{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0DTD1","uniProtkbId":"R1AB_SARS2","entryAudit":{"firstPublicDate":"2020-04-22","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2020-04-22","entryVersion":30,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Severe acute respiratory syndrome coronavirus 2","commonName":"2019-nCoV","synonyms":["SARS-CoV-2"],"taxonId":2697049,"lineage":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus","Betacoronavirus pandemicum"]},"organismHosts":[{"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"}},"alternativeNames":[{"fullName":{"value":"Leader protein"}},{"fullName":{"value":"Non-structural protein 1"},"shortNames":[{"value":"nsp1"}]}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 2"},"shortNames":[{"value":"nsp2"}]},"alternativeNames":[{"fullName":{"value":"p65 homolog"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"32726803"}],"value":"Papain-like protease nsp3"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37242344"}],"value":"3.2.2.-"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32726803"}],"value":"3.4.19.12"},{"value":"3.4.22.-"}]},"alternativeNames":[{"fullName":{"value":"Non-structural protein 3"},"shortNames":[{"value":"nsp3"}]},{"fullName":{"value":"PL2-PRO"}},{"fullName":{"value":"Papain-like proteinase"},"shortNames":[{"value":"PL-PRO"}]}]},{"recommendedName":{"fullName":{"value":"Non-structural protein 4"},"shortNames":[{"value":"nsp4"}]}},{"recommendedName":{"fullName":{"value":"3C-like proteinase nsp5"},"shortNames":[{"value":"3CL-PRO"},{"value":"3CLp"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32198291"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32272481"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40118151"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41289387"}],"value":"3.4.22.69"}]},"alternativeNames":[{"fullName":{"value":"Main protease"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"32272481"}],"value":"Mpro"}]},{"fullName":{"value":"Non-structural protein 5"},"shortNames":[{"value":"nsp5"}]},{"fullName":{"value":"SARS coronavirus main proteinase"}}]},{"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":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"37794589"}],"value":"Viral protein genome-linked nsp9"}},"alternativeNames":[{"fullName":{"value":"Non-structural protein 9"},"shortNames":[{"value":"nsp9"}]},{"fullName":{"value":"RNA-capping enzyme subunit nsp9"}}]},{"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"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"}],"value":"2.7.7.50"}]},"alternativeNames":[{"fullName":{"value":"Non-structural protein 12"},"shortNames":[{"value":"nsp12"}]}]},{"recommendedName":{"fullName":{"value":"Helicase nsp13"},"shortNames":[{"value":"Hel"}],"ecNumbers":[{"value":"3.6.4.12"},{"value":"3.6.4.13"}]},"alternativeNames":[{"fullName":{"value":"Non-structural protein 13"},"shortNames":[{"value":"nsp13"}]}]},{"recommendedName":{"fullName":{"value":"Guanine-N7 methyltransferase nsp14"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"}],"value":"2.1.1.56"},{"value":"3.1.13.-"}]},"alternativeNames":[{"fullName":{"value":"Non-structural protein 14"},"shortNames":[{"value":"nsp14"}]},{"fullName":{"value":"Proofreading exoribonuclease nsp14"},"shortNames":[{"value":"ExoN"}]}]},{"recommendedName":{"fullName":{"value":"Uridylate-specific endoribonuclease nsp15"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33504779"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33564093"}],"value":"4.6.1.-"}]},"alternativeNames":[{"fullName":{"value":"NendoU"}},{"fullName":{"value":"Non-structural protein 15"},"shortNames":[{"value":"nsp15"}]}]},{"recommendedName":{"fullName":{"value":"2'-O-methyltransferase nsp16"},"ecNumbers":[{"value":"2.1.1.57"}]},"alternativeNames":[{"fullName":{"value":"Non-structural protein 16"},"shortNames":[{"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":"Replicase polyprotein 1ab"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32680882"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32908316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32979938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33080218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33479166"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36534661"}],"value":"Inhibits host translation by associating with the open head conformation of the 40S subunit (PubMed:32680882, PubMed:32908316, PubMed:33080218, PubMed:33479166). The C-terminus binds to and obstructs ribosomal mRNA entry tunnel (PubMed:32680882, PubMed:32908316, PubMed:33080218, PubMed:33479166). Thereby inhibits antiviral response triggered by innate immunity or interferons (PubMed:32680882, PubMed:32979938, PubMed:33080218). The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation (By similarity). This inhibits the integrated stress response (ISR) in the infected cell by preventing EIF2S1/eIF2-alpha phosphorylation upstream of stress granule formation and depletes host G3BP1 (PubMed:36534661). Viral mRNAs less susceptible to nsp1-mediated inhibition of translation, because of their 5'-end leader sequence (PubMed:32908316, PubMed:33080218)"}],"commentType":"FUNCTION","molecule":"Host translation inhibitor nsp1"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35878012"}],"value":"Enhances mRNA repression of the 4EHP-GYF2 complex in the host, thereby inhibiting the antiviral response and facilitating SARS-CoV-2 replication. Possibly acts in cooperation with nsp1, which induces ribosome stalling on host mRNA, triggering mRNA repression by the host 4EHP-GYF2 complex which is enhanced by nsp2"}],"commentType":"FUNCTION","molecule":"Non-structural protein 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32578982"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32726803"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32733001"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33727702"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35551511"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37242344"},{"evidenceCode":"ECO:0000305"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32578982"}],"value":"Responsible for the cleavages located at the N-terminus of the replicase polyprotein. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication (PubMed:35551511). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:32733001). Also prevents host NF-kappa-B signaling (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:32726803). Cleaves preferentially ISG15 from antiviral protein IFIH1 (MDA5), but not RIGI (PubMed:33727702). 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 (Probable) (PubMed:37242344). ADP-ribose hydrolase activity allows the virus to interfere with the host immune defenses involving poly-ADP-ribose polymerases (PARPs) (Probable). Plays a role in the formation and maintenance of double membrane vesicles (DMVs) replication organelles (PubMed:35551511). DMVs are formed by nsp3 and nsp4, while nsp6 zippers ER membranes and connects to lipid droplets (PubMed:35551511)"}],"commentType":"FUNCTION","molecule":"Papain-like protease nsp3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35551511"}],"value":"Plays a role in the formation and maintenance of double membrane vesicles (DMVs) replication organelles (PubMed:35551511). DMVs are formed by nsp3 and nsp4, while nsp6 zippers ER membranes and connects to lipid droplets (PubMed:35551511)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32198291"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32272481"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32321856"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35594856"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37073102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38814682"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39773525"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40118151"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41289387"}],"value":"Cleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481). Cleaves and inactivates human TRMT1, preventing tRNA guanine(26)-dimethylation of tRNAs (PubMed:37073102, PubMed:38814682, PubMed:39773525). May cleave human NLRP1 in lung epithelial cells, thereby activating the NLRP1 inflammasome pathway (PubMed:35594856). May cleave human GSDMD, triggering alternative GSDME-mediated epithelial cell death upon activation of the NLRP1 inflammasome, which may enhance the release interleukins 1B, 6, 16 and 18 (PubMed:35594856). Also able to bind an ADP-ribose-1''-phosphate (ADRP) (PubMed:32198291, PubMed:32272481). Cleaves host STIM1 producing two functional fragments: STIM1 N-terminus, which inhibits MAVS-mediated IFNB signaling by disrupting signalosome formation, and STIM1 C-terminus, which suppresses p65-driven IFNB transcription (PubMed:41289387). Inhibits host pyroptosis through the cleavage of host gasdermin D/GSDMD (PubMed:40118151)"}],"commentType":"FUNCTION","molecule":"3C-like proteinase nsp5"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32979938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35551511"}],"value":"Plays a role in the formation and maintenance of double membrane vesicles (DMVs) replication organelles (PubMed:35551511). DMVs are formed by nsp3 and nsp4, while nsp6 zippers ER membranes and connects to lipid droplets (PubMed:35551511). LDs are consumed during DMV formation (PubMed:35551511). Binds to host TBK1 without affecting TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 6"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32277040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32438371"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32526208"}],"value":"Plays a role in viral RNA synthesis (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208). 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 (By similarity)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32277040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32438371"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32526208"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33080218"}],"value":"Plays a role in viral RNA synthesis (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208). 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 (By similarity). Interacts with ribosome signal recognition particle RNA (SRP) (PubMed:33080218). Together with NSP9, suppress protein integration into the cell membrane, thereby disrupting host immune defenses (PubMed:33080218)"}],"commentType":"FUNCTION","molecule":"Non-structural protein 8"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33080218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37794589"}],"value":"Forms a primer, NSP9-pU, which is utilized by the polymerase for the initiation of RNA chains (PubMed:37794589). Interacts with ribosome signal recognition particle RNA (SRP) (PubMed:33080218). Together with NSP8, suppress protein integration into the cell membrane, thereby disrupting host immune defenses (PubMed:33080218)"}],"commentType":"FUNCTION","molecule":"Viral protein genome-linked nsp9"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"}],"value":"Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease (By similarity) and nsp16 2'-O-methyltransferase activities (PubMed:35944563). Therefore plays an essential role in viral mRNAs cap methylation"}],"commentType":"FUNCTION","molecule":"Non-structural protein 10"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35706445"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37794589"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32277040"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32438371"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32526208"}],"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 (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208). 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 (PubMed:37794589). 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 (PubMed:35706445). This creates a series of subgenomic RNAs that are replicated, transcribed and translated (PubMed:35706445). In addition, Nsp12 is a subunit of the viral RNA capping enzyme that catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs (PubMed:35944563). Subsequently, the NiRAN domain transfers RNA to GDP, and forms the core cap structure GpppA-RNA (PubMed:35944563)"}],"commentType":"FUNCTION","molecule":"RNA-directed RNA polymerase nsp12"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32979938"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"33232691"}],"value":"Plays a role in viral RNA synthesis (PubMed:33232691). 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 (By similarity). Binds to host TBK1 and inhibits TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938)"}],"commentType":"FUNCTION","molecule":"Helicase nsp13"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"}],"value":"Plays a role in viral RNA synthesis through two distinct activities. The N7-guanine methyltransferase activity plays a role in the formation of the cap structure GpppA-RNA (PubMed:35944563). The proofreading exoribonuclease reduces the sensitivity of the virus to RNA mutagens during replication (By similarity). This activity acts on both ssRNA and dsRNA in a 3'-5' direction (By similarity)"}],"commentType":"FUNCTION","molecule":"Guanine-N7 methyltransferase nsp14"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33504779"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34562452"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"35706445"}],"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 (PubMed:33504779, PubMed:33564093). 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) (PubMed:33504779, PubMed:33564093). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). May bind genomic dsRNA in association with the replication-transcription complex (RTC), and play a role in nsp12 discontinous transcription (PubMed:34562452, PubMed:35706445)"}],"commentType":"FUNCTION","molecule":"Uridylate-specific endoribonuclease nsp15"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33080218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36285486"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36722972"}],"value":"Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs (PubMed:35944563). N7-methyl guanosine cap is a prerequisite for binding of nsp16 (PubMed:35944563). Therefore, it plays an essential role in cap methylation of viral mRNAs, which is essential to evade the immune system, especially when restricted by human IFIT1 and IFIT3 (PubMed:35944563, PubMed:36722972, PubMed:36285486). May disrupt host mRNA splicing in nucleus by interacting with pre-mRNA Recognition Domains of the U1 and U2 snRNAs (PubMed:33080218)"}],"commentType":"FUNCTION","molecule":"2'-O-methyltransferase nsp16"},{"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:0000269","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32438371"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32526208"}]}},{"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","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}]}},{"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","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}]}},{"commentType":"CATALYTIC ACTIVITY","molecule":"3C-like proteinase nsp5","reaction":{"name":"TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.","ecNumber":"3.4.22.69","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32198291"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32272481"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32321856"}]}},{"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","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32726803"}]}},{"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:0000305","source":"PubMed","id":"37242344"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:54429"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"37242344"}]}]},{"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:0000305","source":"PubMed","id":"37242344"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:58249"},"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"37242344"}]}]},{"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:0000269","source":"PubMed","id":"33504779"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33564093"}]}},{"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:0000269","source":"PubMed","id":"35944563"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:67014"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"}]}]},{"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:0000269","source":"PubMed","id":"35944563"}]}},{"commentType":"COFACTOR","molecule":"Uridylate-specific endoribonuclease nsp15","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33564093"}],"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:0000269","source":"PubMed","id":"35944563"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32726803"}],"value":"Inhibited in vitro by GRL-0617"}],"commentType":"ACTIVITY REGULATION","molecule":"Papain-like protease nsp3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35551511"}],"value":"Inhibited ex vivo by K22. It may shift NSP6 zippering activity towards the nuclear envelope, thereby impairing formation of the NSP6-compartment necessary for viral transcription/replication"}],"commentType":"ACTIVITY REGULATION","molecule":"Non-structural protein 6"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Inhibited by Remdesivir antiviral drug (GS-5734)"}],"commentType":"ACTIVITY REGULATION","molecule":"Guanine-N7 methyltransferase nsp14"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32526208"}],"value":"Inhibited by Remdesivir antiviral drug (GS-5734) through non-obligate RNA chain termination"}],"commentType":"ACTIVITY REGULATION","molecule":"RNA-directed RNA polymerase nsp12"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32198291"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32272481"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32321856"}],"value":"Inhibited by pyridone-containing alpha-ketoamides compounds 13a and 13b. In turn, alpha-ketoamide 13b (tert-butyl (1-((S)-1-(((S)-4-(benzylamino)-3,4-dioxo-1-((S)-2-oxopyrrolidin-3-yl)butan-2-yl)amino)-3-cyclopropyl-1-oxopropan-2-yl)-2-oxo-1,2-dihydropyridin-3-yl)carbamate) inhibits SARS-CoV-2 replication in human lung cells (PubMed:32198291). Inhibited ex vivo by michael acceptor inhibitor N3 (PubMed:32272481). Inhibited ex vivo by compound 11a and 11b (PubMed:32321856)"}],"commentType":"ACTIVITY REGULATION","molecule":"3C-like proteinase nsp5"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35878012"}],"value":"Interacts with host GIGYF2"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32763915"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35044811"}],"value":"May form homohexamers (PubMed:32763915). Interacts with N protein (PubMed:35044811)"}],"commentType":"SUBUNIT","molecule":"Papain-like protease nsp3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32198291"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39223933"}],"value":"3CL-PRO exists as monomer and homodimer. Only the homodimer shows catalytic activity. Interacts with host FBXO22; this interaction promotes the proteasomal degradation of nsp5 (PubMed:39223933)"}],"commentType":"SUBUNIT","molecule":"3C-like proteinase nsp5"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Interacts with PL-PRO and nsp6"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32979938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35551511"}],"value":"Forms homodimers (PubMed:35551511). Interacts with host ZFYVE1 (DFCP1) (PubMed:35551511), which leads to ER and DMVs binding to lipid droplets. Interacts with host TBK1; this interaction decreases IRF3 phosphorylation by 57%, which leads to reduced IFN-beta production"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 6"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32277040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32438371"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32526208"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34562452"}],"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 (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208, PubMed:34562452). Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure (By similarity)"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32277040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32438371"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32526208"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33232691"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34562452"}],"value":"Interacts with nsp7, nsp13 and nsp12 (PubMed:33232691) to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13 (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208, PubMed:34562452). Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure (By similarity)"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 8"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37794589"}],"value":"Is a dimer (By similarity). Interacts with NSP12 (PubMed:35944563). Interacts with host SND1 (PubMed:37794589)"}],"commentType":"SUBUNIT","molecule":"Viral protein genome-linked nsp9"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities"}],"commentType":"SUBUNIT","molecule":"Non-structural protein 10"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32277040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32358203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32438371"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32526208"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35944563"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34562452"}],"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 (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208, PubMed:34562452). Interacts with nsp9 (PubMed:35944563)"}],"commentType":"SUBUNIT","molecule":"RNA-directed RNA polymerase nsp12"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32979938"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33232691"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34562452"}],"value":"Interacts with nsp8 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13 (PubMed:33232691, PubMed:34562452). Interacts with host TBK1; this interaction inhibits TBK1 phosphorylation and decreases by 75% IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938)"}],"commentType":"SUBUNIT","molecule":"Helicase nsp13"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36546776"}],"value":"Interacts (via N-terminus) with DDX1 (By similarity). Interacts with nsp10 (PubMed:36546776)"}],"commentType":"SUBUNIT","molecule":"Guanine-N7 methyltransferase nsp14"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33504779"}],"value":"Homohexamer"}],"commentType":"SUBUNIT","molecule":"Uridylate-specific endoribonuclease nsp15"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C6X7"}],"value":"Interacts with nsp10"}],"commentType":"SUBUNIT","molecule":"2'-O-methyltransferase 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