| IED ID | IndEnz0002015560 |
| Enzyme Type ID | protease015560 |
| Protein Name |
Leishmanolysin homolog EC 3.4.24.36 Cell surface protease Major surface glycoprotein Protein gp63 |
| Gene Name | gp63 |
| Organism | Crithidia fasciculata |
| Taxonomic Lineage | cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Leishmaniinae Crithidia Crithidia fasciculata |
| Enzyme Sequence | MHAPPTATRRSGPRRTHGIMARLVRLAAGVLVVTLVIGALTALSADDAKTHPHKVCIHDELQQSLLDSVAQQGLAPQRVSRVGLPYVASATAAPAAQVGGVDFALAGDSAPDVTRSAEWGELRITVSAEELTDPAYHCATVGQVISNHIDDYVTCTADDIMTAEKLDILMNYLIPEALQMHKDRLQVQQVQGTWKVARMTSYCGRFKVPEEHFTTGLSNTDFVLYVASVPTSPGVLAWANTCQVFSNDQPAVGVINIPAATITERYDHLMVHAVTHEIAHSLGFSNAFFTNTGIGQFVTGVRGNPDTVPVINSPTVVAKAREHYGCDDVTYVELEDAGGSGTMGSHWKIRNAQDELMAGISGVAYYTSLTLSAFEDLGYYKANYSNAETMKWGKDVGCAFLTGKCVVDNVTQFPSMYCDKDENVYRCHTARLNLGSCEVTDYTFDLPDYLQYFTVPSVGGSADYYDYCPYIVRSPIGSCTQAASSASPFVSAFNTFSMASRCIDGTFTPKSTGGATVTAHLGMCTNVACNTADKTYSIQVYGNGAYIPCTPGATISLDTVSDAFEAGGNITCPPYLEVCQSNVKGAMDYESMTNSGSGSSRPAPVEPSGSGSGSSAATTAPSPTRDGSAAADRIAPRTAAVALLALAVAAACV |
| Enzyme Length | 653 |
| Uniprot Accession Number | Q06031 |
| Absorption | |
| Active Site | ACT_SITE 277; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.; EC=3.4.24.36; |
| DNA Binding | |
| EC Number | 3.4.24.36 |
| Enzyme Function | FUNCTION: Plays an integral role during the infection of macrophages in the mammalian host. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (9); Glycosylation (3); Lipidation (1); Metal binding (3); Propeptide (2); Region (1); Signal peptide (1) |
| Keywords | Cell adhesion;Cell membrane;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..44; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 69,171 |
| Kinetics | |
| Metal Binding | METAL 276; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 280; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 346; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |