| IED ID | IndEnz0002004332 |
| Enzyme Type ID | protease004332 |
| 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 Prague C) (RSV-PrC) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Alpharetrovirus Rous sarcoma virus Rous sarcoma virus (strain Prague C) (RSV-PrC) |
| Enzyme Sequence | MEAVIKVISSACKTYCGKTSPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMILGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCYHCGTAIGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPPGAEQSRAEPGHAGQAPGPALTDWARVREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVIAAATRDPRHPANGQGRGERTNLNRLKGLADGMVGNPQGQAALLRPGELVAITASALQAFREVARLAEPAGPWADIMQGPSESFVDFANRLIKAVEGSDLPPSARAPVIIDCFRQKSQPDIQQLIRTAPSTLTTPGEIIKYVLDRQKTAPLTDQGIAAAMSSAIQPLIMAVVNRERDGQTGSGGRARGLCYTCGSPGHYQAQCPKKRKSGNSRERCQLCNGMGHNAKQCRKRDGNQGQRPGKGLSSGPWPGPEPPAVSLAMTMEHKDRPLVRVILTNTGSHPVKQRSVYITALLDSGADITIISEEDWPTDWPVMEAANPQIHGIGGGIPMRKSRDMIELGVINRDGSLERPLLLFPAVAMVRGSILGRDCLQGLGLRLTNL |
| Enzyme Length | 701 |
| Uniprot Accession Number | P03322 |
| 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:0000269|PubMed:26223638}.; 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:0000269|PubMed:10873863, ECO:0000269|PubMed:28588198}.; 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:0000269|PubMed:28588198}.; 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 (18); Chain (9); Domain (1); Helix (21); Motif (4); Mutagenesis (5); Peptide (1); Region (6); Sequence conflict (2); Site (10); Turn (5); Zinc finger (2) |
| Keywords | 3D-structure;Aspartyl protease;Capsid protein;Direct protein sequencing;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:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p12]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Gag polyprotein]: Host nucleus, host nucleolus {ECO:0000269|PubMed:23036987}. Host nucleus, host nucleoplasm {ECO:0000269|PubMed:23036987}. Note=Shuttles between nucleoplasm and nucleolus. {ECO:0000269|PubMed:23036987}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (PubMed:8636100, PubMed:8627817). 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 (PubMed:28588198). {ECO:0000269|PubMed:28588198, ECO:0000269|PubMed:8627817, ECO:0000269|PubMed:8636100}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (3); Electron microscopy (29); X-ray crystallography (11) |
| Cross Reference PDB | 1A6S; 1BAI; 1EM9; 1EOQ; 1P7N; 2IHX; 2RSP; 2X8Q; 3G0V; 3G1G; 3G1I; 3G21; 3G26; 3G28; 3G29; 5A9E; 7NO0; 7NO1; 7NO2; 7NO3; 7NO4; 7NO5; 7NO6; 7NO7; 7NO8; 7NO9; 7NOA; 7NOB; 7NOC; 7NOD; 7NOE; 7NOF; 7NOG; 7NOH; 7NOI; 7NOJ; 7NOK; 7NOL; 7NOM; 7NON; 7NOO; 7NOP; 7NOQ; |
| Mapped Pubmed ID | 17070546; 34050170; |
| Motif | MOTIF 172..175; /note=PPXY motif; /evidence=ECO:0000269|PubMed:20392845; MOTIF 180..184; /note=LYPX(n)L motif; /evidence=ECO:0000269|PubMed:20392845; MOTIF 219..229; /note=Nuclear export signal; /evidence=ECO:0000269|PubMed:23036987; MOTIF 524..527; /note=Nuclear/nucleolar localization signal; /evidence=ECO:0000269|PubMed:23036987 |
| Gene Encoded By | |
| Mass | 74,527 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.B10; |