| IED ID | IndEnz0002003068 |
| Enzyme Type ID | protease003068 |
| Protein Name |
Gag polyprotein Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide SP p3 ; Nucleocapsid protein p12; Protease p15 EC 3.4.23.- |
| Gene Name | gag |
| Organism | Rous sarcoma virus (strain Schmidt-Ruppin B) (RSV-SRB) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Alpharetrovirus Rous sarcoma virus Rous sarcoma virus (strain Schmidt-Ruppin) Rous sarcoma virus (strain Schmidt-Ruppin B) (RSV-SRB) |
| Enzyme Sequence | MEAVIKVISSACKTYCGKTSPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMVLGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCYHCGTAIGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPRGAEQPRAEPGHAGLAPGPALTDWARIREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVIAAATRDPRHPANGQGRGERTNLDRLKGLADGMVGNPQGQAALLRPGELVAITASALQAFREVARLAEPAGPWADITQGPSESFVDFANRLIKAVEGSDLPPSARAPVIIDCFRQKSQPDIQQLIRAAPSTLTTPGEIIKYVLDRQKIAPLTDQGIAAAMSSAIQPLVMAVVNRERDGQTGSGGRARRLCYTCGSPGHYQAQCPKKRKSGNSRERCQLCDGMGHNAKQCRRRDSNQGQRPGRGLSSGPWPVSEQPAVSLAMTMEHKDRPLVRVILTNTGSHPVKQRSVYITALLDSGADITIISEEDWPTDWPVVDTANPQIHGIGGGIPMRKSRDMIELGVINRDGSLERPLLLFPAVAMVRGSILGRDCLQGLGLRLTNL |
| Enzyme Length | 701 |
| Uniprot Accession Number | O92954 |
| Absorption | |
| Active Site | ACT_SITE 614; /note=For protease activity; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: [Gag polyprotein]: The p10 domain folds back and interacts with the capsid protein domain during Gag polyprotein assembly in the immature particle (before the maturation cleavage that splits the 2 domains). {ECO:0000250|UniProtKB:P03322}.; FUNCTION: Capsid protein p27: Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro. {ECO:0000250|UniProtKB:P03322}.; FUNCTION: [Nucleocapsid protein p12]: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}.; FUNCTION: [Spacer peptide]: Plays a role in the oligomerization of the Gag polyprotein and in the stabilization of the immature particle. Essential layering element during tube assembly. {ECO:0000250|UniProtKB:P03322}.; FUNCTION: [Protease p15]: Aspartyl protease that 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); Beta strand (2); Chain (9); Domain (1); Helix (11); Motif (4); Peptide (1); Region (6); Site (10); Turn (4); Zinc finger (2) |
| Keywords | 3D-structure;Aspartyl protease;Capsid protein;Host nucleus;Hydrolase;Metal-binding;Protease;Repeat;Ribosomal frameshifting;Viral capsid assembly;Viral capsid maturation;Viral matrix protein;Viral release from host cell;Virion;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03322}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000250|UniProtKB:P03322}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000250|UniProtKB:P03322}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p12]: Virion {ECO:0000250|UniProtKB:P03322}.; SUBCELLULAR LOCATION: [Gag polyprotein]: Host nucleus, host nucleolus {ECO:0000250|UniProtKB:P03322}. Host nucleus, host nucleoplasm {ECO:0000250|UniProtKB:P03322}. Note=Shuttles between nucleoplasm and nucleolus. {ECO:0000250|UniProtKB:P03322}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. The cleavage at the C-terminus of the Capsid protein p27 is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and a capsid protein C-terminally extended by 3 amino acids in a ratio of 2:1. {ECO:0000250|UniProtKB:P03322}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 1D1D; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 172..175; /note=PPXY motif; /evidence=ECO:0000250|UniProtKB:P03322; MOTIF 180..184; /note=LYPX(n)L motif; /evidence=ECO:0000250|UniProtKB:P03322; MOTIF 219..229; /note=Nuclear export signal; /evidence=ECO:0000250|UniProtKB:P03322; MOTIF 524..527; /note=Nuclear/nucleolar localization signal; /evidence=ECO:0000250|UniProtKB:P03322 |
| Gene Encoded By | |
| Mass | 74,753 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |