IED ID | IndEnz0002006604 |
Enzyme Type ID | protease006604 |
Protein Name |
Genome polyprotein Cleaved into: 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 ; Nuclear inclusion protein B NI-B NIB RNA-directed RNA polymerase EC 2.7.7.48 ; Capsid protein CP Coat protein Fragment |
Gene Name | |
Organism | Plum pox potyvirus (strain El amar) (PPV) |
Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Stelpaviricetes Patatavirales Potyviridae Potyvirus Plum pox virus Plum pox potyvirus (strain El amar) (PPV) |
Enzyme Sequence | LNKLAIPNANVCGWMSVRDYKRQGCNLDLDDNIRVPFYVKDLPETLHEKIWQTVEAHKADAGFGRICSSSACKIAYTLQTDIHSIPRTVKILDALLEQERTKQAHFRSMTSQSCSSSNFSLSSITSAIRSKYAKDHTEENIGVLQMAKAQLLEFKNLNIDPSYPELVRNFGALECVHHQTKEGVSKALRLKGHWNKQLVTRDATLMLGVLGGGAWMIFSYLRDSFKEEVVHQGFNRRQRQKLKFRQARDNRMAREVYGDDSTMEDYFGSAYSKKGKSKGRTRGMGTKTRKFVNMYGYDPTDYNFVRFVDPLTGHTLDENPLMDINLVQEHFSQVRNDYLGDDKITMQHIMSNPGIVAYYIKDATQKALKVDLTPHNPLRVCDKTATIAGFPEREFELRQTGQPVLVEPNAIPQINEEGDEEVGHESKSLFRGLRDYNPIASSICHLTNASGTRQSEIYGLGFGGLIVTNQHLFKRNDGELTIRSHHGEFVVKDTKTLKLLPCKGRDIIIIRLPKDFPPFPRRLQFRTPTAEDRVCLIGSNFQTKSVSSTMSETSATYPVDNSHFWKHWISTKDGHCGLPIVSTRDGSILGLHSLANSTNTQNFYAAFPDNFETTYLANQDNDNWIKQWRYNPDEVCWGSLQLKRDVPQSPFTICKLLTDLDGEFVYNQAKTTHWLRDKLEGNLKAVGACPGQLVTKHVVKGKCTLFETYLLTHPEEREFFQPLMGAYQKSALNKDAYVKDLMKYSKSIVVGAVDCEQFERAVDVVISMLISKGFSECSYVTDPEEIFSALNMKAAVGALYSGKKRDYFKDTSELEKEEFVRASCKRLFMGKKGVWNGSLKAELRPKEKVEANKTRSFTAAPIDTLLGGKVCVDDFNNQFYSLNLHCPWSVGMTKFRGGWDKLLRALPDGWIYCDADGSQFDSSLSPYLINAVLNIRLAFMEEWDIGEQMLSNLYTEIVYTPIATPDGTIVKKFKGNNSGQPSTVVDNTLMVILAMTYSLLKLGYHPDTHECICRYFVNGDDLVLAVHPAYESIYDELQHHFSQLGLNYTFTTKTENKEDLWFMSHKGIMCEGMYIPKLEPERIVSILEWDRSSEPIHRLEAICASMVEAWGYKELLREIRKFYSWVLEQAPYNALSKDGKAPYIAETALKKLYTDTEASETEIERYLEAFYSNLTDEDESNVVVHQADEKEDDEEEVDAGRPLVTTTQQPIVTTTTQQTPITSTTLQATQAMFNPIFTPATTEPTTRTVPHTTTTTPPSFGVIGNEDTAPNASNAVVRTGRDRDVDAGSIGTFTVPRLKAMTSKLSLPKVKGKAIMNLNHLAFYSPAQVDLSNTRAPQSCFQTWYEGVRRDYDVTDDEMSIILNGLMVWCIENGTSPNINGMWVMMDGETQVEYPIKPLLDHAKPTFRQIMAHFSNVAEAYIEKRNYEKAYMPRYGIQRNLTDYSLARYAFDFYEMTSTTPVRAREAHIQMKAAALRNAQNRLFGLDGNVGTQEEDTERHTAGDVNRNMHNLLGMRGV |
Enzyme Length | 1518 |
Uniprot Accession Number | Q01681 |
Absorption | |
Active Site | ACT_SITE 471; /note=For nuclear inclusion protein A activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00766; ACT_SITE 506; /note=For nuclear inclusion protein A activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00766; ACT_SITE 576; /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}; |
DNA Binding | |
EC Number | 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: [Cytoplasmic inclusion protein]: Has helicase activity. It may be involved in replication.; 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:0000250|UniProtKB:P04517}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (7); Domain (2); Modified residue (1); Motif (1); Non-terminal residue (1); Region (1); Site (5) |
Keywords | Capsid protein;Covalent protein-RNA linkage;Host nucleus;Host-virus interaction;Hydrolase;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-directed RNA polymerase;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 295; /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 273..280; /note=Nuclear localization signal; /evidence=ECO:0000255 |
Gene Encoded By | |
Mass | 172,033 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:21248 |
Cross Reference Brenda |