| 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 |