Detail Information for IndEnz0002010654
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