Detail Information for IndEnz0002010763
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