Detail Information for IndEnz0002013786
IED ID IndEnz0002013786
Enzyme Type ID protease013786
Protein Name RNA replication polyprotein
ORF1 protein

Cleaved into: Helicase
EC 3.6.4.13

Includes: Viral methyltransferase
EC 2.1.1.-
; Putative Fe
2+
2-oxoglutarate dioxygenase
EC 1.14.11.-
; Protease
EC 3.4.22.-
; RNA-directed RNA polymerase
EC 2.7.7.48
Gene Name ORF1
Organism Potato virus M (strain Russian) (PVM)
Taxonomic Lineage Viruses Riboviria Orthornavirae Kitrinoviricota Alsuviricetes Tymovirales Betaflexiviridae Quinvirinae Carlavirus Potato virus M Potato virus M (strain Russian) (PVM)
Enzyme Sequence MAVTYRTPMEDIVNCFEPATQAVIANSAATLYKNFEEQHCQYFNYYLSPLAKRKLSMAGIYLSPYSAVVHSHPVCKTLENYILYSVLPSYINSSFYFVGIKERKLQLLKSKCKNLDSVQVVNRYVTSADRMRYTNDFVPYGSYEHECLVHKGVGLDNEALRGLVGPLRRHKAKNLFFHDELHYWSSKVLIDFLDVMRPDKLLGTVVYPPELLFKPTRSLNEWCYTYDIVGDTLMFFPDGVQSEGYQQPLKGGYLLGARSLKLPDGTVYMVDVLCSKFPHHLISITKGEAAAPTHRAFGPFEAVASEALKATLSPDYPCAFPVSYEVVNKIYRYLRTLKKPDEQSAIAKLSQIIAEPSGREIDFVECFARLVIHNSSMCATIMPEQLKEFMGNWLGKMPSVLARRFSSVRAVCVNKFIRGLKPYSFTLRLNEITWWNIWENSYAWFFDTDAEVDVPEKLDSLFMGEGAGLVAHITSRPYVGTVPLADREWNALLCMDSQKLLHAMRRMFMRGAWGAHMCVISREFLLKYVEARLKSSCLIAKARRRGQHKEKLEAWEVLGLKSSDALFRAMTYLCNARLEPMFSESGLRFFLTRGRNNLYGLTNYTEGKRAVTGVQNLWSNVVHEVSTKRHKGMIRLEKARVTEQPRSEFASCVLEPEVWRDVEAALDIELGEVACACNARFVQGVVLSNQAGLNVREQVAGASVGLYTKDRSNLKWGNSELLSNGWGRSLSVWMEINSVSQKFDVAVRLSYSKETQMNVLLPSLDGIERGAGATVVNLRKCGAFIVRCARGWRLALAWMDHICLEVMANVAYGHECYMRSWGTMDVVVFLKRATVSEQVTFESAQEVGPIEGKSDSGAPGVGVNLDLGGVVGSEYPANGAERYKRVSGPGDGCCCWHSFAYLVGMHHMELKRLCTSHVFENAALNVELEQCKASGAFVTHAAILATALRLRAEIRVHNAGTGRVHRFAPKQKNMALDLWLESEHYEPQVLRNGCVIESVAQALGTRNADILAVVEERCCEEVVESVQAGLGLNLHHVEIVLQCFDIVGHCNLGDKEITLNAGGKMPFCFDISDEHMSFCGRRKDPICKLVSGALHGKMFAESALLDLENCGLKIDFEPNWNRAGMLADSMYQGATGVLGSALFNNKRNMREKFVRNVSLSLHAIVGTFGSGKSTLFKNLLKYGAGKSLDFVSPRRALAEDFKRTVGMNERGGRAKAGQENWRVTTLETFLARVEFLTEGQVVILDEMQLYPPGYFDLVVSMLKVDVRLFLVGDPAQSDYDSEKDRLVLGAMEENMSVVLGAREYNYKVRSHRFLNCNFIGRLPCEINKDDCTIDEPHIMRMHLENLLDVAEEYKSVVLVSSFDEKMVVCAHLPEAKVLTFGESTGLTFMHGTIYISAVSERTNERRWITALRRFRFNLCFVNCSGMDYQQLAGRYKGRVRSKFLCKTAIPDDLNSMLPGQALFKSEYPRLIGKDEGVREEKLAGDPWLKTMINLYQAPEVEIAEEPEVVMQEEWFRTHLPRDELESVRAQWVHKILAKEYREVRMGDMVSEQFTHDHTKQLGAKQLTNAAERFETIYPRHRASDTVTFLMAVKKRLSFSNPGKEKGNLFHAASYGKALLSEFLKRVPLKPNHNVRFMEEALWNFEEKKLSKSAATIENHSGRSCRDWPTDVAQIFSKSQLCTKFDNRFRVAKAAQSIVCFQHAVLCRFAPYMRYIEMKVHEVLPKNYYIHSGKGLEELDAWVKKGKFDRICTESDYEAFDASQDEFIMAFELELMKYLRLPSDLIEDYKFIKTSLGSKLGNFAIMRFSGEASTFLFNTLANMLFTFMRYNIRGDEFICFAGDDMCASRRLQPTKKFAHFLDKLKLKAKVQFVQFVNKPTFCGWHLCPDGIYKKPQLVLERMCIAKEMNNLSNCIDNYAIEVAYAYKLGEKAVNRMDEEEVAAFYNCVRIIVRNKHLIRSDVKQVFEVL
Enzyme Length 1968
Uniprot Accession Number P17965
Absorption
Active Site ACT_SITE 994; /evidence=ECO:0000250|UniProtKB:Q65652; ACT_SITE 1075; /evidence=ECO:0000250|UniProtKB:Q65652
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}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
DNA Binding
EC Number 3.6.4.13; 2.1.1.-; 1.14.11.-; 3.4.22.-; 2.7.7.48
Enzyme Function FUNCTION: [RNA replication polyprotein]: RNA-directed RNA polymerase involved in viral RNA replication. {ECO:0000250|UniProtKB:Q65652, ECO:0000255|PROSITE-ProRule:PRU00539}.; FUNCTION: Protease: Thiol protease that cleaves the polyprotein. {ECO:0000250|UniProtKB:Q65652}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 1166..1173; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00990
Features Active site (2); Chain (2); Domain (6); Nucleotide binding (1); Site (1)
Keywords ATP-binding;Dioxygenase;Helicase;Hydrolase;Methyltransferase;Multifunctional enzyme;Nucleotide-binding;Nucleotidyltransferase;Oxidoreductase;Protease;RNA-directed RNA polymerase;Reference proteome;Thiol protease;Transferase;Viral RNA replication
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:Q65652}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 223,386
Kinetics
Metal Binding
Rhea ID RHEA:21248; RHEA:13065
Cross Reference Brenda