| IED ID | IndEnz0002018967 |
| Enzyme Type ID | protease018967 |
| Protein Name |
Viral cathepsin V-cath EC 3.4.22.50 Cysteine proteinase CP |
| Gene Name | VCATH RO120 |
| Organism | Rachiplusia ou multiple nucleopolyhedrovirus (strain R1) (RoMNPV) |
| Taxonomic Lineage | Viruses Naldaviricetes Lefavirales Baculoviridae Alphabaculovirus Autographa californica multiple nucleopolyhedrovirus Rachiplusia ou multiple nucleopolyhedrovirus (RoMNPV) Rachiplusia ou multiple nucleopolyhedrovirus (strain R1) (RoMNPV) |
| Enzyme Sequence | MNKILFYLFVYGVVNSAAYDLLKAPNYFEEFVHRFNKDYGSEVEKLRRFKIFQHNLNEIIIKNQNDSAKYEINKFSDLSKDETIAKYTGLSLPIQTQNFCKVIVLDQPPGKGPLEFDWRRLNKVTSVKNQGMCGACWAFATLASLESQFAIKHNQLINLSEQQMIDCDFVDAGCNGGLLHTAFEAIIKMGGVQLESDYPYEADNNNCRMNTNKFLVQVKDCYRYITVYEEKLKDLLRLVGPIPMAIDAADIVNYKQGIIKYCFNSGLNHAVLLVGYGVENNIPYWTFKNTWGTDWGEEGFFRVQQNINACGMRNELASTAVIY |
| Enzyme Length | 323 |
| Uniprot Accession Number | Q8B9D5 |
| Absorption | |
| Active Site | ACT_SITE 136; /evidence=ECO:0000250; ACT_SITE 269; /evidence=ECO:0000250; ACT_SITE 289; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B.; EC=3.4.22.50; |
| DNA Binding | |
| EC Number | 3.4.22.50 |
| Enzyme Function | FUNCTION: Cysteine protease that plays an essential role in host liquefaction to facilitate horizontal transmission of the virus. May participate in the degradation of foreign protein expressed by the baculovirus system (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Glycosylation (1); Propeptide (1); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Synthesized as an inactive proenzyme and activated by proteolytic removal of the inhibitory propeptide. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 36,965 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |