{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9YLR1","uniProtkbId":"POLN_HEVUS","entryAudit":{"firstPublicDate":"2008-05-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1999-05-01","entryVersion":102,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Hepatitis E virus genotype 3 (isolate Human/United States/US2)","commonName":"HEV-3","taxonId":509615,"lineage":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Hepelivirales","Hepeviridae","Orthohepevirinae","Paslahepevirus","Hepatitis E virus"]},"organismHosts":[{"scientificName":"Bandicota bengalensis","commonName":"lesser bandicoot rat","taxonId":69079},{"scientificName":"Callithrix","taxonId":9481},{"scientificName":"Cercopithecus hamlyni","commonName":"Owl-faced monkey","synonyms":["Hamlyn's monkey"],"taxonId":9536},{"scientificName":"Chlorocebus aethiops","commonName":"Green monkey","synonyms":["Cercopithecus aethiops"],"taxonId":9534},{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606},{"scientificName":"Macaca","commonName":"macaques","taxonId":9539},{"scientificName":"Mus musculus","commonName":"Mouse","taxonId":10090},{"scientificName":"Pan troglodytes","commonName":"Chimpanzee","taxonId":9598},{"scientificName":"Saimiri","commonName":"squirrel monkeys","taxonId":9520},{"scientificName":"Sus scrofa","commonName":"Pig","taxonId":9823}],"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Non-structural polyprotein pORF1"}},"includes":[{"recommendedName":{"fullName":{"value":"Methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q04610"}],"value":"2.1.1.-"},{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}],"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":"P33424"}],"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). Binds to the 3'-end of the genomic RNA to initiate viral replication (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = L-aspartyl-[protein] + ADP-D-ribose + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54428"},{"database":"Rhea","id":"RHEA-COMP:9867"},{"database":"Rhea","id":"RHEA-COMP:13832"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29961"},{"database":"ChEBI","id":"CHEBI:57967"},{"database":"ChEBI","id":"CHEBI:138102"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = L-glutamyl-[protein] + ADP-D-ribose + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58248"},{"database":"Rhea","id":"RHEA-COMP:10208"},{"database":"Rhea","id":"RHEA-COMP:15089"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29973"},{"database":"ChEBI","id":"CHEBI:57967"},{"database":"ChEBI","id":"CHEBI:142540"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21248"},{"database":"Rhea","id":"RHEA-COMP:14527"},{"database":"Rhea","id":"RHEA-COMP:17342"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:140395"}],"ecNumber":"2.7.7.48","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00539"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46948"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:87133"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46949"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"For methyltransferase activity."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"Putative protease: Inhibited by chymostatin"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}],"value":"The protease domain interacts with host EIF2AK4 (via C-terminus); this interaction inhibits dimerization of EIF2AK4 and prevents EIF2AK4-mediated phosphorylation of host EIF2A"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"Host cytoplasm","id":"SL-0381"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}],"value":"Host cytoplasm, host perinuclear region","id":"SL-0382"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}],"value":"The macro domain binds to ADP-ribose (By similarity). 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":1708,"modifier":"EXACT"}},"description":"Non-structural polyprotein pORF1","featureId":"PRO_0000334531"},{"type":"Domain","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"Alphavirus-like MT","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01079"}]},{"type":"Domain","location":{"start":{"value":790,"modifier":"EXACT"},"end":{"value":936,"modifier":"EXACT"}},"description":"Macro","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00490"}]},{"type":"Domain","location":{"start":{"value":949,"modifier":"EXACT"},"end":{"value":1097,"modifier":"EXACT"}},"description":"(+)RNA virus helicase ATP-binding"},{"type":"Domain","location":{"start":{"value":1098,"modifier":"EXACT"},"end":{"value":1231,"modifier":"EXACT"}},"description":"(+)RNA virus helicase C-terminal"},{"type":"Domain","location":{"start":{"value":1469,"modifier":"EXACT"},"end":{"value":1580,"modifier":"EXACT"}},"description":"RdRp