| IED ID | IndEnz0002011523 |
| Enzyme Type ID | protease011523 |
| Protein Name |
Gag-Pro polyprotein Cleaved into: Matrix protein p10; Phosphorylated protein pp21; Protein p3; Protein p8; Protein n; Capsid protein p27; Nucleocapsid protein-dUTPase NC-dUTPase EC 3.6.1.23 ; Protease EC 3.4.23.- |
| Gene Name | gag-pro |
| Organism | Mouse mammary tumor virus (strain C3H) (MMTV) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Betaretrovirus Mouse mammary tumor virus (MMTV) Mouse mammary tumor virus (strain C3H) (MMTV) |
| Enzyme Sequence | MGVSGSKGQKLFVSVLQRLLSERGLHVKESSAIEFYQFLIKVSPWFPEEGGLNLQDWKRVGREMKKYAAEHGTDSIPKQAYPIWLQLREILTEQSDLVLLSAEAKSVTEEELEEGLTGLLSASSQEKTYGTRGTAYAEIDTEVDKLSEHIYDEPYEEKEKADKNEEKDHVRKVKKIVQRKENSEHKRKEKDQKAFLATDWNNDDLSPEDWDDLEEQAAHYHDDDELILPVKRKVDKKKPLALRRKPLPPVGFAGAMAEAREKGDLTFTFPVVFMGESDDDDTPVWEPLPLKTLKELQSAVRTMGPSAPYTLQVVDMVASQWLTPSDWHQTARATLSPGDYVLWRTEYEEKSKETVQKTAGKRKGKVSLDMLLGTGQFLSPSSQIKLSKDVLKDVTTNAVLAWRAIPPPGVKKTVLAGLKQGNEESYETFISRLEEAVYRMMPRGEGSDILIKQLAWENANSLCQDLIRPMRKTGTMQDYIRACLDASPAVVQGMAYAAAMRGQKYSTFVKQTYGGGKGGQGSEGPVCFSCGKTGHIKRDCKEEKGSKRAPPGLCPRCKKGYHWKSECKSKFDKDGNPLPPLETNAENSKNLVKGQSPSPTQKGDKGKDSGLNPEAPPFTIHDLPRGTPGSAGLDLSSQKDLILSLEDGVSLVPTLVKGTLPEGTTGLIIGRSSNYKKGLEVLPGVIDSDFQGEIKVMVKAAKNAVIIHKGERIAQLLLLPYLKLPNPIIKEERGSEGFGSTSHVHWVQEISDSRPMLHISLNGRRFLGLLDTGADKTCIAGRDWPANWPIHQTESSLQGLGMACGVARSSQPLRWQHEDKSGIIHPFVIPTLPFTLWGRDIMKEIKVRLMTDSPDDSQDL |
| Enzyme Length | 860 |
| Uniprot Accession Number | Q9IZT2 |
| Absorption | |
| Active Site | ACT_SITE 771; /note=Protease; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU00275 |
| Activity Regulation | ACTIVITY REGULATION: [Protease]: Inhibited by pepstatin A. {ECO:0000250|UniProtKB:P10271}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000269|PubMed:8091672}; |
| DNA Binding | |
| EC Number | 3.6.1.23; 3.4.23.- |
| Enzyme Function | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: Nucleocapsid protein p14: 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: [Capsid protein p27]: Capsid protein. {ECO:0000305}.; FUNCTION: [Nucleocapsid protein-dUTPase]: NC-dUTPase has dUTPase activity, thereby preventing incorporation of uracil into DNA. {ECO:0000305|PubMed:8091672}.; 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 (9); Compositional bias (1); Domain (1); Initiator methionine (1); Lipidation (1); Motif (1); Natural variant (1); Region (2); Site (7); Zinc finger (2) |
| Keywords | Aspartyl protease;Capsid protein;DNA-binding;Direct protein sequencing;Hydrolase;Lipoprotein;Magnesium;Metal-binding;Myristate;Phosphoprotein;Protease;Reference proteome;Repeat;Ribosomal frameshifting;Viral matrix protein;Viral nucleoprotein;Virion;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000250|UniProtKB:P10258}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000250|UniProtKB:P10258}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000250|UniProtKB:P10258}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Protease]: Released by autocatalytic processing. {ECO:0000250|UniProtKB:P10271}.; 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:0000269|PubMed:2542570}.; PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:2542570}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 305..308; /note=PTAP/PSAP motif; /evidence=ECO:0000305 |
| Gene Encoded By | |
| Mass | 95,593 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:10248 |
| Cross Reference Brenda |