Detail Information for IndEnz0002000877
IED ID IndEnz0002000877
Enzyme Type ID protease000877
Protein Name RNA1 polyprotein
P1

Cleaved into: P1A protein
1A
protease cofactor
; Putative ATP-dependent helicase
EC 3.6.4.-
1B
NTP-binding protein
NTB
membrane-binding protein
; Viral genome-linked protein
1C-VPg
; Picornain 3C-like protease
3C-like protease
EC 3.4.22.-
1D-PRO
; RNA-directed RNA polymerase
EC 2.7.7.48
1E-POL
Gene Name
Organism Tomato black ring virus (strain MJ) (TBRV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Secoviridae Comovirinae Nepovirus Beet ringspot virus (BRSV) (Tomato black ring virus (strain S)) Tomato black ring virus (strain MJ) (TBRV)
Enzyme Sequence MSVTLSPPGDCFTFNHVKYNNSLNKYLFYNNNLDIVLDDFDFYFNFYAKKYNVLSSFFSDRVLSALYTPMSVSEAASLALEDFCELALDKLKINPFHQLWEETLANWPVYPGTSLLDFFRTQYEIRREVAEASAEALRLKKATRADAFADEVKFLIKNGVLPHLAGDFARKIWSTGKDQKKTRTAFLVKIKKANQLKQQWNSARSLAAARAEVLREFEPSPQQIQKAIEAQLFAEKLGRKYATLTARVRAKRAAARELREKQLYQETVDLLNASLLPPMEKVEIERKYRKVRPTGANVVHQVVANPLGSLCPYMGLGAKTADVRCQATLMAGKIHAQYPRLATAIYAWVIGPAAHFECITPVRNFVKGLTFMVDFFPEEALIHELNEITTEAVCIGASMVLDEERAKLEAHAQSANCRANVFMKAMAGVKNMAKCAYTGFKTGCEEAGRSLAEGICSVMMRSFRECIAQIKTELGCAIEMVEVMIKKVKDWFYSMLEKLQCGLETLGSYAMYALAILLGCGLTSLLERCIGGQGILTKLFITGVLAAIGLQAAGGFDNLQREMVQLCTALAAGIFDIQHAGNGKYKPSWDITAEHAREDARDSNVRSIPIISGVIEALAQFGTGLCSMQSATLIEIGKIGAACHSMRMGKEALKEFCATLMYYLGRIADKVTGRETIFFDELSTLVHVDVRGWIKRAQSCMRESFHTEIGNQFFRDMVAQLVDEGQKLQIGVNGIPRKISADYSQLIGQIMKDLVELHKRTIRAGISEGRRCEPVWIYLFGQRHCGKSNFMSTLDNALAKHFNLPNTTAYRNCKDAFYSGYSGQTFFHMDDLSSVKLEPPLEAELINLVSCQEVPLNMADLADKPIYFRSPFIISSSNFEDVPAGCGVRDIEAYRARKACLVEMRRKPGVIYDPENPLLASQARFKDPMYQTLINGQTEETSWMEMDDVVTEIINISARHRSAQEKLQARYMREKALLDPLALASESFLVKEAQKVFLDFDGVELEKAGVPRPEGGHGLYVDGVLYLVNASFEFDEIPIKDGGYQRLWDSRMRKKFLPAIQRDEHLNTKSMVVTGFLRSLVNGECAVLSKDTLTASATTAQLSIFKALRLEERVYLRTLQHQLDLYSQDIPENPYCNSAWVKVLGAIGAGRDYLVQNGCGILMIAAALILILVSGWGFWKLFVGLFSGTMSLGAAITGMSAVDIKAQQSSASQEKGYRARNIPIHHRYAYARSQAGDGLLPAARLCVAIYQPGGGFVSAMQYKNKSVRMTRHQALRFKEGEQLTVIFASTGESQLIRWHKYHMREEHGSEIVTWLAPSLPALSPDLKDLFLEDKEVDLPNHFKTIGYVLRVDSTAFHYDTLDTYGAVDKTPLPLKGVVGNELYLHEIPEKIVFHYESRNDDCGMIMLCQIRGKMRVVGMLVAGKDKTSWADIMPPNSLAELKSQIDYIPEFGEACDGYFKAGYVHKSEAPTLPKKTNMVPVPESLRVPCDVPVKEPAVLTKDDPRCPIGVDPPRAALKKKFTQPMMELEQEILDEVATDILETWYDCEDHVLSDISLSVAINGIPADSEEAELENFVMKTSPGYPYFKNNRAEKLKGKHAYFEEAEDGSLQLKKGGMAAELHENLVEFTKNEVPELVVIECTKDELLPERKIKVGACRLFEIMPLHYNLFLRQKTCAFTQFLQHNRHRLPCQVGTNPYSREWGHMLNRLMRPKTNEAINCDYSGFDGLLNPQLIECIARMINRLYALSGESDVQQAQRYNMLMALVGRYAFVGQQVYKVNCGLPSGFALTVVVNSVFNEILIRYAYKKLAPAPERNRFGSTVCLLVYGDDNLISVSPSIASWFTGEAIRITLAEKKVKITDGSDKDAPTIEAKSFWELDFLKRKFLKLDNGIVQAPLDRSAIFSSLYWLTPDKSKFHESQKPSDFQGEVDVIEELLLNVNVALMELYLHNDVAEFQRVRGFYAQRLPLMVSQLRTWAFCEAFHSAQQTGMQKYDPAVVLDHMSGVDFKRFMHMSEQGNKAHFYTEMLGVSGPHYKPQEGDFIVSNQPLKPGVQGEYVPIVFGEGIGGLPTKKWVGDFGKPSQLKNSKGYLITGLLREQIEAGKRLIFMGPAPYVANNAALISFGSAHKMLIQKDALAHYRNVIPESTSGLEQYFDAPIPQASVGTFYFGDGETYTALCEYKDGKVLQYEGLPTAILNQAAKDRKVPCMVARQWKSKFTVRMACDSNMCPHHSATCANFELAFKQCWLSKCKCAGNNVSKWYGTKFS
Enzyme Length 2266
Uniprot Accession Number Q8B8X3
Absorption
Active Site ACT_SITE 1272; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1310; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1402; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity 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.-; 2.7.7.48
Enzyme Function FUNCTION: Picornain 3C-like protease is a thiol protease that cleaves the P1 and P2 polyproteins. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 781..788; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00551
Features Active site (3); Chain (5); Domain (3); Nucleotide binding (1); Topological domain (2); Transmembrane (1)
Keywords ATP-binding;Covalent protein-RNA linkage;Helicase;Host endoplasmic reticulum;Host membrane;Hydrolase;Membrane;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-binding;RNA-directed RNA polymerase;Thiol protease;Transferase;Transmembrane;Transmembrane helix;Viral RNA replication
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host endoplasmic reticulum lumen {ECO:0000250}.; SUBCELLULAR LOCATION: [Putative ATP-dependent helicase]: Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: Specific enzymatic cleavages by picornain 3C-like protease in vivo yield mature proteins. Picornain 3C-like protease is autocatalytically processed (By similarity). {ECO:0000250}.; PTM: VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 254,131
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda