| IED ID | IndEnz0002000958 |
| Enzyme Type ID | protease000958 |
| Protein Name |
Genome polyprotein Cleaved into: P1 proteinase EC 3.4.-.- N-terminal protein ; Helper component proteinase HC-pro EC 3.4.22.45 ; Protein P3 Fragment |
| Gene Name | |
| Organism | Potato virus Y (strain O) (PVY) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Stelpaviricetes Patatavirales Potyviridae Potyvirus Potato virus Y Potato virus Y (strain O) (PVY) |
| Enzyme Sequence | MATYMSTICFGSFECKLPYSPASCGHIVKEREVPASVDPFADLETQLSARLRKQEYATVRVLKNGTFTYRYKTDAQIMRIQKKLERKDREEYHFQMAAPSIVSKITIAGGDPPSKSEPQAPRGIIHTTPKVRKVKTRPIIKLTEGQMNHLIKQVKQIMSEKRGSVHLISKKTTHVQYKEILGATRAAVRTAHMMGLRRRVDFRCDTWTVGLLQRLARTDKWSNQVRTIHVRRGDSGVILNTKSLKGHFGRSSGDLFIVRGSHEGKLYDARSRVTQSVLNSMIQFSNADNFWKGLDGNWARMRYPSDHTCVAGLPVADCGRVAALTRHSILPCYKITCPTCAQQYASLPVSDLFKLLHKHARDGLNRLGADKDRFIHVNKFLMALEHLTEPVDLNLELFNEIFKSIGEKQQAPFKNLNVLNNFFLKGKENTAHEWQVAQLSLLELARFQKNRTDNIKKGDISFFRNKLSARANWNLYLSCDNQLDKNANFLWGQREYHAKRFFSNFFDEIDPAKGYSAYEIRKHPNGTRKLSIGNLVVPLDLAEFRQKMKGDYRKQPGVSRKCTSSKDGNYVYPCCCTTLDDGSAIESTFYPPTKKHLVIGNSGDQKFVDLPKGDSEMLYIAKQGYCYINVFLAMLINISEEDAKDFTKKVRDMCVPKLGTWPTMMDLATTCAQMRIFYPDVHDAELPRILVDHDTQTCHVVDSFGSQTTGYHILKASSVSQLILFANDELESDIKHYRVGGVPNACPELGSTISPFREGGVIMSESAALKLLLKGIFRPRVMRQLLLDEPYLLILSILSPGILMAMYNNGIFELAVRLWINEKQSIAMIASLLSALALRVSAAETLVAQRIIIDAA |
| Enzyme Length | 856 |
| Uniprot Accession Number | P22602 |
| Absorption | |
| Active Site | ACT_SITE 192; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 201; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 235; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 626; /note=For helper component proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01080; ACT_SITE 699; /note=For helper component proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01080 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.; EC=3.4.22.45; |
| DNA Binding | |
| EC Number | 3.4.-.-; 3.4.22.45 |
| Enzyme Function | FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Seems to act as suppressor of post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (5); Chain (4); Domain (2); Motif (2); Non-terminal residue (1); Site (2) |
| Keywords | Hydrolase;Protease;Serine protease;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 334..337; /note=Involved in interaction with stylet and aphid transmission; /evidence=ECO:0000250; MOTIF 592..594; /note=Involved in virions binding and aphid transmission; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 96,813 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |