| IED ID | IndEnz0002013503 |
| Enzyme Type ID | protease013503 |
| Protein Name |
Gag-Pro-Pol polyprotein Cleaved into: Matrix protein p10; Phosphorylated protein pp24; Phosphorylated protein pp18; 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; Reverse transcriptase/ribonuclease H RT EC 2.7.7.49 EC 2.7.7.7 EC 3.1.26.4 ; Integrase IN EC 2.7.7.- EC 3.1.-.- |
| Gene Name | pol |
| Organism | Simian retrovirus SRV-2 |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Betaretrovirus Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus) Simian retrovirus SRV-2 |
| Enzyme Sequence | MGQELSQHELYVEQLKKALKTRGVKVKGNDLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKIPVTAFSYWNLIKDLIDKKEADPQVMAAVTQTEKILKVSSQTDLRDNSHNKDMDLISLESDDEEAKAPSEKMTMSNKSPKKYPAMLASQNNNTDKDPDLSEVDWDGLEDEAAKYHNPDWPPFLSRPPPYNRTAATAPAVMAVVNPKEELKEKISQLEEQIKLEELHQSLIIRLQKLKTGNERVTSSGNIESHSRTPKWPGQCLPKGKYLINKNTEEYPPKDIFPVTETMDGQGQAWRHHNGFDFTVIKELKTAVSQYGATAPYTLAIVESIADNWLTPTDWNTLVRAVLSGGDHLIWKSEFFENCRDTAKRNQQAGNGWDFDMLTGSGNYANTDAQMQYDPGLFAQIQAAATNAWRKLPVKGDPGASLTGVKQGPDEPFADFVHRLITTAGRIFGNAEAGVDYVKQLAYENANPACQAAIRPYRKKTDLTGYIRLCSDIGPSYQQGLAMAAAFSGQTVKDLLNNKNKDRGGCFKCGKKGHFAKDCRDHSNKNPESKVPGLCPRCKRGKHWANECKSKTDSQGNPLPPHQGNRDEGPAPGPEASLWGSQLCSSQQQQSISKLNRASPGSAGLDLCSTTHTVLTPEMGPQTLATGVYGPLPPNTFGLILGRGSTTVKGLQIYPGVIDNDYTGEFKIMARAISSIITIPQGERIAQLVLLPLLRTAHKIQHPYRGDKNFGSSDIFWVQPITHQKPSLVLWLDGKAFTGLIDTGADVTIIKQEDWPSHWPTTETLTNLRGIGQSNNPRQSSKYLTWKDKENNSGLIKPFVIPNLPVNLWGRDLLSQMKIMMCSPNDIVTAQMLAQGYSPGKGLGKREDGILQPIPNSGQLDRKGFGNFLATAVDILAPQRYADPITWKSDEPVWVDQWPLTQEKLAAAQQLVQEQLQAGHIIESNSPWNTPIFVIKKKSGKWRLLQDLRAVNATMVLMGALQPGLPSPVAIPQGYFKIVIDLKDCFFTIPLQPVDQKRFAFSLPSTNFKQPMKRYQWKVLPQGMANSPTLCQKYVAAAIEPVRKSWAQMYIIHYMDDILIAGKLGEQVLQCFAQLKQALTTTGLQIAPEKVQLQDPYTYLGFQINGPKITNQKAVIRRDKLQTLNDFQKLLGDINWLRPYLHLTTGDLKPLFDILKGDSNPNSPRSLSEAALASLQKVETAIAEQFVTQIDYTQPLTFLIFNTTLTPTGLFWQNNPVMWVHLPASPKKVLLPYYDAIADLIILGRDNSKKYFGLEPSTIIQPYSKSQIHWLMQNTETWPIACASYAGNIDNHYPPNKLIQFCKLHAVVFPRIISKTPLDNALLVFTDGSSTGIAAYTFEKTTVRFKTSHTSAQLVELQALIAVLSAFPHRALNVYTDSAYLAHSIPLLETVSHIKHISDTAKFFLQCQQLIYNRSIPFYLGHIRAHSGLPGPLSQGNHITDLATKVVATTLTTNLTEAQTAHALHHLNAQSLRLMFKITREQARQIVKQCPTCVTYLPIPHFGVNPKGLVPNMLWQMDVTHYSEFGKLKYVHVSIDTFSGFLVATLQTGEATKHVIAHLLHCFSIIGQPIHIKTDNGPGYTSSNFRAFCSKLHIKHTFGIPYNPQGQGIVERAHLSLKNTLEKIKKGEWYPTQGSPRNILNHALFILNFLNLDAQNKSAADRFWHTSSKKEYAMVKWKDPLDNTWHGPDPVLIWGRGSVCVYSQTHDAARWLPERLVRQVSNVTQSRE |
| Enzyme Length | 1768 |
| Uniprot Accession Number | P51517 |
| Absorption | |
| Active Site | ACT_SITE 782; /note=Protease; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU00275 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; 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 | DNA_BIND 1713..1762; /note=Integrase-type; /evidence=ECO:0000255|PROSITE-ProRule:PRU00506 |
| EC Number | 3.6.1.23; 3.4.23.-; 3.4.23.-; 2.7.7.49; 2.7.7.7; 3.1.26.4; 2.7.7.-; 3.1.-.- |
| Enzyme Function | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000250|UniProtKB:P07572}.; FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000250|UniProtKB:P07572}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000250|UniProtKB:P07572}.; 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:P07572, 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:P07572, 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:P07572}.; FUNCTION: [Reverse transcriptase/ribonuclease H]: RT is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to perfom a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perfom the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primers. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends. {ECO:0000255|PROSITE-ProRule:PRU00405}.; FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. {ECO:0000305|PubMed:28458055}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (11); Coiled coil (1); DNA binding (1); Domain (5); Initiator methionine (1); Lipidation (1); Metal binding (14); Motif (1); Peptide (1); Propeptide (1); Region (2); Site (9); Zinc finger (2) |
| Keywords | Aspartyl protease;Coiled coil;DNA integration;DNA recombination;DNA-binding;DNA-directed DNA polymerase;Endonuclease;Hydrolase;Lipoprotein;Magnesium;Metal-binding;Multifunctional enzyme;Myristate;Nuclease;Nucleotidyltransferase;Protease;RNA-binding;RNA-directed DNA polymerase;Repeat;Ribosomal frameshifting;Transferase;Viral genome integration;Viral matrix protein;Viral nucleoprotein;Virion;Virus entry into host cell;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:P07572}.; SUBCELLULAR LOCATION: [Protease 17 kDa]: Virion {ECO:0000250|UniProtKB:P07572}. |
| 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. {ECO:0000250|UniProtKB:P07572}.; PTM: [Gag-Pro-Pol 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-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000250|UniProtKB:P07572}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 200..203; /note=PPXY motif; /evidence=ECO:0000250|UniProtKB:P07572 |
| Gene Encoded By | |
| Mass | 197,910 |
| Kinetics | |
| Metal Binding | METAL 1021; /note=Magnesium 1; catalytic; for reverse transcriptase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405; METAL 1096; /note=Magnesium 1; catalytic; for reverse transcriptase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405; METAL 1097; /note=Magnesium 1; catalytic; for reverse transcriptase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405; METAL 1367; /note=Magnesium; for RNase H activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1396; /note=Magnesium; for RNase H activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1417; /note=Magnesium; for RNase H activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1481; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1502; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 1506; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 1530; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 1533; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 1558; /note=Magnesium 3; catalytic; for integrase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457; METAL 1615; /note=Magnesium 3; catalytic; for integrase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457; METAL 1651; /note=Magnesium 3; catalytic; for integrase activity; /evidence=ECO:0000250|UniProtKB:P03354 |
| Rhea ID | RHEA:22508; RHEA:10248 |
| Cross Reference Brenda |