Detail Information for IndEnz0002009103
IED ID IndEnz0002009103
Enzyme Type ID protease009103
Protein Name Non-structural polyprotein pORF1
Includes: Methyltransferase
EC 2.1.1.-
EC 2.7.7.-
; Putative papain-like cysteine protease
PLP
EC 3.4.22.-
; NTPase/helicase
EC 3.6.4.-
; RNA-directed RNA polymerase
RdRp
EC 2.7.7.48
Gene Name ORF1
Organism Avian hepatitis E virus (isolate Chicken/California/Meng) (AHEV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Kitrinoviricota Alsuviricetes Hepelivirales Hepeviridae Orthohepevirus Orthohepevirus B Avian hepatitis E virus (isolate Chicken/California/Meng) (AHEV)
Enzyme Sequence MDVSQFAESKGVKTALEAAALAAANTALRNARVVTPYLTQQQTKNLLELFRGAQLRFEPRDNWAHPVQRVVHDALEQYVRRAAGPNCLEVGAHPRSINRHQASHRCFLPPVGRDEQRWQVAPRRGLCNLIRRALLNGVKVAREFCQLGFGACSHQCEVGIALYSLHDMRPADVACAMARHNMRTMYVVLHLPEEAMLPPGSYSNKFYNTVNTADKCIITYADDSCAGYVHKREVLQDWITTTGVSGRHPMLIERVRAIGCHFVLLCTATQPCPMPYTPYPSSNTVYVRNVYGPALGAGLFTPKCCVDATFYPVPRRVWQRLMMFGTTLDDDAFCCSRLLTYLRGISTKVTVGNIVANEGWQPEEQQLTAVAIAAYLTVCHQRWVRTQGIARGVRRLQAEHAQQFWFKVWELFTNTGTVPGYSAGFYRQLATWISGGLTIDFERRVFDKRVKCGCCCVCERRPADPGCLCIDDFPDGANGLVKLKKWPIRAGTKSAVSKWAQVRVRADSTEDLIDLSVPKLLTLKELAAAAIRKQPSAPPSLHILDRRPVGDPRRPVNCAPPAVSAGPVPAPPGNPVIESVQGSGAGGPEVSESQPGLTPTREVTNMPLPPQRGQEEVLAVLPSGARVIVGNLLDVAADWLVNPANRDHQPGGGLCGMFHRRWPHLWPVCGEVQDLPTGPVIFQQGPPKVIHAPGPDYRIKPDPDGLRRVYAVVHQAHGTVASPLISAGIYRAPARESFEAWAATARDGDLLVVQRSMAQHIRDFVLNEGRHRPRELHVDRAMADMVNYGLATEPEPYNELVKGVEVAPMTVKYALIAGVPGSGKSSSVDHRGAVVITPTKTLAREWSARGATAVTPHVAASAAPEGRVIVDEAYAIPPHLLVASLRRARDVVMLGDPHQIPALDFDGRCLTSAVDLGLQPTSWRTVSHRCPWDVCIFLRTDYPTITTTSRVLRSVVFTGETIGQKIVFTQVAKQSNPGSITVHEAQGSTFDQTTIIATLDARGLIASSRAHAIVALTRHRERCSVIDVGGVLVEIGVTDAMFNNIEMQLVRPDAAAPAGVLRAPDDTVDGLLDIPPAHTDVAAVLTAEAIGHAPLELAAINPPGPVLEQGLLYMPARLDGRDEVVKLQLSDTVHCRLAAPTSRLAVINTLVGRYGKATKLPEVEYDLMDTIAQFWHHIGPINPSTLEYAEMCEAMLSKGQDGSLIVHLDLQDADCSRITFFQKDCAKFTLDDPVAHGKVGQGISAWPKTLCALFGPWFRAIEKHLVAGLPPGYYYGDLYTEADLHRSVLCAPAGHLVFENDFSEFDSTQNNVSLDLECELMRRFGMPDWMVALYHLVRSYWLLVAPKEALRGCWKKHSGEPGTLLWNTVWNMTVLHHVYEFDRPSVLCFKGDDSVVVCESVRARPEGVSLVADCGLKMKDKTGPCGAFSNLLIFPGAGVVCDLLRQWGRLTDKNWGPDIQRMQDLEQACKDFVARVVTQGKEMLTIQLVAGYYGVEVGMVEVVWGALKACAAARETLVTNRLPVLNLSKED
Enzyme Length 1531
Uniprot Accession Number Q6QLN1
Absorption
Active Site
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 2.1.1.-; 2.7.7.-; 3.4.22.-; 3.6.4.-; 2.7.7.48
Enzyme Function FUNCTION: Methyltransferase displays a cytoplasmic capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP. Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m(7)GTP or m(7)GDP. GMP, GpppG, and GpppA were poor substrates for the methyltransferase. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m(7)GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure. Cap analogs such as m(7)GTP, m(7)GDP, et(2)m(7)GMP, and m(2)et(7)GMP inhibit the methyltransferase reaction (By similarity). {ECO:0000250}.; FUNCTION: RNA-directed RNA polymerase plays an essential role in the virus replication. Binds to the 3'-end of the genomic RNA, probably to initiate replication (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.; FUNCTION: Helicase region exhibits NTPase and RNA unwinding activities. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 818..825; /note=ATP; /evidence=ECO:0000255
Features Chain (1); Domain (5); Nucleotide binding (1); Region (7)
Keywords ATP-binding;Helicase;Hydrolase;Methyltransferase;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-binding;RNA-directed RNA polymerase;Thiol protease;Transferase;Viral RNA replication
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: It is not yet clear whether the ORF1-encoded polyprotein contains multiple biochemical activities, or undergoes cis or trans- processing to release biochemically distinct peptides.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 168,040
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda