{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"K9N7C7","uniProtkbId":"R1AB_MERS1","entryAudit":{"firstPublicDate":"2013-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2013-03-06","entryVersion":79,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012)","commonName":"MERS-CoV","synonyms":["Betacoronavirus England 1"],"taxonId":1263720,"lineage":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Merbecovirus","Betacoronavirus cameli","Middle East respiratory syndrome-related coronavirus"]},"organismHosts":[{"scientificName":"Camelus dromedarius","commonName":"Dromedary","synonyms":["Arabian camel"],"taxonId":9838},{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606}],"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Replicase polyprotein 1ab"},"shortNames":[{"value":"pp1ab"}]},"alternativeNames":[{"fullName":{"value":"ORF1ab polyprotein"}}],"contains":[{"recommendedName":{"fullName":{"value":"Host translation inhibitor nsp1"},"shortNames":[{"value":"nsp1"}]},"alternativeNames":[{"fullName":{"value":"Leader protein"}}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 2"},"shortNames":[{"value":"nsp2"}]},"alternativeNames":[{"fullName":{"value":"p65 homolog"}}]},{"recommendedName":{"fullName":{"value":"Papain-like protease nsp3"},"shortNames":[{"value":"PL-PRO"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"K9N638"}],"value":"3.2.2.-"},{"value":"3.4.19.12"},{"value":"3.4.22.-"}]},"alternativeNames":[{"fullName":{"value":"Non-structural protein 3"},"shortNames":[{"value":"nsp3"}]}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 4"},"shortNames":[{"value":"nsp4"}]}},{"recommendedName":{"fullName":{"value":"3C-like proteinase nsp5"},"shortNames":[{"value":"3CL-PRO"},{"value":"3CLp"}],"ecNumbers":[{"value":"3.4.22.-"}]},"alternativeNames":[{"fullName":{"value":"nsp5"}}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 6"},"shortNames":[{"value":"nsp6"}]}},{"recommendedName":{"fullName":{"value":"Non-structural protein 7"},"shortNames":[{"value":"nsp7"}]}},{"recommendedName":{"fullName":{"value":"Non-structural protein 8"},"shortNames":[{"value":"nsp8"}]}},{"recommendedName":{"fullName":{"value":"Viral protein genome-linked nsp9"}},"alternativeNames":[{"fullName":{"value":"Non-structural protein 9"},"shortNames":[{"value":"nsp9"}]},{"fullName":{"value":"RNA-capping enzyme subunit nsp9"}},{"fullName":{"value":"p12"}}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 10"},"shortNames":[{"value":"nsp10"}]},"alternativeNames":[{"fullName":{"value":"Growth factor-like peptide"},"shortNames":[{"value":"GFL"}]}]},{"recommendedName":{"fullName":{"value":"RNA-directed RNA polymerase nsp12"},"shortNames":[{"value":"Pol"},{"value":"RdRp"}],"ecNumbers":[{"value":"2.7.7.48"},{"value":"2.7.7.50"}]},"alternativeNames":[{"fullName":{"value":"nsp12"}}]},{"recommendedName":{"fullName":{"value":"Helicase nsp13"},"shortNames":[{"value":"Hel"}],"ecNumbers":[{"value":"3.6.4.12"},{"value":"3.6.4.13"}]},"alternativeNames":[{"fullName":{"value":"nsp13"}}]},{"recommendedName":{"fullName":{"value":"Guanine-N7 methyltransferase nsp14"},"shortNames":[{"value":"ExoN"}],"ecNumbers":[{"value":"2.1.1.56"},{"value":"3.1.13.-"}]},"alternativeNames":[{"fullName":{"value":"nsp14"}}]},{"recommendedName":{"fullName":{"value":"Uridylate-specific endoribonuclease nsp15"},"ecNumbers":[{"value":"4.6.1.-"}]},"alternativeNames":[{"fullName":{"value":"NendoU"}},{"fullName":{"value":"nsp15"}}]},{"recommendedName":{"fullName":{"value":"2'-O-methyltransferase nsp16"},"ecNumbers":[{"value":"2.1.1.57"}]},"alternativeNames":[{"fullName":{"value":"nsp16"}}]}]},"genes":[{"geneName":{"value":"rep"},"orfNames":[{"value":"1a-1b"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein"}],"commentType":"FUNCTION","molecule":"Isoform Replicase polyprotein 1ab"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26311885"}],"value":"Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response"}],"commentType":"FUNCTION","molecule":"Host translation inhibitor nsp1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses"}],"commentType":"FUNCTION","molecule":"Non-structural protein 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTC1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25142582"},{"evidenceCode":"ECO:0000305"}],"value":"Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates, together with nsp4, in the assembly of virally induced cytoplasmic double-membrane vesicles necessary for viral replication. Contains an ADP-ribose hydrolase activity that binds ADP-ribose and catalyzes the removal of mono-ADP-ribose (de-MARylation), usually bound to a glutamate or aspartate (By similarity). ADP-ribose hydrolase activity allows the virus to interfere with the host immune defenses involving poly-ADP-ribose polymerases (PARPs) (Probable). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Also prevents host NF-kappa-B. signaling"}],"commentType":"FUNCTION","molecule":"Papain-like protease nsp3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication"}],"commentType":"FUNCTION","molecule":"Non-structural protein 4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00772"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35594856"}],"value":"Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (By similarity). May cleave human NLRP1 in lung epithelial cells, thereby activating the NLRP1 inflammasome pathway (PubMed:35594856). Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity)"}],"commentType":"FUNCTION","molecule":"3C-like proteinase nsp5"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Plays a role in the initial induction of autophagosomes from host endoplasmic reticulum. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes"}],"commentType":"FUNCTION","molecule":"Non-structural protein 6"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers"}],"commentType":"FUNCTION","molecule":"Non-structural protein 7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers"}],"commentType":"FUNCTION","molecule":"Non-structural protein 8"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Forms a primer, NSP9-pU, which is utilized by the polymerase for the initiation of RNA chains. Interacts with ribosome signal recognition particle RNA (SRP). Together with NSP8, suppress protein integration into the cell membrane, thereby disrupting host immune defenses"}],"commentType":"FUNCTION","molecule":"Viral protein genome-linked nsp9"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation"}],"commentType":"FUNCTION","molecule":"Non-structural protein 10"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"RNA-directed RNA polymerase that catalyzes the transcription of viral genomic and subgenomic RNAs. Acts in complex with nsp7 and nsp8 to transcribe both the minus and positive strands of genomic RNA. The kinase-like NiRAN domain of NSP12 attaches one or more nucleotides to the amino terminus of NSP9, forming a covalent RNA-protein intermediate that serves as transcription/replication primer. Subgenomic RNAs (sgRNAs) are formed by discontinuous transcription: The polymerase has the ability to pause at transcription-regulating sequences (TRS) and jump to the leader TRS, resulting in a major deletion. This creates a series of subgenomic RNAs that are replicated, transcribed and translated. In addition, Nsp12 is a subunit of the viral RNA capping enzyme that catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. Subsequently, the NiRAN domain transfers RNA to GDP, and forms the core cap structure GpppA-RNA"}],"commentType":"FUNCTION","molecule":"RNA-directed RNA polymerase nsp12"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium"}],"commentType":"FUNCTION","molecule":"Helicase nsp13"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Plays a role in viral RNA synthesis through two distinct activities: an N7-guanine methyltransferase activity involved in the formation of the cap structure GpppA-RNA; a proofreading exoribonuclease for RNA replication that reduces the sensitivity of the virus to RNA mutagens. This activity acts on both ssRNA and dsRNA in a 3'-5' direction"}],"commentType":"FUNCTION","molecule":"Guanine-N7 methyltransferase nsp14"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity)"}],"commentType":"FUNCTION","molecule":"Uridylate-specific endoribonuclease nsp15"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system"}],"commentType":"FUNCTION","molecule":"2'-O-methyltransferase nsp16"},{"commentType":"CATALYTIC ACTIVITY","molecule":"Papain-like protease nsp3","reaction":{"name":"4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = L-aspartyl-[protein] + ADP-D-ribose + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54428"},{"database":"Rhea","id":"RHEA-COMP:9867"},{"database":"Rhea","id":"RHEA-COMP:13832"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29961"},{"database":"ChEBI","id":"CHEBI:57967"},{"database":"ChEBI","id":"CHEBI:138102"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"K9N638"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54429"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTC1"}]}]},{"commentType":"CATALYTIC ACTIVITY","molecule":"Papain-like protease nsp3","reaction":{"name":"5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = L-glutamyl-[protein] + ADP-D-ribose + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58248"},{"database":"Rhea","id":"RHEA-COMP:10208"},{"database":"Rhea","id":"RHEA-COMP:15089"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29973"},{"database":"ChEBI","id":"CHEBI:57967"},{"database":"ChEBI","id":"CHEBI:142540"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"K9N638"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:58249"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTC1"}]}]},{"commentType":"CATALYTIC ACTIVITY","molecule":"Papain-like protease nsp3","reaction":{"name":"Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).","ecNumber":"3.4.19.12"}},{"commentType":"CATALYTIC ACTIVITY","molecule":"RNA-directed RNA polymerase nsp12","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":"Helicase nsp13","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":"3.6.4.12"}},{"commentType":"CATALYTIC ACTIVITY","molecule":"Helicase nsp13","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":"2'-O-methyltransferase nsp16","reaction":{"name":"a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67020"},{"database":"Rhea","id":"RHEA-COMP:17167"},{"database":"Rhea","id":"RHEA-COMP:17168"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:156461"},{"database":"ChEBI","id":"CHEBI:167609"}],"ecNumber":"2.1.1.57","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}]}},{"commentType":"CATALYTIC ACTIVITY","molecule":"Uridylate-specific endoribonuclease nsp15","reaction":{"name":"uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-RNA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67732"},{"database":"Rhea","id":"RHEA-COMP:13936"},{"database":"Rhea","id":"RHEA-COMP:17334"},{"database":"Rhea","id":"RHEA-COMP:17335"},{"database":"ChEBI","id":"CHEBI:138284"},{"database":"ChEBI","id":"CHEBI:173079"},{"database":"ChEBI","id":"CHEBI:173080"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}]}},{"commentType":"CATALYTIC ACTIVITY","molecule":"RNA-directed RNA polymerase nsp12","reaction":{"name":"a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67012"},{"database":"Rhea","id":"RHEA-COMP:17165"},{"database":"Rhea","id":"RHEA-COMP:17166"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:167616"},{"database":"ChEBI","id":"CHEBI:167617"}],"ecNumber":"2.7.7.50","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67013"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}]}]},{"commentType":"CATALYTIC ACTIVITY","molecule":"Guanine-N7 methyltransferase nsp14","reaction":{"name":"a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:67008"},{"database":"Rhea","id":"RHEA-COMP:17166"},{"database":"Rhea","id":"RHEA-COMP:17167"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:156461"},{"database":"ChEBI","id":"CHEBI:167617"}],"ecNumber":"2.1.1.56","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:67009"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}]}]},{"commentType":"COFACTOR","molecule":"Uridylate-specific endoribonuclease nsp15","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Likely affects Nsp15 binding to RNA."}]}},{"commentType":"COFACTOR","molecule":"RNA-directed RNA polymerase nsp12","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Interacts with host PHB and PHB2"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Interacts with papain-like protease nsp3 and non-structural protein 6"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Monomer. Homodimer. Only the homodimer shows catalytic activity"}],"commentType":"SUBUNIT","molecule":"3C-like proteinase nsp5"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Interacts with nsp8 and nsp12 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Interacts with nsp7, nsp13 and nsp12 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 8"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Interacts with nsp12"}],"commentType":"SUBUNIT","molecule":"Viral protein genome-linked nsp9"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Interacts with proofreading exoribonuclease nsp14 and 2'-O-methyltransferase nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 10"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Interacts with nsp7 and nsp8 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13. Interacts with nsp9"}],"commentType":"SUBUNIT","molecule":"RNA-directed RNA polymerase nsp12"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0DTD1"}],"value":"Interacts with nsp8 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13"}],"commentType":"SUBUNIT","molecule":"Helicase nsp13"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"chainId":"PRO_0000422441","intActId":"EBI-25592237"},"interactantTwo":{"uniProtKBAccession":"P05161","geneName":"ISG15","intActId":"EBI-746466"},"numberOfExperiments":4,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000422441","intActId":"EBI-25592237"},"interactantTwo":{"uniProtKBAccession":"Q96PM5","geneName":"RCHY1","intActId":"EBI-947779"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000422452","intActId":"EBI-25592093"},"interactantTwo":{"uniProtKBAccession":"K9N7C7","geneName":"rep","chainId":"PRO_0000422446","intActId":"EBI-25592080"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000422452","intActId":"EBI-25592093"},"interactantTwo":{"uniProtKBAccession":"K9N7C7","geneName":"rep","chainId":"PRO_0000422452","intActId":"EBI-25592093"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Papain-like protease nsp3","subcellularLocations":[{"location":{"value":"Host membrane","id":"SL-0380"},"topology":{"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Host cytoplasm","id":"SL-0381"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 4","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Localizes in virally-induced cytoplasmic double-membrane vesicles"}]},"subcellularLocations":[{"location":{"value":"Host membrane","id":"SL-0380"},"topology":{"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"value":"Host cytoplasm","id":"SL-0381"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 6","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Host membrane","id":"SL-0380"},"topology":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Non-structural protein 7","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. 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