{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P19712","uniProtkbId":"POLG_CSFAT","entryAudit":{"firstPublicDate":"1991-02-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-07-11","entryVersion":195,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Classical swine fever virus (strain Alfort/Tuebingen)","commonName":"CSFV","synonyms":["Hog cholera virus"],"taxonId":358805,"lineage":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Orthopestivirus","Orthopestivirus suis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Genome polyprotein"}},"contains":[{"recommendedName":{"fullName":{"value":"N-terminal protease"},"shortNames":[{"value":"N-pro"}],"ecNumbers":[{"value":"3.4.22.-"}]},"alternativeNames":[{"fullName":{"value":"Autoprotease p20"}}]},{"recommendedName":{"fullName":{"value":"Capsid protein C"}},"alternativeNames":[{"fullName":{"value":"Core protein"}}]},{"recommendedName":{"fullName":{"value":"E(rns) glycoprotein"}},"alternativeNames":[{"fullName":{"value":"gp44/48"}}]},{"recommendedName":{"fullName":{"value":"Envelope glycoprotein E1"}},"alternativeNames":[{"fullName":{"value":"gp33"}}]},{"recommendedName":{"fullName":{"value":"Envelope glycoprotein E2"}},"alternativeNames":[{"fullName":{"value":"gp55"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"22496228"}],"value":"Viroporin p7"}}},{"recommendedName":{"fullName":{"value":"Non-structural protein 2-3"},"shortNames":[{"value":"NS2-3"}]}},{"recommendedName":{"fullName":{"value":"Cysteine protease NS2"},"ecNumbers":[{"value":"3.4.22.-"}]},"alternativeNames":[{"fullName":{"value":"Non-structural protein 2"}}]},{"recommendedName":{"fullName":{"value":"Serine protease NS3"},"ecNumbers":[{"value":"3.4.21.113"},{"value":"3.6.1.15"},{"value":"3.6.4.13"}]},"alternativeNames":[{"fullName":{"value":"Non-structural protein 3"}}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 4A"},"shortNames":[{"value":"NS4A"}]}},{"recommendedName":{"fullName":{"value":"Non-structural protein 4B"},"shortNames":[{"value":"NS4B"}]}},{"recommendedName":{"fullName":{"value":"Non-structural protein 5A"},"shortNames":[{"value":"NS5A"}]}},{"recommendedName":{"fullName":{"value":"RNA-directed RNA polymerase"},"ecNumbers":[{"value":"2.7.7.48"}]},"alternativeNames":[{"fullName":{"value":"NS5B"}}]}]},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17215286"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19540847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24606708"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27334592"}],"value":"Leader cysteine autoprotease that cleaves itself from the nascent polyprotein during translation of the viral mRNA. Once released, plays a role in the inhibition of host innate immune response by interacting with host IRF3 and inducing its proteasomal degradation"}],"commentType":"FUNCTION","molecule":"N-terminal protease"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28290554"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9617770"}],"value":"Packages viral RNA to form a viral nucleocapsid and thereby protects viral RNA. Also plays a role in transcription regulation. Protects the incoming virus against IFN-induced effectors"}],"commentType":"FUNCTION","molecule":"Capsid protein C"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P21530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15113930"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19264773"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19767841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25694590"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29235980"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8356450"}],"value":"Plays a role in viral entry. Interacts with host RPSA that acts as a cellular attachment receptor for the virus. Also possesses intrinsic ribonuclease (RNase) activity that can inhibit the production of type I interferon and assist in the development of persistent infections. Cleaves preferentially NpU bonds (PubMed:15113930). Binds to heparan sulfate on the host cells for entry (By similarity)"}],"commentType":"FUNCTION","molecule":"E(rns) glycoprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15527858"}],"value":"Plays a role in cell attachment and subsequent fusion of viral and cellular membranes. Therefore, mediates together with envelope glycoprotein E2 the viral entry"}],"commentType":"FUNCTION","molecule":"Envelope glycoprotein E1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P21530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15527858"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684175"}],"value":"Plays a role in cell attachment and subsequent fusion of viral and cellular membranes (PubMed:15527858). Therefore, mediates together with envelope glycoprotein E1 the viral entry (PubMed:15527858). Binds to host ADAM17 receptor for entry (PubMed:33684175). Binds to host ANXA2 for entry (By similarity). Binds to host MERTK for entry (By similarity)"}],"commentType":"FUNCTION","molecule":"Envelope glycoprotein E2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22496228"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24189547"}],"value":"Plays an essential role in the virus replication cycle by acting as a viroporin. Forms ion conductive pores, which alters the cell permeability allowing the transport of ions and other small molecules"}],"commentType":"FUNCTION","molecule":"Viroporin p7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17482232"}],"value":"Autoprotease that associates with the host chaperone JIV and cleaves the NS2-3 protein between NS2 and NS3. Also plays a role in the formation of infectious particles"}],"commentType":"FUNCTION","molecule":"Non-structural protein 2-3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10438869"}],"value":"Plays a role in the regulation of viral RNA replication"}],"commentType":"FUNCTION","molecule":"Cysteine protease NS2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19185595"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28751780"}],"value":"Multifunctional protein that contains an N-terminal protease and a C-terminal helicase, playing essential roles in viral polyprotein processing and viral genome replication. The chymotrypsin-like serine protease activity utilizes NS4A as an essential cofactor and catalyzes the cleavage of the polyprotein leading to the release of NS4A, NS4B, NS5A, and NS5B. Plays a role in the inhibition of host NF-kappa-B activation by interacting with and inhibiting host TRAF6. Interacts with NS5B to enhance RNA-dependent RNA polymerase activity"}],"commentType":"FUNCTION","molecule":"Serine protease NS3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17482232"}],"value":"Acts as a cofactor for the NS3 protease activity"}],"commentType":"FUNCTION","molecule":"Non-structural protein 4A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O56125"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Q6P4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29844394"}],"value":"Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). Antagonizes host cell apoptosis by interacting with host ferritin heavy chain. The ORF4 protein physically binds host FTH1/FHC, resulting in the reduction of FTH1 protein levels in host cells. Reduction of FTH1 concentration further inhibits the accumulation of reactive oxygen in host cells, leading to reduced apoptosis (By similarity) (PubMed:29844394)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 4B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22261205"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22795973"}],"value":"Regulates viral RNA replication by interacting with the 3'-untranslated region of viral RNA in a dose-dependent manner. At small concentrations promotes viral synthesis by interacting with the polymerase NS5B while at large concentrations, inhibits replication"}],"commentType":"FUNCTION","molecule":"Non-structural protein 5A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00539"}],"value":"Replicates the viral (+) and (-) genome"}],"commentType":"FUNCTION","molecule":"RNA-directed RNA polymerase"},{"commentType":"CATALYTIC ACTIVITY","molecule":"Serine protease NS3","reaction":{"name":"Leu is conserved at position P1 for all four cleavage sites. Alanine is found at position P1' of the NS4A-NS4B cleavage site, whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites.","ecNumber":"3.4.21.113"}},{"commentType":"CATALYTIC ACTIVITY","molecule":"RNA-directed RNA polymerase","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","molecule":"Serine protease NS3","reaction":{"name":"a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23680"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57930"},{"database":"ChEBI","id":"CHEBI:61557"}],"ecNumber":"3.6.1.15"}},{"commentType":"CATALYTIC ACTIVITY","molecule":"Serine protease NS3","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"3.6.4.13"}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":84.0,"unit":"uM","substrate":"Sub-UpU","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15113930"}]},{"constant":103.0,"unit":"uM","substrate":"Sub-GpU","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15113930"}]},{"constant":220.0,"unit":"uM","substrate":"Sub-CpU","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15113930"}]},{"constant":259.0,"unit":"uM","substrate":"Sub-ApU","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15113930"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17215286"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18987150"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19540847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27334592"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37796122"}],"value":"Interacts (via N-terminus) with host SP1; this interaction induces proteasomal degradation of SP1 with subsequent down-regulation of HDAC1 and ISG15 expression thereby counteracting the host innate immunity (PubMed:37796122). Interacts (via C-terminus) with host IRF3 (PubMed:17215286, PubMed:18987150, PubMed:19540847, PubMed:27334592)"}],"commentType":"SUBUNIT","molecule":"N-terminal protease"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25010283"}],"value":"Interacts with host OS9 (PubMed:25010283)"}],"commentType":"SUBUNIT","molecule":"Capsid protein C"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1870198"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25694590"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29235980"}],"value":"Homodimer; disulfide-linked (PubMed:1870198, PubMed:29235980). Interacts with host RPSA (PubMed:25694590)"}],"commentType":"SUBUNIT","molecule":"E(rns) glycoprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2370675"}],"value":"Homodimer; disulfide-linked (PubMed:2370675). Heterodimer with E1; disulfide-linked (PubMed:2370675)"}],"commentType":"SUBUNIT","molecule":"Envelope glycoprotein E1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P21530"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2370675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26041303"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33684175"}],"value":"Homodimer; disulfide-linked (PubMed:2370675). Heterodimer with E1; disulfide-linked (PubMed:2370675). Interacts with host TRX2 (PubMed:26041303). Interacts with host receptor ADAM17 (via metalloproteinase domain); this interaction allows binding and probably entry of the virus into the host cell (PubMed:33684175). Interacts with host ANXA2; this interaction allows binding and probably entry of the virus into the host cell (By similarity). Interacts with host MERTK; this interaction allows binding and probably entry of the virus into the host cell (By similarity)"}],"commentType":"SUBUNIT","molecule":"Envelope glycoprotein E2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Interacts with host TRAF6; this interaction inhibits host NF-kappa-B pathway. Interacts with NS5B; this interaction enhances RNA-dependent RNA polymerase activity. Interacts with protein NS4A"}],"commentType":"SUBUNIT","molecule":"Serine protease NS3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28848503"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29844394"}],"value":"Interacts with host RAB5, this interaction facilitates the formation of NS4B-related complex (PubMed:28848503). Interacts with host FTH1; this interaction plays a positive role in viral anti-apoptosis (PubMed:29844394)"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 4B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22795973"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31517388"}],"value":"Interacts with RNA-directed RNA polymerase (PubMed:22795973). Interacts with host RSAD2; this interaction inhibits viral replication (PubMed:31517388)"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 5A"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22795973"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31517388"}],"value":"Interacts with NS5A; this interaction promotes viral replication"}],"commentType":"SUBUNIT","molecule":"RNA-directed RNA polymerase"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"chainId":"PRO_0000038050","intActId":"EBI-10901281"},"interactantTwo":{"uniProtKBAccession":"Q08211","geneName":"DHX9","intActId":"EBI-352022"},"numberOfExperiments":6,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000038050","intActId":"EBI-10901281"},"interactantTwo":{"uniProtKBAccession":"Q764M6","geneName":"IRF3","intActId":"EBI-12512266"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000038050","intActId":"EBI-10901281"},"interactantTwo":{"uniProtKBAccession":"P67809","geneName":"YBX1","intActId":"EBI-354065"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000038060","intActId":"EBI-12513719"},"interactantTwo":{"uniProtKBAccession":"A0A8D1U8F1","geneName":"FKBP8","intActId":"EBI-12512146"},"numberOfExperiments":4,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"N-terminal protease","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17215286"}],"value":"Host cytoplasm","id":"SL-0381"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Capsid protein C","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28290554"}],"value":"Virion","id":"SL-0274"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"E(rns) glycoprotein","note":{"texts":[{"value":"The C-terminus membrane anchor of Erns represents an amphipathic helix embedded in plane into the membrane"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28290554"}],"value":"Host cell membrane","id":"SL-0375"},"topology":{"value":"Peripheral membrane protein","id":"SL-9903"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28290554"}],"value":"Virion membrane","id":"SL-0275"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Envelope glycoprotein E2","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28290554"}],"value":"Host cell surface","id":"SL-0378"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28290554"}],"value":"Virion membrane","id":"SL-0275"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Cysteine protease NS2","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}],"value":"Host membrane","id":"SL-0380"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Serine protease NS3","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28848503"}],"value":"Host cytoplasm","id":"SL-0381"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 4B","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28848503"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29844394"}],"value":"Host cytoplasm","id":"SL-0381"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 5A","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28848503"}],"value":"Host cytoplasm","id":"SL-0381"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9573242"}],"value":"Translated cap independently from an internal ribosome entry site (IRES)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19540847"}],"value":"Contains a zinc-binding TRASH region (PubMed:19540847). This region is required for binding host IRF3 and inducing its proteasomal degradation (PubMed:19540847)"}],"commentType":"DOMAIN","molecule":"N-terminal protease"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1870198"}],"value":"Heavily glycosylated"}],"commentType":"PTM","molecule":"E(rns) glycoprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8230432"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8388499"}],"value":"The viral RNA of pestiviruses is expressed as a single polyprotein which undergoes post-translational proteolytic processing resulting in the production of at least eleven individual proteins. The N-terminal protease cleaves itself from the nascent polyprotein autocatalytically and thereby generates the N-terminus of the adjacent viral capsid protein C"}],"commentType":"PTM"},{"texts":[{"value":"Cleavage between E2 and p7 is partial"}],"commentType":"PTM","molecule":"Genome polyprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the pestivirus polyprotein family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":3898,"modifier":"EXACT"}},"description":"Genome polyprotein","featureId":"PRO_0000450893"},{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"N-terminal protease","featureId":"PRO_0000038050"},{"type":"Chain","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Capsid protein C","featureId":"PRO_0000038051"},{"type":"Chain","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":494,"modifier":"EXACT"}},"description":"E(rns) glycoprotein","featureId":"PRO_0000038052"},{"type":"Chain","location":{"start":{"value":495,"modifier":"EXACT"},"end":{"value":689,"modifier":"EXACT"}},"description":"Envelope glycoprotein E1","featureId":"PRO_0000038053"},{"type":"Chain","location":{"start":{"value":690,"modifier":"EXACT"},"end":{"value":1062,"modifier":"EXACT"}},"description":"Envelope glycoprotein E2","featureId":"PRO_0000038054"},{"type":"Chain","location":{"start":{"value":1063,"modifier":"EXACT"},"end":{"value":1132,"modifier":"EXACT"}},"description":"Viroporin p7","evidences":[{"evidenceCode":"ECO:0000250"}],"featureId":"PRO_0000038055"},{"type":"Chain","location":{"start":{"value":1133,"modifier":"EXACT"},"end":{"value":2272,"modifier":"EXACT"}},"description":"Non-structural protein 2-3","evidences":[{"evidenceCode":"ECO:0000250"}],"featureId":"PRO_0000038056"},{"type":"Chain","location":{"start":{"value":1133,"modifier":"EXACT"},"end":{"value":1589,"modifier":"EXACT"}},"description":"Cysteine protease NS2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}],"featureId":"PRO_0000349361"},{"type":"Chain","location":{"start":{"value":1590,"modifier":"EXACT"},"end":{"value":2272,"modifier":"EXACT"}},"description":"Serine protease NS3","evidences":[{"evidenceCode":"ECO:0000250"}],"featureId":"PRO_0000038057"},{"type":"Chain","location":{"start":{"value":2273,"modifier":"EXACT"},"end":{"value":2336,"modifier":"EXACT"}},"description":"Non-structural protein 4A","evidences":[{"evidenceCode":"ECO:0000250"}],"featureId":"PRO_0000038058"},{"type":"Chain","location":{"start":{"value":2337,"modifier":"EXACT"},"end":{"value":2683,"modifier":"EXACT"}},"description":"Non-structural protein 4B","evidences":[{"evidenceCode":"ECO:0000250"}],"featureId":"PRO_0000038059"},{"type":"Chain","location":{"start":{"value":2684,"modifier":"EXACT"},"end":{"value":3180,"modifier":"EXACT"}},"description":"Non-structural protein 5A","evidences":[{"evidenceCode":"ECO:0000250"}],"featureId":"PRO_0000038060"},{"type":"Chain","location":{"start":{"value":3181,"modifier":"EXACT"},"end":{"value":3898,"modifier":"EXACT"}},"description":"RNA-directed RNA polymerase","evidences":[{"evidenceCode":"ECO:0000250"}],"featureId":"PRO_0000038061"},{"type":"Transmembrane","location":{"start":{"value":1031,"modifier":"EXACT"},"end":{"value":1051,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":1070,"modifier":"EXACT"},"end":{"value":1090,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":1104,"modifier":"EXACT"},"end":{"value":1124,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":1140,"modifier":"EXACT"},"end":{"value":1164,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Transmembrane","location":{"start":{"value":1189,"modifier":"EXACT"},"end":{"value":1209,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Transmembrane","location":{"start":{"value":1217,"modifier":"EXACT"},"end":{"value":1237,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Transmembrane","location":{"start":{"value":1247,"modifier":"EXACT"},"end":{"value":1267,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Transmembrane","location":{"start":{"value":1281,"modifier":"EXACT"},"end":{"value":1301,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Transmembrane","location":{"start":{"value":1360,"modifier":"EXACT"},"end":{"value":1380,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Transmembrane","location":{"start":{"value":1568,"modifier":"EXACT"},"end":{"value":1588,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"Peptidase C53","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01224"}]},{"type":"Domain","location":{"start":{"value":1441,"modifier":"EXACT"},"end":{"value":1589,"modifier":"EXACT"}},"description":"Peptidase C74","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Domain","location":{"start":{"value":1590,"modifier":"EXACT"},"end":{"value":1763,"modifier":"EXACT"}},"description":"Peptidase S31","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00868"}]},{"type":"Domain","location":{"start":{"value":1802,"modifier":"EXACT"},"end":{"value":1960,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00541"}]},{"type":"Domain","location":{"start":{"value":1978,"modifier":"EXACT"},"end":{"value":2179,"modifier":"EXACT"}},"description":"Helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00542"}]},{"type":"Domain","location":{"start":{"value":3519,"modifier":"EXACT"},"end":{"value":3642,"modifier":"EXACT"}},"description":"RdRp catalytic","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00539"}]},{"type":"Region","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Zinc-binding TRASH domain","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19540847"}]},{"type":"Region","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":1910,"modifier":"EXACT"},"end":{"value":1913,"modifier":"EXACT"}},"description":"DEAH box","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00541"}]},{"type":"Compositional bias","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"For N-terminal protease activity","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"9499122"}]},{"type":"Active site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"For N-terminal protease activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01224"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}]},{"type":"Active site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"For N-terminal protease activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01224"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24606708"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}]},{"type":"Active site","location":{"start":{"value":1447,"modifier":"EXACT"},"end":{"value":1447,"modifier":"EXACT"}},"description":"For cysteine protease NS2 activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Active site","location":{"start":{"value":1461,"modifier":"EXACT"},"end":{"value":1461,"modifier":"EXACT"}},"description":"For cysteine protease NS2 activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Active site","location":{"start":{"value":1512,"modifier":"EXACT"},"end":{"value":1512,"modifier":"EXACT"}},"description":"For cysteine protease NS2 activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Active site","location":{"start":{"value":1658,"modifier":"EXACT"},"end":{"value":1658,"modifier":"EXACT"}},"description":"Charge relay system; for serine protease NS3 activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00868"}]},{"type":"Active site","location":{"start":{"value":1695,"modifier":"EXACT"},"end":{"value":1695,"modifier":"EXACT"}},"description":"Charge relay system; for serine protease NS3 activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00868"}]},{"type":"Active site","location":{"start":{"value":1752,"modifier":"EXACT"},"end":{"value":1752,"modifier":"EXACT"}},"description":"Charge relay system; for serine protease NS3 activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00868"}]},{"type":"Binding site","location":{"start":{"value":1815,"modifier":"EXACT"},"end":{"value":1822,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00541"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":3500,"modifier":"EXACT"},"end":{"value":3500,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19711"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":3502,"modifier":"EXACT"},"end":{"value":3502,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19711"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":3697,"modifier":"EXACT"},"end":{"value":3697,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19711"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":3705,"modifier":"EXACT"},"end":{"value":3705,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19711"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"Cleavage; by autolysis","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01224"}]},{"type":"Site","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"Cleavage; by host signal peptidase","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8388499"}]},{"type":"Site","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"Hydrogen donor to release the cleavage products of E(rns) glycoprotein RNase activity","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}]},{"type":"Site","location":{"start":{"value":494,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"Cleavage","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8388499"}]},{"type":"Site","location":{"start":{"value":689,"modifier":"EXACT"},"end":{"value":690,"modifier":"EXACT"}},"description":"Cleavage; by host signal peptidase","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8388499"}]},{"type":"Site","location":{"start":{"value":759,"modifier":"EXACT"},"end":{"value":759,"modifier":"EXACT"}},"description":"Serves as pH sensor to control fusion","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19711"}]},{"type":"Site","location":{"start":{"value":1062,"modifier":"EXACT"},"end":{"value":1063,"modifier":"EXACT"}},"description":"Cleavage; by host signal peptidase; partial","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Site","location":{"start":{"value":1132,"modifier":"EXACT"},"end":{"value":1133,"modifier":"EXACT"}},"description":"Cleavage; by host signal peptidase","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Site","location":{"start":{"value":1589,"modifier":"EXACT"},"end":{"value":1590,"modifier":"EXACT"}},"description":"Cleavage; partial; cysteine protease NS2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01029"}]},{"type":"Site","location":{"start":{"value":2272,"modifier":"EXACT"},"end":{"value":2273,"modifier":"EXACT"}},"description":"Cleavage; by serine protease NS3","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Site","location":{"start":{"value":2336,"modifier":"EXACT"},"end":{"value":2337,"modifier":"EXACT"}},"description":"Cleavage; by serine protease NS3","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Site","location":{"start":{"value":2683,"modifier":"EXACT"},"end":{"value":2684,"modifier":"EXACT"}},"description":"Cleavage; by serine protease NS3","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Site","location":{"start":{"value":3180,"modifier":"EXACT"},"end":{"value":3181,"modifier":"EXACT"}},"description":"Cleavage; by serine protease NS3","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Glycosylation","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":410,"modifier":"EXACT"},"end":{"value":410,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":425,"modifier":"EXACT"},"end":{"value":425,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":500,"modifier":"EXACT"},"end":{"value":500,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":594,"modifier":"EXACT"},"end":{"value":594,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":805,"modifier":"EXACT"},"end":{"value":805,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":810,"modifier":"EXACT"},"end":{"value":810,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":874,"modifier":"EXACT"},"end":{"value":874,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":918,"modifier":"EXACT"},"end":{"value":918,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":949,"modifier":"EXACT"},"end":{"value":949,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":986,"modifier":"EXACT"},"end":{"value":986,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":1713,"modifier":"EXACT"},"end":{"value":1713,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":2134,"modifier":"EXACT"},"end":{"value":2134,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":2217,"modifier":"EXACT"},"end":{"value":2217,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":2494,"modifier":"EXACT"},"end":{"value":2494,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":2787,"modifier":"EXACT"},"end":{"value":2787,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":2815,"modifier":"EXACT"},"end":{"value":2815,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":2891,"modifier":"EXACT"},"end":{"value":2891,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":3211,"modifier":"EXACT"},"end":{"value":3211,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":3316,"modifier":"EXACT"},"end":{"value":3316,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":3689,"modifier":"EXACT"},"end":{"value":3689,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":3698,"modifier":"EXACT"},"end":{"value":3698,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":3794,"modifier":"EXACT"},"end":{"value":3794,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":""},{"type":"Disulfide bond","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}]},{"type":"Disulfide bond","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}]},{"type":"Disulfide bond","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":422,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}]},{"type":"Disulfide bond","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}]},{"type":"Disulfide bond","location":{"start":{"value":438,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"Interchain","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19264773"}]},{"type":"Disulfide bond","location":{"start":{"value":693,"modifier":"EXACT"},"end":{"value":737,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19711"}]},{"type":"Disulfide bond","location":{"start":{"value":983,"modifier":"EXACT"},"end":{"value":983,"modifier":"EXACT"}},"description":"Interchain","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19711"}]},{"type":"Natural variant","location":{"start":{"value":387,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"","featureId":"","alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Natural variant","location":{"start":{"value":3542,"modifier":"EXACT"},"end":{"value":3542,"modifier":"EXACT"}},"description":"","featureId":"","alternativeSequence":{"originalSequence":"R","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Almost complete loss of cleavage between N-pro and C.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["V"]}},{"type":"Mutagenesis","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"No effect.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["L"]}},{"type":"Mutagenesis","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"Complete loss of cleavage between N-pro and C.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["L"]}},{"type":"Mutagenesis","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"Complete loss of cleavage between N-pro and C.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A","S"]}},{"type":"Mutagenesis","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"No effect.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["L"]}},{"type":"Mutagenesis","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"86% loss of zinc-binding by N-terminal protease. Complete loss of interaction with host IRF3. No effect on N-terminal protease enzymatic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19540847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"Almost complete loss of zinc-binding by N-terminal protease.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18987150"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19540847"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["R"]}},{"type":"Mutagenesis","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"No effect on N-terminal protease enzymatic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"No effect on N-terminal protease enzymatic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["L"]}},{"type":"Mutagenesis","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"Almost complete loss of zinc-binding by N-terminal protease. Complete loss of interaction with host IRF3. No effect on N-terminal protease enzymatic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19540847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"No effect on N-terminal protease enzymatic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"74% loss of zinc-binding by N-terminal protease.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18987150"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19540847"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Almost complete loss of zinc-binding by N-terminal protease. Complete loss of interaction with host IRF3. No effect on N-terminal protease enzymatic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19540847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"No effect on N-terminal protease enzymatic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"40% loss of zinc-binding by N-terminal protease. No effect on N-terminal protease enzymatic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19540847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"No effect.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9499122"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":438,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"Complete loss of E(rns) glycoprotein dimerization. Virus shows attenuated phenotype.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19264773"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["F","S"]}},{"type":"Beta strand","location":{"start":{"value":1592,"modifier":"EXACT"},"end":{"value":1602,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Helix","location":{"start":{"value":1607,"modifier":"EXACT"},"end":{"value":1614,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Helix","location":{"start":{"value":1617,"modifier":"EXACT"},"end":{"value":1619,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1632,"modifier":"EXACT"},"end":{"value":1639,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1642,"modifier":"EXACT"},"end":{"value":1649,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1652,"modifier":"EXACT"},"end":{"value":1655,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Helix","location":{"start":{"value":1657,"modifier":"EXACT"},"end":{"value":1660,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1665,"modifier":"EXACT"},"end":{"value":1669,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1672,"modifier":"EXACT"},"end":{"value":1676,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1680,"modifier":"EXACT"},"end":{"value":1682,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Turn","location":{"start":{"value":1683,"modifier":"EXACT"},"end":{"value":1686,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1687,"modifier":"EXACT"},"end":{"value":1691,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1703,"modifier":"EXACT"},"end":{"value":1713,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1718,"modifier":"EXACT"},"end":{"value":1727,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1730,"modifier":"EXACT"},"end":{"value":1734,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Helix","location":{"start":{"value":1745,"modifier":"EXACT"},"end":{"value":1748,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1755,"modifier":"EXACT"},"end":{"value":1758,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Turn","location":{"start":{"value":1759,"modifier":"EXACT"},"end":{"value":1761,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1764,"modifier":"EXACT"},"end":{"value":1767,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1770,"modifier":"EXACT"},"end":{"value":1777,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":1780,"modifier":"EXACT"},"end":{"value":1782,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Helix","location":{"start":{"value":1792,"modifier":"EXACT"},"end":{"value":1803,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":1809,"modifier":"EXACT"},"end":{"value":1814,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":1817,"modifier":"EXACT"},"end":{"value":1819,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":1821,"modifier":"EXACT"},"end":{"value":1823,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":1824,"modifier":"EXACT"},"end":{"value":1833,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":1839,"modifier":"EXACT"},"end":{"value":1845,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":1846,"modifier":"EXACT"},"end":{"value":1859,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":1865,"modifier":"EXACT"},"end":{"value":1871,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":1880,"modifier":"EXACT"},"end":{"value":1885,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":1886,"modifier":"EXACT"},"end":{"value":1889,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":1894,"modifier":"EXACT"},"end":{"value":1901,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":1905,"modifier":"EXACT"},"end":{"value":1910,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":1912,"modifier":"EXACT"},"end":{"value":1914,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":1917,"modifier":"EXACT"},"end":{"value":1927,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":1930,"modifier":"EXACT"},"end":{"value":1932,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":1934,"modifier":"EXACT"},"end":{"value":1939,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":1956,"modifier":"EXACT"},"end":{"value":1958,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Turn","location":{"start":{"value":1970,"modifier":"EXACT"},"end":{"value":1972,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBL"}]},{"type":"Beta strand","location":{"start":{"value":1973,"modifier":"EXACT"},"end":{"value":1976,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Beta strand","location":{"start":{"value":1979,"modifier":"EXACT"},"end":{"value":1982,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Helix","location":{"start":{"value":1983,"modifier":"EXACT"},"end":{"value":1987,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Beta strand","location":{"start":{"value":1990,"modifier":"EXACT"},"end":{"value":1993,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Helix","location":{"start":{"value":1997,"modifier":"EXACT"},"end":{"value":2009,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Beta strand","location":{"start":{"value":2014,"modifier":"EXACT"},"end":{"value":2016,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Beta strand","location":{"start":{"value":2018,"modifier":"EXACT"},"end":{"value":2020,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBM"}]},{"type":"Helix","location":{"start":{"value":2024,"modifier":"EXACT"},"end":{"value":2030,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Beta strand","location":{"start":{"value":2032,"modifier":"EXACT"},"end":{"value":2034,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Beta strand","location":{"start":{"value":2036,"modifier":"EXACT"},"end":{"value":2041,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Helix","location":{"start":{"value":2042,"modifier":"EXACT"},"end":{"value":2045,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBI"}]},{"type":"Beta strand","location":{"start":{"value":2054,"modifier":"EXACT"},"end":{"value":2057,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Beta strand","location":{"start":{"value":2061,"modifier":"EXACT"},"end":{"value":2068,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":2070,"modifier":"EXACT"},"end":{"value":2073,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":2075,"modifier":"EXACT"},"end":{"value":2082,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2086,"modifier":"EXACT"},"end":{"value":2093,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":2096,"modifier":"EXACT"},"end":{"value":2100,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":2103,"modifier":"EXACT"},"end":{"value":2105,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2109,"modifier":"EXACT"},"end":{"value":2111,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Beta strand","location":{"start":{"value":2112,"modifier":"EXACT"},"end":{"value":2114,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBG"}]},{"type":"Helix","location":{"start":{"value":2118,"modifier":"EXACT"},"end":{"value":2124,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2125,"modifier":"EXACT"},"end":{"value":2128,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Turn","location":{"start":{"value":2129,"modifier":"EXACT"},"end":{"value":2132,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2135,"modifier":"EXACT"},"end":{"value":2146,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2153,"modifier":"EXACT"},"end":{"value":2166,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2170,"modifier":"EXACT"},"end":{"value":2172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2173,"modifier":"EXACT"},"end":{"value":2181,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2188,"modifier":"EXACT"},"end":{"value":2193,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Turn","location":{"start":{"value":2194,"modifier":"EXACT"},"end":{"value":2196,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":2204,"modifier":"EXACT"},"end":{"value":2207,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":2210,"modifier":"EXACT"},"end":{"value":2215,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":2234,"modifier":"EXACT"},"end":{"value":2237,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2238,"modifier":"EXACT"},"end":{"value":2246,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2251,"modifier":"EXACT"},"end":{"value":2254,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2257,"modifier":"EXACT"},"end":{"value":2270,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Helix","location":{"start":{"value":2272,"modifier":"EXACT"},"end":{"value":2275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4CBH"}]},{"type":"Beta strand","location":{"start":{"value":2276,"modifier":"EXACT"},"end":{"value":2279,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Beta strand","location":{"start":{"value":2298,"modifier":"EXACT"},"end":{"value":2312,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]},{"type":"Helix","location":{"start":{"value":2315,"modifier":"EXACT"},"end":{"value":2317,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5MZ4"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-1072","category":"Biological process","name":"Activation of host autophagy by virus"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-1170","category":"Biological process","name":"Fusion of virus membrane with host endosomal membrane"},{"id":"KW-1168","category":"Biological process","name":"Fusion of virus membrane with host membrane"},{"id":"KW-0325","category":"PTM","name":"Glycoprotein"},{"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"id":"KW-1032","category":"Cellular component","name":"Host cell membrane"},{"id":"KW-1035","category":"Cellular component","name":"Host cytoplasm"},{"id":"KW-1043","category":"Cellular component","name":"Host membrane"},{"id":"KW-0945","category":"Biological process","name":"Host-virus interaction"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-1090","category":"Biological process","name":"Inhibition of host innate immune response by virus"},{"id":"KW-1092","category":"Biological process","name":"Inhibition of host IRF3 by virus"},{"id":"KW-1113","category":"Biological process","name":"Inhibition of host RLR pathway by virus"},{"id":"KW-0407","category":"Molecular function","name":"Ion channel"},{"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"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-0696","category":"Molecular function","name":"RNA-directed RNA polymerase"},{"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"id":"KW-0788","category":"Molecular function","name":"Thiol protease"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"},{"id":"KW-1161","category":"Biological process","name":"Viral attachment to host cell"},{"id":"KW-1234","category":"Biological process","name":"Viral attachment to host entry receptor"},{"id":"KW-0899","category":"Biological process","name":"Viral immunoevasion"},{"id":"KW-1182","category":"Molecular function","name":"Viral ion channel"},{"id":"KW-1162","category":"Biological process","name":"Viral penetration into host cytoplasm"},{"id":"KW-0693","category":"Biological process","name":"Viral RNA replication"},{"id":"KW-0946","category":"Cellular component","name":"Virion"},{"id":"KW-1160","category":"Biological process","name":"Virus entry into host cell"}],"references":[{"referenceNumber":1,"citation":{"id":"2763466","citationType":"journal article","authors":["Meyers G.","Ruemenapf T.","Thiel H.-J."],"citationCrossReferences":[{"database":"PubMed","id":"2763466"},{"database":"DOI","id":"10.1016/0042-6822(89)90625-9"}],"title":"Molecular cloning and nucleotide sequence of the genome of hog cholera virus.","publicationDate":"1989","journal":"Virology","firstPage":"555","lastPage":"567","volume":"171"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC RNA]"]},{"referenceNumber":2,"citation":{"id":"CI-EBTHTUO9188TV","citationType":"submission","authors":["Meyers G."],"publicationDate":"AUG-1999","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["SEQUENCE REVISION TO 2731"]},{"referenceNumber":3,"citation":{"id":"8388499","citationType":"journal article","authors":["Ruemenapf T.","Unger G.","Strauss J.H.","Thiel H.-J."],"citationCrossReferences":[{"database":"PubMed","id":"8388499"},{"database":"DOI","id":"10.1128/jvi.67.6.3288-3294.1993"}],"title":"Processing of the envelope glycoproteins of pestiviruses.","publicationDate":"1993","journal":"J. Virol.","firstPage":"3288","lastPage":"3294","volume":"67"},"referencePositions":["PROTEIN SEQUENCE OF 169-178; 268-291; 495-518 AND 690-713","PROTEOLYTIC PROCESSING OF POLYPROTEIN (GENOME POLYPROTEIN)"]},{"referenceNumber":4,"citation":{"id":"2370675","citationType":"journal article","authors":["Weiland E.","Stark R.","Haas B.","Ruemenapf T.","Meyers G.","Thiel H.J."],"citationCrossReferences":[{"database":"PubMed","id":"2370675"},{"database":"DOI","id":"10.1128/jvi.64.8.3563-3569.1990"}],"title":"Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer.","publicationDate":"1990","journal":"J. Virol.","firstPage":"3563","lastPage":"3569","volume":"64"},"referencePositions":["SUBUNIT (ENVELOPE GLYCOPROTEIN E1)","SUBUNIT (ENVELOPE GLYCOPROTEIN E2)"]},{"referenceNumber":5,"citation":{"id":"1870198","citationType":"journal article","authors":["Thiel H.-J.","Stark R.","Weiland E.","Ruemenapf T.","Meyers G."],"citationCrossReferences":[{"database":"PubMed","id":"1870198"},{"database":"DOI","id":"10.1128/jvi.65.9.4705-4712.1991"}],"title":"Hog cholera virus: molecular composition of virions from a pestivirus.","publicationDate":"1991","journal":"J. Virol.","firstPage":"4705","lastPage":"4712","volume":"65"},"referencePositions":["SUBUNIT (E(RNS) GLYCOPROTEIN)","GLYCOSYLATION (E(RNS) GLYCOPROTEIN)"]},{"referenceNumber":6,"citation":{"id":"8230432","citationType":"journal article","authors":["Stark R.","Meyers G.","Ruemenapf T.","Thiel H.-J."],"citationCrossReferences":[{"database":"PubMed","id":"8230432"},{"database":"DOI","id":"10.1128/jvi.67.12.7088-7095.1993"}],"title":"Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus.","publicationDate":"1993","journal":"J. Virol.","firstPage":"7088","lastPage":"7095","volume":"67"},"referencePositions":["PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN)"]},{"referenceNumber":7,"citation":{"id":"8356450","citationType":"journal article","authors":["Schneider R.","Unger G.","Stark R.","Schneider-Scherzer E.","Thiel H.J."],"citationCrossReferences":[{"database":"PubMed","id":"8356450"},{"database":"DOI","id":"10.1126/science.8356450"}],"title":"Identification of a structural glycoprotein of an RNA virus as a ribonuclease.","publicationDate":"1993","journal":"Science","firstPage":"1169","lastPage":"1171","volume":"261"},"referencePositions":["FUNCTION (E(RNS) GLYCOPROTEIN)"]},{"referenceNumber":8,"citation":{"id":"9499122","citationType":"journal article","authors":["Ruemenapf T.","Stark R.","Heimann M.","Thiel H.-J."],"citationCrossReferences":[{"database":"PubMed","id":"9499122"},{"database":"DOI","id":"10.1128/jvi.72.3.2544-2547.1998"}],"title":"N-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesis.","publicationDate":"1998","journal":"J. Virol.","firstPage":"2544","lastPage":"2547","volume":"72"},"referencePositions":["ACTIVE SITE (N-TERMINAL PROTEASE)","MUTAGENESIS OF GLU-22; HIS-40; HIS-49; CYS-69; HIS-99; CYS-112; HIS-130; CYS-134; CYS-138 AND CYS-161"]},{"referenceNumber":9,"citation":{"id":"9573242","citationType":"journal article","authors":["Sizova D.V.","Kolupaeva V.G.","Pestova T.V.","Shatsky I.N.","Hellen C.U."],"citationCrossReferences":[{"database":"PubMed","id":"9573242"},{"database":"DOI","id":"10.1128/jvi.72.6.4775-4782.1998"}],"title":"Specific interaction of eukaryotic translation initiation factor 3 with the 5' nontranslated regions of hepatitis C virus and classical swine fever virus RNAs.","publicationDate":"1998","journal":"J. Virol.","firstPage":"4775","lastPage":"4782","volume":"72"},"referencePositions":["INDUCTION"]},{"referenceNumber":10,"citation":{"id":"9617770","citationType":"journal article","authors":["Liu J.J.","Wong M.L.","Chang T.J."],"citationCrossReferences":[{"database":"PubMed","id":"9617770"},{"database":"DOI","id":"10.1016/s0168-1702(97)00132-9"}],"title":"The recombinant nucleocapsid protein of classical swine fever virus can act as a transcriptional regulator.","publicationDate":"1998","journal":"Virus Res.","firstPage":"75","lastPage":"80","volume":"53"},"referencePositions":["FUNCTION (CAPSID PROTEIN C)"]},{"referenceNumber":11,"citation":{"id":"10355762","citationType":"journal article","authors":["Weiland F.","Weiland E.","Unger G.","Saalmuller A.","Thiel H.-J."],"citationCrossReferences":[{"database":"PubMed","id":"10355762"},{"database":"DOI","id":"10.1099/0022-1317-80-5-1157"}],"title":"Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles.","publicationDate":"1999","journal":"J. Gen. Virol.","firstPage":"1157","lastPage":"1165","volume":"80"},"referencePositions":["SUBCELLULAR LOCATION (E(RNS) GLYCOPROTEIN)","SUBCELLULAR LOCATION (ENVELOPE GLYCOPROTEIN E2)"]},{"referenceNumber":12,"citation":{"id":"10438869","citationType":"journal article","authors":["Moser C.","Stettler P.","Tratschin J.D.","Hofmann M.A."],"citationCrossReferences":[{"database":"PubMed","id":"10438869"},{"database":"DOI","id":"10.1128/jvi.73.9.7787-7794.1999"}],"title":"Cytopathogenic and noncytopathogenic RNA replicons of classical swine fever virus.","publicationDate":"1999","journal":"J. Virol.","firstPage":"7787","lastPage":"7794","volume":"73"},"referencePositions":["FUNCTION (ENVELOPE GLYCOPROTEIN E2)"]},{"referenceNumber":13,"citation":{"id":"15527858","citationType":"journal article","authors":["Wang Z.","Nie Y.","Wang P.","Ding M.","Deng H."],"citationCrossReferences":[{"database":"PubMed","id":"15527858"},{"database":"DOI","id":"10.1016/j.virol.2004.09.023"}],"title":"Characterization of classical swine fever virus entry by using pseudotyped viruses: E1 and E2 are sufficient to mediate viral entry.","publicationDate":"2004","journal":"Virology","firstPage":"332","lastPage":"341","volume":"330"},"referencePositions":["FUNCTION (ENVELOPE GLYCOPROTEIN E1)","FUNCTION (ENVELOPE GLYCOPROTEIN E2)"]},{"referenceNumber":14,"citation":{"id":"15113930","citationType":"journal article","authors":["Hausmann Y.","Roman-Sosa G.","Thiel H.J.","Ruemenapf T."],"citationCrossReferences":[{"database":"PubMed","id":"15113930"},{"database":"DOI","id":"10.1128/jvi.78.10.5507-5512.2004"}],"title":"Classical swine fever virus glycoprotein E rns is an endoribonuclease with an unusual base specificity.","publicationDate":"2004","journal":"J. Virol.","firstPage":"5507","lastPage":"5512","volume":"78"},"referencePositions":["BIOPHYSICOCHEMICAL PROPERTIES (E(RNS) GLYCOPROTEIN)","FUNCTION (E(RNS) GLYCOPROTEIN)"]},{"referenceNumber":15,"citation":{"id":"17482232","citationType":"journal article","authors":["Moulin H.R.","Seuberlich T.","Bauhofer O.","Bennett L.C.","Tratschin J.D.","Hofmann M.A.","Ruggli N."],"citationCrossReferences":[{"database":"PubMed","id":"17482232"},{"database":"DOI","id":"10.1016/j.virol.2007.03.056"}],"title":"Nonstructural proteins NS2-3 and NS4A of classical swine fever virus: essential features for infectious particle formation.","publicationDate":"2007","journal":"Virology","firstPage":"376","lastPage":"389","volume":"365"},"referencePositions":["FUNCTION (NON-STRUCTURAL PROTEIN 2-3)","FUNCTION (NON-STRUCTURAL PROTEIN 4A)"]},{"referenceNumber":16,"citation":{"id":"17215286","citationType":"journal article","authors":["Bauhofer O.","Summerfield A.","Sakoda Y.","Tratschin J.D.","Hofmann M.A.","Ruggli N."],"citationCrossReferences":[{"database":"PubMed","id":"17215286"},{"database":"DOI","id":"10.1128/jvi.02032-06"}],"title":"Classical swine fever virus Npro interacts with interferon regulatory factor 3 and induces its proteasomal degradation.","publicationDate":"2007","journal":"J. Virol.","firstPage":"3087","lastPage":"3096","volume":"81"},"referencePositions":["FUNCTION (N-TERMINAL PROTEASE)","INTERACTION WITH HOST IRF3 (N-TERMINAL PROTEASE)","SUBCELLULAR LOCATION (N-TERMINAL PROTEASE)"]},{"referenceNumber":17,"citation":{"id":"19264773","citationType":"journal article","authors":["Tews B.A.","Schuermann E.M.","Meyers G."],"citationCrossReferences":[{"database":"PubMed","id":"19264773"},{"database":"DOI","id":"10.1128/jvi.01710-08"}],"title":"Mutation of cysteine 171 of pestivirus E rns RNase prevents homodimer formation and leads to attenuation of classical swine fever virus.","publicationDate":"2009","journal":"J. Virol.","firstPage":"4823","lastPage":"4834","volume":"83"},"referencePositions":["FUNCTION (E(RNS) GLYCOPROTEIN)","MUTAGENESIS OF CYS-438","DISULFIDE BOND"]},{"referenceNumber":18,"citation":{"id":"19767841","citationType":"journal article","authors":["Luo X.","Ling D.","Li T.","Wan C.","Zhang C.","Pan Z."],"citationCrossReferences":[{"database":"PubMed","id":"19767841"},{"database":"DOI","id":"10.1139/w09-013"}],"title":"Classical swine fever virus Erns glycoprotein antagonizes induction of interferon-beta by double-stranded RNA.","publicationDate":"2009","journal":"Can. J. Microbiol.","firstPage":"698","lastPage":"704","volume":"55"},"referencePositions":["FUNCTION (E(RNS) GLYCOPROTEIN)"]},{"referenceNumber":19,"citation":{"id":"19185595","citationType":"journal article","authors":["Wen G.","Xue J.","Shen Y.","Zhang C.","Pan Z."],"citationCrossReferences":[{"database":"PubMed","id":"19185595"},{"database":"DOI","id":"10.1016/j.virusres.2008.12.014"}],"title":"Characterization of classical swine fever virus (CSFV) nonstructural protein 3 (NS3) helicase activity and its modulation by CSFV RNA-dependent RNA polymerase.","publicationDate":"2009","journal":"Virus Res.","firstPage":"63","lastPage":"70","volume":"141"},"referencePositions":["FUNCTION (NON-STRUCTURAL PROTEIN 3)","INTERACTION WITH RNA-DIRECTED RNA POLYMERASE (NON-STRUCTURAL PROTEIN 3)","INTERACTION WITH NON-STRUCTURAL PROTEIN 3 (RNA-DIRECTED RNA POLYMERASE)"]},{"referenceNumber":20,"citation":{"id":"18987150","citationType":"journal article","authors":["Ruggli N.","Summerfield A.","Fiebach A.R.","Guzylack-Piriou L.","Bauhofer O.","Lamm C.G.","Waltersperger S.","Matsuno K.","Liu L.","Gerber M.","Choi K.H.","Hofmann M.A.","Sakoda Y.","Tratschin J.D."],"citationCrossReferences":[{"database":"PubMed","id":"18987150"},{"database":"DOI","id":"10.1128/jvi.01509-08"}],"title":"Classical swine fever virus can remain virulent after specific elimination of the interferon regulatory factor 3-degrading function of Npro.","publicationDate":"2009","journal":"J. Virol.","firstPage":"817","lastPage":"829","volume":"83"},"referencePositions":["MUTAGENESIS OF CYS-112 AND ASP-136","INTERACTION WITH HOST IRF3 (N-TERMINAL PROTEASE)"]},{"referenceNumber":21,"citation":{"id":"19540847","citationType":"journal article","authors":["Szymanski M.R.","Fiebach A.R.","Tratschin J.D.","Gut M.","Ramanujam V.M.","Gottipati K.","Patel P.","Ye M.","Ruggli N.","Choi K.H."],"citationCrossReferences":[{"database":"PubMed","id":"19540847"},{"database":"DOI","id":"10.1016/j.jmb.2009.06.040"}],"title":"Zinc binding in pestivirus N(pro) is required for interferon regulatory factor 3 interaction and degradation.","publicationDate":"2009","journal":"J. Mol. Biol.","firstPage":"438","lastPage":"449","volume":"391"},"referencePositions":["FUNCTION (N-TERMINAL PROTEASE)","INTERACTION WITH HOST IRF3 (N-TERMINAL PROTEASE)","DOMAIN (N-TERMINAL PROTEASE)","MUTAGENESIS OF CYS-112; CYS-134; ASP-136; CYS-138 AND CYS-161"]},{"referenceNumber":22,"citation":{"id":"22261205","citationType":"journal article","authors":["Sheng C.","Chen Y.","Xiao J.","Xiao J.","Wang J.","Li G.","Chen J.","Xiao M."],"citationCrossReferences":[{"database":"PubMed","id":"22261205"},{"database":"DOI","id":"10.1016/j.virusres.2012.01.004"}],"title":"Classical swine fever virus NS5A protein interacts with 3'-untranslated region and regulates viral RNA synthesis.","publicationDate":"2012","journal":"Virus Res.","firstPage":"636","lastPage":"643","volume":"163"},"referencePositions":["FUNCTION (NON-STRUCTURAL PROTEIN 5A)"]},{"referenceNumber":23,"citation":{"id":"22795973","citationType":"journal article","authors":["Chen Y.","Xiao J.","Xiao J.","Sheng C.","Wang J.","Jia L.","Zhi Y.","Li G.","Chen J.","Xiao M."],"citationCrossReferences":[{"database":"PubMed","id":"22795973"},{"database":"DOI","id":"10.1016/j.virol.2012.04.014"}],"title":"Classical swine fever virus NS5A regulates viral RNA replication through binding to NS5B and 3'UTR.","publicationDate":"2012","journal":"Virology","firstPage":"376","lastPage":"388","volume":"432"},"referencePositions":["FUNCTION (NON-STRUCTURAL PROTEIN 5A)","INTERACTION WITH RNA-DIRECTED RNA POLYMERASE (NON-STRUCTURAL PROTEIN 5A)","INTERACTION WITH NON-STRUCTURAL PROTEIN 5A (RNA-DIRECTED RNA POLYMERASE)"]},{"referenceNumber":24,"citation":{"id":"22496228","citationType":"journal article","authors":["Gladue D.P.","Holinka L.G.","Largo E.","Fernandez Sainz I.","Carrillo C.","O'Donnell V.","Baker-Branstetter R.","Lu Z.","Ambroggio X.","Risatti G.R.","Nieva J.L.","Borca M.V."],"citationCrossReferences":[{"database":"PubMed","id":"22496228"},{"database":"DOI","id":"10.1128/jvi.00560-12"}],"title":"Classical swine fever virus p7 protein is a viroporin involved in virulence in swine.","publicationDate":"2012","journal":"J. Virol.","firstPage":"6778","lastPage":"6791","volume":"86"},"referencePositions":["FUNCTION (VIROPORIN P7)"]},{"referenceNumber":25,"citation":{"id":"24606708","citationType":"journal article","authors":["Gottipati K.","Acholi S.","Ruggli N.","Choi K.H."],"citationCrossReferences":[{"database":"PubMed","id":"24606708"},{"database":"DOI","id":"10.1016/j.virol.2014.01.026"}],"title":"Autocatalytic activity and substrate specificity of the pestivirus N-terminal protease Npro.","publicationDate":"2014","journal":"Virology","firstPage":"303","lastPage":"309","volume":"452"},"referencePositions":["ACTIVE SITE (N-TERMINAL PROTEASE)","FUNCTION (N-TERMINAL PROTEASE)"]},{"referenceNumber":26,"citation":{"id":"25010283","citationType":"journal article","authors":["Gladue D.P.","O'Donnell V.","Fernandez-Sainz I.J.","Fletcher P.","Baker-Branstetter R.","Holinka L.G.","Sanford B.","Carlson J.","Lu Z.","Borca M.V."],"citationCrossReferences":[{"database":"PubMed","id":"25010283"},{"database":"DOI","id":"10.1016/j.virol.2014.05.008"}],"title":"Interaction of structural core protein of classical swine fever virus with endoplasmic reticulum-associated degradation pathway protein OS9.","publicationDate":"2014","journal":"Virology","firstPage":"173","lastPage":"179","volume":"460"},"referencePositions":["INTERACTION WITH HOST OS9 (CAPSID PROTEIN C)"]},{"referenceNumber":27,"citation":{"id":"24189547","citationType":"journal article","authors":["Largo E.","Gladue D.P.","Huarte N.","Borca M.V.","Nieva J.L."],"citationCrossReferences":[{"database":"PubMed","id":"24189547"},{"database":"DOI","id":"10.1016/j.antiviral.2013.10.015"}],"title":"Pore-forming activity of pestivirus p7 in a minimal model system supports genus-specific viroporin function.","publicationDate":"2014","journal":"Antiviral Res.","firstPage":"30","lastPage":"36","volume":"101"},"referencePositions":["FUNCTION (VIROPORIN P7)"]},{"referenceNumber":28,"citation":{"id":"26041303","citationType":"journal article","authors":["Li S.","Wang J.","He W.R.","Feng S.","Li Y.","Wang X.","Liao Y.","Qin H.Y.","Li L.F.","Dong H.","Sun Y.","Luo Y.","Qiu H.J."],"citationCrossReferences":[{"database":"PubMed","id":"26041303"},{"database":"DOI","id":"10.1128/jvi.00429-15"}],"title":"Thioredoxin 2 Is a Novel E2-Interacting Protein That Inhibits the Replication of Classical Swine Fever Virus.","publicationDate":"2015","journal":"J. Virol.","firstPage":"8510","lastPage":"8524","volume":"89"},"referencePositions":["INTERACTION WITH HOST TRX2 (ENVELOPE GLYCOPROTEIN E2)"]},{"referenceNumber":29,"citation":{"id":"25694590","citationType":"journal article","authors":["Chen J.","He W.R.","Shen L.","Dong H.","Yu J.","Wang X.","Yu S.","Li Y.","Li S.","Luo Y.","Sun Y.","Qiu H.J."],"citationCrossReferences":[{"database":"PubMed","id":"25694590"},{"database":"DOI","id":"10.1128/jvi.00019-15"}],"title":"The laminin receptor is a cellular attachment receptor for classical Swine Fever virus.","publicationDate":"2015","journal":"J. Virol.","firstPage":"4894","lastPage":"4906","volume":"89"},"referencePositions":["INTERACTION WITH HOST RPSA (E(RNS) GLYCOPROTEIN)","FUNCTION (E(RNS) GLYCOPROTEIN)"]},{"referenceNumber":30,"citation":{"id":"27334592","citationType":"journal article","authors":["Gottipati K.","Holthauzen L.M.","Ruggli N.","Choi K.H."],"citationCrossReferences":[{"database":"PubMed","id":"27334592"},{"database":"DOI","id":"10.1128/jvi.00318-16"}],"title":"Pestivirus Npro Directly Interacts with Interferon Regulatory Factor 3 Monomer and Dimer.","publicationDate":"2016","journal":"J. Virol.","firstPage":"7740","lastPage":"7747","volume":"90"},"referencePositions":["FUNCTION (N-TERMINAL PROTEASE)","INTERACTION WITH HOST IRF3 (N-TERMINAL PROTEASE)"]},{"referenceNumber":31,"citation":{"id":"28290554","citationType":"journal article","authors":["Riedel C.","Lamp B.","Hagen B.","Indik S.","Ruemenapf T."],"citationCrossReferences":[{"database":"PubMed","id":"28290554"},{"database":"DOI","id":"10.1038/srep44459"}],"title":"The core protein of a pestivirus protects the incoming virus against IFN-induced effectors.","publicationDate":"2017","journal":"Sci. Rep.","firstPage":"44459","lastPage":"44459","volume":"7"},"referencePositions":["FUNCTION (CAPSID PROTEIN C)","SUBCELLULAR LOCATION (CAPSID PROTEIN C)"]},{"referenceNumber":32,"citation":{"id":"28751780","citationType":"journal