| IED ID | IndEnz0002001797 |
| Enzyme Type ID | protease001797 |
| Protein Name |
Subtilisin-like protease 3 EC 3.4.21.62 PfSUB3 |
| Gene Name | SUB3 PF3D7_0507200 |
| Organism | Plasmodium falciparum (isolate 3D7) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate 3D7) |
| Enzyme Sequence | MINRQYFIWYIFIFNIINKIYFENIRYVKNYEVVIRKKKNIERGIGNDFAFIRRYYKSRLLSDVSYKNNSIKGKNRVDKEGDIKKYDNNDDNKMDNSYDYKNKSIKENETKIRKEQVISLDKRYNRNINEKEEIKKKIKDIQRKRLIIYFKQDNTILSSRNYKHIFMKVLSSCGHIEKLTFINFYLYEFPKSINNEDMLLKICLRLLESRRINVENDNQISHTVQMKSYNNNNNKWDNINSKNNCIYQIKDKIKDLPNVSPSASTFTSISTSPYTLKLRDRNKYANDKNHIFKINHSNKHKNNNNNNNNNDYHNNNKSNYHSHSSAKCQTQRLNKKMIGTNILDGYDIIQMEEGLNLSHNYELNDVNVCIIDTGIDENHIDLKDNIIEKKTFMKHSYKKYNIDGINNIESDNIDGINNIESDNIDGINNIESDNIDGINNIESDNIDGINNIESDNIDGINNIKSSDNIKSSDNIKSSDNINSSDNIKSSDNNNVHTMLRNKLYLKKKKECSNYNTSNDGHGHGTFIAGIIAGNSPKGKKGIKGISKKAKLIICKALNNNNAGYISDILECFNFCAKKKARIINASFASTTHYPSLFQALKELQDKDILVISSSGNCSSNSKCKQAFQECNLNIQKLYPAAYSADLNNIISVSNIIQQSNGNIVLSPDSCYSPNYVHLAAPGGNIISTFPNNKYAISSGTSFSASVITGLASLVLSINSNLTSQQVIELFKKSIVQTKSLENKVKWGGFINVYDLVRFTIDSLPKDKDE |
| Enzyme Length | 769 |
| Uniprot Accession Number | Q8I430 |
| Absorption | |
| Active Site | ACT_SITE 372; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 523; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 701; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000269|PubMed:22285468, ECO:0000269|PubMed:24080030}; |
| DNA Binding | |
| EC Number | 3.4.21.62 |
| Enzyme Function | FUNCTION: Serine protease which may cleave PFN/profilin. {ECO:0000269|PubMed:24080030}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (1); Domain (1); Glycosylation (11); Propeptide (1); Region (2); Signal peptide (1) |
| Keywords | Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22285468}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..?; /evidence=ECO:0000305 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19214190; |
| Motif | |
| Gene Encoded By | |
| Mass | 88,047 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |