Detail Information for IndEnz0002007400
IED ID IndEnz0002007400
Enzyme Type ID protease007400
Protein Name Probable proteasome subunit beta type-1
EC 3.4.25.1
26S proteasome beta-type subunit PRE3
Multicatalytic endopeptidase complex subunit PRE3
Gene Name PRE3 ECU10_1450
Organism Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Microsporidia Apansporoblastina Unikaryonidae Encephalitozoon Encephalitozoon cuniculi (Microsporidian parasite) Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Enzyme Sequence MMSNEKEMTGTTIIAIKYDDGVLIGADSRTSMGAYVSSRVTDKLTQITDKIFVCRSGSSADTQMISSYLRMYLSMYSQLEDSIPQVQRAAALASKIIYENPSLLAGLIVAGYDDKPRVFNISLGGSLTERDWAIGGSGSAFIYGYCDVNWRSGMSLEEGIRFVRNAVSCAINRDNASGGCIRMSAISRTGVQRYFYPGDKVLQ
Enzyme Length 203
Uniprot Accession Number Q8SR11
Absorption
Active Site ACT_SITE 11; /note=Nucleophile; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1;
DNA Binding
EC Number 3.4.25.1
Enzyme Function FUNCTION: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Propeptide (1)
Keywords Cytoplasm;Hydrolase;Nucleus;Protease;Proteasome;Reference proteome;Threonine protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 22,189
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda