IED ID | IndEnz0002010763 |
Enzyme Type ID | protease010763 |
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 C) (PVY) (Potato virus C) |
Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Stelpaviricetes Patatavirales Potyviridae Potyvirus Potato virus Y Potato virus Y (strain C) (PVY) (Potato virus C) |
Enzyme Sequence | MAIYMSTICFGSIECKLPYSPASCGHVTEEREVLASVEPFMDLEAQLSARLLRQKHATVRVLKNGTCAYRYKTDAQIVRIQKKLERKERDEYHFQMAAPSIVSKITIAGGDPPSKYEPQTPKRVIHTTPRVRKVKKHSIIKLTESQMNHLIKQVKRIMSAKKGSVHLINKKSTHVQYKEILGTTRAAVRTAHMMGLRRRVDFRCDMWTTERLKCLARTDKWSNRVHTINIRKGDSGVILNADSLKGHFGRSSGGLFIVRGSHEGKLYDARSKVTQGVLNSMVQFSNAENFWKGLDDNWARMRYPSDHTCIDGLPVEDCGRVAALMTHSILPCYEITCPTCAQQYANLPASDLFKLLHKHARDGLSRLGSDKDRFVHVNKFLVALEHLTEPVDLNLELFNEIFKSIGEKQQAPFKNLNVLNNFFLKGKENTAHEWQVAQLSLLELARFQKNRTDNIKKGDISFFRNKLSAKANWNLYLSCDNQLDKNANFLWGQREYHAKRFFSNFFEEVDPAKGYSAYEIRKHPNGTRKLSIGNLVVPLDLAEFRQKMKGDYRKQPGVSKRCTSSKDGNYVYPCCCTTLDDGSAIESTFYPPTKKHLVIGNSGDQKYVDLPKGDSEMLYIAKQGYCYINVFLAMLINVSEEDAKDFTKKVRDMCVPKLGTWPTMMDLATTCAQMRIFYPDVHDAELPRILVDHDTQTCHVVDSFGSQTTGYHILKASSVSQLILFANDELESEIKHYRVGGVPNACPELGSTISPFREGGVIMSESAALKLLLKGIFRPKVMRQLLLDEPHLLILSILSPGILMAMYNNGIFELAVRLWINEKQSIAMIASLLSALALRVSAAETLVAQRIIIDAA |
Enzyme Length | 856 |
Uniprot Accession Number | P22601 |
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]: Inactive with respect to its ability to effect aphid transmission of either PVC or PVY. Between the 2 amino acid changes which are specific to PVC-HC, the Lys to Glu-334 is more probably responsible of loss of binding to aphid stylet and thereby loss of aphid transmissibility. Displays proteolytic activity. 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, ECO:0000269|PubMed:9880030}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (5); Chain (4); Domain (2); Motif (1); Non-terminal residue (1); Site (2) |
Keywords | Hydrolase;Protease;Serine protease;Suppressor of RNA silencing;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 592..594; /note=Involved in virions binding and aphid transmission; /evidence=ECO:0000250 |
Gene Encoded By | |
Mass | 96,829 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |