IED ID | IndEnz0002004419 |
Enzyme Type ID | protease004419 |
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 | Turnip mosaic virus (strain Japanese) (TuMV) |
Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Stelpaviricetes Patatavirales Potyviridae Potyvirus Turnip mosaic virus (strain Japanese) (TuMV) |
Enzyme Sequence | MAAVTFATAITNTTASKPALTGMIQFGNFPPVPLRSTTVTTVATSVAQPKLHTVQFGSLDPVVVKSGAGSFAKATRQQPNVEIDVSLSEAAALEVAKPRPNAVLRMHEEANKERALFLDWEASLKRSSYGIAENEKVVMTTRGVSKIVPRSSGAMKQKRARERRRAQQPIILKWEPKLSGISIGGGLSASAIEVEEARTKWPLHKTPSMKRKTVHRRCKMNDQGIDMLMRSLIKIFKAKSANIEFIGRKSIKVDFVKKEQTKFARVQVVHLLGKRAQRDLSTGMEENHFIDILSGYSGNKTTINPGVVCAGWSGIVVRDGILTQKRSRSPSEAFVIRGEHEGKLYDARIKITRTMSHKIVHFSAAGANFWKGFDRCFLAYRSDNREHTCYSGLDVTECGEVAALMCLAMFPCGKITCPDCVTDSELSQGQASGPSMKHRLVQLRDVIKSSYPRFKHAVQILDRYEQSLRSANENYQDFAEIQSISDGVEKAAFPHVNKLNAILIKGATATGEEFSQATKHLLEIARYLKNRTENIEKGSLKSFRNKISQKAHINPTLMCDNQLDRNGNFIWGERGYHAKRFFSNYFEIIDPKKGYTQYETRVVPNGSRKLAIGKLIVPTNFEVLREQMKGEPVEPYPVTVECVSKLQGDFVHACCCVTTESGDPVLSEIKMPTKHHLVIGNSGDPKYIDLPEIEENKMYIAKEGYCYINIFLAMLVNVKESQAKEFTKVVRDKLVGELGKWPTLLDVATACYFLKVFYPDVANAELPRMLVDHKTKIIHVVDSYGSLSTGYHVLKTNTVEQLIKFTRCNLESSLKHYRVGGTEWEDTHGAKNIDDPQWCIKRLIKGVYRPKQLKEDMLANPFLPLYALLSPGVILAFYNSGSLEYLMNHYIRVDSNVAVLLVVLKSLAKKVSTSQSVLAQLQIIDRSLPELVEARANINRPDDEAARACNRFMGMLLHMSEPNWELADGGYTILRDHSISILEKKLSTNLGRSMERVKLVGALCYKILLVKASNFYTERFANEKRSRFRRQIQRVSRVILRME |
Enzyme Length | 1043 |
Uniprot Accession Number | P0CK11 |
Absorption | |
Active Site | ACT_SITE 270; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 279; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 313; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 706; /note=For helper component proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01080; ACT_SITE 779; /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. {ECO:0000269|PubMed:18408156, ECO:0000269|PubMed:20585568, ECO:0000269|PubMed:22511869}. |
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;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:0000269|PubMed:18408156}. |
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 414..417; /note=Involved in interaction with stylet and aphid transmission; /evidence=ECO:0000250; MOTIF 672..674; /note=Involved in virions binding and aphid transmission; /evidence=ECO:0000250 |
Gene Encoded By | |
Mass | 117,285 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |