IED ID | IndEnz0002013741 |
Enzyme Type ID | protease013741 |
Protein Name |
Metacaspase-5 EC 3.4.22.- TcMCA5 |
Gene Name | MCA5 Tc00.1047053510759.160 |
Organism | Trypanosoma cruzi (strain CL Brener) |
Taxonomic Lineage | cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Trypanosoma Schizotrypanum Trypanosoma cruzi Trypanosoma cruzi (strain CL Brener) |
Enzyme Sequence | MDLLLGVLSSGILQNALPFVAGVGRVKRPKRVKLEEAFREAHLCRPVIPYRAPTPYTGGRVKALFVGINYTGTRNKLSGCVNDVRQMLGTLQRIQFPISECCILVDDMRFPNFTALPTRENIIKHMAWLVHDVRPGDVLFFHYSGHGTETKAERDSEELYDQCLVPLDYQVQGAILDDDLFELLVKGLPAGVRMTAVFDCCHSASLLDLPFAFVGNNNFYSGGRHEMRKVRANNFSMGDVVVFSGCDDSGTSADVSNVSSFGSGLVASGGAATQALTWALVNTSQLSYADIFIRTREILRQKGYKQVPQLSSSKPVDLYKPFSLFGPITVNTSLIHYVPQQYLQPWGPPQPYYPPPQPQQPYYPPPQPQQPYYPSSQLPTQYNNLAPTAGIPLMTSSSEVPPGQYPQALSGDQNGGVPPQYPSDQSTYYSSAQYLSGVGKPL |
Enzyme Length | 442 |
Uniprot Accession Number | Q2VLK8 |
Absorption | |
Active Site | ACT_SITE 146; /evidence=ECO:0000305|PubMed:22402587; ACT_SITE 201; /evidence=ECO:0000305|PubMed:22402587 |
Activity Regulation | ACTIVITY REGULATION: Activated by Ca(2+). {ECO:0000269|PubMed:22402587}. |
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 (PubMed:22402587). May play a role in apoptosis (PubMed:22402587). {ECO:0000269|PubMed:22402587}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Compositional bias (2); Glycosylation (6); Metal binding (4); Mutagenesis (2); Region (3); Signal peptide (1) |
Keywords | Calcium;Endosome;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Signal;Thiol protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250|UniProtKB:Q8IEW1}. Note=Localizes to RAB11-positive recycling endosomes. {ECO:0000250|UniProtKB:Q8IEW1}. |
Modified Residue | |
Post Translational Modification | PTM: In epimastigotes, the unprocessed enzyme appears to be the main form (PubMed:22402587). Auto-processing is dispensable for catalytic activity towards small oligopeptide substrates (PubMed:22402587). {ECO:0000269|PubMed:22402587}. |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 48,698 |
Kinetics | |
Metal Binding | METAL 161; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 177; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 178; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 208; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3 |
Rhea ID | |
Cross Reference Brenda |