IED ID | IndEnz0002010654 |
Enzyme Type ID | protease010654 |
Protein Name |
Metacaspase III c PtMCA-IIIc EC 3.4.22.- Cleaved into: Small subunit p10; Large subunit p20 |
Gene Name | MCA-IIIc PHATRDRAFT_54873 |
Organism | Phaeodactylum tricornutum (strain CCAP 1055/1) |
Taxonomic Lineage | cellular organisms Eukaryota Sar Stramenopiles Ochrophyta Bacillariophyta (diatoms) Bacillariophyceae (Raphid pennate diatoms) Bacillariophycidae Naviculales Phaeodactylaceae Phaeodactylum Phaeodactylum tricornutum (Diatom) Phaeodactylum tricornutum (strain CCAP 1055/1) |
Enzyme Sequence | MGFLRRQLREQFEKKKPEALQADIRMISGCQDVQTSADVSNVSSFQLPDPAGNAGGACTSTLLNVLYKDHQTPEDTMSFVELLNKMRENLEAKGFSQVPQLTASHPIDVNDDFDLVPPAATGTRRALLIGINYVGHEQGVLRGCHNDVKNMVEYIKAVHGFEDENITILMDDGEHTAPTHANMIAAYKKIVALSKADDALFCHFSGHGAKIRDDDRGEEDDGYDETLVPIDYHENGMIRDDDLYDILIKPLVQGVHLVCLMDCCHSGTVLDLPYVYKADGNFTEMEIDENFDFKKLLGKFGIDDFDKFGGEALGKINGDALGKVGKDALGKLNKFFG |
Enzyme Length | 337 |
Uniprot Accession Number | B7G6D3 |
Absorption | |
Active Site | ACT_SITE 207; /evidence=ECO:0000250|UniProtKB:Q08601; ACT_SITE 264; /evidence=ECO:0000250|UniProtKB:Q585F3 |
Activity Regulation | ACTIVITY REGULATION: Activated by Ca(2+). {ECO:0000269|PubMed:34566902}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Cysteine protease that cleaves specifically after arginine residues. {ECO:0000269|PubMed:34566902}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (3); Disulfide bond (1); Metal binding (4); Modified residue (1); Mutagenesis (3); Propeptide (3) |
Keywords | Autocatalytic cleavage;Calcium;Disulfide bond;Hydrolase;Metal-binding;Oxidation;Protease;Reference proteome;Thiol protease;Zymogen |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | MOD_RES 202; /note=Cysteine sulfenic acid (-SOH); /evidence=ECO:0000269|PubMed:34566902 |
Post Translational Modification | PTM: Auto-proteolytic cleavage into a large and a small subunit which probably remain associated by non-covalent bonds. {ECO:0000269|PubMed:34566902}.; PTM: Following oxidative stress, the oxidation of Cys-202 leads to the formation of a disulfide bond between Cys-202 and Cys-259 which enhances catalytic activity. {ECO:0000269|PubMed:34566902}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 37,250 |
Kinetics | |
Metal Binding | METAL 224; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 240; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 241; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3; METAL 271; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q585F3 |
Rhea ID | |
Cross Reference Brenda |