Detail Information for IndEnz0002000946
IED ID IndEnz0002000946
Enzyme Type ID protease000946
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; 6 kDa protein 1
6K1
; Cytoplasmic inclusion protein
CI
EC 3.6.4.-
; 6 kDa protein 2
6K2
; Viral genome-linked protein
VPg
; Nuclear inclusion protein A
NI-a
NIa
EC 3.4.22.44
49 kDa proteinase
49 kDa-Pro
NIa-pro
; Nuclear inclusion protein B
NI-b
NIb
EC 2.7.7.48
RNA-directed RNA polymerase
; Capsid protein
CP
Coat protein
Gene Name
Organism Blackberry virus Y (isolate Blackberry plant/USA:Arkansas/C3ARK/2005) (BVY)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Stelpaviricetes Patatavirales Potyviridae Brambyvirus Blackberry virus Y Blackberry virus Y (isolate Blackberry plant/USA:Arkansas/C3ARK/2005) (BVY)
Enzyme Sequence MPTRYRGADRYGNLGYDKVLQSKADAAKRRGLLFDHGSETYECPRCGEIWRNLDDYMAEGGKMHPKKCLPEECDSDEEQISSCNAALIHEKWGDLDSDTSSKLSEFYKEPSILTYTTRTHCVVEKMRSMTAPQCIEDIVGVRLHGRTAWFFSKDPTLQYGHHPIYYDTHPWNDELDKYLGGAKYNTALVQVYDGTRDLPYHKDDEPCYDITNNPIRTVNVTGTGDLCISKDKRRLYETIPMTSGTVITFPATMQENFYHAVRNPSAGRISITFRNQIRTVERQVAHSANKRWVPIVEARVTTNESRRGDNKQFQEAQSKLQTKTTINFGEFAAEVDGYYPTLSQDHKPALPKIIPELGLPTVDFIYVGNMRVPIDFKKNNVPAIVDTARHVAKIIDSQALTSEPIKVFTEQREVVGNVVTCTGTGFSVADAKEAKALLNGLMYNRASNLFICPSCSDAAVLPEALLTLEHKRSCELASMKKISLARNMQVHVKQEAVARLISQQNSISVPIATLSSCVRGSADTTQVSLHIDEEDSIVDAIHLPNDFITCDHEHAFETDSASDNDVETMKKSEKRRKRRKRNPPPVRQVITRAPVSNIICDVILTCLETQIPVEFIGKSCITFKPVRVGPVHTVGIQLKHQLHKTGFEVDDLPDRETTSDIILAATRALRRLRHAHSNAQQVHNSDITFGTSGAILPWSWLAHDVIVEGPVQDSLVVRGRNVVSGHVTNALNLQQDCLADDYLQYSEELQPLHDDLSELKPLNVINNELIRQNMHITTLYSNMSKLQNDALATKAEMKLPLFGVAQLVVNQLKYNTTTHEWGERGDYVRKFVGKFFADFPTTQVPKQYMTRTTNGHIRITAYKALSLTSDPEIMMSRRMTQPMLTTAKQADCVFQSTTGATCTSASCTTNSSGVVLSNKCADPAPNTLRVRTMWDDIIIELPLQGGRVHVPLEGLCFSTIFLHMYLLVPDESVKLFHRTVTERAMPSLGQWPTLRHLATWVLNLVAMFPVLSTTPMPEILVHHESQSVHIPDCLGTATSGYHRLNIVTPYDFIIFATEIGRNGCQEYRVGGFAHDIKYTVSLMQDKRKLLHELMLTPTWAFYALSSPTLLKILYRSGALKRTYEHAVMANHNAVDLVHELNFLPERVSRAQTLQDEITAWEANVGRVLQQVDGYLTRNHDPPLQRWYADASARLQHLKIDVDLLKNGFRSSQREHVEKKEQLLCDSFERLYNEQNSSLESLKTRCGMGSARALIKPSGKCESPEPAKQLSCKDLICSTKDKYALMLYTQADALKRKIVAGSQSAFTTVCAGVAYRATKVMLRTPFNLLNALNTYSLLIAAVNVMVLVQNYRRDQRKRAQYVNNLETQSMIRHYFAHLEQYIVNYVPRDEQFEVIKAKFDEEFPEYNVMFKEVYKERIQFQSADEGKNMCKIFASAILVMMVFDAHRADLMYKSFSQVRALFNTLYDSGNPFNIIFQAERTIAPTMDVIIQEPKPAIPSTSSCTFETWFRNCVNANNVIPVIPECDLLDFTRDTASSVVATLTSSVKREFVIRGFVGSGKSTYLPHLLTKHGKVLLCEPVRVLASNVFEALSGSPFYQSPTLLMRGTTKFGSGKITVATSGYAANYYNANRHRLNEFAYIIFDESHQHTAHNFLLRSILDVIGYEGTVLHVSATPIGKEIPFRTMHPVEVVNMSTLSFEDFAIGQRKQVRCDVFNKGANILVYVASYNDVDRMSTLLLERGLRVKKIDARTVANVNNITCDGSDGEPLYLVATNIVENGVTLNVDVVVDFGLCVKPVINALQRRVDYVKTPITWGQRIQRNGRVGRYKNGFCLNVGDVYKTPPIISEDVALESALMCFAANVPPIFDNVDPALFGQVTRPQVQTAQMFELPIYITTPMISDAGALQSDIYQVIKKFVLREGSIQLTQDATYLSNMSNWKTIADYFPDISDTHAMRHEKVPFFVKDFGENSYIALAEAIRKARNKSLGARGKLYGDVDATALLLQTDPGSLDRSIMIVETELVAQRSKLEDLNHHVHESTGMFQRYVSHLNHCLRGRYQTDQIQKNIEVLSNMRSTLVGYRQVVDKVEPEEIPHFVQQNPNITMIIDFQSDRTKADGFVKHGINGIYNYTKIASDTFSLLLIACVVIYYVVQYFFREMKSHITFEASGSRRNRLHLRDNKLIKGGYTWAGPSDDMEREFGPEYALKRDKFSEKKARKHMRERIQPRTNMGVKLAPFQVFYGFDVADYDVLQLFDPITGVKIDMDPRATAKEITEEVEDTPFNKEVWSDTHMPEKIQATFVKKGGVNREDVLKQVRVDMTTHNPTMVTGSGGIMGYPEHKGDFRQTGPPKFSIVPEGRSTIKSGNNIAPFISAMGTIKNVYMNGDFDTLACTQIGNKLVVNAHIFMEPVKKQELILQHGVYELPNNGTINIKHVPGIDMVIQTLPMDVPLARQIKAYRGPIPGELIRLLKIERNTKTNSTSLSDPGTARVGPGTIWYHNITTKHGDCGSLVLSEKDNKIVGIHTGQQDGTNLNLFAPITKDAIVAIETVLPGELNDWVFTPDMLDVGSNNAIRKQASDPFPVVKKLLEGITFQNNRTTTTDSVSNTAILPARKYWVASDLPVNIKYQCDMPTFFNTRHTYEGESQPFMAYLRECGDAETFFRPLLSHYIPSNLNGDAFKKDFFKYGKPVPVGLVHGPSFKIASDRVIKRFERVGYERHSIPFEFDAEAIRDDLNKHAAMGAQYVGKKEQHLDGISEEQFCDEFVASCCRLANNCDGVWKGSLKAELRSKEKVQENKTRVFTSAPYDVLLGGKACVMHFNKKFYANNTKGPWTVGINKLGLGWHRLLKSLPEGFVYGTGDGSQFDSSLTPLLINEVCRIRMYFMQDDELGQAMLRGLYRQIIWTLISMPDGSVVRKAKGNPSGQPSTVDDNTIMVMLAVEYVFAYLGITQEEMDTIFKYYANGDDLIFAIHPDRESILNEFTHLFAHLGLNYIFEDRTRNRAELEYMSLTGIEREGFYIPKLSRERISSIVQWRRKGDTRAMFDALNAAILESWGYDDLTYWLRKYYEWLIINRYDIDLPEGEKLPYHTETAVETLYTCDDNTTVYDGRYDFEVPTDASGGVFIIDFQSSSGTDTPPVIPPATSEPALQPVLTRQTSRPPTPPNTILTGQQQQQLMPKSSQPYQLEPLLAPTGVQQPTFGTFGMPQAQQTTTEPVVAAARVRGKQKEGDTSLSQVRDHRRLSPERIVRHDDDLAPPNESTSGESSHYDELTLPDVPRDKRKGLGARLKGKPIITQTQIYNYRPAFGSIHNNKATDIELEAWKKQIADYFQVDDVSTLILGFMAYVIENGTSPEIFTNQKFVMATSSGEQREYPLAPFRSRSVELRKIMRRFSEEAIDYIQIQREHNPQYVPRQAVVRNVKRAIYFPYCFDFIDETILTPDALEIVHQMKAAALESASSKVLGLDGGSARAIDTERHTTEDATARTHNLRGAAMMA
Enzyme Length 3491
Uniprot Accession Number A0AUJ5
Absorption
Active Site ACT_SITE 640; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 651; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 692; /note=For P1 proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01219; ACT_SITE 956; /note=For helper component proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01080; ACT_SITE 1029; /note=For helper component proteinase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01080; ACT_SITE 2400; /note=For nuclear inclusion protein A activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00766; ACT_SITE 2435; /note=For nuclear inclusion protein A activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00766; ACT_SITE 2504; /note=For nuclear inclusion protein A activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00766
Activity Regulation
Binding Site BINDING 268; /note=2-oxoglutarate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.; EC=3.4.22.44; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; 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; 3.6.4.-; 3.4.22.44; 2.7.7.48
Enzyme Function FUNCTION: [Capsid protein]: Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification. {ECO:0000250}.; FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication. {ECO:0000250}.; 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: [Cytoplasmic inclusion protein]: Has helicase activity. It may be involved in replication (By similarity). {ECO:0000250}.; FUNCTION: Both 6K peptides are indispensable for virus replication. {ECO:0000250}.; FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and proteolytic activities. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 1553..1560; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00541
Features Active site (8); Binding site (1); Chain (11); Compositional bias (1); Domain (7); Metal binding (3); Modified residue (1); Motif (1); Nucleotide binding (1); Region (3); Site (9)
Keywords ATP-binding;Capsid protein;Covalent protein-RNA linkage;Dioxygenase;Helical capsid protein;Helicase;Hydrolase;Iron;Metal-binding;Nucleotide-binding;Nucleotidyltransferase;Oxidoreductase;Phosphoprotein;Protease;RNA-directed RNA polymerase;Reference proteome;Serine protease;Suppressor of RNA silencing;Thiol protease;Transferase;Viral RNA replication;Virion
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
Modified Residue MOD_RES 2238; /note=O-(5'-phospho-RNA)-tyrosine; /evidence=ECO:0000250
Post Translational Modification PTM: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250}.; 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 1642..1645; /note=DEAH box
Gene Encoded By
Mass 393,838
Kinetics
Metal Binding METAL 201; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805; METAL 203; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805; METAL 259; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805
Rhea ID RHEA:21248
Cross Reference Brenda