro; IPR036395; Cu_fist_DNA-bd_dom_sf.
DR Pfam; PF00649; Copper-fist; 1.
DR PRINTS; PR00617; COPPERFIST.
DR SMART; SM01090; Copper-fist; 1.
DR SMART; SM00412; Cu_FIST; 1.
DR SUPFAM; SSF57879; SSF57879; 1.
DR PROSITE; PS01119; COPPER_FIST_1; 1.
DR PROSITE; PS50073; COPPER_FIST_2; 1.
PE 4: Predicted;
KW Copper; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..411
FT /note="Copper resistance protein CRF1"
FT /id="PRO_0000194932"
FT DNA_BIND 1..40
FT /note="Copper-fist"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT REGION 115..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
SQ SEQUENCE 411 AA; 43689 MW; 9AD602FA467EACC7 CRC64;
MVVIEGIKYA CERCIRGHRV SSCTHTQQPL IRIKPKGRPA TQCLHCREAR KNKALHVKCK
CGSSSSKHAA TCPCYSGGGC ICTNKHPQVL PPNSTTTGAN GCIVINKAVL DEGSQQQAQQ
AQQQSQSQQA QQQQQQPQPQ ASPILQQPQM PTPVHTTNVT TPPVATPTHS HRALSTTPSL
SPQPQSPHSP ESALKSVNFL GRTNSSSSLS SLHSGRNKNR IEKVRPSHNS LSAASQLANS
PSSPFYAVTP PAWVDSPTLV PTGALDASYL QILNDDLSSP LLDSDVFSSL DMEPVAHSNN
NHGGIPTGGS RALASTDINF DRFESTSPSS ILSSWNLWGG VGGSDAPEMS VAANPSASAS
ASSIQTPPSS NATPEWVQGQ QQPCSVSPAD VMLPFKRDDQ ESVFLTEPLY L
