IED ID | IndEnz0002005245 |
Enzyme Type ID | protease005245 |
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 | Avian leukosis virus RSA (RSV-SRA) (Rous sarcoma virus (strain Schmidt-Ruppin A)) |
Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Alpharetrovirus Rous sarcoma virus Rous sarcoma virus (strain Schmidt-Ruppin) Avian leukosis virus RSA (RSV-SRA) (Rous sarcoma virus (strain Schmidt-Ruppin A)) |
Enzyme Sequence | MEAVIKVISSACKTYCGKISPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMVLGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTAQRDAKMAPEKMATPKTVGTSCYQCGTATGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPWGAEQPRAEPGHAGLAPGPALTDWARIREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVIAAATRDPRHPANGQGRGERTNLDRLKGLADGMVGNPQGQAALLRPGELVAITASALQAFREVARLAEPAGPWADITQGPSESFVDFANRLIKAVEGSDLPPSARAPVIIDCFRQKSQPDIQQLIRAAPSTLTTPGEIIKYVLDRQKIAPLTDQGIAAAMSSAIQPLVMAVVNRERDGQTGSGGRARGLCYTCGSPGHYQAQCPKKRKSGNSRERCQLCDGMGHNAKQCRRRDGNQGQRPGKGLSSGSWPVSEQPAVSLAMTMEHKDRPLVRVILTNTGSHPVKQRSVYITALLDSGADITIISEEDWPTDWPVMEAANPQIHGIGGGIPMRKSRDMIEVGVINRDGSLERPLLLFPAVAMVRGSILGRDCLQGLGLRLTNL |
Enzyme Length | 701 |
Uniprot Accession Number | P0C776 |
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 thatz 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); Chain (9); Domain (1); Motif (4); Peptide (1); Region (5); Site (10); Zinc finger (2) |
Keywords | Aspartyl protease;Capsid protein;Host nucleus;Hydrolase;Metal-binding;Protease;Reference proteome;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 | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 172..175; /note=PPXY motif; 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 | 74,610 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |