UniProtKB - P0C6U8 (R1A_SARS)
Replicase polyprotein 1a
1a
Functioni
Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.
CuratedInhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (PubMed:23035226).
May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371).
2 PublicationsMay play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (PubMed:19640993).
Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (PubMed:19640993).
1 PublicationResponsible 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 (PubMed:17692280).
Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763).
Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069, PubMed:23943763).
Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840).
Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840).
1 Publication5 PublicationsPlays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763, PubMed:24410069).
Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes (PubMed:23943763).
Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069).
1 Publication1 PublicationCleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH.
PROSITE-ProRule annotation1 PublicationPlays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763).
Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069).
Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (PubMed:24991833).
1 Publication2 PublicationsForms 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.
1 PublicationForms 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.
1 PublicationPlays an essential role in viral replication by forming a homodimer that binds single-stranded RNA.
1 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.
1 PublicationCaution
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).3 Publications 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.2 Publications EC:3.4.22.69
Cofactori
Kineticsi
- KM=1.15 mM for peptide TSAVLQSGFRK-NH21 Publication
- KM=0.58 mM for peptide SGVTFQGKFKK1 Publication
- KM=1.44 mM for peptide ATVRLQAGNAT1 Publication
pH dependencei
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 | 1651 | For PL-PRO activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1812 | For PL-PRO activityPROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 1826 | For PL-PRO activity1 Publication | 1 | |
Active sitei | 3281 | For 3CL-PRO activityPROSITE-ProRule annotation1 Publication | 1 | |
Active sitei | 3385 | For 3CL-PRO activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 4304 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4307 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4313 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4320 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4347 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4350 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4358 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 4360 | Zinc 2PROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1729 – 1766 | C4-typePROSITE-ProRule annotation1 PublicationAdd BLAST | 38 | |
Zinc fingeri | 4304 – 4320 | Add BLAST | 17 | |
Zinc fingeri | 4347 – 4360 | Add BLAST | 14 |
GO - Molecular functioni
- cysteine-type endopeptidase activity Source: UniProtKB
- double-stranded RNA binding Source: UniProtKB
- endonuclease activity Source: UniProtKB-KW
- G-quadruplex RNA binding Source: InterPro
- identical protein binding Source: IntAct
- ISG15-specific protease activity Source: UniProtKB
- lyase activity Source: UniProtKB-KW
- protein dimerization activity Source: UniProtKB
- RNA-directed 5'-3' RNA polymerase activity Source: Reactome
- single-stranded RNA binding Source: UniProtKB
- thiol-dependent deubiquitinase Source: UniProtKB-EC
- 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
- viral transcription Source: UniProtKB
Keywordsi
Enzyme and pathway databases
Reactomei | R-HSA-9679504, Translation of Replicase and Assembly of the Replication Transcription Complex R-HSA-9682706, Replication of the SARS-CoV-1 genome R-HSA-9682708, Transcription of SARS-CoV-1 sgRNAs R-HSA-9683439, Assembly of the SARS-CoV-1 Replication-Transcription Complex (RTC) R-HSA-9684325, Maturation of replicase proteins |
SABIO-RKi | P0C6U8 |
Protein family/group databases
MEROPSi | C30.005 |
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 Alternative name(s): Main protease Short name: Mpro Non-structural protein 5 Short name: nsp5 SARS coronavirus main proteinase Alternative name(s): Growth factor-like peptide Short name: GFL |
Gene namesi | ORF Names:1a |
Organismi | Severe acute respiratory syndrome coronavirus (SARS-CoV) |
Taxonomic identifieri | 694009 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Nidovirales › Cornidovirineae › Coronaviridae › Orthocoronavirinae › Betacoronavirus › Sarbecovirus |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] Paguma larvata (Masked palm civet) [TaxID: 9675] |
Proteomesi |
|
Subcellular locationi
- Host cytoplasm By similarity
- Host endosome By similarity
- Host membrane Curated; Multi-pass membrane protein
- Host cytoplasm 1 Publication
- Host membrane ; Multi-pass membrane protein
- Host cytoplasm 1 Publication Note: Localizes in virally-induced cytoplasmic double-membrane vesicles.2 Publications
- Host cytoplasm By similarity
- Host Golgi apparatus By similarity
- Host membrane Curated; Multi-pass membrane protein Curated
- host perinuclear region By similarity
- Host cytoplasm By similarity
- Host endoplasmic reticulum By similarity Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
- host perinuclear region 1 Publication
- Host cytoplasm By similarity
- Host endoplasmic reticulum By similarity Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
- host perinuclear region By similarity
- Host cytoplasm By similarity
- Host endoplasmic reticulum By similarity Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
- host perinuclear region By similarity
- Host cytoplasm By similarity
- Host endoplasmic reticulum By similarity Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 2202 | Cytoplasmic1 PublicationAdd BLAST | 2202 | |
Transmembranei | 2203 – 2223 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 2224 – 2303 | Lumenal1 PublicationAdd BLAST | 80 | |
Transmembranei | 2304 – 2324 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 2325 – 2754 | Cytoplasmic1 PublicationAdd BLAST | 430 | |
Transmembranei | 2755 – 2775 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 2776 – 3021 | Lumenal1 PublicationAdd BLAST | 246 | |
Transmembranei | 3022 – 3042 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 3043 – 3076 | Cytoplasmic1 PublicationAdd BLAST | 34 | |
Transmembranei | 3077 – 3097 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 3098 – 3104 | Lumenal1 Publication | 7 | |
Transmembranei | 3105 – 3125 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 3126 – 3563 | Cytoplasmic1 PublicationAdd BLAST | 438 | |
Transmembranei | 3564 – 3584 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 3585 | Lumenal1 Publication | 1 | |
Transmembranei | 3586 – 3606 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 3607 – 3611 | Cytoplasmic1 Publication | 5 | |
Transmembranei | 3612 – 3632 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 3633 – 3657 | Lumenal1 PublicationAdd BLAST | 25 | |
Transmembranei | 3658 – 3678 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 3679 – 3727 | Cytoplasmic1 PublicationAdd BLAST | 49 | |
Transmembranei | 3728 – 3748 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 3749 – 3755 | Lumenal1 Publication | 7 | |
Transmembranei | 3756 – 3776 | Helical1 PublicationAdd BLAST | 21 | |
Topological domaini | 3777 – 4382 | Cytoplasmic1 PublicationAdd BLAST | 606 |
Keywords - Cellular componenti
Host cytoplasm, Host endoplasmic reticulum, Host endosome, Host Golgi apparatus, Host membrane, MembranePathology & Biotechi
Chemistry databases
ChEMBLi | CHEMBL3927 |
DrugBanki | DB07620, 2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINITRO-5-(TRIFLUOROMETHYL)BENZENE DB08732, NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1R)-4-HYDROXY-1-METHYL-2-OXOBUTYL]-L-PHENYLALANINAMIDE DB07743, S-[5-(TRIFLUOROMETHYL)-4H-1,2,4-TRIAZOL-3-YL] 5-(PHENYLETHYNYL)FURAN-2-CARBOTHIOATE |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000338254 | 1 – 4382 | Replicase polyprotein 1aAdd BLAST | 4382 | |
ChainiPRO_0000338255 | 1 – 180 | Host translation inhibitor nsp1Add BLAST | 180 | |
ChainiPRO_0000338256 | 181 – 818 | Non-structural protein 2Add BLAST | 638 | |
ChainiPRO_0000338257 | 819 – 2740 | Papain-like protease nsp3Add BLAST | 1922 | |
ChainiPRO_0000338258 | 2741 – 3240 | Non-structural protein 4Sequence analysisAdd BLAST | 500 | |
ChainiPRO_0000338259 | 3241 – 3546 | 3C-like proteinase nsp5Add BLAST | 306 | |
ChainiPRO_0000338260 | 3547 – 3836 | Non-structural protein 6Add BLAST | 290 | |
ChainiPRO_0000338261 | 3837 – 3919 | Non-structural protein 7Add BLAST | 83 | |
ChainiPRO_0000338262 | 3920 – 4117 | Non-structural protein 8Add BLAST | 198 | |
ChainiPRO_0000338263 | 4118 – 4230 | Non-structural protein 9Add BLAST | 113 | |
ChainiPRO_0000338264 | 4231 – 4369 | Non-structural protein 10Add BLAST | 139 | |
ChainiPRO_0000338265 | 4370 – 4382 | Non-structural protein 11Add BLAST | 13 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 180 – 181 | Cleavage; by PL-PRO1 Publication | 2 | |
Sitei | 818 – 819 | Cleavage; by PL-PRO1 Publication | 2 | |
Sitei | 2740 – 2741 | Cleavage; by PL-PRO1 Publication | 2 | |
Sitei | 3240 – 3241 | Cleavage; by 3CL-PRO1 Publication | 2 | |
Sitei | 3546 – 3547 | Cleavage; by 3CL-PRO1 Publication | 2 | |
Sitei | 3836 – 3837 | Cleavage; by 3CL-PRO2 Publications | 2 | |
Sitei | 3919 – 3920 | Cleavage; by 3CL-PRO2 Publications | 2 | |
Sitei | 4117 – 4118 | Cleavage; by 3CL-PRO2 Publications | 2 | |
Sitei | 4230 – 4231 | Cleavage; by 3CL-PRO2 Publications | 2 | |
Sitei | 4369 – 4370 | Cleavage; by 3CL-PRO1 Publication | 2 |
Proteomic databases
PRIDEi | P0C6U8 |
Interactioni
Subunit structurei
Interacts with papain-like protease and non-structural protein 6.
1 PublicationExists as monomer and homodimer. Only the homodimer shows catalytic activity.
2 PublicationsEight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure.
1 PublicationBinary interactionsi
P0C6U8
With | #Exp. | IntAct |
---|---|---|
itself | 6 | EBI-15810860,EBI-15810860 |
3C-like proteinase nsp5 (PRO_0000338259) | 3 | EBI-15810860,EBI-25496008 |
Papain-like protease nsp3 (PRO_0000338257)
Non-structural protein 9 (PRO_0000338263)
With | #Exp. | IntAct |
---|---|---|
itself | 4 | EBI-25610723,EBI-25610723 |
Non-structural protein 11 (PRO_0000338265)
With | #Exp. | IntAct |
---|---|---|
Non-structural protein 2 (PRO_0000037310) | 2 | EBI-25492625,EBI-25474098 |
GO - Molecular functioni
- identical protein binding Source: IntAct
- protein dimerization activity Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 4383937, 4 interactors |
DIPi | DIP-48580N |
IntActi | P0C6U8, 21 interactors |
Chemistry databases
BindingDBi | P0C6U8 |
Structurei
Secondary structure
3D structure databases
BMRBi | P0C6U8 |
SASBDBi | P0C6U8 |
SMRi | P0C6U8 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0C6U8 |
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 | 822 – 930 | Ubiquitin-like 1PROSITE-ProRule annotationAdd BLAST | 109 | |
Domaini | 1003 – 1169 | Macro 1PROSITE-ProRule annotationAdd BLAST | 167 | |
Domaini | 1207 – 1335 | Macro 2PROSITE-ProRule annotationAdd BLAST | 129 | |
Domaini | 1343 – 1470 | Macro 3PROSITE-ProRule annotationAdd BLAST | 128 | |
Domaini | 1472 – 1538 | DPUPPROSITE-ProRule annotationAdd BLAST | 67 | |
Domaini | 1542 – 1597 | Ubiquitin-like 2PROSITE-ProRule annotationAdd BLAST | 56 | |
Domaini | 1611 – 1875 | Peptidase C16PROSITE-ProRule annotationAdd BLAST | 265 | |
Domaini | 1888 – 1998 | Nucleic acid-bindingPROSITE-ProRule annotationAdd BLAST | 111 | |
Domaini | 2023 – 2132 | G2MPROSITE-ProRule annotationAdd BLAST | 110 | |
Domaini | 2637 – 2740 | CoV Nsp3 Y3PROSITE-ProRule annotationAdd BLAST | 104 | |
Domaini | 3142 – 3240 | Nsp4CPROSITE-ProRule annotationAdd BLAST | 99 | |
Domaini | 3241 – 3546 | Peptidase C30PROSITE-ProRule annotationAdd BLAST | 306 | |
Domaini | 3837 – 3919 | RdRp Nsp7 cofactorPROSITE-ProRule annotationAdd BLAST | 83 | |
Domaini | 3920 – 4117 | RdRp Nsp8 cofactorPROSITE-ProRule annotationAdd BLAST | 198 | |
Domaini | 4118 – 4230 | Nsp9 ssRNA-bindingPROSITE-ProRule annotationAdd BLAST | 113 | |
Domaini | 4231 – 4369 | ExoN/MTase coactivatorPROSITE-ProRule annotationAdd BLAST | 139 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
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 | 972 – 1003 | DisorderedSequence analysisAdd BLAST | 32 | |
Regioni | 1175 – 1198 | DisorderedSequence analysisAdd BLAST | 24 | |
Regioni | 2203 – 2324 | HD11 PublicationAdd BLAST | 122 | |
Regioni | 2755 – 3125 | HD21 PublicationAdd BLAST | 371 | |
Regioni | 3564 – 3776 | HD31 PublicationAdd BLAST | 213 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 972 – 997 | Acidic residuesSequence analysisAdd BLAST | 26 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1729 – 1766 | C4-typePROSITE-ProRule annotation1 PublicationAdd BLAST | 38 | |
Zinc fingeri | 4304 – 4320 | Add BLAST | 17 | |
Zinc fingeri | 4347 – 4360 | Add BLAST | 14 |
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 cd21562, Macro_cv_SUD-N_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 IPR044374, NSP3_SUD-N_SARS-CoV 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 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
MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT
60 70 80 90 100
CGLVELEKGV LPQLEQPYVF IKRSDALSTN HGHKVVELVA EMDGIQYGRS
110 120 130 140 150
GITLGVLVPH VGETPIAYRN VLLRKNGNKG AGGHSYGIDL KSYDLGDELG
160 170 180 190 200
TDPIEDYEQN WNTKHGSGAL RELTRELNGG AVTRYVDNNF CGPDGYPLDC
210 220 230 240 250
IKDFLARAGK SMCTLSEQLD YIESKRGVYC CRDHEHEIAW FTERSDKSYE
260 270 280 290 300
HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
310 320 330 340 350
RSVYPVASPQ ECNNMHLSTL MKCNHCDEVS WQTCDFLKAT CEHCGTENLV
360 370 380 390 400
IEGPTTCGYL PTNAVVKMPC PACQDPEIGP EHSVADYHNH SNIETRLRKG
410 420 430 440 450
GRTRCFGGCV FAYVGCYNKR AYWVPRASAD IGSGHTGITG DNVETLNEDL
460 470 480 490 500
LEILSRERVN INIVGDFHLN EEVAIILASF SASTSAFIDT IKSLDYKSFK
510 520 530 540 550
TIVESCGNYK VTKGKPVKGA WNIGQQRSVL TPLCGFPSQA AGVIRSIFAR
560 570 580 590 600
TLDAANHSIP DLQRAAVTIL DGISEQSLRL VDAMVYTSDL LTNSVIIMAY
610 620 630 640 650
VTGGLVQQTS QWLSNLLGTT VEKLRPIFEW IEAKLSAGVE FLKDAWEILK
660 670 680 690 700
FLITGVFDIV KGQIQVASDN IKDCVKCFID VVNKALEMCI DQVTIAGAKL
710 720 730 740 750
RSLNLGEVFI AQSKGLYRQC IRGKEQLQLL MPLKAPKEVT FLEGDSHDTV
760 770 780 790 800
LTSEEVVLKN GELEALETPV DSFTNGAIVG TPVCVNGLML LEIKDKEQYC
810 820 830 840 850
ALSPGLLATN NVFRLKGGAP IKGVTFGEDT VWEVQGYKNV RITFELDERV
860 870 880 890 900
DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
910 920 930 940 950
WSVATFYLFD DAGEENFSSR MYCSFYPPDE EEEDDAECEE EEIDETCEHE
960 970 980 990 1000
YGTEDDYQGL PLEFGASAET VRVEEEEEED WLDDTTEQSE IEPEPEPTPE
1010 1020 1030 1040 1050
EPVNQFTGYL KLTDNVAIKC VDIVKEAQSA NPMVIVNAAN IHLKHGGGVA
1060 1070 1080 1090 1100
GALNKATNGA MQKESDDYIK LNGPLTVGGS CLLSGHNLAK KCLHVVGPNL
1110 1120 1130 1140 1150
NAGEDIQLLK AAYENFNSQD ILLAPLLSAG IFGAKPLQSL QVCVQTVRTQ
1160 1170 1180 1190 1200
VYIAVNDKAL YEQVVMDYLD NLKPRVEAPK QEEPPNTEDS KTEEKSVVQK
1210 1220 1230 1240 1250
PVDVKPKIKA CIDEVTTTLE ETKFLTNKLL LFADINGKLY HDSQNMLRGE
1260 1270 1280 1290 1300
DMSFLEKDAP YMVGDVITSG DITCVVIPSK KAGGTTEMLS RALKKVPVDE
1310 1320 1330 1340 1350
YITTYPGQGC AGYTLEEAKT ALKKCKSAFY VLPSEAPNAK EEILGTVSWN
1360 1370 1380 1390 1400
LREMLAHAEE TRKLMPICMD VRAIMATIQR KYKGIKIQEG IVDYGVRFFF
1410 1420 1430 1440 1450
YTSKEPVASI ITKLNSLNEP LVTMPIGYVT HGFNLEEAAR CMRSLKAPAV
1460 1470 1480 1490 1500
VSVSSPDAVT TYNGYLTSSS KTSEEHFVET VSLAGSYRDW SYSGQRTELG
1510 1520 1530 1540 1550
VEFLKRGDKI VYHTLESPVE FHLDGEVLSL DKLKSLLSLR EVKTIKVFTT
1560 1570 1580 1590 1600
VDNTNLHTQL VDMSMTYGQQ FGPTYLDGAD VTKIKPHVNH EGKTFFVLPS
1610 1620 1630 1640 1650
DDTLRSEAFE YYHTLDESFL GRYMSALNHT KKWKFPQVGG LTSIKWADNN
1660 1670 1680 1690 1700
CYLSSVLLAL QQLEVKFNAP ALQEAYYRAR AGDAANFCAL ILAYSNKTVG
1710 1720 1730 1740 1750
ELGDVRETMT HLLQHANLES AKRVLNVVCK HCGQKTTTLT GVEAVMYMGT
1760 1770 1780 1790 1800
LSYDNLKTGV SIPCVCGRDA TQYLVQQESS FVMMSAPPAE YKLQQGTFLC
1810 1820 1830 1840 1850
ANEYTGNYQC GHYTHITAKE TLYRIDGAHL TKMSEYKGPV TDVFYKETSY
1860 1870 1880 1890 1900
TTTIKPVSYK LDGVTYTEIE PKLDGYYKKD NAYYTEQPID LVPTQPLPNA
1910 1920 1930 1940 1950
SFDNFKLTCS NTKFADDLNQ MTGFTKPASR ELSVTFFPDL NGDVVAIDYR
1960 1970 1980 1990 2000
HYSASFKKGA KLLHKPIVWH INQATTKTTF KPNTWCLRCL WSTKPVDTSN
2010 2020 2030 2040 2050
SFEVLAVEDT QGMDNLACES QQPTSEEVVE NPTIQKEVIE CDVKTTEVVG
2060 2070 2080 2090 2100
NVILKPSDEG VKVTQELGHE DLMAAYVENT SITIKKPNEL SLALGLKTIA
2110 2120 2130 2140 2150
THGIAAINSV PWSKILAYVK PFLGQAAITT SNCAKRLAQR VFNNYMPYVF
2160 2170 2180 2190 2200
TLLFQLCTFT KSTNSRIRAS LPTTIAKNSV KSVAKLCLDA GINYVKSPKF
2210 2220 2230 2240 2250
SKLFTIAMWL LLLSICLGSL ICVTAAFGVL LSNFGAPSYC NGVRELYLNS
2260 2270 2280 2290 2300
SNVTTMDFCE GSFPCSICLS GLDSLDSYPA LETIQVTISS YKLDLTILGL
2310 2320 2330 2340 2350
AAEWVLAYML FTKFFYLLGL SAIMQVFFGY FASHFISNSW LMWFIISIVQ
2360 2370 2380 2390 2400
MAPVSAMVRM YIFFASFYYI WKSYVHIMDG CTSSTCMMCY KRNRATRVEC
2410 2420 2430 2440 2450
TTIVNGMKRS FYVYANGGRG FCKTHNWNCL NCDTFCTGST FISDEVARDL
2460 2470 2480 2490 2500
SLQFKRPINP TDQSSYIVDS VAVKNGALHL YFDKAGQKTY ERHPLSHFVN
2510 2520 2530 2540 2550
LDNLRANNTK GSLPINVIVF DGKSKCDESA SKSASVYYSQ LMCQPILLLD
2560 2570 2580 2590 2600
QALVSDVGDS TEVSVKMFDA YVDTFSATFS VPMEKLKALV ATAHSELAKG
2610 2620 2630 2640 2650
VALDGVLSTF VSAARQGVVD TDVDTKDVIE CLKLSHHSDL EVTGDSCNNF
2660 2670 2680 2690 2700
MLTYNKVENM TPRDLGACID CNARHINAQV AKSHNVSLIW NVKDYMSLSE
2710 2720 2730 2740 2750
QLRKQIRSAA KKNNIPFRLT CATTRQVVNV ITTKISLKGG KIVSTCFKLM
2760 2770 2780 2790 2800
LKATLLCVLA ALVCYIVMPV HTLSIHDGYT NEIIGYKAIQ DGVTRDIIST
2810 2820 2830 2840 2850
DDCFANKHAG FDAWFSQRGG SYKNDKSCPV VAAIITREIG FIVPGLPGTV
2860 2870 2880 2890 2900
LRAINGDFLH FLPRVFSAVG NICYTPSKLI EYSDFATSAC VLAAECTIFK
2910 2920 2930 2940 2950
DAMGKPVPYC YDTNLLEGSI SYSELRPDTR YVLMDGSIIQ FPNTYLEGSV
2960 2970 2980 2990 3000
RVVTTFDAEY CRHGTCERSE VGICLSTSGR WVLNNEHYRA LSGVFCGVDA
3010 3020 3030 3040 3050
MNLIANIFTP LVQPVGALDV SASVVAGGII AILVTCAAYY FMKFRRVFGE
3060 3070 3080 3090 3100
YNHVVAANAL LFLMSFTILC LVPAYSFLPG VYSVFYLYLT FYFTNDVSFL
3110 3120 3130 3140 3150
AHLQWFAMFS PIVPFWITAI YVFCISLKHC HWFFNNYLRK RVMFNGVTFS
3160 3170 3180 3190 3200
TFEEAALCTF LLNKEMYLKL RSETLLPLTQ YNRYLALYNK YKYFSGALDT
3210 3220 3230 3240 3250
TSYREAACCH LAKALNDFSN SGADVLYQPP QTSITSAVLQ SGFRKMAFPS
3260 3270 3280 3290 3300
GKVEGCMVQV TCGTTTLNGL WLDDTVYCPR HVICTAEDML NPNYEDLLIR
3310 3320 3330 3340 3350
KSNHSFLVQA GNVQLRVIGH SMQNCLLRLK VDTSNPKTPK YKFVRIQPGQ
3360 3370 3380 3390 3400
TFSVLACYNG SPSGVYQCAM RPNHTIKGSF LNGSCGSVGF NIDYDCVSFC
3410 3420 3430 3440 3450
YMHHMELPTG VHAGTDLEGK FYGPFVDRQT AQAAGTDTTI TLNVLAWLYA
3460 3470 3480 3490 3500
AVINGDRWFL NRFTTTLNDF NLVAMKYNYE PLTQDHVDIL GPLSAQTGIA
3510 3520 3530 3540 3550
VLDMCAALKE LLQNGMNGRT ILGSTILEDE FTPFDVVRQC SGVTFQGKFK
3560 3570 3580 3590 3600
KIVKGTHHWM LLTFLTSLLI LVQSTQWSLF FFVYENAFLP FTLGIMAIAA
3610 3620 3630 3640 3650
CAMLLVKHKH AFLCLFLLPS LATVAYFNMV YMPASWVMRI MTWLELADTS
3660 3670 3680 3690 3700
LSGYRLKDCV MYASALVLLI LMTARTVYDD AARRVWTLMN VITLVYKVYY
3710 3720 3730 3740 3750
GNALDQAISM WALVISVTSN YSGVVTTIMF LARAIVFVCV EYYPLLFITG
3760 3770 3780 3790 3800
NTLQCIMLVY CFLGYCCCCY FGLFCLLNRY FRLTLGVYDY LVSTQEFRYM
3810 3820 3830 3840 3850
NSQGLLPPKS SIDAFKLNIK LLGIGGKPCI KVATVQSKMS DVKCTSVVLL
3860 3870 3880 3890 3900
SVLQQLRVES SSKLWAQCVQ LHNDILLAKD TTEAFEKMVS LLSVLLSMQG
3910 3920 3930 3940 3950
AVDINRLCEE MLDNRATLQA IASEFSSLPS YAAYATAQEA YEQAVANGDS
3960 3970 3980 3990 4000
EVVLKKLKKS LNVAKSEFDR DAAMQRKLEK MADQAMTQMY KQARSEDKRA
4010 4020 4030 4040 4050
KVTSAMQTML FTMLRKLDND ALNNIINNAR DGCVPLNIIP LTTAAKLMVV
4060 4070 4080 4090 4100
VPDYGTYKNT CDGNTFTYAS ALWEIQQVVD ADSKIVQLSE INMDNSPNLA
4110 4120 4130 4140 4150
WPLIVTALRA NSAVKLQNNE LSPVALRQMS CAAGTTQTAC TDDNALAYYN
4160 4170 4180 4190 4200
NSKGGRFVLA LLSDHQDLKW ARFPKSDGTG TIYTELEPPC RFVTDTPKGP
4210 4220 4230 4240 4250
KVKYLYFIKG LNNLNRGMVL GSLAATVRLQ AGNATEVPAN STVLSFCAFA
4260 4270 4280 4290 4300
VDPAKAYKDY LASGGQPITN CVKMLCTHTG TGQAITVTPE ANMDQESFGG
4310 4320 4330 4340 4350
ASCCLYCRCH IDHPNPKGFC DLKGKYVQIP TTCANDPVGF TLRNTVCTVC
4360 4370 4380
GMWKGYGCSC DQLREPLMQS ADASTFLNGF AV
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Mass spectrometryi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 82 | G → C in strain: Isolate GD01. | 1 | |
Natural varianti | 130 | G → R in strain: Isolate GD01. | 1 | |
Natural varianti | 138 | I → T in strain: Isolate SZ16. | 1 | |
Natural varianti | 181 | A → V in strain: Isolate Shanghai LY. | 1 | |
Natural varianti | 225 | K → Q in strain: Isolate GD01. | 1 | |
Natural varianti | 249 | Y → C in strain: Isolate Shanghai LY. | 1 | |
Natural varianti | 306 | V → F in strain: Isolate BJ04. | 1 | |
Natural varianti | 549 | A → S in strain: Isolate SZ3. | 1 | |
Natural varianti | 765 | A → T in strain: Isolate FRA and Isolate Frankfurt-1. | 1 | |
Natural varianti | 852 | K → R in strain: Isolate SZ16. | 1 | |
Natural varianti | 1004 | N → H in strain: Isolate BJ03. | 1 | |
Natural varianti | 1021 | V → A in strain: Isolate SZ3 and Isolate SZ16. | 1 | |
Natural varianti | 1023 | I → T in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 1121 | I → T in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16. | 1 | |
Natural varianti | 1136 | P → L in strain: Isolate SZ3 and Isolate SZ16. | 1 | |
Natural varianti | 1257 | K → E in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 1319 | K → R in strain: Isolate GD01. | 1 | |
Natural varianti | 1329 | F → S in strain: Isolate GD01. | 1 | |
Natural varianti | 1361 | T → A in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 1385 | I → V in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 1538 | S → T in strain: Isolate GD01. | 1 | |
Natural varianti | 1563 | M → K in strain: Isolate BJ02. | 1 | |
Natural varianti | 1663 | L → I in strain: Isolate SZ3 and Isolate SZ16. | 1 | |
Natural varianti | 1762 | I → L in strain: Isolate BJ03. | 1 | |
Natural varianti | 1776 – 1777 | QQ → PP in strain: Isolate BJ03. | 2 | |
Natural varianti | 1790 | E → G in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 1806 | G → V in strain: Isolate BJ02. | 1 | |
Natural varianti | 1962 | L → I in strain: Isolate BJ04. | 1 | |
Natural varianti | 2116 | L → F in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16. | 1 | |
Natural varianti | 2222 | C → Y in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16. | 1 | |
Natural varianti | 2269 | L → S in strain: Isolate SZ3 and Isolate SZ16. | 1 | |
Natural varianti | 2326 | V → A in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 2392 – 2394 | RNR → CNH in strain: Isolate Shanghai QXC1. | 3 | |
Natural varianti | 2480 | L → P in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 2552 | A → V in strain: Isolate Urbani and Isolate Taiwan TC2. | 1 | |
Natural varianti | 2556 | D → N in strain: Isolate HKU-39849. | 1 | |
Natural varianti | 2564 | S → P in strain: Isolate GD01. | 1 | |
Natural varianti | 2648 | N → Y in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 2708 | S → T in strain: Isolate HKU-39849. | 1 | |
Natural varianti | 2718 | R → T in strain: Isolate HKU-39849. | 1 | |
Natural varianti | 2746 | C → W in strain: Isolate SZ3 and Isolate SZ16. | 1 | |
Natural varianti | 2770 | V → L in strain: Isolate BJ01 and Isolate BJ02. | 1 | |
Natural varianti | 2944 | T → I in strain: Isolate SIN2500, Isolate GD01 and Isolate GZ50. | 1 | |
Natural varianti | 2971 | V → A in strain: Isolate GD01 and Isolate SZ16. | 1 | |
Natural varianti | 3020 | V → A in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 3047 | V → A in strain: Isolate CUHK-W1, Isolate GD01, Isolate SZ3, Isolate SZ16, Isolate BJ01, Isolate BJ02, Isolate BJ03 and Isolate Shanghai QXC1. | 1 | |
Natural varianti | 3072 | V → A in strain: Isolate CUHK-W1, Isolate SZ3, Isolate SZ16 and Isolate GD01. | 1 | |
Natural varianti | 3197 | A → V in strain: Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04 and Isolate Shanghai QXC1. | 1 | |
Natural varianti | 3429 | Q → P in strain: Isolate BJ02. | 1 | |
Natural varianti | 3488 | D → E in strain: Isolate BJ04. | 1 | |
Natural varianti | 3717 | V → A in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 3818 | N → T in strain: Isolate BJ04. | 1 | |
Natural varianti | 3903 | D → N in strain: Isolate BJ03. | 1 | |
Natural varianti | 3904 | I → F in strain: Isolate BJ02. | 1 | |
Natural varianti | 3911 | M → V in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 4001 | K → Q in strain: Isolate Shanghai LY. | 1 | |
Natural varianti | 4003 | T → A in strain: Isolate Shanghai LY. | 1 | |
Natural varianti | 4085 | I → H in strain: Isolate ZJ01. | 1 | |
Natural varianti | 4114 | V → A in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 4202 | V → M in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 4240 | N → H in strain: Isolate ZJ01. | 1 | |
Natural varianti | 4296 | E → G in strain: Isolate Shanghai QXC1. | 1 | |
Natural varianti | 4377 – 4378 | LN → FK in strain: Isolate Shanghai QXC1. | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY278741 Genomic RNA Translation: AAP13439.1 AY274119 Genomic RNA No translation available. AY278554 Genomic RNA Translation: AAP13575.1 AY282752 Genomic RNA Translation: AAP30712.1 AY304495 Genomic RNA No translation available. AY304486 Genomic RNA No translation available. AY304488 Genomic RNA No translation available. AY278491 Genomic RNA No translation available. AY283794 Genomic RNA No translation available. AY283795 Genomic RNA No translation available. AY283796 Genomic RNA No translation available. AY283797 Genomic RNA No translation available. AY283798 Genomic RNA No translation available. AY286320 Genomic RNA Translation: AAR16181.1 AY278488 Genomic RNA Translation: AAP30029.1 AY278490 Genomic RNA No translation available. AY279354 Genomic RNA No translation available. AY278489 Genomic RNA Translation: AAP51226.1 AY291451 Genomic RNA Translation: AAP37016.1 AY310120 Genomic RNA Translation: AAP50484.1 AY291315 Genomic RNA Translation: AAP33695.1 AY323977 Genomic RNA Translation: AAP72974.2 AY321118 Genomic RNA No translation available. AY338174 Genomic RNA Translation: AAQ01595.1 AY338175 Genomic RNA Translation: AAQ01607.1 AY348314 Genomic RNA Translation: AAP97880.1 AP006557 Genomic RNA Translation: BAC81347.1 AP006558 Genomic RNA Translation: BAC81361.1 AP006559 Genomic RNA Translation: BAC81375.1 AP006560 Genomic RNA Translation: BAC81389.1 AP006561 Genomic RNA Translation: BAC81403.1 AY427439 Genomic RNA Translation: AAQ94059.1 AY322205 Genomic RNA Translation: AAP82966.1 AY322206 Genomic RNA Translation: AAP82976.1 AY463059 Genomic RNA No translation available. |
Keywords - Coding sequence diversityi
Ribosomal frameshiftingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY278741 Genomic RNA Translation: AAP13439.1 AY274119 Genomic RNA No translation available. AY278554 Genomic RNA Translation: AAP13575.1 AY282752 Genomic RNA Translation: AAP30712.1 AY304495 Genomic RNA No translation available. AY304486 Genomic RNA No translation available. AY304488 Genomic RNA No translation available. AY278491 Genomic RNA No translation available. AY283794 Genomic RNA No translation available. AY283795 Genomic RNA No translation available. AY283796 Genomic RNA No translation available. AY283797 Genomic RNA No translation available. AY283798 Genomic RNA No translation available. AY286320 Genomic RNA Translation: AAR16181.1 AY278488 Genomic RNA Translation: AAP30029.1 AY278490 Genomic RNA No translation available. AY279354 Genomic RNA No translation available. AY278489 Genomic RNA Translation: AAP51226.1 AY291451 Genomic RNA Translation: AAP37016.1 AY310120 Genomic RNA Translation: AAP50484.1 AY291315 Genomic RNA Translation: AAP33695.1 AY323977 Genomic RNA Translation: AAP72974.2 AY321118 Genomic RNA No translation available. AY338174 Genomic RNA Translation: AAQ01595.1 AY338175 Genomic RNA Translation: AAQ01607.1 AY348314 Genomic RNA Translation: AAP97880.1 AP006557 Genomic RNA Translation: BAC81347.1 AP006558 Genomic RNA Translation: BAC81361.1 AP006559 Genomic RNA Translation: BAC81375.1 AP006560 Genomic RNA Translation: BAC81389.1 AP006561 Genomic RNA Translation: BAC81403.1 AY427439 Genomic RNA Translation: AAQ94059.1 AY322205 Genomic RNA Translation: AAP82966.1 AY322206 Genomic RNA Translation: AAP82976.1 AY463059 Genomic RNA No translation available. |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1Q2W | X-ray | 1.86 | A/B | 3241-3544 | [»] | |
1QZ8 | X-ray | 2.70 | A/B | 4118-4230 | [»] | |
1UJ1 | X-ray | 1.90 | A/B | 3241-3546 | [»] | |
1UK2 | X-ray | 2.20 | A/B | 3241-3546 | [»] | |
1UK3 | X-ray | 2.40 | A/B | 3241-3546 | [»] | |
1UK4 | X-ray | 2.50 | A/B | 3241-3546 | [»] | |
1UW7 | X-ray | 2.80 | A | 4118-4230 | [»] | |
1WOF | X-ray | 2.00 | A/B | 3241-3546 | [»] | |
1YSY | NMR | - | A | 3837-3919 | [»] | |
1Z1I | X-ray | 2.80 | A | 3241-3546 | [»] | |
1Z1J | X-ray | 2.80 | A/B | 3241-3546 | [»] | |
2A5A | X-ray | 2.08 | A | 3241-3546 | [»] | |
2A5I | X-ray | 1.88 | A | 3241-3546 | [»] | |
2A5K | X-ray | 2.30 | A/B | 3241-3546 | [»] | |
2ACF | X-ray | 1.40 | A/B/C/D | 1002-1176 | [»] | |
2AHM | X-ray | 2.40 | A/B/C/D | 3837-3919 | [»] | |
E/F/G/H | 3920-4117 | [»] | ||||
2ALV | X-ray | 1.90 | A | 3241-3543 | [»] | |
2AMD | X-ray | 1.85 | A/B | 3241-3546 | [»] | |
2AMQ | X-ray | 2.30 | A/B | 3241-3546 | [»] | |
2BX3 | X-ray | 2.00 | A | 3241-3546 | [»] | |
2BX4 | X-ray | 2.79 | A | 3241-3546 | [»] | |
2C3S | X-ray | 1.90 | A | 3241-3546 | [»] | |
2D2D | X-ray | 2.70 | A/B | 3241-3546 | [»] | |
2DUC | X-ray | 1.70 | A/B | 3241-3546 | [»] | |
2FAV | X-ray | 1.80 | A/B/C | 1000-1173 | [»] | |
2FE8 | X-ray | 1.85 | A/B/C | 1541-1854 | [»] | |
2FYG | X-ray | 1.80 | A | 4240-4362 | [»] | |
2G9T | X-ray | 2.10 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X | 4231-4382 | [»] | |
2GA6 | X-ray | 2.70 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X | 4231-4382 | [»] | |
2GDT | NMR | - | A | 13-127 | [»] | |
2GRI | NMR | - | A | 819-930 | [»] | |
2GT7 | X-ray | 1.82 | A/B | 3241-3546 | [»] | |
2GT8 | X-ray | 2.00 | A | 3241-3546 | [»] | |
2GTB | X-ray | 2.00 | A | 3241-3546 | [»] | |
2GX4 | X-ray | 1.93 | A | 3241-3546 | [»] | |
2GZ7 | X-ray | 1.86 | A | 3241-3546 | [»] | |
2GZ8 | X-ray | 1.97 | A | 3241-3546 | [»] | |
2GZ9 | X-ray | 2.17 | A | 3241-3546 | [»] | |
2H2Z | X-ray | 1.60 | A | 3241-3546 | [»] | |
2HOB | X-ray | 1.95 | A | 3241-3546 | [»] | |
2HSX | NMR | - | A | 13-127 | [»] | |
2IDY | NMR | - | A | 819-930 | [»] | |
2KAF | NMR | - | A | 1473-1538 | [»] | |
2KQV | NMR | - | A | 1345-1538 | [»] | |
2KQW | NMR | - | A | 1345-1538 | [»] | |
2KYS | NMR | - | A | 3837-3919 | [»] | |
2LIZ | NMR | - | A | 3427-3546 | [»] | |
2OP9 | X-ray | 1.80 | A/B | 3241-3541 | [»] | |
2PWX | X-ray | 2.50 | A | 3241-3546 | [»] | |
2W2G | X-ray | 2.22 | A/B | 1207-1470 | [»] | |
2WCT | X-ray | 2.79 | A/B/C/D | 1207-1470 | [»] | |
2Z3C | X-ray | 1.79 | A | 3241-3546 | [»] | |
2Z3D | X-ray | 2.10 | A | 3241-3546 | [»] | |
2Z3E | X-ray | 2.32 | A | 3241-3546 | [»] | |
2ZU4 | X-ray | 1.93 | A | 3241-3546 | [»] | |
2ZU5 | X-ray | 1.65 | A | 3241-3546 | [»] | |
3ATW | X-ray | 2.36 | A/B | 3241-3546 | [»] | |
3AVZ | X-ray | 2.46 | A | 3241-3546 | [»] | |
3AW0 | X-ray | 2.30 | A | 3241-3546 | [»] | |
3AW1 | X-ray | 2.00 | A/B | 3241-3546 | [»] | |
3E91 | X-ray | 2.55 | A/B | 3241-3546 | [»] | |
3EA7 | X-ray | 2.65 | A/B | 3241-3546 | [»] | |
3EA8 | X-ray | 2.25 | A | 3241-3546 | [»] | |
3EA9 | X-ray | 2.40 | A | 3241-3546 | [»] | |
3EAJ | X-ray | 2.70 | A/B | 3241-3546 | [»] | |
3EE7 | X-ray | 2.60 | A/B/C/D | 4118-4230 | [»] | |
3F9E | X-ray | 2.50 | A | 3241-3546 | [»] | |
3F9F | X-ray | 2.30 | A/B | 3241-3546 | [»] | |
3F9G | X-ray | 2.60 | A/B | 3241-3541 | [»] | |
3F9H | X-ray | 2.90 | A/B | 3241-3546 | [»] | |
3FZD | X-ray | 2.35 | A | 3241-3541 | [»] | |
3IWM | X-ray | 3.20 | A/B/C/D | 3241-3546 | [»] | |
3M3S | X-ray | 2.30 | A/B | 3241-3546 | [»] | |
3M3T | X-ray | 2.90 | A | 3241-3546 | [»] | |
3M3V | X-ray | 2.70 | A/B | 3241-3546 | [»] | |
3MJ5 | X-ray | 2.63 | A/B | 1541-1855 | [»] | |
3R24 | X-ray | 2.00 | B | 4240-4382 | [»] | |
3SN8 | X-ray | 1.99 | A | 3241-3546 | [»] | |
3SNA | X-ray | 3.05 | A | 3241-3541 | [»] | |
3SNB | X-ray | 2.40 | A | 3241-3546 | [»] | |
3SNC | X-ray | 2.58 | A | 3241-3546 | [»] | |
3SND | X-ray | 1.89 | A/B | 3241-3546 | [»] | |
3SNE | X-ray | 2.60 | A | 3241-3546 | [»] | |
3SZN | X-ray | 1.69 | A | 3241-3546 | [»] | |
3TIT | X-ray | 1.99 | A | 3241-3546 | [»] | |
3TIU | X-ray | 2.08 | A | 3241-3546 | [»] | |
3TNS | X-ray | 1.99 | A | 3241-3546 | [»] | |
3TNT | X-ray | 1.59 | A | 3241-3546 | [»] | |
3V3M | X-ray | 1.96 | A | 3241-3546 | [»] | |
3VB3 | X-ray | 2.20 | A/B | 3241-3546 | [»] | |
3VB4 | X-ray | 2.20 | A/B | 3241-3546 | [»] | |
3VB5 | X-ray | 1.95 | A/B | 3241-3546 | [»] | |
3VB6 | X-ray | 2.50 | A/B | 3241-3546 | [»] | |
3VB7 | X-ray | 1.95 | A/B | 3241-3546 | [»] | |
4HI3 | X-ray | 2.09 | A/B | 3241-3546 | [»] | |
4M0W | X-ray | 1.40 | A | 1541-1858 | [»] | |
4MDS | X-ray | 1.60 | A | 3241-3542 | [»] | |
4MM3 | X-ray | 2.75 | B | 1541-1855 | [»] | |
4OVZ | X-ray | 2.50 | A/B | 1541-1855 | [»] | |
4OW0 | X-ray | 2.10 | A/B | 1541-1855 | [»] | |
5F22 | X-ray | 2.15 | A | 3837-3919 | [»] | |
5Y3E | X-ray | 1.65 | A | 1541-1854 | [»] | |
5Y3Q | X-ray | 1.65 | A | 1541-1854 | [»] | |
6LNY | X-ray | 2.25 | A | 3241-3546 | [»] | |
6LO0 | X-ray | 1.94 | A | 3241-3546 | [»] | |
6NUR | electron microscopy | 3.10 | B/D | 3920-4117 | [»] | |
6NUS | electron microscopy | 3.50 | B | 3920-4117 | [»] | |
6W2A | X-ray | 1.65 | A/B | 3241-3543 | [»] | |
6XHL | X-ray | 1.47 | A/B | 3241-3546 | [»] | |
6XHN | X-ray | 1.38 | A/B | 3241-3546 | [»] | |
6XHO | X-ray | 1.45 | A/B | 3241-3546 | [»] | |
6Y7M | X-ray | 1.90 | AAA | 3241-3546 | [»] | |
6YXJ | X-ray | 3.50 | A | 1207-1344 | [»] | |
7DQZ | X-ray | 1.99 | A/B | 3241-3546 | [»] | |
7EO8 | X-ray | 2.28 | A/B | 3241-3546 | [»] | |
7K0G | X-ray | 1.85 | A | 3241-3543 | [»] | |
7K0H | X-ray | 1.70 | A/B | 3241-3543 | [»] | |
7LFU | X-ray | 2.29 | D | 1541-1856 | [»] | |
7LFV | X-ray | 2.23 | A/B | 1541-1856 | [»] | |
7LMG | X-ray | 1.60 | AAA | 3241-3546 | [»] | |
7LMH | X-ray | 1.85 | AAA | 3241-3546 | [»] | |
7LMI | X-ray | 1.71 | AAA | 3241-3546 | [»] | |
7LMJ | X-ray | 1.69 | AAA | 3241-3546 | [»] | |
7OPL | electron microscopy | 4.12 | E | 13-127 | [»] | |
7RC1 | X-ray | 1.63 | A | 3241-3546 | [»] | |
BMRBi | P0C6U8 | |||||
SASBDBi | P0C6U8 | |||||
SMRi | P0C6U8 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4383937, 4 interactors |
DIPi | DIP-48580N |
IntActi | P0C6U8, 21 interactors |
Chemistry databases
BindingDBi | P0C6U8 |
ChEMBLi | CHEMBL3927 |
DrugBanki | DB07620, 2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINITRO-5-(TRIFLUOROMETHYL)BENZENE DB08732, NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1R)-4-HYDROXY-1-METHYL-2-OXOBUTYL]-L-PHENYLALANINAMIDE DB07743, S-[5-(TRIFLUOROMETHYL)-4H-1,2,4-TRIAZOL-3-YL] 5-(PHENYLETHYNYL)FURAN-2-CARBOTHIOATE |
Protein family/group databases
MEROPSi | C30.005 |
Proteomic databases
PRIDEi | P0C6U8 |
Enzyme and pathway databases
Reactomei | R-HSA-9679504, Translation of Replicase and Assembly of the Replication Transcription Complex R-HSA-9682706, Replication of the SARS-CoV-1 genome R-HSA-9682708, Transcription of SARS-CoV-1 sgRNAs R-HSA-9683439, Assembly of the SARS-CoV-1 Replication-Transcription Complex (RTC) R-HSA-9684325, Maturation of replicase proteins |
SABIO-RKi | P0C6U8 |
Miscellaneous databases
EvolutionaryTracei | P0C6U8 |
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 cd21562, Macro_cv_SUD-N_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 IPR044374, NSP3_SUD-N_SARS-CoV 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 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_SARS | |
Accessioni | P0C6U8Primary (citable) accession number: P0C6U8 Secondary accession number(s): P59641 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 10, 2008 |
Last sequence update: | June 10, 2008 | |
Last modified: | May 25, 2022 | |
This is version 109 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