catalytic","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00539"}]},{"type":"Region","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"Methyltransferase","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Region","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"Y-domain","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}]},{"type":"Region","location":{"start":{"value":442,"modifier":"EXACT"},"end":{"value":509,"modifier":"EXACT"}},"description":"Putative protease","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}]},{"type":"Region","location":{"start":{"value":510,"modifier":"EXACT"},"end":{"value":691,"modifier":"EXACT"}},"description":"Zinc-binding","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}]},{"type":"Region","location":{"start":{"value":714,"modifier":"EXACT"},"end":{"value":793,"modifier":"EXACT"}},"description":"Hinge","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Region","location":{"start":{"value":747,"modifier":"EXACT"},"end":{"value":792,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":975,"modifier":"EXACT"},"end":{"value":1219,"modifier":"EXACT"}},"description":"NTPase/helicase","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Region","location":{"start":{"value":1222,"modifier":"EXACT"},"end":{"value":1708,"modifier":"EXACT"}},"description":"RNA-directed RNA polymerase","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Compositional bias","location":{"start":{"value":772,"modifier":"EXACT"},"end":{"value":790,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":671,"modifier":"EXACT"},"end":{"value":671,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":673,"modifier":"EXACT"},"end":{"value":673,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":686,"modifier":"EXACT"},"end":{"value":686,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P33424"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":990,"modifier":"EXACT"},"end":{"value":997,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Disulfide bond","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":481,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81862"}]}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"id":"KW-1035","category":"Cellular component","name":"Host cytoplasm"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"id":"KW-0645","category":"Molecular function","name":"Protease"},{"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"id":"KW-0696","category":"Molecular function","name":"RNA-directed RNA polymerase"},{"id":"KW-0788","category":"Molecular function","name":"Thiol protease"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0693","category":"Biological process","name":"Viral RNA replication"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"10092008","citationType":"journal article","authors":["Erker J.C.","Desai S.M.","Schlauder G.G.","Dawson G.J.","Mushahwar I.K."],"citationCrossReferences":[{"database":"PubMed","id":"10092008"},{"database":"DOI","id":"10.1099/0022-1317-80-3-681"}],"title":"A hepatitis E virus variant from the United States: molecular characterization and transmission in cynomolgus macaques.","publicationDate":"1999","journal":"J. Gen. Virol.","firstPage":"681","lastPage":"690","volume":"80"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF060669","properties":[{"key":"ProteinId","value":"AAD15815.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"GO","id":"GO:0030430","properties":[{"key":"GoTerm","value":"C:host cell cytoplasm"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0044220","properties":[{"key":"GoTerm","value":"C:host cell perinuclear region of cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0008234","properties":[{"key":"GoTerm","value":"F:cysteine-type peptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0004386","properties":[{"key":"GoTerm","value":"F:helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0008174","properties":[{"key":"GoTerm","value":"F:mRNA methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0003968","properties":[{"key":"GoTerm","value":"F:RNA-directed RNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016556","properties":[{"key":"GoTerm","value":"P:mRNA modification"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0006396","properties":[{"key":"GoTerm","value":"P:RNA processing"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019082","properties":[{"key":"GoTerm","value":"P:viral protein processing"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0039694","properties":[{"key":"GoTerm","value":"P:viral RNA genome replication"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd23259","properties":[{"key":"EntryName","value":"Hepeviridae_RdRp"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd21557","properties":[{"key":"EntryName","value":"Macro_X_Nsp3-like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18809","properties":[{"key":"EntryName","value":"SF1_C_RecD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:001668","properties":[{"key":"EntryName","value":"Non-structural polyprotein pORF1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:001964","properties":[{"key":"EntryName","value":"Non-structural