Detail Information for IndEnz0002001381
IED ID IndEnz0002001381
Enzyme Type ID protease001381
Protein Name Tripeptidyl-peptidase 2 homolog
TPP-2
EC 3.4.14.10
Multicorn protease
Gene Name tpp2 SPAP8A3.12c
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 MKFRLNANFNFSFRRYCFVQCRNKYHSHVRYLSSAKKSGILRNSYNQRTERYFTNIMIPSDYSNKFYPVDGVVPKHETQAYEFLKKFPEYDGRGVTVGILDTGVDPGAPGLSVTTTGLPKFKNIVDCTGAGDVDTSVEVAAADSNDYLTITGRSGRTLKLSKEWKNPSKKWKVGCKLAYEFFPKDLRKRLQKLETEDMNKSNRKLLQDATDEYAKFKDKFPEAPLDKDNLQTQKELEARIECLKQLAEKFDNPGPLYDVVVFHDGEHWRVVIDSDQTGDIYLHKPLADFNVAQEWSTFGSLDLLSYGVHVYDNGNITSIVAVSGTHGTHVAGIIGANHPETPELNGAAPGCQLVSLMIGDGRLDSLETSHAFSRACSEIIKNEVDIINISFGEDAGIPNKGRVIELLRDELAGKRNVVIVSSAGNNGPAYTTVGAPGGTTFDVISVGAYVTSGMMQAQYNLLSTVHDTPYTWCSRGPTLDGDTGVSIYAPGGAITSVPPYSLQNSQLMNGTSMSSPSACGGISLILSALKAQKKPYTAAAIKKAVMYTSKDLRDDFNTGMLQVDNAYEYLAQSDFQYTGARSFTINGNIGNSKRGVYLRNPTEVCSPSRHMFNVAPKFEDGEEYEKSHFEVQLSLATTQPWIQAPEYVMMAGTGRGIPVRVDPTALAPGHHFGKVLAYDASNESRRCVFEIPVTVMKPSSISNTCFSLRDVSFEPTLIKRHFLVPPKGATYVEIRVKATSELESTNMLWISVNQTIPQTKLNEASTELIMPVTQNEVTTKLVSIDDSYTLELCMAQWWSSLEPMVLDIDVNFHGIKVVNGKEINLISSQGLKRVDCASIRRENFKPDITLKDYVDSFKPTNTVIKPLGDRDIMPDGQQLFELMATYSVEISEKTELKADFAVPHNMYDNGFNGLFFMVFDSQKQRVHYGDMYTSSHTLEKGEYLYKFQLLSVDPSTLERFRNVTLRLTKKLKKPITLPLYADHIDFCDNKTYERENIDAGVVESFVVGTNIEGEQYASELKENSLLTGELKFGDCEKGTVPVTLVLPPKISTKEDTKLGEKCANIVQLQVDLLSKLADQEKEKHLKYLQSSYKNSLEVQLAKLDIVKETNERLSTADSILSLIDTEALSRYYSCQQKVEDTIPRDVVLEKKMALQRDAFIRALVVKCETFSTQGHKDKDNYFQNYQLLLNWLENSDPRVWQIKKDYYKSQNQYGLALKALLELLKENGNSGKMDVAKLLSEEKELLVNLGWNYWHDIVFVETVKRVPPYSYALF
Enzyme Length 1274
Uniprot Accession Number Q9UT05
Absorption
Active Site ACT_SITE 101; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 326; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 512; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide.; EC=3.4.14.10; Evidence={ECO:0000269|PubMed:9740805};
DNA Binding
EC Number 3.4.14.10
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (1); Modified residue (1)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Phosphoprotein;Protease;Reference proteome;Serine protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
Modified Residue MOD_RES 606; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12618370; 20473289; 23173672; 23697806; 25452419; 25720772;
Motif
Gene Encoded By
Mass 142,926
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda