{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P19711","uniProtkbId":"POLG_BVDVN","entryAudit":{"firstPublicDate":"1991-02-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-02-01","entryVersion":195,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Bovine viral diarrhea virus (isolate NADL)","commonName":"BVDV","synonyms":["Mucosal disease virus"],"taxonId":11100,"lineage":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Orthopestivirus","Orthopestivirus bovis"]},"organismHosts":[{"scientificName":"Bos taurus","commonName":"Bovine","taxonId":9913}],"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":"p14"}}]},{"recommendedName":{"fullName":{"value":"E(rns) glycoprotein"}},"alternativeNames":[{"fullName":{"value":"gp44/48"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}],"value":"4.6.1.19"}]}]},{"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:0000250","source":"UniProtKB","id":"P19712"}],"value":"Viroporin p7"}}},{"recommendedName":{"fullName":{"value":"Non-structural protein 2-3"}}},{"recommendedName":{"fullName":{"value":"Cysteine protease NS2"},"ecNumbers":[{"value":"3.4.22.-"}]},"alternativeNames":[{"fullName":{"value":"Non-structural protein 2"}},{"fullName":{"value":"p54"}}]},{"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"}},{"fullName":{"value":"p80"}}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 4A"},"shortNames":[{"value":"NS4A"}]},"alternativeNames":[{"fullName":{"value":"p10"}}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 4B"},"shortNames":[{"value":"NS4B"}]},"alternativeNames":[{"fullName":{"value":"p30"}}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 5A"},"shortNames":[{"value":"NS5A"}]},"alternativeNames":[{"fullName":{"value":"p58"}}]},{"recommendedName":{"fullName":{"value":"RNA-directed RNA polymerase"},"ecNumbers":[{"value":"2.7.7.48"}]},"alternativeNames":[{"fullName":{"value":"NS5B"}},{"fullName":{"value":"p75"}}]}]},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17531282"}],"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 (PubMed:17531282)"}],"commentType":"FUNCTION","molecule":"N-terminal protease"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19712"}],"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":"Q96662"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10644844"}],"value":"Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans (PubMed:10644844). Also possesses intrinsic ribonuclease (RNase) activity that can inhibit the production of type I interferon and assist in the development of persistent infections (By similarity)"}],"commentType":"FUNCTION","molecule":"E(rns) glycoprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"14747544"}],"value":"E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis"}],"commentType":"FUNCTION","molecule":"Envelope glycoprotein E1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23569276"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"14747544"}],"value":"E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (Probable). Probably functions as a coeffector of fusion providing structural integrity to the fusion complex and possibly controlling exposure of the fusion motif in E1 (PubMed:23569276)"}],"commentType":"FUNCTION","molecule":"Envelope glycoprotein E2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19712"}],"value":"Plays an essential role in the virus replication cycle by acting as a viroporin (By similarity). Forms ion conductive pores, which alters the cell permeability allowing the transport of ions and other small molecules (By similarity). Forms a leader sequence to properly orient NS2 in the membrane"}],"commentType":"FUNCTION","molecule":"Viroporin p7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14963137"}],"value":"Uncleaved NS2-3 is required for production of infectious virus"}],"commentType":"FUNCTION","molecule":"Non-structural protein 2-3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19712"}],"value":"Plays a role in the regulation of viral RNA replication"}],"commentType":"FUNCTION","molecule":"Cysteine protease NS2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19712"}],"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. Interacts with NS5B to enhance RNA-dependent RNA polymerase activity"}],"commentType":"FUNCTION","molecule":"Serine protease NS3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19712"}],"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":"P19712"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34097933"}],"value":"Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). Plays a role in the inhibition of host innate immune response by inhibiting RIGI/IFIH1-mediated IFN-beta production (PubMed:34097933)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 4B"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15070734"}],"value":"Replicates the viral (+) and (-) genome. Initiates the primer-independent RNA replication via a de novo mechanism requiring GTP (PubMed:15070734)"}],"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":"CATALYTIC ACTIVITY","molecule":"E(rns) glycoprotein","reaction":{"name":"a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:68052"},{"database":"Rhea","id":"RHEA-COMP:10463"},{"database":"Rhea","id":"RHEA-COMP:13936"},{"database":"Rhea","id":"RHEA-COMP:17355"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:83062"},{"database":"ChEBI","id":"CHEBI:138284"},{"database":"ChEBI","id":"CHEBI:173118"}],"ecNumber":"4.6.1.19","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:68053"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}]}]},{"commentType":"CATALYTIC ACTIVITY","molecule":"E(rns) glycoprotein","reaction":{"name":"a ribonucleotidyl-ribonucleotide-RNA = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67796"},{"database":"Rhea","id":"RHEA-COMP:10464"},{"database":"Rhea","id":"RHEA-COMP:13936"},{"database":"Rhea","id":"RHEA-COMP:17355"},{"database":"ChEBI","id":"CHEBI:83064"},{"database":"ChEBI","id":"CHEBI:138284"},{"database":"ChEBI","id":"CHEBI:173118"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67797"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}]}]},{"commentType":"CATALYTIC ACTIVITY","molecule":"E(rns) glycoprotein","reaction":{"name":"a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:68056"},{"database":"Rhea","id":"RHEA-COMP:10463"},{"database":"Rhea","id":"RHEA-COMP:10464"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:83062"},{"database":"ChEBI","id":"CHEBI:83064"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:68057"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}],"value":"Inhibited by Zn(2+), which binds the catalytic site"}],"commentType":"ACTIVITY REGULATION","molecule":"E(rns) glycoprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"},{"evidenceCode":"ECO:0000305"}],"value":"Homodimer (By similarity). E(rns) homodimer is disulfide-linked in other strains, but the cysteine involved in the bond is not conserved in isolate NADL (Probable)"}],"commentType":"SUBUNIT","molecule":"E(rns) glycoprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19712"}],"value":"Homodimer; disulfide-linked (By similarity). Heterodimer with E1; disulfide-linked (By similarity)"}],"commentType":"SUBUNIT","molecule":"Envelope glycoprotein E1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19712"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23569276"}],"value":"Homodimer; disulfide-linked (PubMed:23569276). Heterodimer with E1; disulfide-linked (By similarity)"}],"commentType":"SUBUNIT","molecule":"Envelope glycoprotein E2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34097933"}],"value":"Interacts with host IFIH1/MDA5; this interaction is involved in the inhibition of IFN-beta production"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 4B"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P19711","intActId":"EBI-9350498"},"interactantTwo":{"uniProtKBAccession":"P19711","geneName":"-","intActId":"EBI-9350498"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000038031","intActId":"EBI-9612504"},"interactantTwo":{"uniProtKBAccession":"Q95J56","geneName":"DNAJC14","intActId":"EBI-9612178"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000038033","intActId":"EBI-9350731"},"interactantTwo":{"uniProtKBAccession":"F1MUM9","geneName":"ADAR","intActId":"EBI-9350738"},"numberOfExperiments":6,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000038035","intActId":"EBI-9350549"},"interactantTwo":{"uniProtKBAccession":"P68103","geneName":"EEF1A1","intActId":"EBI-352178"},"numberOfExperiments":6,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000038035","intActId":"EBI-9350549"},"interactantTwo":{"uniProtKBAccession":"Q32PH0","geneName":"TRAPPC9","intActId":"EBI-9522367"},"numberOfExperiments":7,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Capsid protein C","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19712"}],"value":"Virion","id":"SL-0274"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"E(rns) glycoprotein","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"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":"10355762"}],"value":"Host membrane","id":"SL-0380"},"topology":{"value":"Peripheral membrane protein","id":"SL-9903"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10355762"}],"value":"Virion membrane","id":"SL-0275"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Envelope glycoprotein E1","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}],"value":"The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. This explains that E1 and E2 are mostly lumenal. After cleavage, the C-terminus transmembrane sequence acts as ER membrane anchor"}]},"subcellularLocations":[{"location":{"value":"Host endoplasmic reticulum membrane","id":"SL-0390"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}],"value":"Single-pass type I membrane protein","id":"SL-9905"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19712"}],"value":"Virion membrane","id":"SL-0275"},"topology":{"value":"Single-pass type I membrane protein","id":"SL-9905"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Envelope glycoprotein E2","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}],"value":"The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. This explains that E1 and E2 are mostly lumenal. After cleavage, the C-terminus transmembrane sequence acts as ER membrane anchor"}]},"subcellularLocations":[{"location":{"value":"Host endoplasmic reticulum membrane","id":"SL-0390"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}],"value":"Single-pass type I membrane protein","id":"SL-9905"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10355762"}],"value":"Virion membrane","id":"SL-0275"},"topology":{"value":"Single-pass type I membrane protein","id":"SL-9905"}}]},{"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:0000250","source":"UniProtKB","id":"P19712"}],"value":"Host cytoplasm","id":"SL-0381"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 4B","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19712"}],"value":"Host cytoplasm","id":"SL-0381"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 5A","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}],"value":"The N-terminus membrane anchor represents an amphipathic helix embedded in plane into the membrane"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Host membrane","id":"SL-0380"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}],"value":"The transmembrane domain is responsible for ER localization"}],"commentType":"DOMAIN","molecule":"Envelope glycoprotein E1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q96662"}],"value":"The transmembrane domain is responsible for ER localization"}],"commentType":"DOMAIN","molecule":"Envelope glycoprotein E2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19712"}],"value":"Heavily glycosylated"}],"commentType":"PTM","molecule":"E(rns) glycoprotein"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"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 (By similarity)"}],"commentType":"PTM"},{"texts":[{"value":"Cleavage between E2 and p7 is partial"}],"commentType":"PTM","molecule":"Genome polyprotein"},{"texts":[{"value":"BVDV is divided in two types: cytopathic and non-cytopathic. Both types of viruses can be found in animals suffering from mucosal disease, as a cytopathic BVDV can develop from a non-cytopathic virus within the infected animal by deletions, mutations or insertions. Both types express uncleaved NS2-3, but cytopathic strains also express NS3. The cytopathic NADL strain contains an insertion (Jiv 90) that potentiate the partial cleavage of NS2-3. Removal of this insertion in the NADL Jiv 90(-) strain results in a non-cytopathic strain in which NS2-3 remains uncleaved"}],"commentType":"MISCELLANEOUS"},{"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":3988,"modifier":"EXACT"}},"description":"Genome polyprotein","featureId":"PRO_0000450891"},{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"N-terminal protease","evidences":[{"evidenceCode":"ECO:0000250"}],"featureId":"PRO_0000038024"},{"type":"Chain","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"Capsid protein 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