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Entry version 8 (02 Jun 2021)
Sequence version 1 (22 Apr 2020)
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Protein

Replicase polyprotein 1a

Gene
N/A
Organism
Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.

By similarity

Inhibits host translation by interacting with binds to the host 40S subunit in ribosomal complexes, including the 43S pre-initiation complex and the non-translating 80S ribosome (PubMed:32680882,PubMed:32908316).

The C-terminus binds to and obstructs ribosomal mRNA entry tunnel (PubMed:32680882,PubMed:32908316).

Thereby inhibits antiviral response triggered by innate immunity or interferons (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).

By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity).

By similarity3 Publications

May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.

By similarity

Responsible for the cleavages located at the N-terminus of the replicase polyprotein. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication (By similarity).

Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (By similarity) (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. Cleaves preferentially ISG15 from substrates in vitro (PubMed:32726803).

Can play a role in host ADP-ribosylation by binding ADP-ribose (PubMed:32578982).

By similarity3 Publications

Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.

By similarity

Cleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856).

Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481).

Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity) (PubMed:32198291, PubMed:32272481).

By similarity3 Publications

Plays 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 Publication

Plays 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 Publications

Plays 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).

By similarity4 Publications

May participate in viral replication by acting as a ssRNA-binding protein.

By similarity

Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.

By similarity

Miscellaneous

Produced by conventional translation.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited in vitro by GRL-0617.1 Publication
Inhibited by pyridone-containing alpha-ketoamides compounds 13a and 13b. In turn, alpha-ketoamide 13b (tert-butyl (1-((S)-1-(((S)-4-(benzylamino)-3,4-dioxo-1-((S)-2-oxopyrrolidin-3-yl)butan-2-yl)amino)-3-cyclopropyl-1-oxopropan-2-yl)-2-oxo-1,2-dihydropyridin-3-yl)carbamate) inhibits SARS-CoV-2 replication in human lung cells (PubMed:32198291). Inhibited ex vivo by michael acceptor inhibitor N3 (PubMed:32272481). Inhibited ex vivo by compound 11a and 11b (PubMed:32321856).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1674For PL1-PRO activityPROSITE-ProRule annotation1 Publication1
Active sitei1835For PL2-PRO activityPROSITE-ProRule annotation1
Active sitei3304For 3CL-PRO activityPROSITE-ProRule annotation1 Publication1
Active sitei3408For 3CL-PRO activityPROSITE-ProRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi4327Zinc 1PROSITE-ProRule annotation1
Metal bindingi4330Zinc 1PROSITE-ProRule annotation1
Metal bindingi4336Zinc 1PROSITE-ProRule annotation1
Metal bindingi4343Zinc 1PROSITE-ProRule annotation1
Metal bindingi4370Zinc 2PROSITE-ProRule annotation1
Metal bindingi4373Zinc 2PROSITE-ProRule annotation1
Metal bindingi4381Zinc 2PROSITE-ProRule annotation1
Metal bindingi4383Zinc 2PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1752 – 1789C4-typePROSITE-ProRule annotationAdd BLAST38

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease, Protease, RNA-binding, Thiol protease
Biological processActivation of host autophagy by virus, Decay of host mRNAs by virus, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host IRF3 by virus, Inhibition of host ISG15 by virus, Inhibition of host RLR pathway by virus, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway, Viral immunoevasion
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Replicase polyprotein 1a
Short 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
Non-structural protein 2
Short name:
nsp2
Alternative name(s):
p65 homolog
Non-structural protein 3 (EC:3.4.19.121 Publication, EC:3.4.22.-)
Short name:
nsp3
Alternative name(s):
PL2-PRO
Papain-like protease1 Publication
Papain-like proteinase
Short name:
PL-PRO
Non-structural protein 4
Short name:
nsp4
3C-like proteinase (EC:3.4.22.69)
Short name:
3CL-PRO
Short name:
3CLp
Alternative name(s):
Main protease
Short name:
Mpro1 Publication
Non-structural protein 5
Short name:
nsp5
SARS coronavirus main proteinase
Non-structural protein 6
Short name:
nsp6
Non-structural protein 7
Short name:
nsp7
Non-structural protein 8
Short name:
nsp8
Non-structural protein 9
Short name:
nsp9
Non-structural protein 10
Short name:
nsp10
Alternative name(s):
Growth factor-like peptide
Short name:
GFL
Non-structural protein 11
Short name:
nsp11
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSevere acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri2697049 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesRiboviriaOrthornaviraePisuviricotaPisoniviricetesNidoviralesCornidovirineaeCoronaviridaeOrthocoronavirinaeBetacoronavirusSarbecovirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000464024 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei2226 – 2246HelicalSequence analysisAdd BLAST21
Transmembranei2318 – 2338HelicalSequence analysisAdd BLAST21
Transmembranei2339 – 2359HelicalSequence analysisAdd BLAST21
Transmembranei2361 – 2381HelicalSequence analysisAdd BLAST21
Transmembranei2776 – 2796HelicalSequence analysisAdd BLAST21
Transmembranei3045 – 3065HelicalSequence analysisAdd BLAST21
Transmembranei3077 – 3097HelicalSequence analysisAdd BLAST21
Transmembranei3100 – 3120HelicalSequence analysisAdd BLAST21
Transmembranei3128 – 3148HelicalSequence analysisAdd BLAST21
Transmembranei3165 – 3185HelicalSequence analysisAdd BLAST21
Transmembranei3587 – 3607HelicalSequence analysisAdd BLAST21
Transmembranei3609 – 3629HelicalSequence analysisAdd BLAST21
Transmembranei3635 – 3655HelicalSequence analysisAdd BLAST21
Transmembranei3674 – 3694HelicalSequence analysisAdd BLAST21
Transmembranei3730 – 3750HelicalSequence analysisAdd BLAST21
Transmembranei3779 – 3799HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Host cytoplasm, Host endoplasmic reticulum, Host endosome, Host Golgi apparatus, Host membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi154 – 157YEDF → AEDA: Complete loss of ribosome binding and cellular translation inhibition. 1 Publication4
Mutagenesisi164 – 165KH → AA: Complete loss of ribosome binding and cellular translation inhibition. 1 Publication2
Mutagenesisi164K → A: Complete loss of ribosome binding and cellular translation inhibition. 1 Publication1
Mutagenesisi165H → A: Complete loss of ribosome binding and cellular translation inhibition. 1 Publication1
Mutagenesisi171 – 175RELMR → EELME: Complete loss of ribosome binding and cellular translation inhibition. 1 Publication5
Mutagenesisi1629V → A: Partial loss of ISG15 cleavage in vitro. 1 Publication1
Mutagenesisi1632F → A: Partial loss of ISG15 cleavage in vitro. 1 Publication1
Mutagenesisi1638T → A: Partial loss of ubiquitin cleavage in vitro; no effect on ISG15 cleavage in vitro. 1 Publication1
Mutagenesisi1638T → L: Increased cleavage of ubiquitin in vitro; no effect on ISG15 cleavage in vitro. 1 Publication1
Mutagenesisi1674C → S: Complete loss of PL-pro activity. 1 Publication1
Mutagenesisi1831Y → G or T: Reduced inhibition by GRL-0617. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB15797, GC-373
DB15796, GC-376 free acid

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004496341 – 4405Replicase polyprotein 1aBy similarityAdd BLAST4405
ChainiPRO_00004496351 – 180Host translation inhibitor nsp1By similarityAdd BLAST180
ChainiPRO_0000449636181 – 818Non-structural protein 2By similarityAdd BLAST638
ChainiPRO_0000449637819 – 2763Non-structural protein 3By similarityAdd BLAST1945
ChainiPRO_00004496382764 – 3263Non-structural protein 4By similarityAdd BLAST500
ChainiPRO_00004496393264 – 35693C-like proteinaseBy similarityAdd BLAST306
ChainiPRO_00004496403570 – 3859Non-structural protein 6By similarityAdd BLAST290
ChainiPRO_00004496413860 – 3942Non-structural protein 7By similarityAdd BLAST83
ChainiPRO_00004496423943 – 4140Non-structural protein 8By similarityAdd BLAST198
ChainiPRO_00004496434141 – 4253Non-structural protein 9By similarityAdd BLAST113
ChainiPRO_00004496444254 – 4392Non-structural protein 10By similarityAdd BLAST139
ChainiPRO_00004496454393 – 4405Non-structural protein 11By similarityAdd BLAST13

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei180 – 181Cleavage; by PL-PROBy similarity2
Sitei818 – 819Cleavage; by PL-PROBy similarity2
Sitei2763 – 2764Cleavage; by PL-PROBy similarity2
Sitei3263 – 3264Cleavage; by 3CL-PROBy similarity2
Sitei3569 – 3570Cleavage; by 3CL-PROBy similarity2
Sitei3859 – 3860Cleavage; by 3CL-PROBy similarity2
Sitei3942 – 3943Cleavage; by 3CL-PROBy similarity2
Sitei4140 – 4141Cleavage; by 3CL-PROBy similarity2
Sitei4253 – 4254Cleavage; by 3CL-PROBy similarity2
Sitei4392 – 4393Cleavage; by 3CL-PROBy similarity2

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with host PHB and PHB2.

By similarity

3CL-PRO exists as monomer and homodimer. Only the homodimer shows catalytic activity.

1 Publication

Interacts with PL-PRO and nsp6.

By similarity

Interacts with host TBK1; this interaction decreases IRF3 phosphorylation by 57%, which leads to reduced IFN-beta production.

1 Publication

Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure (By similarity).

Interacts with RNA-directed RNA polymerase (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208).

By similarity4 Publications

Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure (By similarity).

Interacts with RNA-directed RNA polymerase (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208).

By similarity4 Publications

Is a dimer.

By similarity

Forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities.

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4383866, 12 interactors

Protein interaction database and analysis system

More...
IntActi
P0DTC1, 38 interactors

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

14405
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Small Angle Scattering Biological Data Bank

More...
SASBDBi
P0DTC1

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0DTC1

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini12 – 133CoV Nsp1 globularPROSITE-ProRule annotationAdd BLAST122
Domaini148 – 179BetaCoV Nsp1 C-terminalPROSITE-ProRule annotationAdd BLAST32
Domaini820 – 929Ubiquitin-like 1PROSITE-ProRule annotationAdd BLAST110
Domaini1025 – 1194Macro 1PROSITE-ProRule annotationAdd BLAST170
Domaini1231 – 1359Macro 2PROSITE-ProRule annotationAdd BLAST129
Domaini1367 – 1494Macro 3PROSITE-ProRule annotationAdd BLAST128
Domaini1496 – 1561DPUPPROSITE-ProRule annotationAdd BLAST66
Domaini1565 – 1620Ubiquitin-like 2PROSITE-ProRule annotationAdd BLAST56
Domaini1634 – 1898Peptidase C16PROSITE-ProRule annotationAdd BLAST265
Domaini1911 – 2021Nucleic acid-bindingPROSITE-ProRule annotationAdd BLAST111
Domaini3165 – 3263Nsp4CPROSITE-ProRule annotationAdd BLAST99
Domaini3264 – 3569Peptidase C30PROSITE-ProRule annotationAdd BLAST306
Domaini3860 – 3942RdRp Nsp7 cofactorPROSITE-ProRule annotationAdd BLAST83
Domaini3943 – 4140RdRp Nsp8 cofactorPROSITE-ProRule annotationAdd BLAST198
Domaini4141 – 4253Nsp9 ssRNA-bindingPROSITE-ProRule annotationAdd BLAST113
Domaini4254 – 4392ExoN/MTase coactivatorPROSITE-ProRule annotationAdd BLAST139

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni154 – 180Binding to 40s ribosome mRNA entry channel1 PublicationAdd BLAST27
Regioni926 – 999DisorderedSequence analysisAdd BLAST74

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi927 – 947Acidic residuesSequence analysisAdd BLAST21
Compositional biasi984 – 999Polar residuesSequence analysisAdd BLAST16

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1752 – 1789C4-typePROSITE-ProRule annotationAdd BLAST38

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Conserved Domains Database

More...
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

Gene3D Structural and Functional Annotation of Protein Families

More...
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
2.30.30.590, 1 hit
2.40.10.10, 2 hits
2.40.10.250, 1 hit
2.40.10.290, 1 hit
3.10.20.350, 1 hit
3.10.20.540, 1 hit
3.40.220.10, 1 hit
3.40.220.20, 1 hit
3.40.220.30, 1 hit
3.40.50.11020, 1 hit
3.90.70.90, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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_NAR_bCoV
IPR038166, NSP3_PL2pro_sf_CoV
IPR038400, NSP3_SUD-M_sf_bCoV
IPR043478, NSP3_SUD-N_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

Pfam protein domain database

More...
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

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00506, A1pp, 1 hit

Superfamily database of structural and functional annotation

More...
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

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51963, BCOV_NSP1_C, 1 hit
PS51942, BCOV_NSP3C_C, 1 hit
PS51941, BCOV_NSP3C_M, 1 hit
PS51945, BCOV_NSP3E_NAB, 1 hit
PS51952, COV_EXON_MTASE_COACT, 1 hit
PS51962, COV_NSP1, 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by ribosomal frameshifting. AlignAdd to basket
Note: Normal translation results in Replicase polyprotein 1a. Ribosomal frameshifting at the end of this protein occurs at low frequency and produces Replicase polyprotein 1ab.
Isoform Replicase polyprotein 1a (identifier: P0DTC1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        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
Length:4,405
Mass (Da):489,989
Last modified:April 22, 2020 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7F8A21148A7A7E2A
GO
Isoform Replicase polyprotein 1ab (identifier: P0DTD1-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0DTD1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:7,096
Mass (Da):794,058
GO

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Variant B.1.1.7 is also called Variant Of Concern (VOC) 202012/01, Variant Under Investigation (VUI) 202012/01, or 20B/501Y.V1.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti1001T → I in strain: B.1.1.7. 1 Publication1
Natural varianti1708A → D in strain: B.1.1.7. 1 Publication1
Natural varianti2230I → T in strain: B.1.1.7. 1 Publication1
Natural varianti3675 – 3677Missing in strain: B.1.1.7. 1 Publication3

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
MN908947 Genomic RNA Translation: QHD43415.1 Frameshift.

NCBI Reference Sequences

More...
RefSeqi
YP_009725295.1, NC_045512.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
43740578

Keywords - Coding sequence diversityi

Ribosomal frameshifting

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
MN908947 Genomic RNA Translation: QHD43415.1 Frameshift.
RefSeqiYP_009725295.1, NC_045512.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6Y2EX-ray1.75A3264-3569[»]
6Y2FX-ray2.16A3264-3569[»]
6Y2GX-ray2.16A3264-3569[»]
6YHUX-ray2.00A/C3860-3930[»]
B/D4018-4134[»]
6YYTelectron microscopy2.90B3948-4133[»]
C3860-3932[»]
7BV2electron microscopy2.50C3860-3942[»]
B3943-4140[»]
7C33X-ray3.83A/B/C/D1025-1195[»]
7CZ4X-ray2.64A/B1025-1195[»]
7D3IX-ray2.00A3264-3569[»]
7D47X-ray1.97A/B1564-1880[»]
7D6HX-ray1.60A1563-1878[»]
7E35X-ray2.40A/B1564-1878[»]
7JIRX-ray2.09A1564-1878[»]
7JITX-ray1.95A1564-1878[»]
7JIVX-ray2.05A1564-1878[»]
7JIWX-ray2.30A1564-1878[»]
7JN2X-ray1.93A1564-1878[»]
7JRNX-ray2.48A/J1564-1878[»]
7KOJX-ray2.02A1564-1878[»]
7KOKX-ray2.00A1564-1878[»]
7KOLX-ray2.58A1564-1878[»]
7KRXX-ray2.72A1564-1878[»]
SASBDBiP0DTC1
SMRiP0DTC1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4383866, 12 interactors
IntActiP0DTC1, 38 interactors

Chemistry databases

DrugBankiDB15797, GC-373
DB15796, GC-376 free acid

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
43740578

Genome annotation databases

GeneIDi43740578

Enzyme and pathway databases

ReactomeiR-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

Family and domain databases

CDDicd21560, 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
Gene3Di1.10.150.420, 1 hit
1.10.1840.10, 1 hit
1.10.8.1190, 1 hit
1.10.8.370, 1 hit
2.30.30.590, 1 hit
2.40.10.10, 2 hits
2.40.10.250, 1 hit
2.40.10.290, 1 hit
3.10.20.350, 1 hit
3.10.20.540, 1 hit
3.40.220.10, 1 hit
3.40.220.20, 1 hit
3.40.220.30, 1 hit
3.40.50.11020, 1 hit
3.90.70.90, 1 hit
InterProiView 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_NAR_bCoV
IPR038166, NSP3_PL2pro_sf_CoV
IPR038400, NSP3_SUD-M_sf_bCoV
IPR043478, NSP3_SUD-N_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
PfamiView 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
SMARTiView protein in SMART
SM00506, A1pp, 1 hit
SUPFAMiSSF101816, 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
PROSITEiView protein in PROSITE
PS51963, BCOV_NSP1_C, 1 hit
PS51942, BCOV_NSP3C_C, 1 hit
PS51941, BCOV_NSP3C_M, 1 hit
PS51945, BCOV_NSP3E_NAB, 1 hit
PS51952, COV_EXON_MTASE_COACT, 1 hit
PS51962, COV_NSP1, 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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiR1A_SARS2
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0DTC1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 22, 2020
Last sequence update: April 22, 2020
Last modified: June 2, 2021
This is version 8 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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