article","authors":["Lv H.","Dong W.","Cao Z.","Li X.","Wang J.","Qian G.","Lv Q.","Wang C.","Guo K.","Zhang Y."],"citationCrossReferences":[{"database":"PubMed","id":"28751780"},{"database":"DOI","id":"10.1038/s41598-017-06934-1"}],"title":"TRAF6 is a novel NS3-interacting protein that inhibits classical swine fever virus replication.","publicationDate":"2017","journal":"Sci. Rep.","firstPage":"6737","lastPage":"6737","volume":"7"},"referencePositions":["FUNCTION (NON-STRUCTURAL PROTEIN 3)","INTERACTION WITH HOST TRAF6 (NON-STRUCTURAL PROTEIN 3)"],"referenceComments":[{"value":"Shimen","type":"STRAIN"}]},{"referenceNumber":33,"citation":{"id":"28848503","citationType":"journal article","authors":["Lin J.","Wang C.","Zhang L.","Wang T.","Zhang J.","Liang W.","Li C.","Qian G.","Ouyang Y.","Guo K.","Zhang Y."],"citationCrossReferences":[{"database":"PubMed","id":"28848503"},{"database":"DOI","id":"10.3389/fmicb.2017.01468"}],"title":"Rab5 Enhances Classical Swine Fever Virus Proliferation and Interacts with Viral NS4B Protein to Facilitate Formation of NS4B Related Complex.","publicationDate":"2017","journal":"Front. Microbiol.","firstPage":"1468","lastPage":"1468","volume":"8"},"referencePositions":["FUNCTION (NON-STRUCTURAL PROTEIN 4B)","INTERACTION WITH HOST RAB5 (NON-STRUCTURAL PROTEIN 4B)","SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4B)","SUBCELLULAR LOCATION (SERINE PROTEASE NS3)","SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 5A)"]},{"referenceNumber":34,"citation":{"id":"29235980","citationType":"journal article","authors":["Tucakov A.K.","Yavuz S.","Schuermann E.M.","Mischler M.","Klingebeil A.","Meyers G."],"citationCrossReferences":[{"database":"PubMed","id":"29235980"},{"database":"DOI","id":"10.1099/jgv.0.000990"}],"title":"dimerization via pseudoreversion partially restores virulence of classical swine fever virus.","publicationDate":"2018","journal":"J. Gen. Virol.","firstPage":"86","lastPage":"96","volume":"99"},"referencePositions":["FUNCTION (E(RNS) GLYCOPROTEIN)","SUBUNIT (E(RNS) GLYCOPROTEIN)"]},{"referenceNumber":35,"citation":{"id":"29844394","citationType":"journal article","authors":["Qian G.","Lv H.","Lin J.","Li X.","Lv Q.","Wang T.","Zhang J.","Dong W.","Guo K.","Zhang Y."],"citationCrossReferences":[{"database":"PubMed","id":"29844394"},{"database":"DOI","id":"10.1038/s41598-018-26777-8"}],"title":"FHC, an NS4B-interacting Protein, Enhances Classical Swine Fever Virus Propagation and Acts Positively in Viral Anti-apoptosis.","publicationDate":"2018","journal":"Sci. Rep.","firstPage":"8318","lastPage":"8318","volume":"8"},"referencePositions":["FUNCTION (NON-STRUCTURAL PROTEIN 4B)","INTERACTION WITH HOST FTH1 (NON-STRUCTURAL PROTEIN 4B)","SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4B)"]},{"referenceNumber":36,"citation":{"id":"31517388","citationType":"journal article","authors":["Xu C.","Feng L.","Chen P.","Li A.","Guo S.","Jiao X.","Zhang C.","Zhao Y.","Jin X.","Zhong K.","Guo Y.","Zhu H.","Han L.","Yang G.","Li H.","Wang Y."],"citationCrossReferences":[{"database":"PubMed","id":"31517388"},{"database":"DOI","id":"10.1002/jmv.25595"}],"title":"Viperin inhibits classical swine fever virus replication by interacting with viral nonstructural 5A protein.","publicationDate":"2020","journal":"J. Med. Virol.","firstPage":"149","lastPage":"160","volume":"92"},"referencePositions":["INTERACTION WITH HOST RSAD2 (NON-STRUCTURAL PROTEIN 5A)"]},{"referenceNumber":37,"citation":{"id":"33684175","citationType":"journal article","authors":["Yuan F.","Li D.","Li C.","Zhang Y.","Song H.","Li S.","Deng H.","Gao G.F.","Zheng A."],"citationCrossReferences":[{"database":"PubMed","id":"33684175"},{"database":"DOI","id":"10.1371/journal.ppat.1009393"}],"title":"ADAM17 is an essential attachment factor for classical swine fever virus.","publicationDate":"2021","journal":"PLoS Pathog.","firstPage":"e1009393","lastPage":"e1009393","volume":"17"},"referencePositions":["FUNCTION (ENVELOPE GLYCOPROTEIN E2)","INTERACTION WITH HOST ADAM17 (ENVELOPE GLYCOPROTEIN E2)"]},{"referenceNumber":38,"citation":{"id":"37796122","citationType":"journal article","authors":["Chen R.","Han X.","Xu H.","Xu J.","Cao T.","Shan Y.","He F.","Fang W.","Li X."],"citationCrossReferences":[{"database":"PubMed","id":"37796122"},{"database":"DOI","id":"10.1128/jvi.01115-23"}],"title":"N-terminal domain of classical swine fever virus Npro induces proteasomal degradation of specificity protein 1 with reduced HDAC1 expression to evade from innate immune responses.","publicationDate":"2023","journal":"J. Virol.","firstPage":"e0111523","lastPage":"e0111523","volume":"97"},"referencePositions":["FUNCTION (N-TERMINAL PROTEASE)","INTERACTION WITH HOST SP1 (N-TERMINAL PROTEASE)"],"referenceComments":[{"value":"Shimen","type":"STRAIN"}]},{"referenceNumber":39,"citation":{"id":"25653438","citationType":"journal article","authors":["Tortorici M.A.","Duquerroy S.","Kwok J.","Vonrhein C.","Perez J.","Lamp B.","Bricogne G.","Ruemenapf T.","Vachette P.","Rey F.A."],"citationCrossReferences":[{"database":"PubMed","id":"25653438"},{"database":"DOI","id":"10.1128/jvi.03165-14"}],"title":"X-ray structure of the pestivirus NS3 helicase and its conformation in solution.","publicationDate":"2015","journal":"J. Virol.","firstPage":"4356","lastPage":"4371","volume":"89"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1782-2280"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"4CBG"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4CBH"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4CBI"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4CBL"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4CBM"}]},{"referenceNumber":40,"citation":{"id":"28151973","citationType":"journal article","authors":["Dubrau D.","Tortorici M.A.","Rey F.A.","Tautz N."],"citationCrossReferences":[{"database":"PubMed","id":"28151973"},{"database":"DOI","id":"10.1371/journal.ppat.1006134"}],"title":"A positive-strand RNA virus uses alternative protein-protein interactions within a viral protease/cofactor complex to switch between RNA replication and virion morphogenesis.","publicationDate":"2017","journal":"PLoS Pathog.","firstPage":"E1006134","lastPage":"E1006134","volume":"13"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 1590-2280","INTERACTION WITH NS4A (SERINE PROTEASE NS3)"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"5MZ4"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"J04358","properties":[{"key":"ProteinId","value":"AAA43844.2"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_RNA"}]},{"database":"PDB","id":"4CBG","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.82 A"},{"key":"Chains","value":"A/B/C/D=1782-2280"}]},{"database":"PDB","id":"4CBH","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.51 A"},{"key":"Chains","value":"A/B/C/D=1782-2280"}]},{"database":"PDB","id":"4CBI","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.00 A"},{"key":"Chains","value":"A/B/C/D=1782-2280"}]},{"database":"PDB","id":"4CBL","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.05 A"},{"key":"Chains","value":"A/B/C/D=1792-2280"}]},{"database":"PDB","id":"4CBM","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.27 A"},{"key":"Chains","value":"A/B/C/D=1782-2280"}]},{"database":"PDB","id":"5MZ4","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.05 A"},{"key":"Chains","value":"A/B=1590-2280, A/B=2293-2329"}]},{"database":"PDBsum","id":"4CBG","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"4CBH","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"4CBI","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"4CBL","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"4CBM","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"5MZ4","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P19712","properties":[{"key":"Description","value":"-"}]},{"database":"IntAct","id":"P19712","properties":[{"key":"Interactions","value":"96"}]},{"database":"MEROPS","id":"C53.001","properties":[{"key":"Description","value":"-"}]},{"database":"MEROPS","id":"S31.001","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.4.21.113","properties":[{"key":"OrganismId","value":"1439"}]},{"database":"GO","id":"GO:0030430","properties":[{"key":"GoTerm","value":"C:host cell cytoplasm"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17215286"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28848503"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29844394"}]},{"database":"GO","id":"GO:0020002","properties":[{"key":"GoTerm","value":"C:host cell plasma membrane"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28290554"}]},{"database":"GO","id":"GO:0044228","properties":[{"key":"GoTerm","value":"C:host cell surface"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28290554"}]},{"database":"GO","id":"GO:0055036","properties":[{"key":"GoTerm","value":"C:virion membrane"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28290554"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0015267","properties":[{"key":"GoTerm","value":"F:channel activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0004197","properties":[{"key":"GoTerm","value":"F:cysteine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0033897","properties":[{"key":"GoTerm","value":"F:ribonuclease T2 activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15113930"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003724","properties":[{"key":"GoTerm","value":"F:RNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"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:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070008","properties":[{"key":"GoTerm","value":"F:serine-type exopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0098670","properties":[{"key":"GoTerm","value":"P:entry receptor-mediated virion attachment to host cell"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0039654","properties":[{"key":"GoTerm","value":"P:fusion of virus membrane with host endosome membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0034220","properties":[{"key":"GoTerm","value":"P:monoatomic ion transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0046718","properties":[{"key":"GoTerm","value":"P:symbiont entry into host cell"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0039520","properties":[{"key":"GoTerm","value":"P:symbiont-mediated activation of host autophagy"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"database":"GO","id":"GO:0039548","properties":[{"key":"GoTerm","value":"P:symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-KW"}]},{"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":"cd17931","properties":[{"key":"EntryName","value":"DEXHc_viral_Ns3"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd23201","properties":[{"key":"EntryName","value":"Pestivirus_RdRp"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.320.20:FF:000001","properties":[{"key":"EntryName","value":"Envelope glycoprotein E2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.270:FF:000083","properties":[{"key":"EntryName","value":"Genome polyprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:001125","properties":[{"key":"EntryName","value":"Genome polyprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:001127","properties":[{"key":"EntryName","value":"Genome polyprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.730.10:FF:000005","properties":[{"key":"EntryName","value":"Genome polyprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.270","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.60.40.4200","properties":[{"key":"EntryName","value":"Pestivirus envelope glycoprotein E2, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.320.20","properties":[{"key":"EntryName","value":"Pestivirus envelope glycoprotein E2, domain A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.3000","properties":[{"key":"EntryName","value":"Pestivirus envelope glycoprotein E2, domain B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.140.40","properties":[{"key":"EntryName","value":"Pestivirus Npro endopeptidase C53, interaction domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.730.10","properties":[{"key":"EntryName","value":"Ribonuclease T2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR021824","properties":[{"key":"EntryName","value":"Capsid-C_pestivirus"}]},{"database":"InterPro","id":"IPR043502","properties":[{"key":"EntryName","value":"DNA/RNA_pol_sf"}]},{"database":"InterPro","id":"IPR011492","properties":[{"key":"EntryName","value":"Flavi_DEAD"}]},{"database":"InterPro","id":"IPR014001","properties":[{"key":"EntryName","value":"Helicase_ATP-bd"}]},{"database":"InterPro","id":"IPR001650","properties":[{"key":"EntryName","value":"Helicase_C-like"}]},{"database":"InterPro","id":"IPR022120","properties":[{"key":"EntryName","value":"NS2"}]},{"database":"InterPro","id":"IPR030399","properties":[{"key":"EntryName","value":"NS2_C74"}]},{"database":"InterPro","id":"IPR049486","properties":[{"key":"EntryName","value":"NS3-hel_C_flaviviridae"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR008751","properties":[{"key":"EntryName","value":"Peptidase_C53"}]},{"database":"InterPro","id":"IPR042542","properties":[{"key":"EntryName","value":"Peptidase_C53_interaction"}]},{"database":"InterPro","id":"IPR032521","properties":[{"key":"EntryName","value":"Pestivirus_E2"}]},{"database":"InterPro","id":"IPR042309","properties":[{"key":"EntryName","value":"Pestivirus_E2_A"}]},{"database":"InterPro","id":"IPR042310","properties":[{"key":"EntryName","value":"Pestivirus_E2_B"}]},{"database":"InterPro","id":"IPR042311","properties":[{"key":"EntryName","value":"Pestivirus_E2_D"}]},{"database":"InterPro","id":"IPR000280","properties":[{"key":"EntryName","value":"Pestivirus_NS3_S31"}]},{"database":"InterPro","id":"IPR043128","properties":[{"key":"EntryName","value":"Rev_trsase/Diguanyl_cyclase"}]},{"database":"InterPro","id":"IPR007094","properties":[{"key":"EntryName","value":"RNA-dir_pol_PSvirus"}]},{"database":"InterPro","id":"IPR002166","properties":[{"key":"EntryName","value":"RNA_pol_HCV"}]},{"database":"InterPro","id":"IPR036430","properties":[{"key":"EntryName","value":"RNase_T2-like_sf"}]},{"database":"InterPro","id":"IPR033130","properties":[{"key":"EntryName","value":"RNase_T2_His_AS_2"}]},{"database":"PANTHER","id":"PTHR18934","properties":[{"key":"EntryName","value":"ATP-DEPENDENT RNA HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR18934:SF91","properties":[{"key":"EntryName","value":"PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11889","properties":[{"key":"EntryName","value":"Capsid_pestivir"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20907","properties":[{"key":"EntryName","value":"Flav_NS3-hel_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07652","properties":[{"key":"EntryName","value":"Flavi_DEAD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00271","properties":[{"key":"EntryName","value":"Helicase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05550","properties":[{"key":"EntryName","value":"Peptidase_C53"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12387","properties":[{"key":"EntryName","value":"Peptidase_C74"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05578","properties":[{"key":"EntryName","value":"Peptidase_S31"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16329","properties":[{"key":"EntryName","value":"Pestivirus_E2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00998","properties":[{"key":"EntryName","value":"RdRP_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00729","properties":[{"key":"EntryName","value":"CDVENDOPTASE"}]},{"database":"SMART","id":"SM00487","properties":[{"key":"EntryName","value":"DEXDc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00490","properties":[{"key":"EntryName","value":"HELICc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56672","properties":[{"key":"EntryName","value":"DNA/RNA polymerases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55895","properties":[{"key":"EntryName","value":"Ribonuclease Rh-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51192","properties":[{"key":"EntryName","value":"HELICASE_ATP_BIND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51194","properties":[{"key":"EntryName","value":"HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51692","properties":[{"key":"EntryName","value":"PESTIVIRUS_NS2_PRO"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51535","properties":[{"key":"EntryName","value":"PESTIVIRUS_NS3PRO"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51876","properties":[{"key":"EntryName","value":"PV_NPRO"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50507","properties":[{"key":"EntryName","value":"RDRP_SSRNA_POS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00531","properties":[{"key":"EntryName","value":"RNASE_T2_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MELNHFELLYKTSKQKPVGVEEPVYDTAGRPLFGNPSEVHPQSTLKLPHDRGRGDIRTTLRDLPRKGDCRSGNHLGPVSGIYIKPGPVYYQDYTGPVYHRAPLEFFDEAQFCEVTKRIGRVTGSDGKLYHIYVCVDGCILLKLAKRGTPRTLKWIRNFTNCPLWVTSCSDDGASGSKDKKPDRMNKGKLKIAPREHEKDSKTKPPDATIVVEGVKYQIKKKGKVKGKNTQDGLYHNKNKPPESRKKLEKALLAWAVITILLYQPVAAENITQWNLSDNGTNGIQRAMYLRGVNRSLHGIWPEKICKGVPTHLATDTELKEIRGMMDASERTNYTCCRLQRHEWNKHGWCNWYNIDPWIQLMNRTQTNLTEGPPDKECAVTCRYDKNTDVNVVTQARNRPTTLTGCKKGKNFSFAGTVIEGPCNFNVSVEDILYGDHECGSLLQDTALYLLDGMTNTIENARQGAARVTSWLGRQLSTAGKKLERRSKTWFGAYALSPYCNVTRKIGYIWYTNNCTPACLPKNTKIIGPGKFDTNAEDGKILHEMGGHLSEFLLLSLVILSDFAPETASTLYLILHYAIPQSHEEPEGCDTNQLNLTVKLRTEDVVPSSVWNIGKYVCVRPDWWPYETKVALLFEEAGQVIKLVLRALRDLTRVWNSASTTAFLICLIKVLRGQVVQGIIWLLLVTGAQGRLACKEDYRYAISSTNEIGLLGAEGLTTTWKEYSHGLQLDDGTVKAVCTAGSFKVTALNVVSRRYLASLHKRALPTSVTFELLFDGTNPAIEEMDDDFGFGLCPFDTSPVIKGKYNTTLLNGSAFYLVCPIGWTGVVECTAVSPTTLRTEVVKTFRRDKPFPHRVDCVTTIVEKEDLFHCKLGGNWTCVKGDPVTYKGGQVKQCRWCGFEFKEPYGLPHYPIGKCILTNETGYRVVDSTDCNRDGVVISTEGEHECLIGNTTVKVHALDERLGPMPCRPKEIVSSEGPVRKTSCTFNYTKTLRNKYYEPRDSYFQQYMLKGEYQYWFNLDVTDHHTDYFAEFVVLVVVALLGGRYVLWLIVTYIILTEQLAAGLQLGQGEVVLIGNLITHTDNEVVVYFLLLYLVIRDEPIKKWILLLFHAMTNNPVKTITVALLMISGVAKGGKIDGGWQRQPVTSFDIQLALAVVVVVVMLLAKRDPTTFPLVITVATLRTAKITNGFSTDLVIATVSAALLTWTYISDYYKYKTWLQYLVSTVTGIFLIRVLKGIGELDLHAPTLPSHRPLFYILVYLISTAVVTRWNLDVAGLLLQCVPTLLMVFTMWADILTLILILPTYELTKLYYLKEVKIGAERGWLWKTNYKRVNDIYEVDQTSEGVYLFPSKQRTSAITSTMLPLIKAILISCISNKWQLIYLLYLIFEVSYYLHKKVIDEIAGGTNFVSRLVAALIEVNWAFDNEEVKGLKKFFLLSSRVKELIIKHKVRNEVVVRWFGDEEIYGMPKLIGLVKAATLSRNKHCMLCTVCEDRDWRGETCPKCGRFGPPVVCGMTLADFEEKHYKRIFIREDQSGGPLREEHAGYLQYKARGQLFLRNLPVLATKVKMLLVGNLGTEIGDLEHLGWVLRGPAVCKKVTEHERCTTSIMDKLTAFFGVMPRGTTPRAPVRFPTSLLKIRRGLETGWAYTHQGGISSVDHVTCGKDLLVCDTMGRTRVVCQSNNKMTDESEYGVKTDSGCPEGARCYVFNPEAVNISGTKGAMVHLQKTGGEFTCVTASGTPAFFDLKNLKGWSGLPIFEASSGRVVGRVKVGKNEDSKPTKLMSGIQTVSKSATDLTEMVKKITTMNRGEFRQITLATGAGKTTELPRSVIEEIGRHKRVLVLIPLRAAAESVYQYMRQKHPSIAFNLRIGEMKEGDMATGITYASYGYFCQMSQPKLRAAMVEYSFIFLDEYHCATPEQLAIMGKIHRFSENLRVVAMTATPAGTVTTTGQKHPIEEFIAPEVMKGEDLGSEYLDIAGLKIPVEEMKNNMLVFVPTRNMAVEAAKKLKAKGYNSGYYYSGEDPSNLRVVTSQSPYVVVATNAIESGVTLPDLDVVVDTGLKCEKRIRLSPKMPFIVTGLKRMAVTIGEQAQRRGRVGRVKPGRYYRSQETPVGSKDYHYDLLQAQRYGIEDGINITKSFREMNYDWSLYEEDSLMITQLEILNNLLISEELPMAVKNIMARTDHPEPIQLAYNSYETQVPVLFPKIRNGEVTDTYDNYTFLNARKLGDDVPPYVYATEDEDLAVELLGLDWPDPGNQGTVEAGRALKQVVGLSTAENALLVALFGYVGYQALSKRHIPVVTDIYSVEDHRLEDTTHLQYAPNAIKTEGKETELKELAQGDVQRCVEAVTNYAREGIQFMKSQALKVRETPTYKETMNTVADYVKKFIEALTDSKEDIIKYGLWGAHTALYKSIGARLGHETAFATLVVKWLAFGGESISDHIKQAATDLVVYYIINRPQFPGDTETQQEGRKFVASLLVSALATYTYKSWNYNNLSKIVEPALATLPYAAKALKLFAPTRLESVVILSTAIYKTYLSIRRGKSDGLLGTGVSAAMEIMSQNPVSVGIAVMLGVGAVAAHNAIEASEQKRTLLMKVFVKNFLDQAATDELVKESPEKIIMALFEAVQTVGNPLRLVYHLYGVFYKGWEAKELAQRTAGRNLFTLIMFEAVELLGVDSEGKIRQLSSNYILELLYKFRDNIKSSVREIAISWAPAPFSCDWTPTDDRIGLPHENYLRVETKCPCGYRMKAVKNCAGELRLLEEGGSFLCRNKFGRGSQNYRVTKYYDDNLSEIKPVIRMEGHVELYYKGATIKLDFNNSKTVLATDKWEVDHSTLVRALKRYTGAGYRGAYLGEKPNHKHLIQRDCATITKDKVCFIKMKRGCAFTYDLSLHNLTRLIELVHKNNLEDREIPAVTVTTWLAYTFVNEDIGTIKPTFGEKVTPEKQEEVVLQPAVVVDTTDVAVTVVGETSTMTTGETPTTFTSLGSDSKVRQVLKLGVDDGQYPGPNQQRASLLEAIQGVDERPSVLILGSDKATSNRVKTAKNVKIYRSRDPLELREMMKRGKILVVALSRVDTALLKFVDYKGTFLTRETLEALSLGKPKKRDITKAEAQWLLRLEDQIEELPDWFAAKEPIFLEANIKRDKYHLVGDIATIKEKAKQLGATDSTKISKEVGAKVYSMKLSNWVIQEENKQGSLAPLFEELLQQCPPGGQNKTTHMVSAYQLAQGNWVPVSCHVFMGTIPARRTKTHPYEAYVKLRELVDEHKMKALCGGSGLSKHNEWVIGKVKYQGNLRTKHMLNPGKVAEQLHREGYRHNVYNKTIGSVMTATGIRLEKLPVVRAQTDTTNFHQAIRDKIDKEENLQTPGLHKKLMEVFNALKRPELEASYDAVDWEELERGINRKGAAGFFERKNIGEVLDSEKNKVEEVIDSLKKGRNIRYYETAIPKNEKRDVNDDWTAGDFVDEKKPRVIQYPEAKTRLAITKVMYKWVKQKPVVIPGYEGKTPLFQIFDKVKKEWDQFQNPVAVSFDTKAWDTQVTTRDLELIRDIQKFYFKKKWHKFIDTLTKHMSEVPVISADGEVYIRKGQRGSGQPDTSAGNSMLNVLTMVYAFCEATGVPYKSFDRVAKIHVCGDDGFLITERALGEKFASKGVQILYEAGKPQKITEGDKMKVAYQFDDIEFCSHTPVQVRWSDNTSSYMPGRNTTTILAKMATRLDSSGERGTIAYEKAVAFSFLLMYSWNPLIRRICLLVLSTELQVRPGKSTTYYYEGDPISAYKEVIGHNLFDLKRTSFEKLAKLNLSMSTLGVWTRHTSKRLLQDCVNVGTKEGNWLVNADRLVSSKTGNRYIPGEGHTLQGKHYEELILARKPIGNFEGTDRYNLGPIVNVVLRRLKIMMMALIGRGV","length":3898,"molWeight":438578,"crc64":"2C1F17B8A359D0F6","md5":"CA816A4F6946762180C8206870DAA154"},"extraAttributes":{"countByCommentType":{"FUNCTION":13,"CATALYTIC ACTIVITY":4,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":9,"INTERACTION":4,"SUBCELLULAR LOCATION":8,"INDUCTION":1,"DOMAIN":1,"PTM":3,"SIMILARITY":1},"countByFeatureType":{"Chain":14,"Transmembrane":10,"Domain":6,"Region":4,"Motif":1,"Compositional bias":2,"Active site":9,"Binding site":5,"Site":13,"Glycosylation":30,"Disulfide bond":7,"Natural variant":2,"Mutagenesis":17,"Beta strand":43,"Helix":30,"Turn":5},"uniParcId":"UPI0000131E1A"}}