IED ID | IndEnz0002005569 |
Enzyme Type ID | protease005569 |
Protein Name |
Achelase-1 EC 3.4.21.- Achelase I |
Gene Name | |
Organism | Lonomia achelous (Giant silkworm moth) (Saturnid moth) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Bombycoidea (hawk-moths) Saturniidae (emperor moths) Hemileucinae Lonomia Lonomia achelous (Giant silkworm moth) (Saturnid moth) |
Enzyme Sequence | IVGGSVTTIGQYPSMASLLFNNRQVCGGVIINNRSVLTAAHCPFGDAVSSWRFRVGSTNANSGGTVFTLSTIINHPSYNRWTLDNDISIMRAASNIGTSASVQPAGIAGSNYNLGDNQVVWATGWGATSAGGSLARFPGVNARHVQIWTVNQNTCASRYAAIGRTVTANMLCSGWLDVGGRDQCQGDSGGPLYHNRIVVAVVSRYTSWIQSNA |
Enzyme Length | 213 |
Uniprot Accession Number | P23604 |
Absorption | |
Active Site | ACT_SITE 41; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 86; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 188; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Sensitive to serine proteinase inhibitors and thiol proteinase inhibitors. {ECO:0000269|PubMed:1911844}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Fibrinolytic activity; shows preferential cleavage of Arg-Gly bonds in all three fibrinogen chains. Contact with the caterpillars causes severe bleeding, due the anticoagulant effect of the protein. {ECO:0000269|PubMed:1911844}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (2); Domain (1) |
Keywords | Blood coagulation;Direct protein sequencing;Disulfide bond;Fibrinolysis;Hemostasis;Hydrolase;Protease;Secreted;Serine protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:1911844}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 22,472 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |