UniProtKB - P0DTC1 (R1A_SARS2)
Replicase polyprotein 1a
Functioni
Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.
By similarityInhibits host translation by associating with the open head conformation of the 40S subunit (PubMed:33479166, PubMed:33080218, PubMed:32680882, PubMed:32908316).
The C-terminus binds to and obstructs ribosomal mRNA entry tunnel (PubMed:33479166, PubMed:33080218, PubMed:32680882, PubMed:32908316).
Thereby inhibits antiviral response triggered by innate immunity or interferons (PubMed:33080218, PubMed:32680882, PubMed:32979938).
The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation (By similarity).
Viral mRNAs less susceptible to nsp1-mediated inhibition of translation, because of their 5'-end leader sequence (PubMed:32908316, PubMed:33080218).
By similarity5 PublicationsMay 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.
By similarityResponsible 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 (By similarity).
Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:32733001).
Prevents also 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 DDX58 (RIG-I) (PubMed:33727702).
Can play a role in host ADP-ribosylation by ADP-ribose (PubMed:32578982).
By similarity4 PublicationsParticipates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.
By similarityCleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856).
Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481).
Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity) (PubMed:32198291, PubMed:32272481).
By similarity3 PublicationsPlays a role in the initial induction of autophagosomes from host reticulum endoplasmic (By similarity).
Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (By similarity).
Binds to host TBK1 without affecting TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938).
By similarity1 PublicationPlays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, 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).
By similarity4 PublicationsPlays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, 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).
By similarity5 PublicationsMay participate in viral replication by acting as a ssRNA-binding protein (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).
By similarity1 PublicationPlays 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.
By similarityMiscellaneous
Catalytic activityi
- 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).1 Publication EC:3.4.19.12
- TSAVLQ-|-SGFRK-NH(2) 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.3 Publications EC:3.4.22.69
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 200 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 231 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 234 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 236 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 323 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 326 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 341 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 344 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 370 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 373 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 382 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 416 | Zinc 3PROSITE-ProRule annotation | 1 | |
Active sitei | 1674 | For PL1-PRO activityPROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 1835 | For PL2-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 3304 | For 3CL-PRO activityPROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 3408 | For 3CL-PRO activityPROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 4327 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4330 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4336 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4343 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4370 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4373 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4381 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4383 | Zinc 2PROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1752 – 1789 | C4-typePROSITE-ProRule annotationAdd BLAST | 38 |
GO - Molecular functioni
- cysteine-type endopeptidase activity Source: UniProtKB
- cysteine-type peptidase activity Source: UniProtKB
- endonuclease activity Source: UniProtKB-KW
- G-quadruplex RNA binding Source: InterPro
- ISG15-specific protease activity Source: UniProtKB
- protein dimerization activity Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- single-stranded RNA binding Source: UniProtKB
- thiol-dependent deubiquitinase Source: UniProtKB-EC
- transferase activity Source: InterPro
- zinc ion binding Source: InterPro
GO - Biological processi
- induction by virus of catabolism of host mRNA Source: UniProtKB-KW
- induction by virus of host autophagy Source: UniProtKB-KW
- modulation by virus of host autophagy Source: UniProtKB
- modulation by virus of host protein ubiquitination Source: UniProtKB-KW
- positive stranded viral RNA replication Source: UniProtKB
- protein autoprocessing Source: UniProtKB
- protein K48-linked deubiquitination Source: UniProtKB
- protein K63-linked deubiquitination Source: UniProtKB
- suppression by virus of host gene expression Source: UniProtKB-KW
- suppression by virus of host ISG15-protein conjugation Source: UniProtKB
- suppression by virus of host NF-kappaB cascade Source: UniProtKB
- suppression by virus of host toll-like receptor signaling pathway Source: UniProtKB
- suppression by virus of host TRAF activity Source: UniProtKB
- suppression by virus of host translation Source: UniProtKB
- suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB
- suppression by virus of host type I interferon production Source: UniProtKB
- suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity Source: UniProtKB
- viral genome replication Source: InterPro
- viral protein processing Source: InterPro
- viral RNA genome replication Source: UniProtKB
Keywordsi
Enzyme and pathway databases
Reactomei | R-HSA-9694271, Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) R-HSA-9694301, Maturation of replicase proteins R-HSA-9694676, Translation of Replicase and Assembly of the Replication Transcription Complex R-HSA-9694686, Replication of the SARS-CoV-2 genome R-HSA-9694786, Transcription of SARS-CoV-2 sgRNAs |
SABIO-RKi | P0DTC1 |
Names & Taxonomyi
Protein namesi | Recommended name: Replicase polyprotein 1aShort name: pp1a Alternative name(s): ORF1a polyprotein Cleaved into the following 11 chains: Alternative name(s): Leader protein Non-structural protein 1 Short name: nsp1 Alternative name(s): p65 homolog Alternative name(s): Non-structural protein 3 Short name: nsp3 PL2-PRO Papain-like proteinase Short name: PL-PRO Alternative name(s): Main protease Short name: Mpro1 Publication Non-structural protein 5 Short name: nsp5 SARS coronavirus main proteinase Alternative name(s): Growth factor-like peptide Short name: GFL |
Organismi | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
Taxonomic identifieri | 2697049 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Nidovirales › Cornidovirineae › Coronaviridae › Orthocoronavirinae › Betacoronavirus › Sarbecovirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Proteomesi |
|
Subcellular locationi
- Host cytoplasm 1 Publication
- Host cytoplasm 1 Publication
- Host endosome 1 Publication
- Host membrane By similarity; Multi-pass membrane protein By similarity
- Host cytoplasm By similarity
- Host membrane By similarity; Multi-pass membrane protein By similarity
- Host cytoplasm By similarity Note: Localizes in virally-induced cytoplasmic double-membrane vesicles.By similarity
- Host cytoplasm 1 Publication
- Host Golgi apparatus 1 Publication
- Host membrane By similarity; Multi-pass membrane protein By similarity
- host perinuclear region By similarity
- Host cytoplasm 1 Publication
- Host endoplasmic reticulum 1 Publication Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.By similarity
- host perinuclear region By similarity
- Host cytoplasm 2 Publications
- Host endoplasmic reticulum 1 Publication Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.By similarity
- host perinuclear region By similarity
- Host cytoplasm 2 Publications
- Host endoplasmic reticulum 1 Publication Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.By similarity
- host perinuclear region By similarity
- Host cytoplasm 1 Publication
- Host endoplasmic reticulum 1 Publication Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.By similarity
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 2226 – 2246 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2318 – 2338 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2339 – 2359 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2361 – 2381 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 2776 – 2796 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3045 – 3065 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3077 – 3097 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3100 – 3120 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3128 – 3148 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3165 – 3185 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3587 – 3607 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3609 – 3629 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3635 – 3655 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3674 – 3694 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3730 – 3750 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 3779 – 3799 | HelicalSequence analysisAdd BLAST | 21 |
Keywords - Cellular componenti
Host cytoplasm, Host endoplasmic reticulum, Host endosome, Host Golgi apparatus, Host membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 154 – 157 | YEDF → AEDA: Complete loss of ribosome binding and cellular translation inhibition. 1 Publication | 4 | |
Mutagenesisi | 164 – 165 | KH → AA: Complete loss of ribosome binding and cellular translation inhibition. 1 Publication | 2 | |
Mutagenesisi | 164 | K → A: Complete loss of ribosome binding and cellular translation inhibition. 1 Publication | 1 | |
Mutagenesisi | 165 | H → A: Complete loss of ribosome binding and cellular translation inhibition. 1 Publication | 1 | |
Mutagenesisi | 171 – 175 | RELMR → EELME: Complete loss of ribosome binding and cellular translation inhibition. 1 Publication | 5 | |
Mutagenesisi | 1629 | V → A: Partial loss of ISG15 cleavage in vitro. 1 Publication | 1 | |
Mutagenesisi | 1632 | F → A: Partial loss of ISG15 cleavage in vitro. 1 Publication | 1 | |
Mutagenesisi | 1638 | T → A: Partial loss of ubiquitin cleavage in vitro; no effect on ISG15 cleavage in vitro. 1 Publication | 1 | |
Mutagenesisi | 1638 | T → L: Increased cleavage of ubiquitin in vitro; no effect on ISG15 cleavage in vitro. 1 Publication | 1 | |
Mutagenesisi | 1674 | C → A: Unable to remove host IFIH1 (MDA5) ISGylation. 1 Publication | 1 | |
Mutagenesisi | 1674 | C → S: Complete loss of PL-pro activity. 1 Publication | 1 | |
Mutagenesisi | 1831 | Y → G or T: Reduced inhibition by GRL-0617. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB15797, GC-373 DB15796, GC-376 free acid |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000449634 | 1 – 4405 | Replicase polyprotein 1aBy similarityAdd BLAST | 4405 | |
ChainiPRO_0000449635 | 1 – 180 | Host translation inhibitor nsp1By similarityAdd BLAST | 180 | |
ChainiPRO_0000449636 | 181 – 818 | Non-structural protein 2By similarityAdd BLAST | 638 | |
ChainiPRO_0000449637 | 819 – 2763 | Papain-like protease nsp3By similarityAdd BLAST | 1945 | |
ChainiPRO_0000449638 | 2764 – 3263 | Non-structural protein 4By similarityAdd BLAST | 500 | |
ChainiPRO_0000449639 | 3264 – 3569 | 3C-like proteinase nsp5By similarityAdd BLAST | 306 | |
ChainiPRO_0000449640 | 3570 – 3859 | Non-structural protein 6By similarityAdd BLAST | 290 | |
ChainiPRO_0000449641 | 3860 – 3942 | Non-structural protein 7By similarityAdd BLAST | 83 | |
ChainiPRO_0000449642 | 3943 – 4140 | Non-structural protein 8By similarityAdd BLAST | 198 | |
ChainiPRO_0000449643 | 4141 – 4253 | Non-structural protein 9By similarityAdd BLAST | 113 | |
ChainiPRO_0000449644 | 4254 – 4392 | Non-structural protein 10By similarityAdd BLAST | 139 | |
ChainiPRO_0000449645 | 4393 – 4405 | Non-structural protein 11By similarityAdd BLAST | 13 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 180 – 181 | Cleavage; by PL-PROBy similarity | 2 | |
Sitei | 818 – 819 | Cleavage; by PL-PROBy similarity | 2 | |
Sitei | 2763 – 2764 | Cleavage; by PL-PROBy similarity | 2 | |
Sitei | 3263 – 3264 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3569 – 3570 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3859 – 3860 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 3942 – 3943 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 4140 – 4141 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 4253 – 4254 | Cleavage; by 3CL-PROBy similarity | 2 | |
Sitei | 4392 – 4393 | Cleavage; by 3CL-PROBy similarity | 2 |
Interactioni
Subunit structurei
3CL-PRO exists as monomer and homodimer. Only the homodimer shows catalytic activity.
1 PublicationInteracts with host TBK1; this interaction decreases IRF3 phosphorylation by 57%, which leads to reduced IFN-beta production.
1 PublicationForms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities.
By similarityBinary interactionsi
Non-structural protein 11 (PRO_0000449645)
With | #Exp. | IntAct |
---|---|---|
TBCA [O75347] from Homo sapiens. | 2 | EBI-25475882,EBI-2686341 |
GO - Molecular functioni
- protein dimerization activity Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 4383866, 89 interactors |
IntActi | P0DTC1, 47 interactors |
Structurei
Secondary structure
3D structure databases
SASBDBi | P0DTC1 |
SMRi | P0DTC1 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 12 – 127 | CoV Nsp1 globularPROSITE-ProRule annotationAdd BLAST | 116 | |
Domaini | 148 – 179 | BetaCoV Nsp1 C-terminalPROSITE-ProRule annotationAdd BLAST | 32 | |
Domaini | 183 – 456 | CoV Nsp2 N-terminalPROSITE-ProRule annotationAdd BLAST | 274 | |
Domaini | 458 – 688 | CoV Nsp2 middlePROSITE-ProRule annotationAdd BLAST | 231 | |
Domaini | 690 – 818 | CoV Nsp2 C-terminalPROSITE-ProRule annotationAdd BLAST | 129 | |
Domaini | 821 – 929 | Ubiquitin-like 1PROSITE-ProRule annotationAdd BLAST | 109 | |
Domaini | 1025 – 1194 | Macro 1PROSITE-ProRule annotationAdd BLAST | 170 | |
Domaini | 1231 – 1359 | Macro 2PROSITE-ProRule annotationAdd BLAST | 129 | |
Domaini | 1367 – 1494 | Macro 3PROSITE-ProRule annotationAdd BLAST | 128 | |
Domaini | 1496 – 1561 | DPUPPROSITE-ProRule annotationAdd BLAST | 66 | |
Domaini | 1565 – 1620 | Ubiquitin-like 2PROSITE-ProRule annotationAdd BLAST | 56 | |
Domaini | 1634 – 1898 | Peptidase C16PROSITE-ProRule annotationAdd BLAST | 265 | |
Domaini | 1911 – 2021 | Nucleic acid-bindingPROSITE-ProRule annotationAdd BLAST | 111 | |
Domaini | 2046 – 2155 | G2MPROSITE-ProRule annotationAdd BLAST | 110 | |
Domaini | 2660 – 2763 | CoV Nsp3 Y3PROSITE-ProRule annotationAdd BLAST | 104 | |
Domaini | 3165 – 3263 | Nsp4CPROSITE-ProRule annotationAdd BLAST | 99 | |
Domaini | 3264 – 3569 | Peptidase C30PROSITE-ProRule annotationAdd BLAST | 306 | |
Domaini | 3860 – 3942 | RdRp Nsp7 cofactorPROSITE-ProRule annotationAdd BLAST | 83 | |
Domaini | 3943 – 4140 | RdRp Nsp8 cofactorPROSITE-ProRule annotationAdd BLAST | 198 | |
Domaini | 4141 – 4253 | Nsp9 ssRNA-bindingPROSITE-ProRule annotationAdd BLAST | 113 | |
Domaini | 4254 – 4392 | ExoN/MTase coactivatorPROSITE-ProRule annotationAdd BLAST | 139 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 154 – 180 | Binding to 40s ribosome mRNA entry channel1 PublicationAdd BLAST | 27 | |
Regioni | 200 – 236 | C2H2PROSITE-ProRule annotationAdd BLAST | 37 | |
Regioni | 323 – 344 | C4PROSITE-ProRule annotationAdd BLAST | 22 | |
Regioni | 370 – 416 | C2HCPROSITE-ProRule annotationAdd BLAST | 47 | |
Regioni | 926 – 999 | DisorderedSequence analysisAdd BLAST | 74 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 927 – 947 | Acidic residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 984 – 999 | Polar residuesSequence analysisAdd BLAST | 16 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1752 – 1789 | C4-typePROSITE-ProRule annotationAdd BLAST | 38 |
Keywords - Domaini
Repeat, Transmembrane, Transmembrane helix, Zinc-fingerFamily and domain databases
CDDi | cd21560, betaCoV-Nsp6, 1 hit cd21666, betaCoV_Nsp5_Mpro, 1 hit cd21516, cv_beta_Nsp2_SARS-like, 1 hit cd21473, cv_Nsp4_TM, 1 hit cd21563, Macro_cv_SUD-M_Nsp3-like, 1 hit cd21557, Macro_X_Nsp3-like, 1 hit cd21525, SUD_C_SARS-CoV_Nsp3, 1 hit cd21467, Ubl1_cv_Nsp3_N-like, 1 hit cd21466, Ubl2_cv_PLpro_N_Nsp3-like, 1 hit |
Gene3Di | 1.10.150.420, 1 hit 1.10.1840.10, 1 hit 1.10.8.1190, 1 hit 1.10.8.370, 1 hit 2.40.10.10, 2 hits 2.40.10.250, 1 hit 2.60.120.1680, 1 hit 3.10.20.350, 1 hit 3.10.20.540, 1 hit 3.30.70.3540, 1 hit 3.40.220.10, 1 hit 3.40.220.20, 1 hit 3.40.220.30, 1 hit 3.40.30.150, 1 hit 3.40.50.11020, 1 hit |
InterProi | View protein in InterPro IPR043613, CoV_NSP2_C IPR043611, CoV_NSP3_C IPR043612, CoV_NSP4_N IPR022733, DPUP_SUD_C_bCoV IPR002589, Macro_dom IPR043472, Macro_dom-like IPR044371, Macro_X_NSP3-like IPR042570, NAR_sf IPR036333, NSP10_sf_CoV IPR021590, NSP1_bCoV IPR038030, NSP1_sf_bCoV IPR043615, NSP2_N_CoV IPR044389, NSP2_SARS-CoV-like IPR024375, NSP3_bCoV IPR024358, NSP3_N_bCoV IPR032592, NSP3_NAB_bCoV IPR038166, NSP3_PL2pro_sf_CoV IPR038400, NSP3_SUD-M_sf_bCoV IPR044864, NSP3_SUD-N_bCoV IPR043478, NSP3_SUD-N_sf_bCoV IPR044357, NSP3_Ubl1_dom_CoV IPR044353, Nsp3_Ubl2_dom_CoV IPR038083, NSP3A-like IPR032505, NSP4_C_CoV IPR038123, NSP4_C_sf_CoV IPR044367, NSP6_betaCoV IPR043610, NSP6_CoV IPR014828, NSP7_CoV IPR037204, NSP7_sf_CoV IPR014829, NSP8_CoV-like IPR037230, NSP8_sf_CoV IPR014822, NSP9_CoV IPR036499, NSP9_sf_CoV IPR013016, Peptidase_C16_CoV IPR008740, Peptidase_C30_CoV IPR043477, Peptidase_C30_dom3_CoV IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR043177, PLpro_N_sf_CoV IPR043503, PLpro_palm_finger_dom_CoV IPR043178, PLpro_thumb_sf_CoV IPR018995, RNA_synth_NSP10_CoV |
Pfami | View protein in Pfam PF16251, bCoV_NAR, 1 hit PF11501, bCoV_NSP1, 1 hit PF12379, bCoV_NSP3_N, 1 hit PF12124, bCoV_SUD_C, 1 hit PF11633, bCoV_SUD_M, 1 hit PF09401, CoV_NSP10, 1 hit PF19212, CoV_NSP2_C, 1 hit PF19211, CoV_NSP2_N, 1 hit PF19218, CoV_NSP3_C, 1 hit PF16348, CoV_NSP4_C, 1 hit PF19217, CoV_NSP4_N, 1 hit PF19213, CoV_NSP6, 1 hit PF08716, CoV_NSP7, 1 hit PF08717, CoV_NSP8, 1 hit PF08710, CoV_NSP9, 1 hit PF08715, CoV_peptidase, 1 hit PF01661, Macro, 1 hit PF05409, Peptidase_C30, 1 hit |
SMARTi | View protein in SMART SM00506, A1pp, 1 hit |
SUPFAMi | SSF101816, SSF101816, 1 hit SSF140367, SSF140367, 1 hit SSF143076, SSF143076, 1 hit SSF144246, SSF144246, 1 hit SSF159936, SSF159936, 1 hit SSF160099, SSF160099, 1 hit SSF50494, SSF50494, 1 hit SSF52949, SSF52949, 1 hit |
PROSITEi | View protein in PROSITE PS51963, BCOV_NSP1_C, 1 hit PS51942, BCOV_NSP3C_C, 1 hit PS51941, BCOV_NSP3C_M, 1 hit PS51994, BCOV_NSP3E_G2M, 1 hit PS51945, BCOV_NSP3E_NAB, 1 hit PS51952, COV_EXON_MTASE_COACT, 1 hit PS51962, COV_NSP1, 1 hit PS51991, COV_NSP2_C, 1 hit PS51990, COV_NSP2_M, 1 hit PS51989, COV_NSP2_N, 1 hit PS51992, COV_NSP3_Y3, 1 hit PS51943, COV_NSP3A_UBL, 1 hit PS51944, COV_NSP3D_UBL, 1 hit PS51946, COV_NSP4C, 1 hit PS51949, COV_NSP7, 1 hit PS51950, COV_NSP8, 1 hit PS51951, COV_NSP9_SSRNA_BD, 1 hit PS00867, CPSASE_2, 1 hit PS51442, M_PRO, 1 hit PS51154, MACRO, 1 hit PS51124, PEPTIDASE_C16, 1 hit PS51940, SARS_NSP3C_N, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsiribosomal frameshifting. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MESLVPGFNE KTHVQLSLPV LQVRDVLVRG FGDSVEEVLS EARQHLKDGT
60 70 80 90 100
CGLVEVEKGV LPQLEQPYVF IKRSDARTAP HGHVMVELVA ELEGIQYGRS
110 120 130 140 150
GETLGVLVPH VGEIPVAYRK VLLRKNGNKG AGGHSYGADL KSFDLGDELG
160 170 180 190 200
TDPYEDFQEN WNTKHSSGVT RELMRELNGG AYTRYVDNNF CGPDGYPLEC
210 220 230 240 250
IKDLLARAGK ASCTLSEQLD FIDTKRGVYC CREHEHEIAW YTERSEKSYE
260 270 280 290 300
LQTPFEIKLA KKFDTFNGEC PNFVFPLNSI IKTIQPRVEK KKLDGFMGRI
310 320 330 340 350
RSVYPVASPN ECNQMCLSTL MKCDHCGETS WQTGDFVKAT CEFCGTENLT
360 370 380 390 400
KEGATTCGYL PQNAVVKIYC PACHNSEVGP EHSLAEYHNE SGLKTILRKG
410 420 430 440 450
GRTIAFGGCV FSYVGCHNKC AYWVPRASAN IGCNHTGVVG EGSEGLNDNL
460 470 480 490 500
LEILQKEKVN INIVGDFKLN EEIAIILASF SASTSAFVET VKGLDYKAFK
510 520 530 540 550
QIVESCGNFK VTKGKAKKGA WNIGEQKSIL SPLYAFASEA ARVVRSIFSR
560 570 580 590 600
TLETAQNSVR VLQKAAITIL DGISQYSLRL IDAMMFTSDL ATNNLVVMAY
610 620 630 640 650
ITGGVVQLTS QWLTNIFGTV YEKLKPVLDW LEEKFKEGVE FLRDGWEIVK
660 670 680 690 700
FISTCACEIV GGQIVTCAKE IKESVQTFFK LVNKFLALCA DSIIIGGAKL
710 720 730 740 750
KALNLGETFV THSKGLYRKC VKSREETGLL MPLKAPKEII FLEGETLPTE
760 770 780 790 800
VLTEEVVLKT GDLQPLEQPT SEAVEAPLVG TPVCINGLML LEIKDTEKYC
810 820 830 840 850
ALAPNMMVTN NTFTLKGGAP TKVTFGDDTV IEVQGYKSVN ITFELDERID
860 870 880 890 900
KVLNEKCSAY TVELGTEVNE FACVVADAVI KTLQPVSELL TPLGIDLDEW
910 920 930 940 950
SMATYYLFDE SGEFKLASHM YCSFYPPDED EEEGDCEEEE FEPSTQYEYG
960 970 980 990 1000
TEDDYQGKPL EFGATSAALQ PEEEQEEDWL DDDSQQTVGQ QDGSEDNQTT
1010 1020 1030 1040 1050
TIQTIVEVQP QLEMELTPVV QTIEVNSFSG YLKLTDNVYI KNADIVEEAK
1060 1070 1080 1090 1100
KVKPTVVVNA ANVYLKHGGG VAGALNKATN NAMQVESDDY IATNGPLKVG
1110 1120 1130 1140 1150
GSCVLSGHNL AKHCLHVVGP NVNKGEDIQL LKSAYENFNQ HEVLLAPLLS
1160 1170 1180 1190 1200
AGIFGADPIH SLRVCVDTVR TNVYLAVFDK NLYDKLVSSF LEMKSEKQVE
1210 1220 1230 1240 1250
QKIAEIPKEE VKPFITESKP SVEQRKQDDK KIKACVEEVT TTLEETKFLT
1260 1270 1280 1290 1300
ENLLLYIDIN GNLHPDSATL VSDIDITFLK KDAPYIVGDV VQEGVLTAVV
1310 1320 1330 1340 1350
IPTKKAGGTT EMLAKALRKV PTDNYITTYP GQGLNGYTVE EAKTVLKKCK
1360 1370 1380 1390 1400
SAFYILPSII SNEKQEILGT VSWNLREMLA HAEETRKLMP VCVETKAIVS
1410 1420 1430 1440 1450
TIQRKYKGIK IQEGVVDYGA RFYFYTSKTT VASLINTLND LNETLVTMPL
1460 1470 1480 1490 1500
GYVTHGLNLE EAARYMRSLK VPATVSVSSP DAVTAYNGYL TSSSKTPEEH
1510 1520 1530 1540 1550
FIETISLAGS YKDWSYSGQS TQLGIEFLKR GDKSVYYTSN PTTFHLDGEV
1560 1570 1580 1590 1600
ITFDNLKTLL SLREVRTIKV FTTVDNINLH TQVVDMSMTY GQQFGPTYLD
1610 1620 1630 1640 1650
GADVTKIKPH NSHEGKTFYV LPNDDTLRVE AFEYYHTTDP SFLGRYMSAL
1660 1670 1680 1690 1700
NHTKKWKYPQ VNGLTSIKWA DNNCYLATAL LTLQQIELKF NPPALQDAYY
1710 1720 1730 1740 1750
RARAGEAANF CALILAYCNK TVGELGDVRE TMSYLFQHAN LDSCKRVLNV
1760 1770 1780 1790 1800
VCKTCGQQQT TLKGVEAVMY MGTLSYEQFK KGVQIPCTCG KQATKYLVQQ
1810 1820 1830 1840 1850
ESPFVMMSAP PAQYELKHGT FTCASEYTGN YQCGHYKHIT SKETLYCIDG
1860 1870 1880 1890 1900
ALLTKSSEYK GPITDVFYKE NSYTTTIKPV TYKLDGVVCT EIDPKLDNYY
1910 1920 1930 1940 1950
KKDNSYFTEQ PIDLVPNQPY PNASFDNFKF VCDNIKFADD LNQLTGYKKP
1960 1970 1980 1990 2000
ASRELKVTFF PDLNGDVVAI DYKHYTPSFK KGAKLLHKPI VWHVNNATNK
2010 2020 2030 2040 2050
ATYKPNTWCI RCLWSTKPVE TSNSFDVLKS EDAQGMDNLA CEDLKPVSEE
2060 2070 2080 2090 2100
VVENPTIQKD VLECNVKTTE VVGDIILKPA NNSLKITEEV GHTDLMAAYV
2110 2120 2130 2140 2150
DNSSLTIKKP NELSRVLGLK TLATHGLAAV NSVPWDTIAN YAKPFLNKVV
2160 2170 2180 2190 2200
STTTNIVTRC LNRVCTNYMP YFFTLLLQLC TFTRSTNSRI KASMPTTIAK
2210 2220 2230 2240 2250
NTVKSVGKFC LEASFNYLKS PNFSKLINII IWFLLLSVCL GSLIYSTAAL
2260 2270 2280 2290 2300
GVLMSNLGMP SYCTGYREGY LNSTNVTIAT YCTGSIPCSV CLSGLDSLDT
2310 2320 2330 2340 2350
YPSLETIQIT ISSFKWDLTA FGLVAEWFLA YILFTRFFYV LGLAAIMQLF
2360 2370 2380 2390 2400
FSYFAVHFIS NSWLMWLIIN LVQMAPISAM VRMYIFFASF YYVWKSYVHV
2410 2420 2430 2440 2450
VDGCNSSTCM MCYKRNRATR VECTTIVNGV RRSFYVYANG GKGFCKLHNW
2460 2470 2480 2490 2500
NCVNCDTFCA GSTFISDEVA RDLSLQFKRP INPTDQSSYI VDSVTVKNGS
2510 2520 2530 2540 2550
IHLYFDKAGQ KTYERHSLSH FVNLDNLRAN NTKGSLPINV IVFDGKSKCE
2560 2570 2580 2590 2600
ESSAKSASVY YSQLMCQPIL LLDQALVSDV GDSAEVAVKM FDAYVNTFSS
2610 2620 2630 2640 2650
TFNVPMEKLK TLVATAEAEL AKNVSLDNVL STFISAARQG FVDSDVETKD
2660 2670 2680 2690 2700
VVECLKLSHQ SDIEVTGDSC NNYMLTYNKV ENMTPRDLGA CIDCSARHIN
2710 2720 2730 2740 2750
AQVAKSHNIA LIWNVKDFMS LSEQLRKQIR SAAKKNNLPF KLTCATTRQV
2760 2770 2780 2790 2800
VNVVTTKIAL KGGKIVNNWL KQLIKVTLVF LFVAAIFYLI TPVHVMSKHT
2810 2820 2830 2840 2850
DFSSEIIGYK AIDGGVTRDI ASTDTCFANK HADFDTWFSQ RGGSYTNDKA
2860 2870 2880 2890 2900
CPLIAAVITR EVGFVVPGLP GTILRTTNGD FLHFLPRVFS AVGNICYTPS
2910 2920 2930 2940 2950
KLIEYTDFAT SACVLAAECT IFKDASGKPV PYCYDTNVLE GSVAYESLRP
2960 2970 2980 2990 3000
DTRYVLMDGS IIQFPNTYLE GSVRVVTTFD SEYCRHGTCE RSEAGVCVST
3010 3020 3030 3040 3050
SGRWVLNNDY YRSLPGVFCG VDAVNLLTNM FTPLIQPIGA LDISASIVAG
3060 3070 3080 3090 3100
GIVAIVVTCL AYYFMRFRRA FGEYSHVVAF NTLLFLMSFT VLCLTPVYSF
3110 3120 3130 3140 3150
LPGVYSVIYL YLTFYLTNDV SFLAHIQWMV MFTPLVPFWI TIAYIICIST
3160 3170 3180 3190 3200
KHFYWFFSNY LKRRVVFNGV SFSTFEEAAL CTFLLNKEMY LKLRSDVLLP
3210 3220 3230 3240 3250
LTQYNRYLAL YNKYKYFSGA MDTTSYREAA CCHLAKALND FSNSGSDVLY
3260 3270 3280 3290 3300
QPPQTSITSA VLQSGFRKMA FPSGKVEGCM VQVTCGTTTL NGLWLDDVVY
3310 3320 3330 3340 3350
CPRHVICTSE DMLNPNYEDL LIRKSNHNFL VQAGNVQLRV IGHSMQNCVL
3360 3370 3380 3390 3400
KLKVDTANPK TPKYKFVRIQ PGQTFSVLAC YNGSPSGVYQ CAMRPNFTIK
3410 3420 3430 3440 3450
GSFLNGSCGS VGFNIDYDCV SFCYMHHMEL PTGVHAGTDL EGNFYGPFVD
3460 3470 3480 3490 3500
RQTAQAAGTD TTITVNVLAW LYAAVINGDR WFLNRFTTTL NDFNLVAMKY
3510 3520 3530 3540 3550
NYEPLTQDHV DILGPLSAQT GIAVLDMCAS LKELLQNGMN GRTILGSALL
3560 3570 3580 3590 3600
EDEFTPFDVV RQCSGVTFQS AVKRTIKGTH HWLLLTILTS LLVLVQSTQW
3610 3620 3630 3640 3650
SLFFFLYENA FLPFAMGIIA MSAFAMMFVK HKHAFLCLFL LPSLATVAYF
3660 3670 3680 3690 3700
NMVYMPASWV MRIMTWLDMV DTSLSGFKLK DCVMYASAVV LLILMTARTV
3710 3720 3730 3740 3750
YDDGARRVWT LMNVLTLVYK VYYGNALDQA ISMWALIISV TSNYSGVVTT
3760 3770 3780 3790 3800
VMFLARGIVF MCVEYCPIFF ITGNTLQCIM LVYCFLGYFC TCYFGLFCLL
3810 3820 3830 3840 3850
NRYFRLTLGV YDYLVSTQEF RYMNSQGLLP PKNSIDAFKL NIKLLGVGGK
3860 3870 3880 3890 3900
PCIKVATVQS KMSDVKCTSV VLLSVLQQLR VESSSKLWAQ CVQLHNDILL
3910 3920 3930 3940 3950
AKDTTEAFEK MVSLLSVLLS MQGAVDINKL CEEMLDNRAT LQAIASEFSS
3960 3970 3980 3990 4000
LPSYAAFATA QEAYEQAVAN GDSEVVLKKL KKSLNVAKSE FDRDAAMQRK
4010 4020 4030 4040 4050
LEKMADQAMT QMYKQARSED KRAKVTSAMQ TMLFTMLRKL DNDALNNIIN
4060 4070 4080 4090 4100
NARDGCVPLN IIPLTTAAKL MVVIPDYNTY KNTCDGTTFT YASALWEIQQ
4110 4120 4130 4140 4150
VVDADSKIVQ LSEISMDNSP NLAWPLIVTA LRANSAVKLQ NNELSPVALR
4160 4170 4180 4190 4200
QMSCAAGTTQ TACTDDNALA YYNTTKGGRF VLALLSDLQD LKWARFPKSD
4210 4220 4230 4240 4250
GTGTIYTELE PPCRFVTDTP KGPKVKYLYF IKGLNNLNRG MVLGSLAATV
4260 4270 4280 4290 4300
RLQAGNATEV PANSTVLSFC AFAVDAAKAY KDYLASGGQP ITNCVKMLCT
4310 4320 4330 4340 4350
HTGTGQAITV TPEANMDQES FGGASCCLYC RCHIDHPNPK GFCDLKGKYV
4360 4370 4380 4390 4400
QIPTTCANDP VGFTLKNTVC TVCGMWKGYG CSCDQLREPM LQSADAQSFL
NGFAV
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Polymorphismi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 135 | S → R in strain: Omicron/BA.2. Curated | 1 | |
Natural varianti | 265 | T → I in strain: Iota/B.1.526, Beta/B.1.351 and Epsilon/B.1.427/B.1.429. Curated | 1 | |
Natural varianti | 842 | T → I in strain: Omicron/BA.2. Curated | 1 | |
Natural varianti | 856 | K → R in strain: Omicron/BA.1. Curated | 1 | |
Natural varianti | 1001 | T → I in strain: Alpha/B.1.1.7. 1 Publication | 1 | |
Natural varianti | 1055 | T → A in strain: Mu/B.1.621. Curated | 1 | |
Natural varianti | 1188 | S → L in strain: Gamma/P.1. Curated | 1 | |
Natural varianti | 1246 | T → I in strain: Lambda/C.37. Curated | 1 | |
Natural varianti | 1307 | G → S in strain: Omicron/BA.2. | 1 | |
Natural varianti | 1538 | T → I in strain: Mu/B.1.621. Curated | 1 | |
Natural varianti | 1554 | D → G in strain: Theta/P.3. Curated | 1 | |
Natural varianti | 1567 | T → I in strain: Kappa/B.1.617.1. Curated | 1 | |
Natural varianti | 1655 | K → N in strain: Beta/B.1.351. Curated | 1 | |
Natural varianti | 1708 | A → D in strain: Alpha/B.1.1.7. 1 Publication | 1 | |
Natural varianti | 1795 | K → Q in strain: Gamma/P.1. Curated | 1 | |
Natural varianti | 2007 | T → I in strain: Eta/B.1.525. Curated | 1 | |
Natural varianti | 2083 – 2084 | SL → I in strain:Omicron/BA.1. Curated | 2 | |
Natural varianti | 2230 | I → T in strain: Alpha/B.1.1.7. 1 Publication | 1 | |
Natural varianti | 2287 | P → S in strain: Lambda/C.37. Curated | 1 | |
Natural varianti | 2387 | F → V in strain: Lambda/C.37. Curated | 1 | |
Natural varianti | 2625 | S → F in strain: Theta/P.3. Curated | 1 | |
Natural varianti | 2710 | A → T in strain:Omicron/BA.1. Curated | 1 | |
Natural varianti | 2980 | D → N in strain: Theta/P.3. Curated | 1 | |
Natural varianti | 3027 | L → F in strain: Omicron/BA.2. Curated | 1 | |
Natural varianti | 3090 | T → I in strain: Omicron/BA.2. Curated | 1 | |
Natural varianti | 3201 | L → F in strain: Omicron/BA.2. Curated | 1 | |
Natural varianti | 3201 | L → P in strain: Iota/B.1.526, Lambda/C.37 and Theta/P.3. Curated | 1 | |
Natural varianti | 3255 | T → I in strain: Lambda/C.37, Mu/B.1.621, Omicron/BA.1, Omicron/BA.2. Curated | 1 | |
Natural varianti | 3353 | K → R in strain: Beta/B.1.351. Curated | 1 | |
Natural varianti | 3395 | P → H in strain: Omicron/BA.1, Omicron/BA.2. Curated | 1 | |
Natural varianti | 3468 | L → V in strain: Zeta/P.2. Curated | 1 | |
Natural varianti | 3646 | T → A in strain: Kappa/B.1.617.1. | 1 | |
Natural varianti | 3674 – 3676 | Missing in strain: Omicron/BA.1. Curated | 3 | |
Natural varianti | 3675 – 3677 | Missing in strain: Omicron/BA.2. Curated | 3 | |
Natural varianti | 3675 | S → K in strain: Alpha/B.1.1.7, Beta/B.1.351, Gamma/P.1, Eta/B.1.525, Iota/B.1.526 and Lambda/C.37. Curated | 1 | |
Natural varianti | 3676 – 3678 | Missing in strain: Alpha/B.1.1.7, Beta/B.1.351, Gamma/P.1, Eta/B.1.525, Iota/B.1.526 and Lambda/C.37. Curated | 3 | |
Natural varianti | 3681 | D → E in strain: Theta/P.3. Curated | 1 | |
Natural varianti | 3729 | Q → R in strain: Mu/B.1.621. Curated | 1 | |
Natural varianti | 3758 | I → V in strain: Omicron/BA.1. Curated | 1 | |
Natural varianti | 3930 | L → F in strain: Theta/P.3 and Zeta/P.2. Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | MN908947 Genomic RNA Translation: QHD43415.1 Frameshift. |
RefSeqi | YP_009725295.1, NC_045512.2 |
Genome annotation databases
GeneIDi | 43740578 |
Keywords - Coding sequence diversityi
Ribosomal frameshiftingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | MN908947 Genomic RNA Translation: QHD43415.1 Frameshift. |
RefSeqi | YP_009725295.1, NC_045512.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6Y2E | X-ray | 1.75 | A | 3264-3569 | [»] | |
6Y2F | X-ray | 2.16 | A | 3264-3569 | [»] | |
6Y2G | X-ray | 2.16 | A | 3264-3569 | [»] | |
6YHU | X-ray | 2.00 | A/C | 3860-3930 | [»] | |
B/D | 4018-4134 | [»] | ||||
6YYT | electron microscopy | 2.90 | B | 3948-4133 | [»] | |
C | 3860-3932 | [»] | ||||
7BV2 | electron microscopy | 2.50 | C | 3860-3942 | [»] | |
B | 3943-4140 | [»] | ||||
7C33 | X-ray | 3.83 | A/B/C/D | 1025-1195 | [»] | |
7CZ4 | X-ray | 2.64 | A/B | 1025-1195 | [»] | |
7D3I | X-ray | 2.00 | A | 3264-3569 | [»] | |
7D47 | X-ray | 1.97 | A/B | 1564-1880 | [»] | |
7D64 | X-ray | 2.45 | A | 3264-3569 | [»] | |
7D6H | X-ray | 1.60 | A | 1563-1878 | [»] | |
7DAT | X-ray | 2.75 | A | 3264-3569 | [»] | |
7DAU | X-ray | 1.72 | A | 3264-3569 | [»] | |
7DAV | X-ray | 1.77 | A | 3264-3569 | [»] | |
7DCD | X-ray | 2.57 | A/C/E/G | 3860-3942 | [»] | |
B/D/F/H | 4019-4140 | [»] | ||||
7DGB | X-ray | 1.68 | A | 3264-3569 | [»] | |
7DGF | X-ray | 1.64 | A | 3264-3569 | [»] | |
7DGG | X-ray | 2.00 | A/B | 3264-3569 | [»] | |
7DGH | X-ray | 1.97 | A | 3264-3569 | [»] | |
7DGI | X-ray | 1.90 | A/B | 3264-3569 | [»] | |
7DHJ | X-ray | 1.96 | A | 3264-3569 | [»] | |
7DJR | X-ray | 1.45 | A | 3264-3569 | [»] | |
7DK1 | X-ray | 1.90 | A/B | 3264-3569 | [»] | |
7DPP | X-ray | 2.10 | A | 3264-3564 | [»] | |
7DPU | X-ray | 1.75 | A/B | 3264-3569 | [»] | |
7DPV | X-ray | 2.35 | A/B/C/D | 3264-3569 | [»] | |
7E35 | X-ray | 2.40 | A/B | 1564-1878 | [»] | |
7EIN | X-ray | 1.70 | A/B | 3264-3569 | [»] | |
7EIZ | electron microscopy | - | C | 3860-3942 | [»] | |
7EXM | X-ray | 1.96 | A/B/C/D | 181-456 | [»] | |
7FAY | X-ray | 2.10 | A | 3264-3569 | [»] | |
7FAZ | X-ray | 2.10 | A/B | 3264-3569 | [»] | |
7JIR | X-ray | 2.09 | A | 1564-1878 | [»] | |
7JIT | X-ray | 1.95 | A | 1564-1878 | [»] | |
7JIV | X-ray | 2.05 | A | 1564-1878 | [»] | |
7JIW | X-ray | 2.30 | A | 1564-1878 | [»] | |
7JN2 | X-ray | 1.93 | A | 1564-1878 | [»] | |
7JRN | X-ray | 2.48 | A/J | 1564-1878 | [»] | |
7KOJ | X-ray | 2.02 | A | 1564-1878 | [»] | |
7KOK | X-ray | 2.00 | A | 1564-1878 | [»] | |
7KOL | X-ray | 2.58 | A | 1564-1878 | [»] | |
7KRX | X-ray | 2.72 | A | 1564-1878 | [»] | |
7M1Y | X-ray | 2.02 | A/B | 1564-1878 | [»] | |
7NT1 | X-ray | 2.85 | A/B | 3264-3569 | [»] | |
7NT2 | X-ray | 2.15 | A/B | 3264-3569 | [»] | |
7NT3 | X-ray | 2.33 | A/B | 3264-3569 | [»] | |
7NTV | X-ray | 2.06 | A/B | 3264-3569 | [»] | |
7NUK | X-ray | 2.19 | A/B | 3264-3569 | [»] | |
7NW2 | X-ray | 2.10 | A/B | 3264-3569 | [»] | |
7NWX | X-ray | 1.80 | A | 3264-3569 | [»] | |
7NXH | X-ray | 2.10 | A | 3264-3569 | [»] | |
7OFS | X-ray | 1.90 | A | 1564-1878 | [»] | |
7OFT | X-ray | 1.95 | A | 1564-1878 | [»] | |
7OFU | X-ray | 1.72 | AAA | 1564-1878 | [»] | |
7P51 | X-ray | 1.47 | A | 3264-3569 | [»] | |
7RBR | X-ray | 1.88 | A | 1564-1878 | [»] | |
7RBS | X-ray | 2.98 | A/C/E/G/I | 1564-1878 | [»] | |
7RZC | X-ray | 2.04 | A/B/C | 1564-1878 | [»] | |
7SDR | X-ray | 2.72 | A/B/C | 1564-1878 | [»] | |
7SGU | X-ray | 1.79 | A | 1564-1878 | [»] | |
7SGV | X-ray | 2.00 | A | 1564-1878 | [»] | |
7SGW | X-ray | 1.95 | A | 1564-1878 | [»] | |
7SQE | X-ray | 2.00 | A/B/C | 1564-1878 | [»] | |
7TLL | X-ray | 1.63 | A/B | 3264-3569 | [»] | |
7VH8 | X-ray | 1.59 | A | 3264-3569 | [»] | |
7VJW | X-ray | 2.20 | A/B | 3264-3569 | [»] | |
7VJX | X-ray | 2.20 | A/B | 3264-3569 | [»] | |
7VJY | X-ray | 1.90 | A | 3264-3569 | [»] | |
7VJZ | X-ray | 1.90 | A | 3264-3569 | [»] | |
7VK0 | X-ray | 2.10 | A/B | 3264-3569 | [»] | |
7VK1 | X-ray | 1.93 | A | 3264-3569 | [»] | |
7VK2 | X-ray | 2.00 | A | 3264-3569 | [»] | |
7VK3 | X-ray | 2.10 | A/B | 3264-3569 | [»] | |
7VK4 | X-ray | 2.10 | A/B | 3264-3569 | [»] | |
7VK5 | X-ray | 2.17 | A/B | 3264-3569 | [»] | |
7VK6 | X-ray | 2.25 | A/B | 3264-3569 | [»] | |
7VK7 | X-ray | 2.40 | A/B | 3264-3569 | [»] | |
7VK8 | X-ray | 2.40 | A | 3264-3569 | [»] | |
SASBDBi | P0DTC1 | |||||
SMRi | P0DTC1 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4383866, 89 interactors |
IntActi | P0DTC1, 47 interactors |
Chemistry databases
DrugBanki | DB15797, GC-373 DB15796, GC-376 free acid |
Protocols and materials databases
DNASUi | 43740578 |
Genome annotation databases
GeneIDi | 43740578 |
Enzyme and pathway databases
Reactomei | R-HSA-9694271, Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC) R-HSA-9694301, Maturation of replicase proteins R-HSA-9694676, Translation of Replicase and Assembly of the Replication Transcription Complex R-HSA-9694686, Replication of the SARS-CoV-2 genome R-HSA-9694786, Transcription of SARS-CoV-2 sgRNAs |
SABIO-RKi | P0DTC1 |
Family and domain databases
CDDi | cd21560, betaCoV-Nsp6, 1 hit cd21666, betaCoV_Nsp5_Mpro, 1 hit cd21516, cv_beta_Nsp2_SARS-like, 1 hit cd21473, cv_Nsp4_TM, 1 hit cd21563, Macro_cv_SUD-M_Nsp3-like, 1 hit cd21557, Macro_X_Nsp3-like, 1 hit cd21525, SUD_C_SARS-CoV_Nsp3, 1 hit cd21467, Ubl1_cv_Nsp3_N-like, 1 hit cd21466, Ubl2_cv_PLpro_N_Nsp3-like, 1 hit |
Gene3Di | 1.10.150.420, 1 hit 1.10.1840.10, 1 hit 1.10.8.1190, 1 hit 1.10.8.370, 1 hit 2.40.10.10, 2 hits 2.40.10.250, 1 hit 2.60.120.1680, 1 hit 3.10.20.350, 1 hit 3.10.20.540, 1 hit 3.30.70.3540, 1 hit 3.40.220.10, 1 hit 3.40.220.20, 1 hit 3.40.220.30, 1 hit 3.40.30.150, 1 hit 3.40.50.11020, 1 hit |
InterProi | View protein in InterPro IPR043613, CoV_NSP2_C IPR043611, CoV_NSP3_C IPR043612, CoV_NSP4_N IPR022733, DPUP_SUD_C_bCoV IPR002589, Macro_dom IPR043472, Macro_dom-like IPR044371, Macro_X_NSP3-like IPR042570, NAR_sf IPR036333, NSP10_sf_CoV IPR021590, NSP1_bCoV IPR038030, NSP1_sf_bCoV IPR043615, NSP2_N_CoV IPR044389, NSP2_SARS-CoV-like IPR024375, NSP3_bCoV IPR024358, NSP3_N_bCoV IPR032592, NSP3_NAB_bCoV IPR038166, NSP3_PL2pro_sf_CoV IPR038400, NSP3_SUD-M_sf_bCoV IPR044864, NSP3_SUD-N_bCoV IPR043478, NSP3_SUD-N_sf_bCoV IPR044357, NSP3_Ubl1_dom_CoV IPR044353, Nsp3_Ubl2_dom_CoV IPR038083, NSP3A-like IPR032505, NSP4_C_CoV IPR038123, NSP4_C_sf_CoV IPR044367, NSP6_betaCoV IPR043610, NSP6_CoV IPR014828, NSP7_CoV IPR037204, NSP7_sf_CoV IPR014829, NSP8_CoV-like IPR037230, NSP8_sf_CoV IPR014822, NSP9_CoV IPR036499, NSP9_sf_CoV IPR013016, Peptidase_C16_CoV IPR008740, Peptidase_C30_CoV IPR043477, Peptidase_C30_dom3_CoV IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR043177, PLpro_N_sf_CoV IPR043503, PLpro_palm_finger_dom_CoV IPR043178, PLpro_thumb_sf_CoV IPR018995, RNA_synth_NSP10_CoV |
Pfami | View protein in Pfam PF16251, bCoV_NAR, 1 hit PF11501, bCoV_NSP1, 1 hit PF12379, bCoV_NSP3_N, 1 hit PF12124, bCoV_SUD_C, 1 hit PF11633, bCoV_SUD_M, 1 hit PF09401, CoV_NSP10, 1 hit PF19212, CoV_NSP2_C, 1 hit PF19211, CoV_NSP2_N, 1 hit PF19218, CoV_NSP3_C, 1 hit PF16348, CoV_NSP4_C, 1 hit PF19217, CoV_NSP4_N, 1 hit PF19213, CoV_NSP6, 1 hit PF08716, CoV_NSP7, 1 hit PF08717, CoV_NSP8, 1 hit PF08710, CoV_NSP9, 1 hit PF08715, CoV_peptidase, 1 hit PF01661, Macro, 1 hit PF05409, Peptidase_C30, 1 hit |
SMARTi | View protein in SMART SM00506, A1pp, 1 hit |
SUPFAMi | SSF101816, SSF101816, 1 hit SSF140367, SSF140367, 1 hit SSF143076, SSF143076, 1 hit SSF144246, SSF144246, 1 hit SSF159936, SSF159936, 1 hit SSF160099, SSF160099, 1 hit SSF50494, SSF50494, 1 hit SSF52949, SSF52949, 1 hit |
PROSITEi | View protein in PROSITE PS51963, BCOV_NSP1_C, 1 hit PS51942, BCOV_NSP3C_C, 1 hit PS51941, BCOV_NSP3C_M, 1 hit PS51994, BCOV_NSP3E_G2M, 1 hit PS51945, BCOV_NSP3E_NAB, 1 hit PS51952, COV_EXON_MTASE_COACT, 1 hit PS51962, COV_NSP1, 1 hit PS51991, COV_NSP2_C, 1 hit PS51990, COV_NSP2_M, 1 hit PS51989, COV_NSP2_N, 1 hit PS51992, COV_NSP3_Y3, 1 hit PS51943, COV_NSP3A_UBL, 1 hit PS51944, COV_NSP3D_UBL, 1 hit PS51946, COV_NSP4C, 1 hit PS51949, COV_NSP7, 1 hit PS51950, COV_NSP8, 1 hit PS51951, COV_NSP9_SSRNA_BD, 1 hit PS00867, CPSASE_2, 1 hit PS51442, M_PRO, 1 hit PS51154, MACRO, 1 hit PS51124, PEPTIDASE_C16, 1 hit PS51940, SARS_NSP3C_N, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | R1A_SARS2 | |
Accessioni | P0DTC1Primary (citable) accession number: P0DTC1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 22, 2020 |
Last sequence update: | April 22, 2020 | |
Last modified: | May 25, 2022 | |
This is version 11 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families