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P41772 (AMT1_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metal-activated transcriptional activator protein AMT1
Gene names
Name:AMT1
Ordered Locus Names:CAGL0I04180g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Trans-acting regulatory protein that activates transcription of the MT genes (metallothionein) in response to copper or silver ions.

Subcellular location

Nucleus.

Sequence similarities

Contains 1 copper-fist DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandCopper
DNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processtranscription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

copper ion binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 265265Metal-activated transcriptional activator protein AMT1
PRO_0000194927

Regions

DNA binding1 – 4040Copper-fist

Sites

Metal binding111Zinc
Metal binding141Zinc
Metal binding231Zinc
Metal binding251Zinc

Secondary structure

.......... 265
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41772 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7AC1E182C4D70F64

FASTA26529,426
        10         20         30         40         50         60 
MVVINGVKYA CDSCIKSHKA AQCEHNDRPL KILKPRGRPP TTCDHCKDMR KTKNVNPSGS 

        70         80         90        100        110        120 
CNCSKLEKIR QEKGITIEED MLMSGNMDMC LCVRGEPCRC HARRKRTQKS NKKDNLSINS 

       130        140        150        160        170        180 
PTNNSPSPAL SVNIGGMVVA NDDILKSLGP IQNVDLTAPL DFPPNGIDNK PMESFYTQTS 

       190        200        210        220        230        240 
KSDAVDSLEF DHLMNMQMRN DNSLSFPMSA NQNEVGYQFN NEGNNSMNST MKNTITQMDQ 

       250        260 
GNSHSMTLHD IDEILNNGIE LGNVN 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a metal-activated transcription factor gene from Candida glabrata by complementation in Saccharomyces cerevisiae."
Zhou P., Thiele D.J.
Proc. Natl. Acad. Sci. U.S.A. 88:6112-6116(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.
[3]"Regulation of metallothionein genes by the ACE1 and AMT1 transcription factors."
Thorvaldsen J.L., Sewell A.K., McCowen C.L., Winge D.R.
J. Biol. Chem. 268:12512-12518(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors."
Turner R.B., Smith D.L., Zawrotny M.E., Summers M.F., Posewitz M.C., Winge D.R.
Nat. Struct. Biol. 5:551-555(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M69146 Genomic DNA. Translation: AAA35271.1.
CR380955 Genomic DNA. Translation: CAG60367.1.
PIRA41116.
RefSeqXP_447430.1. XM_447430.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CO4NMR-A1-42[»]
ProteinModelPortalP41772.
SMRP41772. Positions 1-42.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2889368.
KEGGcgr:CAGL0I04180g.

Phylogenomic databases

OrthoDBEOG4X0R35.

Family and domain databases

Gene3D3.90.430.10. 1 hit.
InterProIPR001083. Cu_fist_DNA-bd.
[Graphical view]
PfamPF00649. Copper-fist. 1 hit.
[Graphical view]
PRINTSPR00617. COPPERFIST.
SMARTSM00412. Cu_FIST. 1 hit.
[Graphical view]
SUPFAMSSF57879. Cu_fist_DNA_bd. 1 hit.
PROSITEPS01119. COPPER_FIST_1. 1 hit.
PS50073. COPPER_FIST_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP41772.

Entry information

Entry nameAMT1_CANGA
AccessionPrimary (citable) accession number: P41772
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families