Top Level Name

  ⌊ Superfamily (core) Glutathione Transferase (cytosolic)

    ⌊ Subgroup Main (cytGST)

  Main.2: Nu-like

  ⌊ FunctionalDomain Cytosolic GST-like protein, similar to Nu class GSTs (ID 58481)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onOct. 14, 2016

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Saccharomyces cerevisiae S288c Taxon ID: 559292 6324100 NP_014170.1 (RefSeq) PRP URP
Saccharomyces cerevisiae YJM1434 Taxon ID: 1294371 803444203 AKB00873.1 (Genbank) URP
Saccharomyces cerevisiae YJM1615 Taxon ID: 1294388 767256186 AJT34680.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Transcriptional regulator URE2 P23202 1.8.4.- URE2_YEAST (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 354 | Length of Functional Domain: 231

1       10        20        30        40        50        60

MMNNNGNQVSNLSNALRQVNIGNRNSNTTTDQSNINFEFSTGVNNNNNNNSSSNNNNVQN
NNSGRNGSQNNDNENNIKNTLEQHRQQQQAFSDMSHVEYSRITKFFQEQPLEGYTLFSHR
SAPNGFKVAIVLSELGFHYNTIFLDFNLGEHRAPEFVSVNPNARVPALIDHGMDNLSIWE
SGAILLHLVNKYYKETGNPLLWSDDLADQSQINAWLFFQTSGHAPMIGQALHFRYFHSQK
IASAVERYTDEVRRVYGVVEMALAERREALVMELDTENAAAYSAGTTPMSQSRFFDYPVW
LVGDKLTIADLAFVPWNNVVDRIGINIKIEFPEVYKWTKHMMRR
PAVIKALRGE
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Links
1G6Y Crystal Structure Of The Globular Region Of The Prion Protien Ure2 From Yeast Saccharomyces Cerevisiae Ure2 Protein 13 2.8 CSA • PDB • PDBSum
1G6W Crystal Structure Of The Globular Region Of The Prion Protein Ure2 From The Yeast Saccaromyces Cerevisiae Ure2 Protein 13 2.5 CSA • PDB • PDBSum
1K0D Ure2P In Complex With Glutathione Ure2 Protein 13 2.2 Glutathione CSA • PDB • PDBSum
1K0C Ure2P In Complex With S-P-Nitrobenzylglutathione Ure2 Protein 13 2.5 S-(P-Nitrobenzyl)Glutathione • Glutathione CSA • PDB • PDBSum
1JZR Ure2P In Complex With Glutathione Ure2 Protein 13 2.9 Glutathione CSA • PDB • PDBSum
1K0B Ure2P In Complex With Glutathione Ure2 Protein 13 2.5 Glutathione CSA • PDB • PDBSum
1K0A Ure2P In Complex With S-Hexylglutathione Ure2 Protein 13 2.5 S-Hexylglutathione • Glutathione CSA • PDB • PDBSum
1HQO Crystal Structure Of The Nitrogen Regulation Fragment Of The Yeast Prion Protein Ure2P Ure2 Protein 13 2.3 Selenomethionine CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History

Time Change Annotation Old Value New Value
May 3, 2014, 6:45 a.m. update curation agent smashiya setDomainBoundaries.py
update domain end position 354 344
EC number assigned by UniProtKB accession ID.