| IED ID | IndEnz0002004853 |
| Enzyme Type ID | protease004853 |
| Protein Name |
P3N-PIPO polyprotein Cleaved into: P1 proteinase EC 3.4.-.- N-terminal protein ; Helper component proteinase HC-pro EC 3.4.22.45 ; Movement protein P3N-PIPO Pretty interesting potyviridae ORF PIPO |
| Gene Name | |
| Organism | Potato virus Y (strain N) (PVY) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Stelpaviricetes Patatavirales Potyviridae Potyvirus Potato virus Y Potato virus Y (strain N) (PVY) |
| Enzyme Sequence | MATYMSTICFGSFECKLPYSPASCEHIVKEREVPASVDPFADLETQLSARLLKQKYATVRVLKNGTFTYRYKTDAQIMRIQKKLERKDREEYHFQMAAPSIVSKITIAGGDPPSKSEPQAPRGIIHTTPRMRKVKTRPIIKLTEGQMNHLIKQIKQIMSEKRGSVHLISKKTTHVQYKKILGAYSAAVRTAHMMGLRRRVDFRCDMWTVGLLQRLARTDKWSNQVRTINIRRGDSGVILNTKSLKGHFGRSSGGLFIVRGSHEGKLYDARSRVTQSILNSMIQFSNADNFWKGLDGNWARMRYPSDHTCVAGLPVEDCGRVAALMAHSILPCYKITCPTCAQQYASLPVSDLFKLLHKHARDGLNRLGADKDRFIHVNKFLIALEHLTEPVDLNLELFNEIFKSIGEKQQAPFKNLNVLNNFFLKGKENTAHEWQVAQLSLLELARFQKNRTDNIKKGDISFFRNKLSAKANWNLYLSCDNQLDKNANFLWGQREYHAKRFFSNFFEEIDPAKGYSAYEIRKHPSGTRKLSIGNLVVPLDLAEFRQKMKGDYRKQPGVSKKCTSSKDGNYVYPCCCTTLDDGSAIESTFYPPTKKHLVIGNSGDQKFVDLPKGDSEMLYIAKQGYCYINVFLAMLINISEEDAKDFTKKVRDMCVPKLGTWPTMMDLATTCAQMRIFYPDVHDAELPRILVDHDTQTCHVVDSFGSQTTGYHILKASSVSQLILFANDELESDIKHYRVGGVPNASPELGSTISPFREGGVIMSESAALKLLLKGIFRPKVMRQLLLDEPYLLILSILSPGILMAMYNNGIFELAVRLWINEKQSIAMIASLLSALALRVSAAETLVAQRIIIDAAATDLLDATCDGFNLHLTYPTALMVLQVVKNRNECDDTLFKAGFPSYNTSVVQIMEKKLSKSLERCLERFNLARKLSATWYSYRAKRSIHSVHKTHRKGRFERVIQHITTSVLGPKRPGGQRHCLRIERAI |
| Enzyme Length | 986 |
| Uniprot Accession Number | P0CJ93 |
| 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. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity (By similarity). {ECO:0000250}.; FUNCTION: [Movement protein P3N-PIPO]: Allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (5); Chain (4); Domain (2); Motif (2); Sequence uncertainty (1); Site (2) |
| Keywords | Host cell junction;Host-virus interaction;Hydrolase;Protease;Reference proteome;Ribosomal frameshifting;Serine protease;Suppressor of RNA silencing;Transport;Viral movement protein |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Host cell junction, host plasmodesma {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically (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 | 111,724 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |