IED ID | IndEnz0002015845 |
Enzyme Type ID | protease015845 |
Protein Name |
Metacaspase-2 EC 3.4.22.- TbMCA2 Cleaved into: Large subunit p20; Small subunit p10 |
Gene Name | MCA2 |
Organism | Trypanosoma brucei brucei |
Taxonomic Lineage | cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Trypanosoma Trypanozoon Trypanosoma brucei Trypanosoma brucei brucei |
Enzyme Sequence | MCSLITQLCDAGQLADYVGLGWLNAVSSQPYLVQALGLQPPPRRVDVDAAFRDAEGLHGHQPWVATPLPGRTVRALFIGINYYGTSAALSGCCNDVKQMLATLQKKGLPINEAVILVDEDNFPGRTDQPTRDNIVRYMAWLVKDAKPGDVLFFHYSGHGTQCKSRGDSDEKYDQCIAPVDFQKSGCIVDDDIHKLLFSRLPEKVRLTAVFDCCHSGSIMDLPFTYVCSGGEQASGTPHMKRIREGNDVLGDVMMISGCADEQTSADVKNTATFGTGSTGAGGAATQCITCMLMNNQSLSYGKLLIETRDMLKRKGFKQVPQLSASKAIDLDQTFSLTEMFSVDRSVQ |
Enzyme Length | 347 |
Uniprot Accession Number | Q8T8E7 |
Absorption | |
Active Site | ACT_SITE 158; /evidence=ECO:0000250|UniProtKB:Q08601; ACT_SITE 213; /evidence=ECO:0000250|UniProtKB:Q585F3 |
Activity Regulation | ACTIVITY REGULATION: Activated by Ca(2+). In response to calcium binding, the 280-loop, the 280-loop, a disordered loop consisting of residues 269-275, undergoes a conformational change which stabilizes substrates in the active site. The binding to the substrate triggers the release of the N-terminal region resulting in the activation of the enzyme. Proteolytic cleavage is required for catalytic activity towards large protein substrates. {ECO:0000250|UniProtKB:Q585F3}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Cysteine protease that cleaves specifically after arginine or lysine residues. {ECO:0000250|UniProtKB:Q585F3}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (3); Metal binding (4); Propeptide (1); Region (1); Site (3) |
Keywords | Autocatalytic cleavage;Calcium;Endosome;Hydrolase;Metal-binding;Protease;Thiol protease;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Recycling endosome {ECO:0000305|PubMed:16507595}. |
Modified Residue | |
Post Translational Modification | PTM: Auto-proteolytic cleavage of the propeptide after Lys-55 and between the large and small subunits after Lys-268 is required for catalytic activity towards large protein substrates but is dispensable towards small oligopeptide substrates. After processing, the propeptide and the large and small subunits remain associated by non-covalent bonds (By similarity). In vivo, the unprocessed enzyme appears to be the predominant form (PubMed:16507595). {ECO:0000250|UniProtKB:Q585F3, ECO:0000269|PubMed:16507595}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 37,794 |
Kinetics | |
Metal Binding | METAL 173; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 189; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 190; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 220; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3 |
Rhea ID | |
Cross Reference Brenda |