polyprotein pORF1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.220.10","properties":[{"key":"EntryName","value":"Leucine Aminopeptidase, subunit E, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR027351","properties":[{"key":"EntryName","value":"(+)RNA_virus_helicase_core_dom"}]},{"database":"InterPro","id":"IPR002588","properties":[{"key":"EntryName","value":"Alphavirus-like_MT_dom"}]},{"database":"InterPro","id":"IPR043502","properties":[{"key":"EntryName","value":"DNA/RNA_pol_sf"}]},{"database":"InterPro","id":"IPR008748","properties":[{"key":"EntryName","value":"Hepatitis-E_Cys-pept"}]},{"database":"InterPro","id":"IPR022202","properties":[{"key":"EntryName","value":"Hepatitis-E_hinge"}]},{"database":"InterPro","id":"IPR047307","properties":[{"key":"EntryName","value":"Hepeviridae_RdRp"}]},{"database":"InterPro","id":"IPR002589","properties":[{"key":"EntryName","value":"Macro_dom"}]},{"database":"InterPro","id":"IPR043472","properties":[{"key":"EntryName","value":"Macro_dom-like"}]},{"database":"InterPro","id":"IPR044371","properties":[{"key":"EntryName","value":"Macro_X_NSP3-like"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR001788","properties":[{"key":"EntryName","value":"RNA-dep_RNA_pol_alsuvir"}]},{"database":"InterPro","id":"IPR007094","properties":[{"key":"EntryName","value":"RNA-dir_pol_PSvirus"}]},{"database":"Pfam","id":"PF12526","properties":[{"key":"EntryName","value":"DUF3729"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01661","properties":[{"key":"EntryName","value":"Macro"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05417","properties":[{"key":"EntryName","value":"Peptidase_C41"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00978","properties":[{"key":"EntryName","value":"RdRP_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01443","properties":[{"key":"EntryName","value":"Viral_helicase1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01660","properties":[{"key":"EntryName","value":"Vmethyltransf"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00506","properties":[{"key":"EntryName","value":"A1pp"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56672","properties":[{"key":"EntryName","value":"DNA/RNA polymerases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52949","properties":[{"key":"EntryName","value":"Macro domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51743","properties":[{"key":"EntryName","value":"ALPHAVIRUS_MT"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51154","properties":[{"key":"EntryName","value":"MACRO"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51657","properties":[{"key":"EntryName","value":"PSRV_HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50507","properties":[{"key":"EntryName","value":"RDRP_SSRNA_POS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEAHQFIKAPGITTAIEQAALAAANSALANAVVVRPFLSRVQTEILINLMQPRQLVFRPEVLWNHPIQRVIHNELEQYCRARAGRCLEVGAHPRSINDNPNVLHRCFLRPVGRDVQRWYSAPTRGPAANCRRSALRGLPPVDRTYCFDGFSRCAFAAETGVALYSLHDLWPADVAEAMARHGMTRLYAALHLPPEVLLPPGTYHTTSYLLIHDGNRAVVTYEGDTSAGYNHDVSILRAWIRTTKIVGDHPLVIERVRAIGCHFVLLLTAAPEPSPMPYVPYPRSTEVYVRSIFGPGGSPSLFPSACSTKSTFHAVPVHIWDXLMLFGATLXDQAFCCSRLMTYLRGISYKVTVGALVANEGWNASEDALTAVITAAYLTICHQRYLRTQAISKGMRRLEVEHAQKFITRLYSWLFEKSGRDYIPGRQLQFYAQCRRWLSAGFHLXPRXLVFDESVPCRCRTFLKKVAGKFCCFMRWLGQECTCFLEPAEGLVGDQGHDNEAYEGSEVDPAEPAHLDVSGTYAVHGHQLEALYRALNVPHDIAARASRLTATVELVASPDRLECRTVLGNKTFRTTVVDGAHLEANGPEEYVLSFDASRQSMGAGSHSLTYELTPAGLQVKISSNGLDCTATFPPGGAPSAAPGEVAAFCSALYRYNRFTQRHSLTGGLWLHPEGLLGIFPPFSPGHIWESANPFCGEGTLYTRTWSTSGFSSDFSPPEAAAPASAAAPGLPYPTPPVSDIWVLPPPSEESHVDAASVPSVPEPAGLTSPIVLTPPPPPPPVRKPATSPPPRTRRLLYTYPDGAKVYAGSLXESDCDWLVNASNPGHRPGGGLCHAFYQRFPEAFYSTEFIMREGLAAYTLTPRPIIHAVAPDYRVEQNPKRLEAAYRETCSRRGTAAYPLLGSGIYQVPVSLSFDAWERNHRPGDELYLTEPAAAWFEANKPAQPALTITEDTARTANLALEIDAATEVGRACAGCTISPGIVHYQFTAGVPGSGKSRSIQQGDVDVVVVPTRELRNSWRRRGFAAFTPHTAARVTIGRRVVIDEAPSLPPHLLLLHMQRASSVHLLGDPNQIPAIDFEHAGLVPAIRPELAPTSWWHVTHRCPADVCELIRGAYPKIQTTSRVLRSLFWNEPAIGQKLVFTQAAKAANPGAITVHEAQGATFTETTIIATADARGLIQSSRAHAIVALTRHTEKCVILDAPGLLREVGISDVIVNNFFLAGGEVGHHRPSVIPRGNPDQNLGTLQAFPPSCQISAYHQLAEELGHRPAPVAAVLPPCPELEQGLLYMPQELTVSDSVLVFELTDIVHCRMAAPSQRKAVLSTLVGRYGRRTKLYEAAHSDVRESLARFIPTIGPVRATTCELYELVEAMVEKGQDGSAVLELDLCNRDVSRITFFQKDCNKFTTGETIAHGKVGQGISAWSKTFCALFGPWFRAIEKEILALLPPNIFYGDAYEESVFAAAVSGAGSCMVFENDFSEFDSTQNNFSLGLECVVMEECGMPQWLIRLYHLVRSAWILQAPKESLKGFWKKHSGEPGTLLWNTVWNMAIIAHCYEFRDFRVAAFKGDDSVVLCSDYRQXRNAAALIAGCGLKLKVDYRPIGLYAGVVVAPGLGTLPDVVRFAGRLSEKNWGPGPERAEQLRLAVCDFLRGLTNVAQVCVDVVSRVYGVSPGLVHNLIGMLQTIADGKAHFTENIKPVLDLTNSIIQRVE","length":1708,"molWeight":187269,"crc64":"BE0DF5EBEEDAB547","md5":"B8F1FF313B8EBBAFC2E00268C36C4F35"},"extraAttributes":{"countByCommentType":{"FUNCTION":6,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":2,"PTM":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":5,"Region":8,"Compositional bias":1,"Binding site":4,"Disulfide bond":1},"uniParcId":"UPI00000F4820"}}