Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 1 (22 Apr 2020)
Sequence version 1 (22 Apr 2020)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Replicase polyprotein 1ab

Gene

rep

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 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.By similarity
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. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.By similarity
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. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291). Also able to bind an ADP-ribose-1''-phosphate (ADRP).By similarity1 Publication
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.By similarity
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
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
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
Responsible for replication and transcription of the viral RNA genome.By similarity
Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.By similarity
Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens.By similarity
Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.By similarity
Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.By similarity

Miscellaneous

Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.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

  • 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.1 Publication EC:3.4.22.69
  • 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).By similarity EC:3.4.19.12

<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 by Remdesivir (GS-5734).By similarity
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.1 Publication

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
Active sitei1835For PL2-PRO activityPROSITE-ProRule annotation1
Active sitei3304For 3CL-PRO activityPROSITE-ProRule annotation1 Publication1
Active sitei3408Nucleophile; for 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 bindingi5329Zinc 1PROSITE-ProRule annotation1
Metal bindingi5332Zinc 1PROSITE-ProRule annotation1
Metal bindingi5340Zinc 2PROSITE-ProRule annotation1
Metal bindingi5343Zinc 1PROSITE-ProRule annotation1
Metal bindingi5350Zinc 1PROSITE-ProRule annotation1
Metal bindingi5353Zinc 2; via tele nitrogenPROSITE-ProRule annotation1
Metal bindingi5357Zinc 2; via pros nitrogenPROSITE-ProRule annotation1
Metal bindingi5363Zinc 2PROSITE-ProRule annotation1
Metal bindingi5374Zinc 3PROSITE-ProRule annotation1
Metal bindingi5379Zinc 3; via pros nitrogenPROSITE-ProRule annotation1
Metal bindingi5396Zinc 3PROSITE-ProRule annotation1
Metal bindingi5399Zinc 3PROSITE-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>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi5606 – 5613NTPPROSITE-ProRule annotation8

<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, Exonuclease, Helicase, Hydrolase, Methyltransferase, Nuclease, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase
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 ISG15 by virus, Inhibition of host NF-kappa-B by virus, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway, Viral immunoevasion, Viral RNA replication
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

<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 1ab
Short name:
pp1ab
Alternative name(s):
ORF1ab polyprotein
Cleaved into the following 15 chains:
Alternative name(s):
Leader protein
Non-structural protein 2
Short name:
nsp2
Alternative name(s):
p65 homolog
Non-structural protein 3 (EC:3.4.19.12, EC:3.4.22.-)
Short name:
nsp3
Alternative name(s):
PL2-PRO
Papain-like proteinase
Short name:
PL-PRO
SARS coronavirus main proteinase
Non-structural protein 4
Short name:
nsp4
3C-like proteinase (EC:3.4.22.691 Publication)
Short name:
3CL-PRO
Short name:
3CLp
Alternative name(s):
nsp5
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
RNA-directed RNA polymerase (EC:2.7.7.48)
Short name:
Pol
Short name:
RdRp
Alternative name(s):
nsp12
Helicase (EC:3.6.4.12, EC:3.6.4.13)
Short name:
Hel
Alternative name(s):
nsp13
Proofreading exoribonuclease (EC:3.1.13.-)
Short name:
ExoN
Alternative name(s):
Guanine-N7 methyltransferase
Non-structural protein 14
Short name:
nsp14
Uridylate-specific endoribonuclease (EC:3.1.-.-)
Alternative name(s):
NendoU
nsp15
2'-O-methyltransferase (EC:2.1.1.-)
Alternative name(s):
nsp16
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:rep
ORF Names:1a-1b
<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 lineageiVirusesRiboviriaNidoviralesCornidovirineaeCoronaviridaeOrthocoronavirinaeBetacoronavirusSarbecovirus
<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 subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 2225CytoplasmicCuratedAdd BLAST2225
<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
Topological domaini2247 – 2317LumenalCuratedAdd BLAST71
Transmembranei2318 – 2338HelicalSequence analysisAdd BLAST21
Topological domaini2339 – 2775CytoplasmicCuratedAdd BLAST437
Transmembranei2776 – 2796HelicalSequence analysisAdd BLAST21
Topological domaini2797 – 3044LumenalCuratedAdd BLAST248
Transmembranei3045 – 3065HelicalSequence analysisAdd BLAST21
Topological domaini3066 – 3099CytoplasmicCuratedAdd BLAST34
Transmembranei3100 – 3120HelicalSequence analysisAdd BLAST21
Topological domaini3121 – 3127LumenalCurated7
Transmembranei3128 – 3148HelicalSequence analysisAdd BLAST21
Topological domaini3149 – 3586CytoplasmicCuratedAdd BLAST438
Transmembranei3587 – 3607HelicalSequence analysisAdd BLAST21
Topological domaini3608LumenalCurated1
Transmembranei3609 – 3629HelicalSequence analysisAdd BLAST21
Topological domaini3630 – 3634CytoplasmicCurated5
Transmembranei3635 – 3655HelicalSequence analysisAdd BLAST21
Topological domaini3656 – 3673LumenalCuratedAdd BLAST18
Transmembranei3674 – 3694HelicalSequence analysisAdd BLAST21
Topological domaini3695 – 3729CytoplasmicCuratedAdd BLAST35
Transmembranei3730 – 3750HelicalSequence analysisAdd BLAST21
Topological domaini3751 – 3778LumenalCuratedAdd BLAST28
Transmembranei3779 – 3799HelicalSequence analysisAdd BLAST21
Topological domaini3800 – 7096CytoplasmicCuratedAdd BLAST3297

GO - Cellular componenti

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Membrane

<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_00004496181 – 7096Replicase polyprotein 1abAdd BLAST7096
ChainiPRO_00004496191 – 180Host translation inhibitor nsp1By similarityAdd BLAST180
ChainiPRO_0000449620181 – 818Non-structural protein 2By similarityAdd BLAST638
ChainiPRO_0000449621819 – 2763Non-structural protein 3By similarityAdd BLAST1945
ChainiPRO_00004496222764 – 3263Non-structural protein 4By similarityAdd BLAST500
ChainiPRO_00004496233264 – 35693C-like proteinaseBy similarityAdd BLAST306
ChainiPRO_00004496243570 – 3859Non-structural protein 6By similarityAdd BLAST290
ChainiPRO_00004496253860 – 3942Non-structural protein 7By similarityAdd BLAST83
ChainiPRO_00004496263943 – 4140Non-structural protein 8By similarityAdd BLAST198
ChainiPRO_00004496274141 – 4253Non-structural protein 9By similarityAdd BLAST113
ChainiPRO_00004496284254 – 4392Non-structural protein 10By similarityAdd BLAST139
ChainiPRO_00004496294393 – 5324RNA-directed RNA polymeraseBy similarityAdd BLAST932
ChainiPRO_00004496305325 – 5925HelicaseBy similarityAdd BLAST601
ChainiPRO_00004496315926 – 6452Proofreading exoribonucleaseBy similarityAdd BLAST527
ChainiPRO_00004496326453 – 6798Uridylate-specific endoribonucleaseBy similarityAdd BLAST346
ChainiPRO_00004496336799 – 70962'-O-methyltransferaseBy similarityAdd BLAST298

<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; aby 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
Sitei5324 – 5325Cleavage; by 3CL-PROBy similarity2
Sitei5925 – 5926Cleavage; by 3CL-PROBy similarity2
Sitei6452 – 6453Cleavage; by 3CL-PROBy similarity2
Sitei6798 – 6799Cleavage; 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

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

By similarity

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

By similarity

Is a dimer.

By similarity

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

By similarity

Interacts (via N-terminus) with DDX1.

Interacts with nsp10.

By similarity

Interacts with nsp10.

By similarity

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P0DTD1, 171 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

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

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 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati545 – 569LRR 1Sequence analysisAdd BLAST25
Repeati697 – 719LRR 2Sequence analysisAdd BLAST23
<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>Domaini1025 – 1194MacroPROSITE-ProRule annotationAdd BLAST170
Domaini1634 – 1898Peptidase C16PROSITE-ProRule annotationAdd BLAST265
Repeati1680 – 1702LRR 3Sequence analysisAdd BLAST23
Repeati3185 – 3206LRR 4Sequence analysisAdd BLAST22
Domaini3264 – 3569Peptidase C30PROSITE-ProRule annotationAdd BLAST306
Repeati3935 – 3959LRR 5Sequence analysisAdd BLAST25
Repeati3977 – 4004LRR 6Sequence analysisAdd BLAST28
Repeati4591 – 4616LRR 7Sequence analysisAdd BLAST26
Domaini5004 – 5166RdRp catalyticPROSITE-ProRule annotationAdd BLAST163
Domaini5325 – 5408CV ZBDPROSITE-ProRule annotationAdd BLAST84
Repeati5552 – 5572LRR 8Sequence analysisAdd BLAST21
Domaini5581 – 5762(+)RNA virus helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST182
Domaini5763 – 5932(+)RNA virus helicase C-terminalPROSITE-ProRule annotationAdd BLAST170
Repeati6817 – 6841LRR 9Sequence analysisAdd BLAST25

<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

Leucine-rich repeat, Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Conserved Domains Database

More...
CDDi
cd15239 7tm_YRO2_fungal-like, 1 hit
cd17934 DEXXQc_Upf1-like, 1 hit
cd18808 SF1_C_Upf1, 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
2.20.25.360, 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
3.40.50.11580, 1 hit
3.40.50.150, 1 hit
3.40.50.300, 2 hits
3.90.70.90, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027351 (+)RNA_virus_helicase_core_dom
IPR032505 Corona_NSP4_C
IPR009461 Coronavirus_NSP16
IPR027352 CV_ZBD
IPR037227 EndoU-like
IPR002589 Macro_dom
IPR032592 NAR_dom
IPR042570 NAR_sf
IPR021590 NSP1
IPR036333 NSP10_sf
IPR009466 NSP11
IPR042515 Nsp15_N
IPR038030 NSP1_sf
IPR024375 Nsp3_coronavir
IPR038400 Nsp3_coronavir_sf
IPR022733 Nsp3_PL2pro
IPR038166 Nsp3_PL2pro_sf
IPR038123 NSP4_C_sf
IPR014828 NSP7
IPR037204 NSP7_sf
IPR014829 NSP8
IPR037230 NSP8_sf
IPR014822 NSP9
IPR036499 NSP9_sf
IPR027417 P-loop_NTPase
IPR008740 Peptidase_C30
IPR013016 Peptidase_C30/C16
IPR009003 Peptidase_S1_PA
IPR038083 R1a/1ab
IPR007094 RNA-dir_pol_PSvirus
IPR009469 RNA_pol_N_coronovir
IPR018995 RNA_synth_NSP10_coronavirus
IPR029063 SAM-dependent_MTases
IPR024358 SARS-CoV_Nsp3_N
IPR014827 Viral_protease

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13604 AAA_30, 1 hit
PF16348 Corona_NSP4_C, 1 hit
PF06478 Corona_RPol_N, 1 hit
PF12379 DUF3655, 1 hit
PF01661 Macro, 1 hit
PF16251 NAR, 1 hit
PF11501 Nsp1, 1 hit
PF09401 NSP10, 1 hit
PF06471 NSP11, 1 hit
PF06460 NSP16, 1 hit
PF12124 Nsp3_PL2pro, 1 hit
PF08716 nsp7, 1 hit
PF08717 nsp8, 1 hit
PF08710 nsp9, 1 hit
PF05409 Peptidase_C30, 1 hit
PF11633 SUD-M, 1 hit
PF08715 Viral_protease, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00506 YBR022w_8, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF101816 SSF101816, 1 hit
SSF140367 SSF140367, 1 hit
SSF142877 SSF142877, 1 hit
SSF143076 SSF143076, 1 hit
SSF144246 SSF144246, 1 hit
SSF159936 SSF159936, 1 hit
SSF160099 SSF160099, 1 hit
SSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 1 hit
SSF52949 SSF52949, 1 hit
SSF53335 SSF53335, 1 hit
SSF56672 SSF56672, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00867 CPSASE_2, 1 hit
PS51653 CV_ZBD, 1 hit
PS00213 LIPOCALIN, 1 hit
PS51442 M_PRO, 1 hit
PS51154 MACRO, 1 hit
PS51124 PEPTIDASE_C16, 1 hit
PS51657 PSRV_HELICASE, 1 hit
PS50507 RDRP_SSRNA_POS, 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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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 1ab (identifier: P0DTD1-1) [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
4410 4420 4430 4440 4450
NRVCGVSAAR LTPCGTGTST DVVYRAFDIY NDKVAGFAKF LKTNCCRFQE
4460 4470 4480 4490 4500
KDEDDNLIDS YFVVKRHTFS NYQHEETIYN LLKDCPAVAK HDFFKFRIDG
4510 4520 4530 4540 4550
DMVPHISRQR LTKYTMADLV YALRHFDEGN CDTLKEILVT YNCCDDDYFN
4560 4570 4580 4590 4600
KKDWYDFVEN PDILRVYANL GERVRQALLK TVQFCDAMRN AGIVGVLTLD
4610 4620 4630 4640 4650
NQDLNGNWYD FGDFIQTTPG SGVPVVDSYY SLLMPILTLT RALTAESHVD
4660 4670 4680 4690 4700
TDLTKPYIKW DLLKYDFTEE RLKLFDRYFK YWDQTYHPNC VNCLDDRCIL
4710 4720 4730 4740 4750
HCANFNVLFS TVFPPTSFGP LVRKIFVDGV PFVVSTGYHF RELGVVHNQD
4760 4770 4780 4790 4800
VNLHSSRLSF KELLVYAADP AMHAASGNLL LDKRTTCFSV AALTNNVAFQ
4810 4820 4830 4840 4850
TVKPGNFNKD FYDFAVSKGF FKEGSSVELK HFFFAQDGNA AISDYDYYRY
4860 4870 4880 4890 4900
NLPTMCDIRQ LLFVVEVVDK YFDCYDGGCI NANQVIVNNL DKSAGFPFNK
4910 4920 4930 4940 4950
WGKARLYYDS MSYEDQDALF AYTKRNVIPT ITQMNLKYAI SAKNRARTVA
4960 4970 4980 4990 5000
GVSICSTMTN RQFHQKLLKS IAATRGATVV IGTSKFYGGW HNMLKTVYSD
5010 5020 5030 5040 5050
VENPHLMGWD YPKCDRAMPN MLRIMASLVL ARKHTTCCSL SHRFYRLANE
5060 5070 5080 5090 5100
CAQVLSEMVM CGGSLYVKPG GTSSGDATTA YANSVFNICQ AVTANVNALL
5110 5120 5130 5140 5150
STDGNKIADK YVRNLQHRLY ECLYRNRDVD TDFVNEFYAY LRKHFSMMIL
5160 5170 5180 5190 5200
SDDAVVCFNS TYASQGLVAS IKNFKSVLYY QNNVFMSEAK CWTETDLTKG
5210 5220 5230 5240 5250
PHEFCSQHTM LVKQGDDYVY LPYPDPSRIL GAGCFVDDIV KTDGTLMIER
5260 5270 5280 5290 5300
FVSLAIDAYP LTKHPNQEYA DVFHLYLQYI RKLHDELTGH MLDMYSVMLT
5310 5320 5330 5340 5350
NDNTSRYWEP EFYEAMYTPH TVLQAVGACV LCNSQTSLRC GACIRRPFLC
5360 5370 5380 5390 5400
CKCCYDHVIS TSHKLVLSVN PYVCNAPGCD VTDVTQLYLG GMSYYCKSHK
5410 5420 5430 5440 5450
PPISFPLCAN GQVFGLYKNT CVGSDNVTDF NAIATCDWTN AGDYILANTC
5460 5470 5480 5490 5500
TERLKLFAAE TLKATEETFK LSYGIATVRE VLSDRELHLS WEVGKPRPPL
5510 5520 5530 5540 5550
NRNYVFTGYR VTKNSKVQIG EYTFEKGDYG DAVVYRGTTT YKLNVGDYFV
5560 5570 5580 5590 5600
LTSHTVMPLS APTLVPQEHY VRITGLYPTL NISDEFSSNV ANYQKVGMQK
5610 5620 5630 5640 5650
YSTLQGPPGT GKSHFAIGLA LYYPSARIVY TACSHAAVDA LCEKALKYLP
5660 5670 5680 5690 5700
IDKCSRIIPA RARVECFDKF KVNSTLEQYV FCTVNALPET TADIVVFDEI
5710 5720 5730 5740 5750
SMATNYDLSV VNARLRAKHY VYIGDPAQLP APRTLLTKGT LEPEYFNSVC
5760 5770 5780 5790 5800
RLMKTIGPDM FLGTCRRCPA EIVDTVSALV YDNKLKAHKD KSAQCFKMFY
5810 5820 5830 5840 5850
KGVITHDVSS AINRPQIGVV REFLTRNPAW RKAVFISPYN SQNAVASKIL
5860 5870 5880 5890 5900
GLPTQTVDSS QGSEYDYVIF TQTTETAHSC NVNRFNVAIT RAKVGILCIM
5910 5920 5930 5940 5950
SDRDLYDKLQ FTSLEIPRRN VATLQAENVT GLFKDCSKVI TGLHPTQAPT
5960 5970 5980 5990 6000
HLSVDTKFKT EGLCVDIPGI PKDMTYRRLI SMMGFKMNYQ VNGYPNMFIT
6010 6020 6030 6040 6050
REEAIRHVRA WIGFDVEGCH ATREAVGTNL PLQLGFSTGV NLVAVPTGYV
6060 6070 6080 6090 6100
DTPNNTDFSR VSAKPPPGDQ FKHLIPLMYK GLPWNVVRIK IVQMLSDTLK
6110 6120 6130 6140 6150
NLSDRVVFVL WAHGFELTSM KYFVKIGPER TCCLCDRRAT CFSTASDTYA
6160 6170 6180 6190 6200
CWHHSIGFDY VYNPFMIDVQ QWGFTGNLQS NHDLYCQVHG NAHVASCDAI
6210 6220 6230 6240 6250
MTRCLAVHEC FVKRVDWTIE YPIIGDELKI NAACRKVQHM VVKAALLADK
6260 6270 6280 6290 6300
FPVLHDIGNP KAIKCVPQAD VEWKFYDAQP CSDKAYKIEE LFYSYATHSD
6310 6320 6330 6340 6350
KFTDGVCLFW NCNVDRYPAN SIVCRFDTRV LSNLNLPGCD GGSLYVNKHA
6360 6370 6380 6390 6400
FHTPAFDKSA FVNLKQLPFF YYSDSPCESH GKQVVSDIDY VPLKSATCIT
6410 6420 6430 6440 6450
RCNLGGAVCR HHANEYRLYL DAYNMMISAG FSLWVYKQFD TYNLWNTFTR
6460 6470 6480 6490 6500
LQSLENVAFN VVNKGHFDGQ QGEVPVSIIN NTVYTKVDGV DVELFENKTT
6510 6520 6530 6540 6550
LPVNVAFELW AKRNIKPVPE VKILNNLGVD IAANTVIWDY KRDAPAHIST
6560 6570 6580 6590 6600
IGVCSMTDIA KKPTETICAP LTVFFDGRVD GQVDLFRNAR NGVLITEGSV
6610 6620 6630 6640 6650
KGLQPSVGPK QASLNGVTLI GEAVKTQFNY YKKVDGVVQQ LPETYFTQSR
6660 6670 6680 6690 6700
NLQEFKPRSQ MEIDFLELAM DEFIERYKLE GYAFEHIVYG DFSHSQLGGL
6710 6720 6730 6740 6750
HLLIGLAKRF KESPFELEDF IPMDSTVKNY FITDAQTGSS KCVCSVIDLL
6760 6770 6780 6790 6800
LDDFVEIIKS QDLSVVSKVV KVTIDYTEIS FMLWCKDGHV ETFYPKLQSS
6810 6820 6830 6840 6850
QAWQPGVAMP NLYKMQRMLL EKCDLQNYGD SATLPKGIMM NVAKYTQLCQ
6860 6870 6880 6890 6900
YLNTLTLAVP YNMRVIHFGA GSDKGVAPGT AVLRQWLPTG TLLVDSDLND
6910 6920 6930 6940 6950
FVSDADSTLI GDCATVHTAN KWDLIISDMY DPKTKNVTKE NDSKEGFFTY
6960 6970 6980 6990 7000
ICGFIQQKLA LGGSVAIKIT EHSWNADLYK LMGHFAWWTA FVTNVNASSS
7010 7020 7030 7040 7050
EAFLIGCNYL GKPREQIDGY VMHANYIFWR NTNPIQLSSY SLFDMSKFPL
7060 7070 7080 7090
KLRGTAVMSL KEGQINDMIL SLLSKGRLII RENNRVVISS DVLVNN
Length:7,096
Mass (Da):794,058
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:iA4E62D97150BB8CC
GO
Isoform Replicase polyprotein 1a (identifier: P0DTC1-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0DTC1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:4,405
Mass (Da):489,989
GO

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

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

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
5R7YX-ray1.65A3264-3569[»]
5R7ZX-ray1.59A3264-3569[»]
5R80X-ray1.93A3264-3569[»]
5R81X-ray1.95A3264-3569[»]
5R82X-ray1.31A3264-3569[»]
5R83X-ray1.58A3264-3569[»]
5R84X-ray1.83A3264-3569[»]
5RE4X-ray1.88A3264-3569[»]
5RE5X-ray2.07A3264-3569[»]
5RE6X-ray1.87A3264-3569[»]
5RE7X-ray1.79A3264-3569[»]
5RE8X-ray1.81A3264-3569[»]
5RE9X-ray1.72A3264-3569[»]
5REAX-ray1.63A3264-3569[»]
5REBX-ray1.68A3264-3569[»]
5RECX-ray1.73A3264-3569[»]
5REDX-ray1.47A3264-3569[»]
5REEX-ray1.77A3264-3569[»]
5REFX-ray1.61A3264-3569[»]
5REGX-ray1.67A3264-3569[»]
5REHX-ray1.80A3264-3569[»]
5REIX-ray1.82A3264-3569[»]
5REJX-ray1.72A3264-3569[»]
5REKX-ray1.74A3264-3569[»]
5RELX-ray1.62A3264-3569[»]
5REMX-ray1.96A3264-3569[»]
5RENX-ray2.15A3264-3569[»]
5REOX-ray1.88A3264-3569[»]
5REPX-ray1.81A3264-3569[»]
5RERX-ray1.88A3264-3569[»]
5RESX-ray1.65A3264-3569[»]
5RETX-ray1.68A3264-3569[»]
5REUX-ray1.69A3264-3569[»]
5REVX-ray1.60A3264-3569[»]
5REWX-ray1.55A3264-3569[»]
5REXX-ray2.07A3264-3569[»]
5REYX-ray1.96A3264-3569[»]
5REZX-ray1.79A3264-3569[»]
5RF0X-ray1.65A3264-3569[»]
5RF1X-ray1.73A3264-3569[»]
5RF2X-ray1.53A3264-3569[»]
5RF3X-ray1.50A3264-3569[»]
5RF4X-ray1.61A3264-3569[»]
5RF5X-ray1.74A3264-3569[»]
5RF6X-ray1.45A3264-3569[»]
5RF7X-ray1.54A3264-3569[»]
5RF8X-ray1.44A3264-3569[»]
5RF9X-ray1.43A3264-3569[»]
5RFAX-ray1.52A3264-3569[»]
5RFBX-ray1.48A3264-3569[»]
5RFCX-ray1.40A3264-3569[»]
5RFDX-ray1.41A3264-3569[»]
5RFEX-ray1.46A3264-3569[»]
5RFFX-ray1.78A3264-3569[»]
5RFGX-ray2.32A3264-3569[»]
5RFHX-ray1.58A3264-3569[»]
5RFIX-ray1.69A3264-3569[»]
5RFJX-ray1.80A3264-3569[»]
5RFKX-ray1.75A3264-3569[»]
5RFLX-ray1.64A3264-3569[»]
5RFMX-ray2.06A3264-3569[»]
5RFNX-ray1.80A3264-3569[»]
5RFOX-ray1.83A3264-3569[»]
5RFPX-ray2.03A3264-3569[»]
5RFQX-ray1.76A3264-3569[»]
5RFRX-ray1.71A3264-3569[»]
5RFSX-ray1.70A3264-3569[»]
5RFTX-ray1.58A3264-3569[»]
5RFUX-ray1.53A3264-3569[»]
5RFVX-ray1.48A3264-3569[»]
5RFWX-ray1.43A3264-3569[»]
5RFXX-ray1.55A3264-3569[»]
5RFYX-ray1.90A3264-3569[»]
5RFZX-ray1.68A3264-3569[»]
5RG0X-ray1.72A3264-3569[»]
6LU7X-ray2.16A3264-3569[»]
6M03X-ray2.00A3264-3569[»]
6VWWX-ray2.20A/B6453-6798[»]
6W01X-ray1.90A/B6453-6798[»]
6W02X-ray1.50A/B1024-1192[»]
6W61X-ray2.00B4254-4392[»]
A6799-7096[»]
6W63X-ray2.10A3264-3569[»]
6W6YX-ray1.45A/B1024-1192[»]
6W75X-ray1.95B/D4254-4392[»]
A/C6799-7096[»]
6Y2EX-ray1.75A3264-3569[»]
6Y2FX-ray2.16A3264-3569[»]
6Y2GX-ray2.16A3264-3569[»]
6Y84X-ray1.39A3264-3569[»]
6YB7X-ray1.25A3264-3569[»]
ModBaseiSearch...
SWISS-MODEL-WorkspaceiSubmit a new modelling project...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP0DTD1, 171 interactors

Family and domain databases

CDDicd15239 7tm_YRO2_fungal-like, 1 hit
cd17934 DEXXQc_Upf1-like, 1 hit
cd18808 SF1_C_Upf1, 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
2.20.25.360, 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
3.40.50.11580, 1 hit
3.40.50.150, 1 hit
3.40.50.300, 2 hits
3.90.70.90, 1 hit
InterProiView protein in InterPro
IPR027351 (+)RNA_virus_helicase_core_dom
IPR032505 Corona_NSP4_C
IPR009461 Coronavirus_NSP16
IPR027352 CV_ZBD
IPR037227 EndoU-like
IPR002589 Macro_dom
IPR032592 NAR_dom
IPR042570 NAR_sf
IPR021590 NSP1
IPR036333 NSP10_sf
IPR009466 NSP11
IPR042515 Nsp15_N
IPR038030 NSP1_sf
IPR024375 Nsp3_coronavir
IPR038400 Nsp3_coronavir_sf
IPR022733 Nsp3_PL2pro
IPR038166 Nsp3_PL2pro_sf
IPR038123 NSP4_C_sf
IPR014828 NSP7
IPR037204 NSP7_sf
IPR014829 NSP8
IPR037230 NSP8_sf
IPR014822 NSP9
IPR036499 NSP9_sf
IPR027417 P-loop_NTPase
IPR008740 Peptidase_C30
IPR013016 Peptidase_C30/C16
IPR009003 Peptidase_S1_PA
IPR038083 R1a/1ab
IPR007094 RNA-dir_pol_PSvirus
IPR009469 RNA_pol_N_coronovir
IPR018995 RNA_synth_NSP10_coronavirus
IPR029063 SAM-dependent_MTases
IPR024358 SARS-CoV_Nsp3_N
IPR014827 Viral_protease
PfamiView protein in Pfam
PF13604 AAA_30, 1 hit
PF16348 Corona_NSP4_C, 1 hit
PF06478 Corona_RPol_N, 1 hit
PF12379 DUF3655, 1 hit
PF01661 Macro, 1 hit
PF16251 NAR, 1 hit
PF11501 Nsp1, 1 hit
PF09401 NSP10, 1 hit
PF06471 NSP11, 1 hit
PF06460 NSP16, 1 hit
PF12124 Nsp3_PL2pro, 1 hit
PF08716 nsp7, 1 hit
PF08717 nsp8, 1 hit
PF08710 nsp9, 1 hit
PF05409 Peptidase_C30, 1 hit
PF11633 SUD-M, 1 hit
PF08715 Viral_protease, 1 hit
SMARTiView protein in SMART
SM00506 YBR022w_8, 1 hit
SUPFAMiSSF101816 SSF101816, 1 hit
SSF140367 SSF140367, 1 hit
SSF142877 SSF142877, 1 hit
SSF143076 SSF143076, 1 hit
SSF144246 SSF144246, 1 hit
SSF159936 SSF159936, 1 hit
SSF160099 SSF160099, 1 hit
SSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 1 hit
SSF52949 SSF52949, 1 hit
SSF53335 SSF53335, 1 hit
SSF56672 SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS00867 CPSASE_2, 1 hit
PS51653 CV_ZBD, 1 hit
PS00213 LIPOCALIN, 1 hit
PS51442 M_PRO, 1 hit
PS51154 MACRO, 1 hit
PS51124 PEPTIDASE_C16, 1 hit
PS51657 PSRV_HELICASE, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 nameiR1AB_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: P0DTD1
<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: April 22, 2020
This is version 1 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again