| IED ID | IndEnz0002007903 |
| Enzyme Type ID | protease007903 |
| Protein Name |
Putative enzymatic polyprotein Includes: Protease PR EC 3.4.23.- ; Reverse transcriptase RT EC 2.7.7.49 ; Ribonuclease H EC 3.1.26.4 |
| Gene Name | ORF 3 |
| Organism | Cassava vein mosaic virus (CsVMV) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Caulimoviridae Cavemovirus Cassava vein mosaic virus (CsVMV) |
| Enzyme Sequence | MNKITYMTIKISIPKYMSRIYHGLFDTGANICICKKKVLPDELWHKTENLVLRGFNDEKHVAEYRADNITIMIAKEKFIIPYIYAMDEMSPDIIIGATFYNKYSPIELDIGKGIIKFTKNNEKYPNYLVKYPKKRKLVPWTKGNPSVTETMENIGINQIESRNPIEEEINQILGTDIYGENPLEKWEKHKTLAKIELKNETDNIYKPPMLYQETDLPEFKMHIEEMIKEGFIEEKTNFEDKKYSSPAFIVNKHSEQKRGKTRMVIDYKDLNKKAKVVKYPIPNKDTLIHRSIQARYYSKFDCKSGFYHIKLEEDSKKYTAFTVPQGYYQWKVLPFGYHNSPSIFQQFMDRIFRPYYDFIIVYIDDILVFSKTIEEHKIHIAKFRDITLANGLIISKKKTELCKEKIDFLGVQIEQGGIELQPHIINKILEKHTKIKNKTELQSILGLLNQIRHFIPHLAQILLPIQKKLKIKDEEIWTWTKEDEEKIKLIQDYSKNLVIKMKYPINKEDMNWIIEVDASNNAYGSCLKYKPKNSKIEYLCRYNSGTFKENEQKYDINRKELIAVYQGLQSYSLFTCEGNKLVRTDNSQVYYWIKNDTNKKSIEFRNIKYLLAKIAVYNFEIQLIDGKTNIIADYLSRYNSSDTDGRYDEANT |
| Enzyme Length | 652 |
| Uniprot Accession Number | Q89703 |
| Absorption | |
| Active Site | ACT_SITE 26; /evidence=ECO:0000250 |
| 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=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; |
| DNA Binding | |
| EC Number | 3.4.23.-; 2.7.7.49; 3.1.26.4 |
| Enzyme Function | FUNCTION: Encodes for at least two polypeptides: protease (PR) and reverse transcriptase (RT). The protease processes the polyprotein in cis. Reverse transcriptase is multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. 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. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated, and reverse-transcribed inside the nucleocapsid. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA) (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (2); Metal binding (3) |
| Keywords | Aspartyl protease;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;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 77,054 |
| Kinetics | |
| Metal Binding | METAL 301; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405; METAL 364; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405; METAL 365; /note=Magnesium; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00405 |
| Rhea ID | RHEA:22508 |
| Cross Reference Brenda |