| IED ID | IndEnz0002011246 |
| Enzyme Type ID | protease011246 |
| Protein Name |
Gag-Pol polyprotein Pr170Gag-Pol Cleaved into: Matrix protein p16 MA ; Capsid protein p26 CA ; Transframe peptide p11 ; Protease EC 3.4.23.- P119 Retropepsin ; Reverse transcriptase/ribonuclease H RT EC 2.7.7.49 EC 2.7.7.7 EC 3.1.26.13 Exoribonuclease H EC 3.1.13.2 P72 ; Integrase IN EC 2.7.7.- EC 3.1.-.- |
| Gene Name | gag-pol |
| Organism | Jembrana disease virus (JDV) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Lentivirus Jembrana disease virus (JDV) |
| Enzyme Sequence | MKLSKLEKALKKVRVTPQRDDTYTIGNVLWAIRMCRLMGLDCCIDEATAAEVAILIGRFQSLDLQDSPLKGKDEKAILTTLKVLWSLLAGHHPENSDMAEKYWEAWTIRERESQKEEEGEITSIYPQLRKNFPAVSTSDGSPRYDPDLTKQLKIWADATEKHGVDHHAVNILGVITANLTQSEIRLLLQSTPQWRLDIQLIESKLNAREHAHRVWKESHPEAPKTDEIIGKGLTAAEQATLTTQECRDTYRQWVLEAALEVAQGKHDRPGPINIHQGPKEPYPEFVNKLVTALEGMAAPETTKQYLLDHLSVDHANEDCRAVLLPLGPSAPMERKLEACRAVGSSKQKMQFLAEAFAAINVKGDGEVQRCYGCGKPGHIRRDCKNQKCFKCGKPGHLQRNCKSKNREALLCPFWAEERIPSGEDFCDPVCSPVGIRLNRQPFIKIFLGGRWVRALIDTGADEVVLKDIHWDRIKGVPAASVVQVGVTGRNIARRKSNVEWRFKNRYGIVDVLFSNTPVNLLGRSVLQSIVTKFTLAAHTKQIQPLPVKLHGPGPRVPQWPLTLEKYKALKEIVEELLKDGKISRTPWDNPFNTPVFVIKKKGGSKWRMLMDFRALNKVTNKGQEFQIGLPYPPGIQQCEHITAIDIKDAYFTIPLDENFRQYTAFSVVPVNREGPLERYHWNVLPQGWVCSPAIYQTTTQEIIAEIKDRFPDIVLYQYMDDLLIGSDRPDHKRVVSEIREELGAYGFKTPEEKIQEEQVQWLGYELTPKRWRFQPRQIKIKKVVTVNELQQMIGNCVWVQPEVKIPLSPLSDLLKGKTDLKDKIKLTEEAIQCLETVNKRLKDPEWKERIKEGTELVVKIQLIPEGVVYDLLQDGNPIWGGVKGWDYNHANKIKKMLSIMKKLSRIVMIMTGREVSFLIPGDSEDWESALQRINTLTEIPEVKFYKHACRWTSVCGPVIERYPTYYTDGGKKGSKAAAAYWREGKIRREVFPGTNQQAELKAVLMALQDGPAKMNIITDSRYAFEGMREEPETWGREGLWKEIGEELRRKEYVGVSWVPGHKGIGGNTEVDQEVQKALQGPITVSLPQEILLEAGETKLVKTGIFWEGLRPCKLRPEEGLKLKGSLIDEELQLEITNTQNSRVGIRQGQTIGTCFIEAIPQAIEEHEKWHTTAEILAREFQLPRRVAREIVHRCQACKRTVSCPRRGTNPRERFLWQMDNTHLEGKIIWVAVETNSGLIEARVIPEESAQSIVFCILMLVYRYTVYHIHSDNGPCFIAQKVEALCKYLKITKTTGIPYNPQAQAIVERTHRDIKDKIAAFREDCETVEAALSLTLVALNKKRGGIGGHTPYEIYLESEYNKYQEQQNHYNNFKTEKWAYVRDKRKVWKGPYKVLWDGEGAAVVEENAMPTLYPHRHMRFIPPPNTDTQDGNL |
| Enzyme Length | 1432 |
| Uniprot Accession Number | Q82851 |
| Absorption | |
| Active Site | ACT_SITE 457; /note=For protease activity; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| 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=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.; EC=3.1.26.13; CATALYTIC ACTIVITY: Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.; EC=3.1.13.2; |
| DNA Binding | DNA_BIND 1376..1422; /note=Integrase-type; /evidence=ECO:0000255|PROSITE-ProRule:PRU00506 |
| EC Number | 3.4.23.-; 2.7.7.49; 2.7.7.7; 3.1.26.13; 3.1.13.2; 2.7.7.-; 3.1.-.- |
| Enzyme Function | FUNCTION: Matrix protein p16 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane. {ECO:0000250}.; FUNCTION: Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.; FUNCTION: 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 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 (By similarity). {ECO:0000250}.; FUNCTION: Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (7); Coiled coil (1); DNA binding (1); Domain (4); Metal binding (13); Site (5); Zinc finger (3) |
| Keywords | Aspartyl protease;Capsid protein;Coiled coil;DNA integration;DNA recombination;DNA-binding;DNA-directed DNA polymerase;Endonuclease;Hydrolase;Magnesium;Metal-binding;Multifunctional enzyme;Nuclease;Nucleotidyltransferase;Protease;RNA-binding;RNA-directed DNA polymerase;Reference proteome;Repeat;Ribosomal frameshifting;Transferase;Viral genome integration;Viral matrix protein;Viral nucleoprotein;Viral release from host cell;Virion;Virion maturation;Virus entry into host cell;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Matrix protein p16]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p26]: Virion {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 163,421 |
| Kinetics | |
| Metal Binding | METAL 645; /note=Magnesium; catalytic; /evidence=ECO:0000250; METAL 720; /note=Magnesium; catalytic; /evidence=ECO:0000250; METAL 721; /note=Magnesium; catalytic; /evidence=ECO:0000250; METAL 968; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 999; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1019; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1071; /note=Magnesium; /evidence=ECO:0000255|PROSITE-ProRule:PRU00408; METAL 1166; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 1170; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 1194; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 1197; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00450; METAL 1219; /note=Magnesium; catalytic; /evidence=ECO:0000250; METAL 1271; /note=Magnesium; catalytic; /evidence=ECO:0000250 |
| Rhea ID | RHEA:22508 |
| Cross Reference Brenda |