Detail Information for IndEnz0002000969
IED ID IndEnz0002000969
Enzyme Type ID protease000969
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 BR6) (MMTV)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Betaretrovirus Mouse mammary tumor virus (MMTV) Mouse mammary tumor virus (strain BR6) (MMTV)
Enzyme Sequence MGVSGSKGQKLFVSVLQRLLSERGLHVKESSAIEFYQFLIKVSPWFPEEGGLNLQDWKRVGREMKRYAAEHGTDSIPKQAYPIWLQLREILTEQSDLVLLSAEAKSVTEEELEEGLTGLLSTSSQEKTYGTRGTAYAEIDTEVDKLSEHIYDEPYEEKEKADKNEEKDHVRKIKKVVQRKENSEGKRKEKDSKAFLATDWNDDDLSPEDWDDLEEQAAHYHDDDELILPVKRKVVKKKPQALRRKPLPPVGFAGAMAEAREKGDLTFTFPVVFMGESDEDDTPVWEPLPLKTLKELQSAVRTMGPSAPYTLQVVDMVASQWLTPSDWHQTARATLSPGDYVLWRTEYEEKSKEMVQKAAGKRKGKVSLDMLLGTGQFLSPSSQIKLSKDVLKDVTTNAVLAWRAIPPPGVKKTVLAGLKQGNEESYETFISRLEEAVYRMMPRGEGSDILIKQLAWENANSLCQDLIRPIRKTGTIQDYIRACLDASPAVVQGMAYAAAMRGQKYSTFVKQTYGGGKGGQGAEGPVCFSCGKTGHIRKDCKDEKGSKRAPPGLCPRCKKGYHWKSECKSKFDKDGNPLPPLETNAENSKNLVKGQSPSPAQKGDGVKGSGLNPEAPPFTIHDLPRGTPGSAGLDLSSQKDLILSLEDGVSLVPTLVKGTLPEGTTGLIIGRSSNYKKGLEVLPGVIDSDFQGEIKVMVKAAKNAVIIHKGERIAQLLLLPYLKLPNPVIKEERGSEGFGSTSHVHWVQEISDSRPMLHIYLNGRRFLGLLDTGADKTCIAGRDWPANWPIHQTESSLQGLGMACGVARSSQPLRWQHEDKSGIIHPFVIPTLPFTLWGRDIMKDIKVRLMTDSPDDSQDL
Enzyme Length 860
Uniprot Accession Number P10271
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:0000269|PubMed:1331110}.
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:0000250|UniProtKB:P11283};
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: [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 BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6 for protease. {ECO:0000269|PubMed:1331110};
Pathway
nucleotide Binding
Features Active site (1); Chain (9); Compositional bias (1); Domain (1); Frameshift (1); Initiator methionine (1); Lipidation (1); Motif (1); Region (2); Site (7); Zinc finger (2)
Keywords Aspartyl protease;Capsid protein;DNA-binding;Hydrolase;Lipoprotein;Magnesium;Metal-binding;Myristate;Protease;Reference proteome;Ribosomal frameshifting;Viral matrix protein;Viral nucleoprotein;Virion;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000269|PubMed:205999}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000269|PubMed:205999}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000269|PubMed:205999}.
Modified Residue
Post Translational Modification PTM: [Protease]: Released by autocatalytic processing. {ECO:0000269|PubMed:1331110}.; 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:P10258}.; PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:1331110}.
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 95,409
Kinetics
Metal Binding
Rhea ID RHEA:10248
Cross Reference Brenda