| IED ID | IndEnz0002011918 |
| Enzyme Type ID | protease011918 |
| 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 3 (isolate Human/United States/US2) (HEV-3) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Kitrinoviricota Alsuviricetes Hepelivirales Hepeviridae Orthohepevirus Hepatitis E virus (HEV) Hepatitis E virus type 3 Hepatitis E virus genotype 3 (isolate Human/United States/US2) (HEV-3) |
| Enzyme Sequence | MEAHQFIKAPGITTAIEQAALAAANSALANAVVVRPFLSRVQTEILINLMQPRQLVFRPEVLWNHPIQRVIHNELEQYCRARAGRCLEVGAHPRSINDNPNVLHRCFLRPVGRDVQRWYSAPTRGPAANCRRSALRGLPPVDRTYCFDGFSRCAFAAETGVALYSLHDLWPADVAEAMARHGMTRLYAALHLPPEVLLPPGTYHTTSYLLIHDGNRAVVTYEGDTSAGYNHDVSILRAWIRTTKIVGDHPLVIERVRAIGCHFVLLLTAAPEPSPMPYVPYPRSTEVYVRSIFGPGGSPSLFPSACSTKSTFHAVPVHIWDXLMLFGATLXDQAFCCSRLMTYLRGISYKVTVGALVANEGWNASEDALTAVITAAYLTICHQRYLRTQAISKGMRRLEVEHAQKFITRLYSWLFEKSGRDYIPGRQLQFYAQCRRWLSAGFHLXPRXLVFDESVPCRCRTFLKKVAGKFCCFMRWLGQECTCFLEPAEGLVGDQGHDNEAYEGSEVDPAEPAHLDVSGTYAVHGHQLEALYRALNVPHDIAARASRLTATVELVASPDRLECRTVLGNKTFRTTVVDGAHLEANGPEEYVLSFDASRQSMGAGSHSLTYELTPAGLQVKISSNGLDCTATFPPGGAPSAAPGEVAAFCSALYRYNRFTQRHSLTGGLWLHPEGLLGIFPPFSPGHIWESANPFCGEGTLYTRTWSTSGFSSDFSPPEAAAPASAAAPGLPYPTPPVSDIWVLPPPSEESHVDAASVPSVPEPAGLTSPIVLTPPPPPPPVRKPATSPPPRTRRLLYTYPDGAKVYAGSLXESDCDWLVNASNPGHRPGGGLCHAFYQRFPEAFYSTEFIMREGLAAYTLTPRPIIHAVAPDYRVEQNPKRLEAAYRETCSRRGTAAYPLLGSGIYQVPVSLSFDAWERNHRPGDELYLTEPAAAWFEANKPAQPALTITEDTARTANLALEIDAATEVGRACAGCTISPGIVHYQFTAGVPGSGKSRSIQQGDVDVVVVPTRELRNSWRRRGFAAFTPHTAARVTIGRRVVIDEAPSLPPHLLLLHMQRASSVHLLGDPNQIPAIDFEHAGLVPAIRPELAPTSWWHVTHRCPADVCELIRGAYPKIQTTSRVLRSLFWNEPAIGQKLVFTQAAKAANPGAITVHEAQGATFTETTIIATADARGLIQSSRAHAIVALTRHTEKCVILDAPGLLREVGISDVIVNNFFLAGGEVGHHRPSVIPRGNPDQNLGTLQAFPPSCQISAYHQLAEELGHRPAPVAAVLPPCPELEQGLLYMPQELTVSDSVLVFELTDIVHCRMAAPSQRKAVLSTLVGRYGRRTKLYEAAHSDVRESLARFIPTIGPVRATTCELYELVEAMVEKGQDGSAVLELDLCNRDVSRITFFQKDCNKFTTGETIAHGKVGQGISAWSKTFCALFGPWFRAIEKEILALLPPNIFYGDAYEESVFAAAVSGAGSCMVFENDFSEFDSTQNNFSLGLECVVMEECGMPQWLIRLYHLVRSAWILQAPKESLKGFWKKHSGEPGTLLWNTVWNMAIIAHCYEFRDFRVAAFKGDDSVVLCSDYRQXRNAAALIAGCGLKLKVDYRPIGLYAGVVVAPGLGTLPDVVRFAGRLSEKNWGPGPERAEQLRLAVCDFLRGLTNVAQVCVDVVSRVYGVSPGLVHNLIGMLQTIADGKAHFTENIKPVLDLTNSIIQRVE |
| Enzyme Length | 1708 |
| Uniprot Accession Number | Q9YLR1 |
| 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}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 990..997; /note=ATP; /evidence=ECO:0000255 |
| Features | Chain (1); Compositional bias (1); Domain (5); Nucleotide binding (1); Region (9) |
| 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 | |
| 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 | - |
| Motif | |
| Gene Encoded By | |
| Mass | 187,269 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21248 |
| Cross Reference Brenda |