Detail Information for IndEnz0002011229
IED ID IndEnz0002011229
Enzyme Type ID protease011229
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 Hepatitis E virus genotype 1 (isolate Human/India/Hyderabad) (HEV-1)
Taxonomic Lineage Viruses Riboviria Orthornavirae Kitrinoviricota Alsuviricetes Hepelivirales Hepeviridae Orthohepevirus Hepatitis E virus (HEV) Hepatitis E virus type 1 Hepatitis E virus genotype 1 (isolate Human/India/Hyderabad) (HEV-1)
Enzyme Sequence MEAHQFLKAPGITTAVEQAALATANSALANAVVVRPFLSHQQIEILINLMQPRQLVFRPEVFWNQPIQRVIHNELELYCRARSGRCLEIGAHPRSINDNPNVVHRCFLRPVGRDVQRWYTAPTRGPAANCRRSALRGLPAADRTYCFDGFSGCSCPAETGIALYSLHDMSPSDVAEAMFRHGMTRLYAALHLPPEVLLPPGTYRTASYLLIHDGRRVVVTYEGDTSAGYNHDVSNLRSWIRTTKVTGDHPLVIERVRAIGCHFVLLLTAAPEPSPMPYVPYPRSTEVYVRSIFGPGGTPSLFPTSCSTKSTFHAVPAHIWDRLMLFGATLDDQAFCCSRLMTYLRGISYKVTVGTLVANEGRNASEDALTAVITAAYLTICHQRYLRTQAISKGIRRLEREHDQKFITRLYSWLFEKSGRDYIPGRQLEFYAQCRRWLSAGFHLDPRVLVFDESAPCHCRTVIRKALSKFCCFMKWLGQECTCFLQPAEGVVGDQGHDNESYEGSDVDPAESAISDISGSYVVPGTALQPLYQALDLPDEIVARACRLTATVKVSQVDGRIDCETLLGNKTFRTSFVDGAVLETNGPERHNLSFDASQSTMAAGPFSLTYAASAAGLEVRYVGAGLDHRAIFAPGVSPRSNPGEVTAFCSALYRFNREAQRHSLTGNLWFHPEGLIGLFAPFSPGHVWESAKPFCGESTLYTRTWSEVDAVSSPTRPDLGFMSEPPIPSRAATPTLAAPLPPLAPDPSPPSSAPALDEPASAATSGVPAITHQTARHRRLLFTYPDGSKVFAGSLFESTCTWLVNASNVDHCPGGGLCHAFYQRYPASFDAACFVMRDGAAAYTLTPRPIIHRVAPDYRLEHNPKRLEAAYRETCSRLGTAAYPLLGTGIYQVPIGPSFDAWERNHRPGDELYLPELAARWFEANRPTRPTLTITEDAARTANLAIELDSATDVGRACAGCRVTPGVVQYQFTAGVPGSGKSRSITRADVDVVVVPTRELRNAWRRRGFAAFTPHTAARVTDGRRVVIDEAPSLPPHLLLLHMQRAATVHLLGDPNQIPAIDFEHPGLVPAIRPDLAPTSWWHVTHRCPADVCELIRGAYPMIQTTSRVLRSLFWGEPAVGQKLVFTQAAKPANPGSVTVHDSQGATYTYTTIIATADARGLIQSSRAHAIVALTRHTEKWVIIDAPGLLREVGISDAIVNNFFLAGGEIGHQRPSVIPRGNPDANVDTLAAFPPSCQISAFHQLAEELGHRPAPVAAVLPPCPELEQGLLYLPQELTTCDSVVTFELTDIVHCRMAAPSQRKAVVSTLVGRYGRRTKLYNASHSDVRDSLARFIPAIGPVQVTTCELYELVEAMVEKGQDGSAVLELDLCNRDVSRITFFQKDCNKFTTGETIAHGKVGQGISAWSKTFCALFGPWFRAIEKAILALLPQGVFYGDAFDDTVFSAAVAAAKASMVFENDFSEFDSTQNNFSLGLECAIMEECGMPQGLIRLYHLIRSAWILQAPKESLLGFWKKHSGEPGTLLWNTVWNMAVITHCYDFRDLQVAAFKGDDSIVLCSEYRQSPGAAVLIAGCGLKLKVDFRPMRLYAGVVVAPGLGALPDVVRFAGRLTEKNWGPGPERADELRIAVSDFLRKLTNVAQMCVDVVSRVYGVSPGLVHNLIGMLQAVADGKAHFTESVKPVLDLTNSILCRVE
Enzyme Length 1693
Uniprot Accession Number Q9WC28
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:0000250|UniProtKB:Q81862};
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 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. 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. {ECO:0000250|UniProtKB:Q81862}.; FUNCTION: Papain-like cysteine protease: May participate in the processing of polyprotein pORF1 together with cellular proteases and the cleavage of capsid protein ORF2. {ECO:0000250|UniProtKB:Q81862}.; FUNCTION: NTPase/helicase: Multi-functional protein that exhibits NTPase and RNA unwinding activities. Hydrolyzes all NTPs efficiently and unwinds RNA duplexes containing 5' overhangs. Possesses a sequence independent RNA-5'-triphosphatase (RTPase) activity suggestive of its role in forming viral cap structure (By similarity). Participates also in viral genome replication, RNA translocation and genome packaging/unpackaging (By similarity). {ECO:0000250|UniProtKB:P29324, ECO:0000250|UniProtKB:Q81862}.; FUNCTION: RNA-directed RNA polymerase: Plays an essential role in the virus replication. Binds to the 3'-end of the genomic RNA to initiate viral replication. {ECO:0000250|UniProtKB:Q81862, ECO:0000269|PubMed:11259193}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 975..982; /note=ATP; /evidence=ECO:0000255
Features Chain (1); Compositional bias (1); Domain (5); Nucleotide binding (1); Region (8); Sequence conflict (1)
Keywords ATP-binding;Helicase;Host cytoplasm;Hydrolase;Methyltransferase;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-binding;RNA-directed RNA polymerase;Thiol protease;Transferase;Viral RNA replication
Interact With Itself; Q68985; O90299
Induction
Subcellular Location SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:Q81862}.
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. No processing has been observed in mammalian expression systems. However, the baculovirus expressed polyprotein is processed into smaller protein, probably by a cysteine protease.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 26463011;
Motif
Gene Encoded By
Mass 185,580
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda