| IED ID | IndEnz0002003229 |
| Enzyme Type ID | protease003229 |
| Protein Name |
Cysteine proteinase B EC 3.4.22.- |
| Gene Name | LMCPB LMCPB2.8 |
| Organism | Leishmania mexicana |
| Taxonomic Lineage | cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Leishmaniinae Leishmania Leishmania Leishmania mexicana species complex Leishmania mexicana |
| Enzyme Sequence | MATSRAALCAVAVVCVVLAAACAPARAIHVGTPAAALFEEFKRTYGRAYETLAEEQQRLANFERNLELMREHQARNPHAQFGITKFFDLSEAEFAARYLNGAAYFAAAKRHAAQHYRKARADLSAVPDAVDWREKGAVTPVKDQGACGSCWAFSAVGNIEGQWYLAGHELVSLSEQQLVSCDDMNDGCDGGLMLQAFDWLLQNTNGHLHTEDSYPYVSGNGYVPECSNSSELVVGAQIDGHVLIGSSEKAMAAWLAKNGPIAIALDASSFMSYKSGVLTACIGKQLNHGVLLVGYDMTGEVPYWVIKNSWGGDWGEQGYVRVVMGVNACLLSEYPVSAHVRESAAPGTSTSSETPAPRPVMVEQVICFDKNCTQGCRKTLIKANECHKNGGGGASMIKCSPQKVTMCTYSNEFCVGGGLCFETPDGKCAPYFLGSIMNTCHYT |
| Enzyme Length | 443 |
| Uniprot Accession Number | P36400 |
| Absorption | |
| Active Site | ACT_SITE 150; /evidence=ECO:0000250; ACT_SITE 288; /evidence=ECO:0000250; ACT_SITE 308; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (12); Chain (1); Disulfide bond (3); Glycosylation (1); Helix (6); Propeptide (1); Sequence conflict (7); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Disulfide bond;Glycoprotein;Hydrolase;Protease;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6P4E; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,728 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B5; |