Detail Information for IndEnz0002000866
IED ID IndEnz0002000866
Enzyme Type ID protease000866
Protein Name RNA1 polyprotein
P1

Cleaved into: Protein X1; Protein X2; Putative ATP-dependent helicase
EC 3.6.4.-
Membrane-binding protein
NTP-binding protein
NTB
; Viral genome-linked protein
VPg
; Picornain 3C-like protease
3C-like protease
PRO
EC 3.4.22.-
; RNA-directed RNA polymerase
POL
EC 2.7.7.48
Gene Name
Organism Blackcurrant reversion association virus (BRAV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Secoviridae Comovirinae Nepovirus Blackcurrant reversion association virus (BRAV)
Enzyme Sequence MVKIGSDTLAPKQLVLENKYIAACLSKPANFALSFLAQGASLKPSVVARAAINGVIACDTTTFQLLAMDGTPLSFAAAAVVVRQFQLAHNRFVKIGLRQFYKECTRRCNAFNLQKAARQSRERRAACKRILASLDADLPCSRSSRRAIVTAHYAGVATAARKSALFRQMRADKRASRALAAAMQPLVLAPPTCARIPYVCPLSSSVEESVSRRSLERCSKRVPREHASPRVASEMQPFADRPRLFSRVLLLPLSEITRAFFSRVFVPGSAMYDCATDLAHVVLDWWSITPMAHYLAMLDNFLGTPTEESVRQASTNLLEEVEAMRALCRDHRANGVFAWVTETAGTIGSTLKTAAVAPFHGAGVALKAVLTPCASATLAWGEKFFQTLKSKFFEFLKPYIQHAIYASAEIEKYWAFIHGWATKMWNNVGVELQALGDAAWWAIGITMVCGIVTLVEKLLVYLGALNAGGILCSLMLTGLLGAAGLLATGKFAEASSTLVGAMRSLIFTLFGSWKPTEASDGLTCNANALDFPLKVLETVGTGLISAPLGTLQYIGKYGQAMDQIRKGKDAIKEFVGFCMDRVADAWDYMTGRKDSFLREIASAAKVDIVYWIKQTQSVLLQAQTIAVTDIVLLDTVTHLLYKGQILQLTLAKASRTTSLDYARIVSTLIGELTKIRATCARAGSFDGRRPEPFWCYIYGKSHCGKSLFMEDVSRALLKENGHAPNDIYAKNARDSFWSGYLQHACVQVDDLSACVTRPSLESEFLQLVGSKMYSLNMAAVEDKGMSFNSSIIVTTANVYTAPTSAEITDKDAYGNRRNVVVQCRAAPDVEFDPRNPSASCEARLVHRTDESPLGNGQWRNCSAVLEDIIHHAAIHRNKENLLMENYRERSDTQHPVFVGAKSFIHRLAKEKNFAHIVCDDVLYYHDSYIDSTRVSEGTINIGMEDACIQSVVQWSELVGGVKDLGLLYAFVHAFTEGPCHVDSVEALNSEATSCQRDFFQSLSLLERIYMRLVQKQLDRIRANPDFLFSVDIKTRILQSFRHGYDEMITHGGKVLAIFAALLLVLLLYSSFFALYQTFVAGTSSALVSAGMITQLSANAGSVCTSASNPSGAASYVSSNIPIHHRWRSNYSERSYALNSNLEDKYLLDLLVWLQIPGDSIISCIRFKGRSLLLTKHQALAIPEGARVYCNYYGRGRAVQTIPLSWSYKKVREFADTEAVLFLDAQLSTMPAGREHYFNVPVERLPSVFDMNGVVMKQKRYMTDSDDSLAAFTPNQPVVNTWENSRAKLNCERQGINTFAYGGNYRNELPRSISSNCNTSPEDCGAIMTMIFEGRRVVVGMHVASGKNPQGRYMSTACLLPDYHEDLSLNSMLQYTPYDGICKEGYRQIGNIENIGARPYTSGKTAFVAVPQHLLYSPPVLQEKLPGSAQPVTIQVEVKQPAILSKDDPRIPEGTSYDPLIDGMAKFSHPMAVLDENVCNEVAQDIVESWHDCFQDLQDVSDEIAINGSTEMDYEPFNLQSSEGYPYVTQRKPGESGKIRFFEMDPYTGLKSLIPNTLPAMRYEALQRDCFTSVPEMVCIETPKDECLPLRKICIKPKTRLFSILPLEFNLLLRKKFLHFSSSLQMHRDTLPTQVGVNPYSREWGELLQRLRAQSSVAINCDYASFDGLLTGQILEKIGTMINKMYIGSEASKIQRLNLLMSIVNRKSICGARVYEVRAGIPSGCALTVLLNSIFNEFLIRFVWRTTIIGVPRERFSQYVTLLIYGDDNLIAVHPDYLPHFNGEIIRTRLADVNVIITDGSDKTAEKIEEKPLVQLDFLKRRFRKLNDGTVYAPLDLASVYTSLQNVTMGAGSIHIALQNNVHNALLELYLHGNETWFNHLRDFYRKSHAWVNLPSWREAFAFHQGQISGVTPWTPYQMFDVPVDGGRLRAMMANQGEAAFSTHLGREIYICGPKWCVSDPEHQFVVSTTPLRSADRGSGIHRAIEYPCNGVGRLPSQDWVTKFKSSAHRVTAEIRKAHASGKAIYFRDDPPYVANWCAAIGFAQGLGYDYKSMINLYHDVSVPGSDALYFYFEQRARRALPEPYIPPHLRTRVR
Enzyme Length 2094
Uniprot Accession Number Q8V5E0
Absorption
Active Site ACT_SITE 1176; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1217; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1323; /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 at Gln-|-Gly or Gln-|-Ser sites in the P1 and P2 polyproteins. {ECO:0000250}.; FUNCTION: The VPg-NTB polyprotein may act as a membrane-anchor for the replication complex. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 699..706; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00551
Features Active site (3); Chain (6); Domain (3); Glycosylation (1); Nucleotide binding (1); Site (1); Topological domain (2); Transmembrane (1)
Keywords ATP-binding;Covalent protein-RNA linkage;Glycoprotein;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}. Note=The NTB-VPg polyprotein is associated with endoplasmic-derived membranes that are active in viral replication. {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. NTB exists as NTB-VPg polyprotein as well as NTB mature protein (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 233,298
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda