| IED ID | IndEnz0002008212 |
| Enzyme Type ID | protease008212 |
| Protein Name |
Gag-Pro polyprotein Cleaved into: Matrix protein p15 MA ; Capsid protein p24 CA ; Nucleocapsid protein p12-pro; Protease EC 3.4.23.- ; p13 |
| Gene Name | |
| Organism | Bovine leukemia virus (isolate Japanese BLV-1) (BLV) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Deltaretrovirus Bovine leukemia virus (BLV) Bovine leukemia virus (isolate Japanese BLV-1) (BLV) |
| Enzyme Sequence | MGNSPSYNPPAGISPSDWLNLLQSAQRLNPRPSPSDFTDLKNYIHWFHKTQKKPWTFTSGGPTSCPPGRFGRVPLVLATLNEVLSNEGGAPGASAPEEQPPPYDPPAILPIISEGNRNRHRAWALRELQDIKKEIENKAPGSQVWIQTLRLAILQADPTPADLEQLCQYIASPVDQTAHMTSLTAAIAAAEAANTLQGFNPKTGTLTQQSAQPNAGDLRSQYQNLWLQAGKNLPTRPSAPWSTIVQGPAESSVEFVNRLQISLADNLPDGVPKEPIIDSLSYANANRECQQILQGRGPVAAVGQKLQACAQWAPKNKQPALLVHTPGPKMPGPRQPAPKRPPPGPCYRCLKEGHWARDCPTKATGPPPGPCPICKDPSHWKRDCPTLKSKNKLIEGGLSAPQTITPITDSLSEAELECLLSIPLARSRPSVAVYLSGPWLQPSQNQALMLVDTGAENTVLPQNWLVRDYPRIPAAVLGAGGVSRNRYNWLQGPLTLALKPEGPFITIPKILVDTSDKWQILGRDVPSRLQASISIPEEVRPPVVGVLDTPPSHIGLEHLPPPPEVPQFPLN |
| Enzyme Length | 571 |
| Uniprot Accession Number | P0DOI0 |
| Absorption | |
| Active Site | ACT_SITE 453; /note=Protease; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU00275 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: [Gag-Pro polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p15]: Matrix protein. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Capsid protein p24]: Forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250|UniProtKB:P10274}.; FUNCTION: [Nucleocapsid protein p12-pro]: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000250|UniProtKB:P10274}.; FUNCTION: [Protease]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (6); Initiator methionine (1); Lipidation (1); Motif (1); Repeat (2); Site (4); Zinc finger (2) |
| Keywords | Aspartyl protease;Capsid protein;Host-virus interaction;Hydrolase;Lipoprotein;Metal-binding;Myristate;Phosphoprotein;Protease;Repeat;Ribosomal frameshifting;Viral budding;Viral budding via the host ESCRT complexes;Viral matrix protein;Viral nucleoprotein;Viral release from host cell;Virion;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p12-pro]: Virion {ECO:0000250|UniProtKB:P03345}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini. {ECO:0000250|UniProtKB:P10274}.; PTM: [Gag-Pro polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250|UniProtKB:P03345, ECO:0000250|UniProtKB:P10274}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 100..103; /note=PPXY motif; /evidence=ECO:0000250|UniProtKB:P0DOI1 |
| Gene Encoded By | |
| Mass | 61,933 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |