{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q04610","uniProtkbId":"POLN_HEVMY","entryAudit":{"firstPublicDate":"1993-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1993-10-01","entryVersion":117,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Hepatitis E virus genotype 1 (isolate Human/Myanmar/HEVNE8L)","commonName":"HEV-1","taxonId":31769,"lineage":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Hepelivirales","Hepeviridae","Orthohepevirinae","Paslahepevirus","Hepatitis E virus"]},"organismHosts":[{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606}],"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Non-structural polyprotein pORF1"}},"includes":[{"recommendedName":{"fullName":{"value":"Methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11413290"}],"value":"2.1.1.-"},{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"2.7.7.-"}]}},{"recommendedName":{"fullName":{"value":"Macro domain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}],"value":"3.2.2.-"}]}},{"recommendedName":{"fullName":{"value":"Putative protease"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"3.4.-.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}],"value":"Putative papain-like cysteine protease"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}],"value":"PCP"}]}]},{"recommendedName":{"fullName":{"value":"NTPase/helicase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"3.6.4.-"}]}},{"recommendedName":{"fullName":{"value":"RNA-directed RNA polymerase"},"shortNames":[{"value":"RdRp"}],"ecNumbers":[{"value":"2.7.7.48"}]}}]},"genes":[{"orfNames":[{"value":"ORF1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"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. GDP is a better substrate than GTP. 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"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"},{"evidenceCode":"ECO:0000305"}],"value":"Macro domain: Contains an ADP-ribose hydrolase activity that binds ADP-ribose and catalyzes the removal of mono-ADP-ribose (de-MARylation) and poly-ADP-ribose (de-PARylation), usually bound to a glutamate or aspartate residue (By similarity). De-MARylation reaction is 16-folder quicker than de-PARylation. ADP-ribose hydrolase activity allows the virus to interfere with the host immune defenses involving poly-ADP-ribose polymerases (PARPs) (Probable)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"Y-domain: Indispensable for virus replication"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"Putative protease: The putative protease domain although necessary for replication of the virus may not be a protease but rather a structural Zn(2+)-binding domain. Inhibits induction of IFN-beta by MDA5 and RIG-I pathways and down-regulates the expression of MDA5"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P29324"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"NTPase/helicase: Multi-functional protein that exhibits NTPase and RNA unwinding activities (By similarity). Hydrolyzes all NTPs efficiently and unwinds RNA duplexes containing 5' overhangs (By similarity). Possesses a sequence independent RNA-5'-triphosphatase (RTPase) activity suggestive of its role in forming viral cap structure. Also participates in viral genome replication, RNA translocation and genome packaging/unpackaging (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9WC28"}],"value":"RNA-directed RNA polymerase: Plays an essential role in the virus replication (By similarity). 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The helicase activity stimulates the de-PARylation (By similarity)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"Contains a methyltransferase domain, a Y-domain, a putative protease region, a zinc-binding region with similarity to calycins, a proline-rich disordered hypervariable region (HVR), a macro domain (also called X-domain), a helicase domain and an RNA-dependent RNA polymerase domain (By similarity). Since the boundaries and the activity of the putative protease are not clearly defined, the zinc-binding region might be part of the putative protease (By similarity)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"ORF1 polyprotein does not seem to be processed into distinct enzymatic domains by a viral protease belonging to ORF1, but could be processed by a host serine protease like thrombin"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the hepevirus non-structural polyprotein family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1693,"modifier":"EXACT"}},"description":"Non-structural polyprotein pORF1","featureId":"PRO_0000100134"},{"type":"Domain","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"Alphavirus-like 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