| IED ID | IndEnz0002011525 |
| Enzyme Type ID | protease011525 |
| Protein Name |
Gag-Pro polyprotein Pr76Gag-Pro Cleaved into: Matrix protein p19 MA ; Capsid protein p24 CA ; Nucleocapsid protein p15-pro NC' NC-pro ; Protease PR EC 3.4.23.- ; p1; Transframe peptide TFP p8 |
| Gene Name | gag-pro |
| Organism | Human T-cell leukemia virus 2 (HTLV-2) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Deltaretrovirus Primate T-lymphotropic virus 2 Human T-cell leukemia virus 2 (HTLV-2) |
| Enzyme Sequence | MGQIHGLSPTPIPKAPRGLSTHHWLNFLQAAYRLQPRPSDFDFQQLRRFLKLALKTPIWLNPIDYSLLASLIPKGYPGRVVEIINILVKNQVSPSAPAAPVPTPICPTTTPPPPPPPSPEAHVPPPYVEPTTTQCFPILHPPGAPSAHRPWQMKDLQAIKQEVSSSALGSPQFMQTLRLAVQQFDPTAKDLQDLLQYLCSSLVVSLHHQQLNTLITEAETRGMTGYNPMAGPLRMQANNPAQQGLRREYQNLWLAAFSTLPGNTRDPSWAAILQGLEEPYCAFVERLNVALDNGLPEGTPKEPILRSLAYSNANKECQKILQARGHTNSPLGEMLRTCQAWTPKDKTKVLVVQPRRPPPTQPCFRCGKVGHWSRDCTQPRPPPGPCPLCQDPSHWKRDCPQLKPPQEEGEPLLLDLPSTSGTTEEKNLLKGGDLISPHPDQDISILPLIPLRQQQQPILGVRISVMGQTPQPTQALLDTGADLTVIPQTLVPGPVKLHDTLILGASGQTNTQFKLLQTPLHIFLPFRRSPVILSSCLLDTHNKWTIIGRDALQQCQGLLYLPDDPSPHQLLPIATPNTIGLEHLPPPPQVDQFPLNLSASRP |
| Enzyme Length | 602 |
| Uniprot Accession Number | P03353 |
| Absorption | |
| Active Site | ACT_SITE 478; /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 p19]: 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 p15-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 (Potential). Cleaves the translation initiation factor eIF4G leading to the inhibition of host cap-dependent translation (By similarity). {ECO:0000250|UniProtKB:P10274, ECO:0000255|PROSITE-ProRule:PRU00275}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (6); Compositional bias (1); Domain (1); Initiator methionine (1); Lipidation (1); Motif (2); Peptide (1); Region (3); Site (5); Zinc finger (2) |
| Keywords | 3D-structure;Aspartyl protease;Capsid protein;Eukaryotic host gene expression shutoff by virus;Eukaryotic host translation shutoff by virus;Host gene expression shutoff by virus;Host-virus interaction;Hydrolase;Lipoprotein;Metal-binding;Myristate;Protease;Reference proteome;Repeat;Ribosomal frameshifting;Viral nucleoprotein;Virion;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-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: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in budding. {ECO:0000250|UniProtKB:P03345}.; 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}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 1JVR; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 94..97; /note=PTAP/PSAP motif; /evidence=ECO:0000250|UniProtKB:P03345; MOTIF 124..127; /note=PPXY motif; /evidence=ECO:0000250|UniProtKB:P03345 |
| Gene Encoded By | |
| Mass | 66,435 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |