AMT1_CANGA
ID AMT1_CANGA Reviewed; 265 AA.
AC P41772;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Metal-activated transcriptional activator protein AMT1;
GN Name=AMT1; OrderedLocusNames=CAGL0I04180g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2068090; DOI=10.1073/pnas.88.14.6112;
RA Zhou P., Thiele D.J.;
RT "Isolation of a metal-activated transcription factor gene from Candida
RT glabrata by complementation in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6112-6116(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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).
RN [3]
RP CHARACTERIZATION.
RX PubMed=8509391; DOI=10.1016/s0021-9258(18)31418-2;
RA Thorvaldsen J.L., Sewell A.K., McCowen C.L., Winge D.R.;
RT "Regulation of metallothionein genes by the ACE1 and AMT1 transcription
RT factors.";
RL J. Biol. Chem. 268:12512-12518(1993).
RN [4]
RP STRUCTURE BY NMR OF 1-42.
RX PubMed=9665167; DOI=10.1038/805;
RA Turner R.B., Smith D.L., Zawrotny M.E., Summers M.F., Posewitz M.C.,
RA Winge D.R.;
RT "Solution structure of a zinc domain conserved in yeast copper-regulated
RT transcription factors.";
RL Nat. Struct. Biol. 5:551-555(1998).
CC -!- FUNCTION: Trans-acting regulatory protein that activates transcription
CC of the MT genes (metallothionein) in response to copper or silver ions.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; M69146; AAA35271.1; -; Genomic_DNA.
DR EMBL; CR380955; CAG60367.1; -; Genomic_DNA.
DR PIR; A41116; A41116.
DR RefSeq; XP_447430.1; XM_447430.1.
DR PDB; 1CO4; NMR; -; A=1-42.
DR PDBsum; 1CO4; -.
DR AlphaFoldDB; P41772; -.
DR SMR; P41772; -.
DR STRING; 5478.XP_447430.1; -.
DR PRIDE; P41772; -.
DR EnsemblFungi; CAG60367; CAG60367; CAGL0I04180g.
DR GeneID; 2889368; -.
DR KEGG; cgr:CAGL0I04180g; -.
DR CGD; CAL0132636; AMT1.
DR VEuPathDB; FungiDB:CAGL0I04180g; -.
DR eggNOG; ENOG502S7CA; Eukaryota.
DR HOGENOM; CLU_1220290_0_0_1; -.
DR InParanoid; P41772; -.
DR EvolutionaryTrace; P41772; -.
DR Proteomes; UP000002428; Chromosome I.
DR GO; GO:0005634; C:nucleus; ISA:CGD.
DR GO; GO:0005507; F:copper ion binding; IDA:CGD.
DR GO; GO:0003677; F:DNA binding; IDA:CGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:CGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:CGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IMP:CGD.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Copper; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..265
FT /note="Metal-activated transcriptional activator protein
FT AMT1"
FT /id="PRO_0000194927"
FT DNA_BIND 1..40
FT /note="Copper-fist"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT REGION 103..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
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 BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1CO4"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1CO4"
FT TURN 12..17
FT /evidence="ECO:0007829|PDB:1CO4"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:1CO4"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1CO4"
SQ SEQUENCE 265 AA; 29426 MW; 7AC1E182C4D70F64 CRC64;
MVVINGVKYA CDSCIKSHKA AQCEHNDRPL KILKPRGRPP TTCDHCKDMR KTKNVNPSGS
CNCSKLEKIR QEKGITIEED MLMSGNMDMC LCVRGEPCRC HARRKRTQKS NKKDNLSINS
PTNNSPSPAL SVNIGGMVVA NDDILKSLGP IQNVDLTAPL DFPPNGIDNK PMESFYTQTS
KSDAVDSLEF DHLMNMQMRN DNSLSFPMSA NQNEVGYQFN NEGNNSMNST MKNTITQMDQ
GNSHSMTLHD IDEILNNGIE LGNVN
