| IED ID | IndEnz0002012096 |
| Enzyme Type ID | protease012096 |
| 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 | Turnip mosaic virus (strain Quebec) (TuMV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Stelpaviricetes Patatavirales Potyviridae Potyvirus Turnip mosaic virus (strain Japanese) (TuMV) Turnip mosaic virus (strain Quebec) (TuMV) |
| Enzyme Sequence | MAAVTFASAITNAITNKTTSTGMVQFGSFPPMPLRSTTVTTVATPVGQPKLYTVRFGSLDPVIVKGGAGSLAKATRQQPSVEIDVSLSEAAALEVAKPKSSAVLRMHEEANKERALFLDWEASLKRRSYGIAENEKVVMTTRGVSKIVPRSSRAMKQKRARERRRAQQPIILKWEPKLSGFSIGGGFSASAIEAEEVRTKWPLHKTPSMKKRMVHKTCKMSDQGVDMLIRSLVKIFKAKSANIEYIGKKPIKVDFIRKERTKFARIQVAHLLGKRAQRDLLAGMEENHFIDILSEYSGNGTTINPGVVCAGWSGIVVRNETLTQKRSRSPSKAFVIRGEHEDKLYDARIKITKTMSLKIVHFSARGANFWKGFDRCFLAYRSDNREHTCYSGLDVTECGEVAALMCLAMFPCGKITCPDCVIDSELSQGQASGPSMKHRLTQLRDVIKSSYPRFKHAVQILDRYEQSLSSANENYQDFAEIQSISDGVEKAAFPHVNKLNAILIKGATATGEEFSQATKHLLEIARYLKNRTENIEKGSLKSFRNKVSQKAHINPTLMCDNQLDKNGNFIWGERGYHAKRFFSNYFEIIDPKKGYTQYETRVVPNGSRKLAIGKLIVPTNFEVLREQMRGEPVEPYPVTVECVSKSQGDFVHACCCVTTESGDPVLSEIKMPTKHHLVIGNSGDPKYIDLPEIEENKMYIAKEGYCYINIFLAMLVNVKESQAKEFTKVVRDKLVSELGKWPTLLDVATACYFLKVFYPDVANAELPRMLVDHKTKIIHVVDSYGSLSTGYHVLKTNTVEQLIKFTRCNLESSLKHYRVGGTEWENAHGADNIDNPQWCIKRLVKGVYRPKQLKEDMLANPFLPLYALLSPGVILAFYNSGSLEHLMNHYISADSNVAVLLVVLKSLAKKVSTSQSVLAQLQIIERSLPELIEAKANINGPDDAATRACNRFMGMLLHMAEPNYELANGGYTFLRDHSISILEKSYLQILDEAWNELSWSERCVIRYYPSKQAIFTQKDLPMQSEADLGGRYSESVISSYEWSKQQAKGVKDSVVNKLRSSMSWTSSKVSNSVCRTINYLVPDVFKFMNVLVCISLLIKMTAEANHIITTQRRLKLDIEETERKKIEWELAFHHNILTHSASQHPTLDEFTAYIAEKAPHLSEHIEPEEKEVVHQAKRQSEQELERVIAFVALVLMMFDAERSDCVTKILNKLKGLVATVEPTVYHQTLNEIEDDLNERNLFVDFELSSDSEMLQQLPAEKTFASWWSHQLSRGFTIPHYRTEGKFMTFTRATATEVAGKIAHESDKDILLMGAVGSGKSTGLPYHLSRKGNVLLLEPTRPLAENVHKQLSQAPFHQNTTLRMRGLTAFGSAPISVMTSGFALNYFANNRSRIEEFDFVIFDECHVHDANAMAMRCLIHECDYSGKIIKVSATPPGREVEFSTQYPVSISTEDTLSFQDFVNAQGSGSNCDVISKGDNILVYVASYNEVDTLSKLLIERDFKVTKVDGRTMKVGNIEITTSGTPSRKHFIVATNIIENGVTLDIDVVADFGTKVLPYLDTDNRMLSTTKTSINYGERIQRLGRVGRHKPGHALRIGHTERGLSEVPSCIATEAALKCFTYGLPVITNNVSTSILGNVTVKQARTMSVFEITPFYTSQVVRYDGSMHPQVHALLKRFKLRDSEIVLTKLAIPNRGVNAGSQPVSMHDSVQMLKIGVTLRIPFMCRDIPEKLHLDMWDVVVKFKGDAGFGRLSSSASKVAYTLQTDVNSIQRTVTIIDTLIAEERRKQEYFKTVTSNCVSSSNFSLQSITNAIKSRMMKDHPCENISVLEGAKSQLLEFRNLNSDHSFVTKTDGISRSFMRDYGALEAVNHQSTNEMSKFLQLKGKWNKTLITRDVLVICGVLGGGVWMVVQHFRSKVSEPVTHEAKGKKQRQKLKFRNARDNKMGREVYGDDDTIEHFFGDAYTKKGKSKGRTRGIGHKNRKFINMYGFDPEDFSAVRFVDPLTGATLDDNPFTDITLVQKHFGDIRMDLLGEDELDSNEIRMNKTIQAYYMNNKTGKALKVDLTPHIPLKVCDLHATIAGFPERENELRQTGKAQPINIDEVPRANNELVPVDHESNSMFRGLRDYNPISNNICHLTNVSDGASNSLYGVGFGPLILTNRHLFERNNGELIIKSRHGEFVIKNTTQLHLLPIPDRDLLLIRLPKDVPPFPQKLGFRQPEKGERICMVGSNFQTKSITSIVSETSTIMPVENSQFWKHWISTKDGQCGSPMVSTKDGKILGLHSLANFQNSINYFAAFPDDFTEKYLHTIEAHEWVKHWKYNTSAISWGSLNIQASQPVSLFKVSKLISDLDSTAVYAQTQQNRWMFEQLTGNLKAIAHCPSQLVTKHTVKGKCQMFDLYLKLHDEAREYFQPMLGQYQKSKLNREAYAKDLLKYATPIEAGNIDCDLFEKTVEIVISDLRGYGFETCNYVTDENDIFEALNMKSAVGALYKGKKKDYFAEFTPEVKEEILKQSCERLFLGKMGVWNGSLKAELRPLEKVEANKTRTFTAAPLDTLLGGKVCVDDFNNQFYDHNLRAPWDVGMTKFYCGWDRLLESLPDGWVYCDADGSQFDSSLSPYLINAVLNIRLGFMEEWDVGEVMLRNLYTEIVYTPISTPDGTLVKKFKGNNSGQPSTVVDNTLMVILAVNYSLKKGGIPSELRDSIIRFFVNGDDLLLSVHPEYEYILDTMADNFRELGLKYTFDSRTREKGDLWFMSHQGHRREGIWIPKLEPERIVSILEWDRSKEPCHRLEAICAAMIESWGYDKLTHEIRKFYAWMIEQAPFSSLAQEGKAPYIAETALRKLYLDKEPAQEDLTQYLQAIFEDYEDGVEACVYHQAGETLDADLTEEQKQAEKEKKEREKAEKERERQKQLAFKKGKDVAQEEGKRDKEVNAGTSGTFSVPRLKSLTSKMRVPRYEKRVALNLDHLILYTPEQTDLSNTRSTRKQFDTWFEGVMADYELTEDKMQIILNGLRVWCIENGTSPNINGMWVMMDGDDQVEFPIKPLIDHAKPTFRQIMAHFSDVAEAYIEKRNQDRPYMPRYGLQRNLTDMSLARYAFDFYEMTSRTPIRAREAHIQMKAAALRGANNNLFGLDGNVGTTVENTERHTTEDVNRNMHNLLGVQGL |
| Enzyme Length | 3163 |
| Uniprot Accession Number | Q02597 |
| 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; ACT_SITE 2161; /note=For nuclear inclusion protein A activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00766; ACT_SITE 2196; /note=For nuclear inclusion protein A activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00766; ACT_SITE 2266; /note=For nuclear inclusion protein A activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00766 |
| Activity Regulation | |
| Binding Site | |
| 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.; FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication.; 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.; FUNCTION: [Viral genome-linked protein]: Recruits the host translation initiation complex for viral genome translation by binding to host plant eIF4E/eIF(iso)4E and eIF4G/eIF(iso)4G proteins. {ECO:0000269|PubMed:28199446, ECO:0000269|PubMed:29504210}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 1313..1320; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00541 |
| Features | Active site (8); Chain (11); Compositional bias (1); Domain (6); Modified residue (1); Motif (4); Natural variant (2); Nucleotide binding (1); Region (1); Sequence conflict (1); Site (8) |
| Keywords | ATP-binding;Capsid protein;Covalent protein-RNA linkage;Direct protein sequencing;Helical capsid protein;Helicase;Host nucleus;Host-virus interaction;Hydrolase;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-directed RNA polymerase;Ribosomal frameshifting;Serine protease;Suppressor of RNA silencing;Thiol protease;Transferase;Viral RNA replication;Virion |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host nucleus {ECO:0000250|UniProtKB:P21231}. Note=Binds to host plant eIF4E proteins in the host nucleus. {ECO:0000250|UniProtKB:P21231}.; SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}. |
| Modified Residue | MOD_RES 1986; /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: 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 polyprotein 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. 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 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; MOTIF 1402..1405; /note=DECH box; MOTIF 1964..1971; /note=Nuclear localization signal; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 357,822 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21248 |
| Cross Reference Brenda |