| IED ID | IndEnz0002008067 |
| Enzyme Type ID | protease008067 |
| Protein Name |
Gag-Pro polyprotein Cleaved into: Matrix protein p10; Phosphorylated protein; p12; Capsid protein p27; Nucleocapsid protein-dUTPase NC-dUTPase EC 3.6.1.23 ; Protease 17 kDa EC 3.4.23.- ; Protease 13 kDa EC 3.4.23.- ; G-patch peptide |
| Gene Name | pro |
| Organism | Sheep pulmonary adenomatosis virus (Jaagsiekte sheep retrovirus) (JSRV) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Betaretrovirus Sheep pulmonary adenomatosis virus (Jaagsiekte sheep retrovirus) (JSRV) |
| Enzyme Sequence | MGHTHSRQLFVHMLSVMLKHRGITVSKTKLINFLSFIEEVCPWFPREGTVNLETWKKVGEQIRTHYTLHGPEKVPVETLSFWTLIRDCLDFDNDELKRLGNLLKQEEDPLHTPDSVPSYDPPPPPPPSLKMHPSDNDDSLSSTDEAELDEEAAKYHQEDWGFLAQEKGALTSKDELVECFKNLTIALQNAGIQLPSNNNTFPSAPPFPPAYTPTVMAGLDPPPGFPPPSKHMSPLQKALRQAQRLGEVVSDFSLAFPVFENNNQRYYESLPFKQLKELKIACSQYGPTAPFTIAMIESLGTQALPPNDWKQTARACLSGGDYLLWKSEFFEQCARIADVNRQQGIQTSYEMLIGEGPYQATDTQLNFLPGAYAQISNAARQAWKKLPSSSTKTEDLSKVRQGPDEPYQDFVARLLDTIGKIMSDEKAGMVLAKQLAFENANSACQAALRPYRKKGDLSDFIRICADIGPSYMQGIAMAAALQGKSIKEVLFQQQARNKKGLQKSGNSGCFVCGQPGHRAAVCPQKHQTSVNTPNLCPRCKKGKHWARDCRSKTDVQGNPLPPVSGNLGEGPAPGPETMLWGNTAGSKRTIADLCRATRGSAGLDLCATSYTVLTPEMGVQTLATGVFGPLPPGTVGLLLGRSSASLKGILIHPGVIDSDYTGEIKILASAPNKIIVINAGQRIAQLLLVPLVIQGKTINRDRQDKGFGSSDAYWVQNVTEARPELELRINANFFRGVLDTGADISVISDKYWPTTWPKQMAISTLQGIGQTTNPEQSSSLLTWKDKDGHTGQFKPYILPYLPVNLWGRDILSKMGVYLYSPSPTVTDLMLDQGLLPNQGLGKQHQGIILPLDLKPNQDRKGLGCFP |
| Enzyme Length | 866 |
| Uniprot Accession Number | P31625 |
| Absorption | |
| Active Site | ACT_SITE 739; /note=Protease; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU00275 |
| Activity Regulation | |
| 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:P07570}; |
| DNA Binding | |
| EC Number | 3.6.1.23; 3.4.23.-; 3.4.23.- |
| Enzyme Function | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.; FUNCTION: [Protease 17 kDa]: 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:0000250|UniProtKB:P07570, ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [Protease 13 kDa]: 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:0000250|UniProtKB:P07570, ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [G-patch peptide]: Enhances the activity of the reverse transcriptase. May be part of the mature RT. {ECO:0000250|UniProtKB:P07570}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (8); Compositional bias (1); Domain (2); Initiator methionine (1); Motif (3); Peptide (1); Region (2); Site (5); Zinc finger (1) |
| Keywords | Aspartyl protease;Capsid protein;DNA-binding;Hydrolase;Lipoprotein;Magnesium;Metal-binding;Multifunctional enzyme;Myristate;Nucleotide metabolism;Protease;Repeat;Ribosomal frameshifting;Viral matrix protein;Viral nucleoprotein;Virion;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion {ECO:0000250|UniProtKB:P07570}.; SUBCELLULAR LOCATION: [Protease 17 kDa]: Virion {ECO:0000250|UniProtKB:P07570}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Protease 17 kDa]: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa without the GDP domain. {ECO:0000250|UniProtKB:P07570}.; 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:0000250|UniProtKB:P07570}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 202..205; /note=PTAP/PSAP motif; /evidence=ECO:0000305; MOTIF 208..211; /note=PPXY motif; /evidence=ECO:0000305; MOTIF 287..290; /note=PTAP/PSAP motif; /evidence=ECO:0000250|UniProtKB:P10258 |
| Gene Encoded By | |
| Mass | 95,245 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:10248 |
| Cross Reference Brenda |