| IED ID | IndEnz0002013619 |
| Enzyme Type ID | protease013619 |
| Protein Name |
Gag-Pro-Pol polyprotein Cleaved into: Matrix protein p15 MA ; Capsid protein p24 CA ; Nucleocapsid protein p12-pro; Protease EC 3.4.23.- ; 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 | Bovine leukemia virus (isolate Australian) (BLV) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Deltaretrovirus Bovine leukemia virus (BLV) Bovine leukemia virus (isolate Australian) (BLV) |
| Enzyme Sequence | MGNSPSYNPPAGISPSDWLNLLQSAQRLNPRPSPSDFTDLKNYIHWFHKTQKKPWTFTSGGPASCPPGKFGRVPLVLATLNEVLSNDEGAPGASAPEEQPPPYDPPAVLPIISEGNRNRHRAWALRELQDIKKEIENKAPGSQVWIQTLRLAILQADPTPADLEQLCQYIASPVDQTAHMTSLTAAIAAEAANTLQGFNPQNGTLTQQSAQPNAGDLRSQYQNLWLQAWKNLPTRPSVQPWSTIVQGPAESYVEFVNRLQISLADNLPDGVPKEPIIDSLSYANANKECQQILQGRGLVAAPVGQKLQACAHWAPKTKQPAILVHTPGPKMPGPRQPAPKRPPPGPCYRCLKEGHWARDCPTKTTGPPPGPCPICKDPSHWKRDCPTLKSKKLIEGGPSAPQIITPITDSLSEAELECLLSIPLARSRPSVAVYLSGPWLQPSQNQALMLVDTGAENTVLPQNWLVRDYPRTPAAVLGAGGISRNRYNWLQGPLTLALKPEGPFITIPKILVDTFDKWQILGRDVLSRLQASISIPEEVHPPVVGVLDAPPSHIGLEHLPPPPEVPQFPLNLERLQALQDLVHRSLEAGYISPWDGPGNNPVFPVRKPNGAWRFVHDLRVTNALTKPIPALSPGPPDLTAIPTHLPHIICLDLKDAFFQIPVEDRFRSYFAFTLPTPGGLQPHRRFAWRVLPQGFINSPALFERALQEPLRQVSAAFSQSLLVSYMDDILYVSPTEEQRLQCYQTMAAHLRDLGFQVASEKTRQTPSPVPFLGQMVHERMVTYQSLPTLQISSPISLHQLQTVLGDLQWVSRGTPTTRRPLQLLYSSLKGIDDPRAIIHLSPEQQQGIAELRQALSHNARSRYNEQEPLLAYVHLTRAGSTLVLFQKGAQFPLAYFQTPLTDNQASPWGLLLLLGCQYLQAQALSSYAKTILKYYHNLPKTSLDNWIQSSEDPRVQELLQLWPQISSQGIQPPGPWKTLVTRAEVFLTPQFSPEPIPAALCLFSDGAARRGAYCLWKDHLLDFQAVPAPESAQKGELAGLLAGLAAAPPEPLNIWVDSKYLYSLLRTLVLGAWLQPDPVPSYALLYKSLLRHPAIFVGHVRSHSSASHPIASLNNYVDQLLPLETPEQWHKLTHCNSRALSRWPNPRISAWDPRSPATLCETCQRLNPTGGGKMRTIQRGWAPNHIWQADITHYKYKQFTYALHVFVDTYSGATHASAKRGLTTQTTIEGLLEAIVHLGRPKKLNTDQGANYTSKTFVRFCQQFGISLSHHVPYNPTSSGLVERTNGLLKLLLSKYHLDEPHLPMTQALSRALWTHNQINLLPILKTRWELHHSPPLAVISEGGETPKGSDKLFLYKLPGQNNRRWLGPLPALVEASGGALLATNPPVWVPWRLLKAFKCLKNDGPEDAPNRSSDG |
| Enzyme Length | 1416 |
| Uniprot Accession Number | P25059 |
| Absorption | |
| Active Site | ACT_SITE 452; /note=Protease; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU00275 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; 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}; |
| DNA Binding | DNA_BIND 1352..1400; /note=Integrase-type; /evidence=ECO:0000255|PROSITE-ProRule:PRU00506 |
| EC Number | 3.4.23.-; 2.7.7.49; 2.7.7.7; 3.1.26.4; 2.7.7.-; 3.1.-.- |
| Enzyme Function | FUNCTION: [Gag-Pro-Pol polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p15]: Matrix protein. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Capsid protein p24]: Forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250|UniProtKB:P03362}.; FUNCTION: [Nucleocapsid protein p12-pro]: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000250|UniProtKB:P03345}.; 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}.; FUNCTION: [Reverse transcriptase/ribonuclease H]: RT is a multifunctional enzyme that converts the viral 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-Pro 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 perform 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 perform 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 primer. 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:0000250}.; FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. {ECO:0000250|UniProtKB:P03362}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (7); DNA binding (1); Domain (4); Erroneous gene model prediction (1); Initiator methionine (1); Lipidation (1); Metal binding (9); Motif (1); Mutagenesis (1); Site (5); Zinc finger (2) |
| Keywords | Aspartyl protease;Capsid protein;DNA integration;DNA recombination;DNA-binding;Endonuclease;Host-virus interaction;Hydrolase;Lipoprotein;Magnesium;Metal-binding;Multifunctional enzyme;Myristate;Nuclease;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-directed DNA polymerase;Repeat;Ribosomal frameshifting;Transferase;Viral budding;Viral budding via the host ESCRT complexes;Viral genome integration;Viral matrix protein;Viral nucleoprotein;Viral release from host cell;Virion;Virus entry into host cell;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p12-pro]: Virion {ECO:0000250|UniProtKB:P03345}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Matrix protein p15]: Phosphorylation of the matrix protein p15 by MAPK1 seems to play a role in budding. {ECO:0000250|UniProtKB:P03345}.; 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:P03345}.; PTM: [Gag-Pro-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini. {ECO:0000250|UniProtKB:P03362}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 100..103; /note=PPXY motif; /evidence=ECO:0000269|PubMed:12134053 |
| Gene Encoded By | |
| Mass | 156,937 |
| Kinetics | |
| Metal Binding | METAL 652; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405; METAL 727; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405; METAL 728; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405; METAL 1005; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1036; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1057; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1118; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1190; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457; METAL 1247; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00457 |
| Rhea ID | RHEA:22508 |
| Cross Reference Brenda |