Detail Information for IndEnz0002009344
IED ID IndEnz0002009344
Enzyme Type ID protease009344
Protein Name Probable proteasome subunit beta type-5
EC 3.4.25.1
Macropain subunit pts1
Multicatalytic endopeptidase complex subunit pts1
Proteasome component pts1
Gene Name pts1 SPAC4A8.13c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Enzyme Sequence MNSIVSKYTQSTNNDDPKKIIEEEGFTNRFDVVPVPQSSLYLRNLTDETKNKHCLIKMNHGTTTLAFRYQHGIVVCVDSRASAGPLIASQTVKKVIEINPYLLGTLAGGAADCQFWETVLGMECRLHQLRNKELISVSAASKILSNITYSYKGYGLSMGTMLAGTGKGGTALYYIDSDGTRLKGDLFSVGSGSTFAYGVLDSGYRWDLSKQEALYLAQRSIVAATHRDAYSGGSVNLYHIDENGWVFHGNFDVDSLIWEAKDNENSFAHIPR
Enzyme Length 272
Uniprot Accession Number P30655
Absorption
Active Site ACT_SITE 62; /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 is a multicatalytic proteinase complex which 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. The proteasome has an ATP-dependent proteolytic activity.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Erroneous initiation (1); Propeptide (1)
Keywords Cytoplasm;Hydrolase;Nucleus;Protease;Proteasome;Reference proteome;Threonine protease;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 20133687; 20473289; 21712547; 23697806; 24710126; 30726745;
Motif
Gene Encoded By
Mass 29,987
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda