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Entry version 111 (17 Jun 2020)
Sequence version 1 (10 Jun 2008)
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Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome coronavirus)
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.
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 (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371).2 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.1 Publication
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 (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling.1 Publication3 Publications
Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes. Nsp3, nsp4 and nsp6 together are sufficient to form DMV.1 Publication1 Publication
Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH.PROSITE-ProRule annotation2 Publications
Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication. Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069). Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (PubMed:24991833).1 Publication1 Publication
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.1 Publication
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.1 Publication
May participate in viral replication by acting as a ssRNA-binding protein.1 Publication
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.1 Publication
Responsible for replication and transcription of the viral RNA genome.1 Publication
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.2 Publications
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 (PubMed:16549795, PubMed:20421945, PubMed:22635272). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (PubMed:23966862, PubMed:29511076, PubMed:21593585).6 Publications
Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.
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.Curated2 Publications

Caution

Isolates SZ3 and SZ16 have been isolated from Paguma larvata and are described as SARS-like in literature.Curated

<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).1 Publication 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).1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

The kinetic parameters are studied for the 3C-like proteinase domain.
  1. KM=1.15 mM for peptide TSAVLQSGFRK-NH21 Publication
  2. KM=0.58 mM for peptide SGVTFQGKFKK1 Publication
  3. KM=1.44 mM for peptide ATVRLQAGNAT1 Publication

    pH dependencei

    Optimum pH is 7.0 for 3C-like proteinase activity.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 sitei1651For PL-PRO activityPROSITE-ProRule annotation1
    Active sitei1812For PL-PRO activityPROSITE-ProRule annotation1
    Active sitei3281For 3CL-PRO activityPROSITE-ProRule annotation1
    Active sitei3385For 3CL-PRO activityPROSITE-ProRule annotation1
    <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 bindingi4304Zinc1
    Metal bindingi4307Zinc1
    Metal bindingi4313Zinc1
    Metal bindingi4320Zinc1
    Metal bindingi4347Zinc1
    Metal bindingi4350Zinc1
    Metal bindingi4358Zinc1
    Metal bindingi5306Zinc 1PROSITE-ProRule annotation1
    Metal bindingi5309Zinc 1PROSITE-ProRule annotation1
    Metal bindingi5317Zinc 2PROSITE-ProRule annotation1
    Metal bindingi5320Zinc 1PROSITE-ProRule annotation1
    Metal bindingi5327Zinc 1PROSITE-ProRule annotation1
    Metal bindingi5330Zinc 2PROSITE-ProRule annotation1
    Metal bindingi5334Zinc 2PROSITE-ProRule annotation1
    Metal bindingi5340Zinc 2PROSITE-ProRule annotation1
    Metal bindingi5351Zinc 3PROSITE-ProRule annotation1
    Metal bindingi5356Zinc 3PROSITE-ProRule annotation1
    Metal bindingi5373Zinc 3PROSITE-ProRule annotation1
    Metal bindingi5376Zinc 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 fingeri1729 – 1766C4-typePROSITE-ProRule annotationAdd BLAST38
    Zinc fingeri4304 – 4320Add BLAST17
    Zinc fingeri4347 – 4360Add BLAST14
    <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 bindingi5583 – 5590ATPBy similarity8

    <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

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.7.48 7599
    3.4.22.B14 7599
    3.6.4.12 7599

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0C6X7

    <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:3.4.22.69)
    Short name:
    nsp3
    Alternative name(s):
    PL2-PRO
    Papain-like proteinase
    Short name:
    PL-PRO
    Non-structural protein 4
    Short name:
    nsp4
    3C-like proteinase (EC:3.4.22.-)
    Short name:
    3CL-PRO
    Short name:
    3CLp
    Alternative name(s):
    SARS coronavirus main proteinase
    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 exoribonuclease2 Publications (EC:2.1.1.-, 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>OrganismiHuman SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome coronavirus)
    <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 identifieri694009 [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]
    Paguma larvata (Masked palm civet) [TaxID: 9675]
    <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

    <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

    • host perinuclear region By similarity
    • Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
    • host perinuclear region By similarity
    • Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
    • host perinuclear region By similarity
    • Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
    • host perinuclear region By similarity
    • Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity

    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 – 2202CytoplasmicCuratedAdd BLAST2202
    <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>Transmembranei2203 – 2223HelicalSequence analysisAdd BLAST21
    Topological domaini2224 – 2303LumenalCuratedAdd BLAST80
    Transmembranei2304 – 2324HelicalSequence analysisAdd BLAST21
    Topological domaini2325 – 2350CytoplasmicCuratedAdd BLAST26
    Transmembranei2351 – 2371HelicalSequence analysisAdd BLAST21
    Topological domaini2372 – 2754LumenalCuratedAdd BLAST383
    Transmembranei2755 – 2775HelicalSequence analysisAdd BLAST21
    Topological domaini2776 – 2991CytoplasmicCuratedAdd BLAST216
    Transmembranei2992 – 3012HelicalSequence analysisAdd BLAST21
    Topological domaini3013 – 3021LumenalCurated9
    Transmembranei3022 – 3042HelicalSequence analysisAdd BLAST21
    Topological domaini3043 – 3053CytoplasmicCuratedAdd BLAST11
    Transmembranei3054 – 3074HelicalSequence analysisAdd BLAST21
    Topological domaini3075 – 3076LumenalCurated2
    Transmembranei3077 – 3097HelicalSequence analysisAdd BLAST21
    Topological domaini3098 – 3104CytoplasmicCurated7
    Transmembranei3105 – 3125HelicalSequence analysisAdd BLAST21
    Topological domaini3126 – 3141LumenalCuratedAdd BLAST16
    Transmembranei3142 – 3162HelicalSequence analysisAdd BLAST21
    Topological domaini3163 – 3563CytoplasmicCuratedAdd BLAST401
    Transmembranei3564 – 3584HelicalSequence analysisAdd BLAST21
    Topological domaini3585LumenalCurated1
    Transmembranei3586 – 3606HelicalSequence analysisAdd BLAST21
    Topological domaini3607 – 3611CytoplasmicCurated5
    Transmembranei3612 – 3632HelicalSequence analysisAdd BLAST21
    Topological domaini3633 – 3657LumenalCuratedAdd BLAST25
    Transmembranei3658 – 3678HelicalSequence analysisAdd BLAST21
    Topological domaini3679 – 3684CytoplasmicCurated6
    Transmembranei3685 – 3704HelicalSequence analysisAdd BLAST20
    Topological domaini3705 – 3727LumenalCuratedAdd BLAST23
    Transmembranei3728 – 3748HelicalSequence analysisAdd BLAST21
    Topological domaini3749 – 3755CytoplasmicCurated7
    Transmembranei3756 – 3776HelicalSequence analysisAdd BLAST21
    Topological domaini3777 – 7073LumenalCuratedAdd BLAST3297

    GO - Cellular componenti

    Keywords - Cellular componenti

    Host cytoplasm, 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>Mutagenesisi4217G → E: Complete loss of nsp9 dimerization. 1 Publication1
    Mutagenesisi4221G → E: Complete loss of nsp9 dimerization. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5118

    Drug and drug target database

    More...
    DrugBanki
    DB07620 2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINITRO-5-(TRIFLUOROMETHYL)BENZENE
    DB08748 4-(DIMETHYLAMINO)BENZOIC ACID
    DB08656 5-amino-2-methyl-N-[(1R)-1-naphthalen-1-ylethyl]benzamide
    DB07293 benzyl (2-oxopropyl)carbamate
    DB08732 NALPHA-[(BENZYLOXY)CARBONYL]-N-[(1R)-4-HYDROXY-1-METHYL-2-OXOBUTYL]-L-PHENYLALANINAMIDE
    DB07743 S-[5-(TRIFLUOROMETHYL)-4H-1,2,4-TRIAZOL-3-YL] 5-(PHENYLETHYNYL)FURAN-2-CARBOTHIOATE

    DrugCentral

    More...
    DrugCentrali
    P0C6X7

    <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_00000373091 – 180Host translation inhibitor nsp1By similarityAdd BLAST180
    ChainiPRO_0000037310181 – 818Non-structural protein 2By similarityAdd BLAST638
    ChainiPRO_0000037311819 – 2740Non-structural protein 3By similarityAdd BLAST1922
    ChainiPRO_00002838412741 – 3240Non-structural protein 4Sequence analysisAdd BLAST500
    ChainiPRO_00000373123241 – 35463C-like proteinaseBy similarityAdd BLAST306
    ChainiPRO_00000373133547 – 3836Non-structural protein 6By similarityAdd BLAST290
    ChainiPRO_00000373143837 – 3919Non-structural protein 7By similarityAdd BLAST83
    ChainiPRO_00000373153920 – 4117Non-structural protein 8By similarityAdd BLAST198
    ChainiPRO_00000373164118 – 4230Non-structural protein 9By similarityAdd BLAST113
    ChainiPRO_00000373174231 – 4369Non-structural protein 10By similarityAdd BLAST139
    ChainiPRO_00000373184370 – 5301RNA-directed RNA polymeraseBy similarityAdd BLAST932
    ChainiPRO_00000373195302 – 5902HelicaseBy similarityAdd BLAST601
    ChainiPRO_00000373205903 – 6429Proofreading exoribonucleaseBy similarityAdd BLAST527
    ChainiPRO_00000373216430 – 6775Uridylate-specific endoribonucleaseBy similarityAdd BLAST346
    ChainiPRO_00000373226776 – 70732'-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 (PubMed:32083638). 3CL-PRO and PL-PRO proteinases are autocatalytically processed (By similarity).By similarity1 Publication

    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 – 181CleavageBy similarity2
    Sitei818 – 819Cleavage; by PL-PROBy similarity2
    Sitei2740 – 2741Cleavage; by PL-PROBy similarity2
    Sitei3240 – 3241Cleavage; by 3CL-PROBy similarity2
    Sitei3546 – 3547Cleavage; by 3CL-PROBy similarity2
    Sitei3836 – 3837Cleavage; by 3CL-PRO1 Publication2
    Sitei3919 – 3920Cleavage; by 3CL-PRO1 Publication2
    Sitei4117 – 4118Cleavage; by 3CL-PRO1 Publication2
    Sitei4230 – 4231Cleavage; by 3CL-PRO1 Publication2
    Sitei4369 – 4370Cleavage; by 3CL-PROBy similarity2
    Sitei5301 – 5302Cleavage; by 3CL-PROBy similarity2
    Sitei5902 – 5903Cleavage; by 3CL-PROBy similarity2
    Sitei6429 – 6430Cleavage; by 3CL-PROBy similarity2
    Sitei6775 – 6776Cleavage; by 3CL-PROBy similarity2

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0C6X7

    <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. 3CL-PRO exists as monomer and homodimer.

    2 Publications

    Interacts with PL-PRO and nsp6. Only the homodimer shows catalytic activity.

    1 Publication

    Homodimer.

    1 Publication

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

    1 Publication

    Homodimerizes.

    1 Publication

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

    3 Publications

    Interacts (via N-terminus) with DDX1.

    1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">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

    P0C6X7
    With#Exp.IntAct
    7b [Q7TFA1]2EBI-7843867,EBI-25492846
    itself2EBI-7843867,EBI-7843867
    Host translation inhibitor nsp1 (PRO_0000037309)
    With#Exp.IntAct
    E [P59637]2EBI-25475797,EBI-25487741
    CHMP2B [Q9UQN3] from Homo sapiens.2EBI-25475797,EBI-718324
    FKBP1A [P62942] from Homo sapiens.4EBI-25475797,EBI-1027571
    LAS1L [Q9Y4W2] from Homo sapiens.2EBI-25475797,EBI-1051591
    PPIA [P62937] from Homo sapiens.4EBI-25475797,EBI-437708
    PPIG [Q13427] from Homo sapiens.4EBI-25475797,EBI-396072
    PPIH [O43447] from Homo sapiens.4EBI-25475797,EBI-1055615
    RCAN3 [Q9UKA8] from Homo sapiens.2EBI-25475797,EBI-9091952
    Non-structural protein 2 (PRO_0000037310)
    With#Exp.IntAct
    Non-structural protein 11 (PRO_0000338265)2EBI-25474098,EBI-25492625
    3a [P59632]2EBI-25474098,EBI-15595051
    itself2EBI-25474098,EBI-25474098
    Non-structural protein 3 (PRO_0000037311)3EBI-25474098,EBI-25474079
    Non-structural protein 8 (PRO_0000037315)4EBI-25474098,EBI-25487941
    SERPING1 [P05155] from Homo sapiens.2EBI-25474098,EBI-1223454
    Non-structural protein 3 (PRO_0000037311)
    With#Exp.IntAct
    3C-like proteinase (PRO_0000037312)2EBI-25474079,EBI-25487250
    Non-structural protein 8 (PRO_0000037315)2EBI-25474079,EBI-25487941
    RNA-directed RNA polymerase (PRO_0000037318)3EBI-25474079,EBI-25487684
    MKRN2 [Q9H000] from Homo sapiens.2EBI-25474079,EBI-2341005
    MKRN3 [Q13064] from Homo sapiens.2EBI-25474079,EBI-2340269
    3C-like proteinase (PRO_0000037312)
    With#Exp.IntAct
    Non-structural protein 8 (PRO_0000037315)2EBI-25487250,EBI-25487941
    FKBP1A [P62942] from Homo sapiens.2EBI-25487250,EBI-1027571
    Non-structural protein 6 (PRO_0000037313)
    With#Exp.IntAct
    Non-structural protein 2 (PRO_0000037310)3EBI-25487192,EBI-25474098
    Non-structural protein 7 (PRO_0000037314)
    With#Exp.IntAct
    Non-structural protein 8 (PRO_0000037315)3EBI-25487672,EBI-25487941
    DDAH2 [O95865] from Homo sapiens.2EBI-25487672,EBI-749139
    MIF4GD [A9UHW6] from Homo sapiens.2EBI-25487672,EBI-373498
    Non-structural protein 8 (PRO_0000037315)
    With#Exp.IntAct
    E [P59637]2EBI-25487941,EBI-25487741
    itself2EBI-25487941,EBI-25487941
    H2AFY2 [Q9P0M6] from Homo sapiens.2EBI-25487941,EBI-3922608
    NOMO3 [P69849] from Homo sapiens.2EBI-25487941,EBI-947048
    TERF1 [P54274] from Homo sapiens.2EBI-25487941,EBI-710997
    Non-structural protein 9 (PRO_0000037316)
    With#Exp.IntAct
    Host translation inhibitor nsp1 (PRO_0000037309)2EBI-25475825,EBI-25475797
    Non-structural protein 7 (PRO_0000037314)2EBI-25475825,EBI-25487672
    Non-structural protein 8 (PRO_0000037315)3EBI-25475825,EBI-25487941
    Proofreading exoribonuclease (PRO_0000037320)2EBI-25475825,EBI-25487328
    CHMP2B [Q9UQN3] from Homo sapiens.2EBI-25475825,EBI-718324
    SNAP47 [Q5SQN1] from Homo sapiens.2EBI-25475825,EBI-10244848
    RNA-directed RNA polymerase (PRO_0000037318)
    With#Exp.IntAct
    Non-structural protein 8 (PRO_0000037315)4EBI-25487684,EBI-25487941
    Helicase (PRO_0000037319)
    With#Exp.IntAct
    Non-structural protein 3 (PRO_0000037311)2EBI-25487926,EBI-25474079
    Non-structural protein 8 (PRO_0000037315)3EBI-25487926,EBI-25487941
    RNA-directed RNA polymerase (PRO_0000037318)3EBI-25487926,EBI-25487684
    CHEK2 [O96017] from Homo sapiens.2EBI-25487926,EBI-1180783
    RYBP [Q8N488] from Homo sapiens.2EBI-25487926,EBI-752324
    Proofreading exoribonuclease (PRO_0000037320)
    With#Exp.IntAct
    9b [P59636]3EBI-25487328,EBI-9021274
    Non-structural protein 3 (PRO_0000037311)2EBI-25487328,EBI-25474079
    Non-structural protein 8 (PRO_0000037315)3EBI-25487328,EBI-25487941
    SERPING1 [P05155] from Homo sapiens.2EBI-25487328,EBI-1223454
    Uridylate-specific endoribonuclease (PRO_0000037321)
    With#Exp.IntAct
    Non-structural protein 8 (PRO_0000037315)2EBI-25487301,EBI-25487941
    2'-O-methyltransferase (PRO_0000037322)
    With#Exp.IntAct
    Non-structural protein 2 (PRO_0000037310)2EBI-25487235,EBI-25474098
    Non-structural protein 3 (PRO_0000037311)3EBI-25487235,EBI-25474079

    GO - Molecular functioni

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    P0C6X7, 69 interactors

    Molecular INTeraction database

    More...
    MINTi
    P0C6X7

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P0C6X7

    <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

    17073
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    P0C6X7

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0C6X7

    <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>Domaini1003 – 1169MacroPROSITE-ProRule annotationAdd BLAST167
    Domaini1611 – 1875Peptidase C16PROSITE-ProRule annotationAdd BLAST265
    Domaini3241 – 3546Peptidase C30PROSITE-ProRule annotationAdd BLAST306
    Domaini4981 – 5143RdRp catalyticPROSITE-ProRule annotationAdd BLAST163
    Domaini5302 – 5385CV ZBDPROSITE-ProRule annotationAdd BLAST84
    Domaini5558 – 5739(+)RNA virus helicase ATP-bindingAdd BLAST182
    Domaini5740 – 5909(+)RNA virus helicase C-terminalAdd BLAST170

    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>Regioni2092 – 2371HD1Add BLAST280
    Regioni2755 – 3162HD2Add BLAST408
    Regioni3564 – 3776HD3Add BLAST213

    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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi930 – 1001Glu-richAdd BLAST72
    Compositional biasi2210 – 2213Poly-Leu4
    Compositional biasi3766 – 3769Poly-Cys4

    <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.

    <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 fingeri1729 – 1766C4-typePROSITE-ProRule annotationAdd BLAST38
    Zinc fingeri4304 – 4320Add BLAST17
    Zinc fingeri4347 – 4360Add BLAST14

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.150.420, 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
    2.40.10.250, 1 hit
    2.40.10.290, 1 hit
    3.10.20.350, 1 hit
    3.10.20.540, 1 hit
    3.40.220.20, 1 hit
    3.40.50.11020, 1 hit
    3.40.50.11580, 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
    IPR043174 Nsp15_middle
    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
    IPR043177 R1a/1ab_N
    IPR043178 R1a/1ab_thumb
    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
    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 A1pp, 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
    SSF53335 SSF53335, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51653 CV_ZBD, 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
    Isoform Replicase polyprotein 1ab (identifier: P0C6X7-1) [UniParc]FASTAAdd to basket
    Also known as: pp1ab

    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
    MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT
    60 70 80 90 100
    CGLVELEKGV LPQLEQPYVF IKRSDALSTN HGHKVVELVA EMDGIQYGRS
    110 120 130 140 150
    GITLGVLVPH VGETPIAYRN VLLRKNGNKG AGGHSYGIDL KSYDLGDELG
    160 170 180 190 200
    TDPIEDYEQN WNTKHGSGAL RELTRELNGG AVTRYVDNNF CGPDGYPLDC
    210 220 230 240 250
    IKDFLARAGK SMCTLSEQLD YIESKRGVYC CRDHEHEIAW FTERSDKSYE
    260 270 280 290 300
    HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
    310 320 330 340 350
    RSVYPVASPQ ECNNMHLSTL MKCNHCDEVS WQTCDFLKAT CEHCGTENLV
    360 370 380 390 400
    IEGPTTCGYL PTNAVVKMPC PACQDPEIGP EHSVADYHNH SNIETRLRKG
    410 420 430 440 450
    GRTRCFGGCV FAYVGCYNKR AYWVPRASAD IGSGHTGITG DNVETLNEDL
    460 470 480 490 500
    LEILSRERVN INIVGDFHLN EEVAIILASF SASTSAFIDT IKSLDYKSFK
    510 520 530 540 550
    TIVESCGNYK VTKGKPVKGA WNIGQQRSVL TPLCGFPSQA AGVIRSIFAR
    560 570 580 590 600
    TLDAANHSIP DLQRAAVTIL DGISEQSLRL VDAMVYTSDL LTNSVIIMAY
    610 620 630 640 650
    VTGGLVQQTS QWLSNLLGTT VEKLRPIFEW IEAKLSAGVE FLKDAWEILK
    660 670 680 690 700
    FLITGVFDIV KGQIQVASDN IKDCVKCFID VVNKALEMCI DQVTIAGAKL
    710 720 730 740 750
    RSLNLGEVFI AQSKGLYRQC IRGKEQLQLL MPLKAPKEVT FLEGDSHDTV
    760 770 780 790 800
    LTSEEVVLKN GELEALETPV DSFTNGAIVG TPVCVNGLML LEIKDKEQYC
    810 820 830 840 850
    ALSPGLLATN NVFRLKGGAP IKGVTFGEDT VWEVQGYKNV RITFELDERV
    860 870 880 890 900
    DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
    910 920 930 940 950
    WSVATFYLFD DAGEENFSSR MYCSFYPPDE EEEDDAECEE EEIDETCEHE
    960 970 980 990 1000
    YGTEDDYQGL PLEFGASAET VRVEEEEEED WLDDTTEQSE IEPEPEPTPE
    1010 1020 1030 1040 1050
    EPVNQFTGYL KLTDNVAIKC VDIVKEAQSA NPMVIVNAAN IHLKHGGGVA
    1060 1070 1080 1090 1100
    GALNKATNGA MQKESDDYIK LNGPLTVGGS CLLSGHNLAK KCLHVVGPNL
    1110 1120 1130 1140 1150
    NAGEDIQLLK AAYENFNSQD ILLAPLLSAG IFGAKPLQSL QVCVQTVRTQ
    1160 1170 1180 1190 1200
    VYIAVNDKAL YEQVVMDYLD NLKPRVEAPK QEEPPNTEDS KTEEKSVVQK
    1210 1220 1230 1240 1250
    PVDVKPKIKA CIDEVTTTLE ETKFLTNKLL LFADINGKLY HDSQNMLRGE
    1260 1270 1280 1290 1300
    DMSFLEKDAP YMVGDVITSG DITCVVIPSK KAGGTTEMLS RALKKVPVDE
    1310 1320 1330 1340 1350
    YITTYPGQGC AGYTLEEAKT ALKKCKSAFY VLPSEAPNAK EEILGTVSWN
    1360 1370 1380 1390 1400
    LREMLAHAEE TRKLMPICMD VRAIMATIQR KYKGIKIQEG IVDYGVRFFF
    1410 1420 1430 1440 1450
    YTSKEPVASI ITKLNSLNEP LVTMPIGYVT HGFNLEEAAR CMRSLKAPAV
    1460 1470 1480 1490 1500
    VSVSSPDAVT TYNGYLTSSS KTSEEHFVET VSLAGSYRDW SYSGQRTELG
    1510 1520 1530 1540 1550
    VEFLKRGDKI VYHTLESPVE FHLDGEVLSL DKLKSLLSLR EVKTIKVFTT
    1560 1570 1580 1590 1600
    VDNTNLHTQL VDMSMTYGQQ FGPTYLDGAD VTKIKPHVNH EGKTFFVLPS
    1610 1620 1630 1640 1650
    DDTLRSEAFE YYHTLDESFL GRYMSALNHT KKWKFPQVGG LTSIKWADNN
    1660 1670 1680 1690 1700
    CYLSSVLLAL QQLEVKFNAP ALQEAYYRAR AGDAANFCAL ILAYSNKTVG
    1710 1720 1730 1740 1750
    ELGDVRETMT HLLQHANLES AKRVLNVVCK HCGQKTTTLT GVEAVMYMGT
    1760 1770 1780 1790 1800
    LSYDNLKTGV SIPCVCGRDA TQYLVQQESS FVMMSAPPAE YKLQQGTFLC
    1810 1820 1830 1840 1850
    ANEYTGNYQC GHYTHITAKE TLYRIDGAHL TKMSEYKGPV TDVFYKETSY
    1860 1870 1880 1890 1900
    TTTIKPVSYK LDGVTYTEIE PKLDGYYKKD NAYYTEQPID LVPTQPLPNA
    1910 1920 1930 1940 1950
    SFDNFKLTCS NTKFADDLNQ MTGFTKPASR ELSVTFFPDL NGDVVAIDYR
    1960 1970 1980 1990 2000
    HYSASFKKGA KLLHKPIVWH INQATTKTTF KPNTWCLRCL WSTKPVDTSN
    2010 2020 2030 2040 2050
    SFEVLAVEDT QGMDNLACES QQPTSEEVVE NPTIQKEVIE CDVKTTEVVG
    2060 2070 2080 2090 2100
    NVILKPSDEG VKVTQELGHE DLMAAYVENT SITIKKPNEL SLALGLKTIA
    2110 2120 2130 2140 2150
    THGIAAINSV PWSKILAYVK PFLGQAAITT SNCAKRLAQR VFNNYMPYVF
    2160 2170 2180 2190 2200
    TLLFQLCTFT KSTNSRIRAS LPTTIAKNSV KSVAKLCLDA GINYVKSPKF
    2210 2220 2230 2240 2250
    SKLFTIAMWL LLLSICLGSL ICVTAAFGVL LSNFGAPSYC NGVRELYLNS
    2260 2270 2280 2290 2300
    SNVTTMDFCE GSFPCSICLS GLDSLDSYPA LETIQVTISS YKLDLTILGL
    2310 2320 2330 2340 2350
    AAEWVLAYML FTKFFYLLGL SAIMQVFFGY FASHFISNSW LMWFIISIVQ
    2360 2370 2380 2390 2400
    MAPVSAMVRM YIFFASFYYI WKSYVHIMDG CTSSTCMMCY KRNRATRVEC
    2410 2420 2430 2440 2450
    TTIVNGMKRS FYVYANGGRG FCKTHNWNCL NCDTFCTGST FISDEVARDL
    2460 2470 2480 2490 2500
    SLQFKRPINP TDQSSYIVDS VAVKNGALHL YFDKAGQKTY ERHPLSHFVN
    2510 2520 2530 2540 2550
    LDNLRANNTK GSLPINVIVF DGKSKCDESA SKSASVYYSQ LMCQPILLLD
    2560 2570 2580 2590 2600
    QALVSDVGDS TEVSVKMFDA YVDTFSATFS VPMEKLKALV ATAHSELAKG
    2610 2620 2630 2640 2650
    VALDGVLSTF VSAARQGVVD TDVDTKDVIE CLKLSHHSDL EVTGDSCNNF
    2660 2670 2680 2690 2700
    MLTYNKVENM TPRDLGACID CNARHINAQV AKSHNVSLIW NVKDYMSLSE
    2710 2720 2730 2740 2750
    QLRKQIRSAA KKNNIPFRLT CATTRQVVNV ITTKISLKGG KIVSTCFKLM
    2760 2770 2780 2790 2800
    LKATLLCVLA ALVCYIVMPV HTLSIHDGYT NEIIGYKAIQ DGVTRDIIST
    2810 2820 2830 2840 2850
    DDCFANKHAG FDAWFSQRGG SYKNDKSCPV VAAIITREIG FIVPGLPGTV
    2860 2870 2880 2890 2900
    LRAINGDFLH FLPRVFSAVG NICYTPSKLI EYSDFATSAC VLAAECTIFK
    2910 2920 2930 2940 2950
    DAMGKPVPYC YDTNLLEGSI SYSELRPDTR YVLMDGSIIQ FPNTYLEGSV
    2960 2970 2980 2990 3000
    RVVTTFDAEY CRHGTCERSE VGICLSTSGR WVLNNEHYRA LSGVFCGVDA
    3010 3020 3030 3040 3050
    MNLIANIFTP LVQPVGALDV SASVVAGGII AILVTCAAYY FMKFRRVFGE
    3060 3070 3080 3090 3100
    YNHVVAANAL LFLMSFTILC LVPAYSFLPG VYSVFYLYLT FYFTNDVSFL
    3110 3120 3130 3140 3150
    AHLQWFAMFS PIVPFWITAI YVFCISLKHC HWFFNNYLRK RVMFNGVTFS
    3160 3170 3180 3190 3200
    TFEEAALCTF LLNKEMYLKL RSETLLPLTQ YNRYLALYNK YKYFSGALDT
    3210 3220 3230 3240 3250
    TSYREAACCH LAKALNDFSN SGADVLYQPP QTSITSAVLQ SGFRKMAFPS
    3260 3270 3280 3290 3300
    GKVEGCMVQV TCGTTTLNGL WLDDTVYCPR HVICTAEDML NPNYEDLLIR
    3310 3320 3330 3340 3350
    KSNHSFLVQA GNVQLRVIGH SMQNCLLRLK VDTSNPKTPK YKFVRIQPGQ
    3360 3370 3380 3390 3400
    TFSVLACYNG SPSGVYQCAM RPNHTIKGSF LNGSCGSVGF NIDYDCVSFC
    3410 3420 3430 3440 3450
    YMHHMELPTG VHAGTDLEGK FYGPFVDRQT AQAAGTDTTI TLNVLAWLYA
    3460 3470 3480 3490 3500
    AVINGDRWFL NRFTTTLNDF NLVAMKYNYE PLTQDHVDIL GPLSAQTGIA
    3510 3520 3530 3540 3550
    VLDMCAALKE LLQNGMNGRT ILGSTILEDE FTPFDVVRQC SGVTFQGKFK
    3560 3570 3580 3590 3600
    KIVKGTHHWM LLTFLTSLLI LVQSTQWSLF FFVYENAFLP FTLGIMAIAA
    3610 3620 3630 3640 3650
    CAMLLVKHKH AFLCLFLLPS LATVAYFNMV YMPASWVMRI MTWLELADTS
    3660 3670 3680 3690 3700
    LSGYRLKDCV MYASALVLLI LMTARTVYDD AARRVWTLMN VITLVYKVYY
    3710 3720 3730 3740 3750
    GNALDQAISM WALVISVTSN YSGVVTTIMF LARAIVFVCV EYYPLLFITG
    3760 3770 3780 3790 3800
    NTLQCIMLVY CFLGYCCCCY FGLFCLLNRY FRLTLGVYDY LVSTQEFRYM
    3810 3820 3830 3840 3850
    NSQGLLPPKS SIDAFKLNIK LLGIGGKPCI KVATVQSKMS DVKCTSVVLL
    3860 3870 3880 3890 3900
    SVLQQLRVES SSKLWAQCVQ LHNDILLAKD TTEAFEKMVS LLSVLLSMQG
    3910 3920 3930 3940 3950
    AVDINRLCEE MLDNRATLQA IASEFSSLPS YAAYATAQEA YEQAVANGDS
    3960 3970 3980 3990 4000
    EVVLKKLKKS LNVAKSEFDR DAAMQRKLEK MADQAMTQMY KQARSEDKRA
    4010 4020 4030 4040 4050
    KVTSAMQTML FTMLRKLDND ALNNIINNAR DGCVPLNIIP LTTAAKLMVV
    4060 4070 4080 4090 4100
    VPDYGTYKNT CDGNTFTYAS ALWEIQQVVD ADSKIVQLSE INMDNSPNLA
    4110 4120 4130 4140 4150
    WPLIVTALRA NSAVKLQNNE LSPVALRQMS CAAGTTQTAC TDDNALAYYN
    4160 4170 4180 4190 4200
    NSKGGRFVLA LLSDHQDLKW ARFPKSDGTG TIYTELEPPC RFVTDTPKGP
    4210 4220 4230 4240 4250
    KVKYLYFIKG LNNLNRGMVL GSLAATVRLQ AGNATEVPAN STVLSFCAFA
    4260 4270 4280 4290 4300
    VDPAKAYKDY LASGGQPITN CVKMLCTHTG TGQAITVTPE ANMDQESFGG
    4310 4320 4330 4340 4350
    ASCCLYCRCH IDHPNPKGFC DLKGKYVQIP TTCANDPVGF TLRNTVCTVC
    4360 4370 4380 4390 4400
    GMWKGYGCSC DQLREPLMQS ADASTFLNRV CGVSAARLTP CGTGTSTDVV
    4410 4420 4430 4440 4450
    YRAFDIYNEK VAGFAKFLKT NCCRFQEKDE EGNLLDSYFV VKRHTMSNYQ
    4460 4470 4480 4490 4500
    HEETIYNLVK DCPAVAVHDF FKFRVDGDMV PHISRQRLTK YTMADLVYAL
    4510 4520 4530 4540 4550
    RHFDEGNCDT LKEILVTYNC CDDDYFNKKD WYDFVENPDI LRVYANLGER
    4560 4570 4580 4590 4600
    VRQSLLKTVQ FCDAMRDAGI VGVLTLDNQD LNGNWYDFGD FVQVAPGCGV
    4610 4620 4630 4640 4650
    PIVDSYYSLL MPILTLTRAL AAESHMDADL AKPLIKWDLL KYDFTEERLC
    4660 4670 4680 4690 4700
    LFDRYFKYWD QTYHPNCINC LDDRCILHCA NFNVLFSTVF PPTSFGPLVR
    4710 4720 4730 4740 4750
    KIFVDGVPFV VSTGYHFREL GVVHNQDVNL HSSRLSFKEL LVYAADPAMH
    4760 4770 4780 4790 4800
    AASGNLLLDK RTTCFSVAAL TNNVAFQTVK PGNFNKDFYD FAVSKGFFKE
    4810 4820 4830 4840 4850
    GSSVELKHFF FAQDGNAAIS DYDYYRYNLP TMCDIRQLLF VVEVVDKYFD
    4860 4870 4880 4890 4900
    CYDGGCINAN QVIVNNLDKS AGFPFNKWGK ARLYYDSMSY EDQDALFAYT
    4910 4920 4930 4940 4950
    KRNVIPTITQ MNLKYAISAK NRARTVAGVS ICSTMTNRQF HQKLLKSIAA
    4960 4970 4980 4990 5000
    TRGATVVIGT SKFYGGWHNM LKTVYSDVET PHLMGWDYPK CDRAMPNMLR
    5010 5020 5030 5040 5050
    IMASLVLARK HNTCCNLSHR FYRLANECAQ VLSEMVMCGG SLYVKPGGTS
    5060 5070 5080 5090 5100
    SGDATTAYAN SVFNICQAVT ANVNALLSTD GNKIADKYVR NLQHRLYECL
    5110 5120 5130 5140 5150
    YRNRDVDHEF VDEFYAYLRK HFSMMILSDD AVVCYNSNYA AQGLVASIKN
    5160 5170 5180 5190 5200
    FKAVLYYQNN VFMSEAKCWT ETDLTKGPHE FCSQHTMLVK QGDDYVYLPY
    5210 5220 5230 5240 5250
    PDPSRILGAG CFVDDIVKTD GTLMIERFVS LAIDAYPLTK HPNQEYADVF
    5260 5270 5280 5290 5300
    HLYLQYIRKL HDELTGHMLD MYSVMLTNDN TSRYWEPEFY EAMYTPHTVL
    5310 5320 5330 5340 5350
    QAVGACVLCN SQTSLRCGAC IRRPFLCCKC CYDHVISTSH KLVLSVNPYV
    5360 5370 5380 5390 5400
    CNAPGCDVTD VTQLYLGGMS YYCKSHKPPI SFPLCANGQV FGLYKNTCVG
    5410 5420 5430 5440 5450
    SDNVTDFNAI ATCDWTNAGD YILANTCTER LKLFAAETLK ATEETFKLSY
    5460 5470 5480 5490 5500
    GIATVREVLS DRELHLSWEV GKPRPPLNRN YVFTGYRVTK NSKVQIGEYT
    5510 5520 5530 5540 5550
    FEKGDYGDAV VYRGTTTYKL NVGDYFVLTS HTVMPLSAPT LVPQEHYVRI
    5560 5570 5580 5590 5600
    TGLYPTLNIS DEFSSNVANY QKVGMQKYST LQGPPGTGKS HFAIGLALYY
    5610 5620 5630 5640 5650
    PSARIVYTAC SHAAVDALCE KALKYLPIDK CSRIIPARAR VECFDKFKVN
    5660 5670 5680 5690 5700
    STLEQYVFCT VNALPETTAD IVVFDEISMA TNYDLSVVNA RLRAKHYVYI
    5710 5720 5730 5740 5750
    GDPAQLPAPR TLLTKGTLEP EYFNSVCRLM KTIGPDMFLG TCRRCPAEIV
    5760 5770 5780 5790 5800
    DTVSALVYDN KLKAHKDKSA QCFKMFYKGV ITHDVSSAIN RPQIGVVREF
    5810 5820 5830 5840 5850
    LTRNPAWRKA VFISPYNSQN AVASKILGLP TQTVDSSQGS EYDYVIFTQT
    5860 5870 5880 5890 5900
    TETAHSCNVN RFNVAITRAK IGILCIMSDR DLYDKLQFTS LEIPRRNVAT
    5910 5920 5930 5940 5950
    LQAENVTGLF KDCSKIITGL HPTQAPTHLS VDIKFKTEGL CVDIPGIPKD
    5960 5970 5980 5990 6000
    MTYRRLISMM GFKMNYQVNG YPNMFITREE AIRHVRAWIG FDVEGCHATR
    6010 6020 6030 6040 6050
    DAVGTNLPLQ LGFSTGVNLV AVPTGYVDTE NNTEFTRVNA KPPPGDQFKH
    6060 6070 6080 6090 6100
    LIPLMYKGLP WNVVRIKIVQ MLSDTLKGLS DRVVFVLWAH GFELTSMKYF
    6110 6120 6130 6140 6150
    VKIGPERTCC LCDKRATCFS TSSDTYACWN HSVGFDYVYN PFMIDVQQWG
    6160 6170 6180 6190 6200
    FTGNLQSNHD QHCQVHGNAH VASCDAIMTR CLAVHECFVK RVDWSVEYPI
    6210 6220 6230 6240 6250
    IGDELRVNSA CRKVQHMVVK SALLADKFPV LHDIGNPKAI KCVPQAEVEW
    6260 6270 6280 6290 6300
    KFYDAQPCSD KAYKIEELFY SYATHHDKFT DGVCLFWNCN VDRYPANAIV
    6310 6320 6330 6340 6350
    CRFDTRVLSN LNLPGCDGGS LYVNKHAFHT PAFDKSAFTN LKQLPFFYYS
    6360 6370 6380 6390 6400
    DSPCESHGKQ VVSDIDYVPL KSATCITRCN LGGAVCRHHA NEYRQYLDAY
    6410 6420 6430 6440 6450
    NMMISAGFSL WIYKQFDTYN LWNTFTRLQS LENVAYNVVN KGHFDGHAGE
    6460 6470 6480 6490 6500
    APVSIINNAV YTKVDGIDVE IFENKTTLPV NVAFELWAKR NIKPVPEIKI
    6510 6520 6530 6540 6550
    LNNLGVDIAA NTVIWDYKRE APAHVSTIGV CTMTDIAKKP TESACSSLTV
    6560 6570 6580 6590 6600
    LFDGRVEGQV DLFRNARNGV LITEGSVKGL TPSKGPAQAS VNGVTLIGES
    6610 6620 6630 6640 6650
    VKTQFNYFKK VDGIIQQLPE TYFTQSRDLE DFKPRSQMET DFLELAMDEF
    6660 6670 6680 6690 6700
    IQRYKLEGYA FEHIVYGDFS HGQLGGLHLM IGLAKRSQDS PLKLEDFIPM
    6710 6720 6730 6740 6750
    DSTVKNYFIT DAQTGSSKCV CSVIDLLLDD FVEIIKSQDL SVISKVVKVT
    6760 6770 6780 6790 6800
    IDYAEISFML WCKDGHVETF YPKLQASQAW QPGVAMPNLY KMQRMLLEKC
    6810 6820 6830 6840 6850
    DLQNYGENAV IPKGIMMNVA KYTQLCQYLN TLTLAVPYNM RVIHFGAGSD
    6860 6870 6880 6890 6900
    KGVAPGTAVL RQWLPTGTLL VDSDLNDFVS DADSTLIGDC ATVHTANKWD
    6910 6920 6930 6940 6950
    LIISDMYDPR TKHVTKENDS KEGFFTYLCG FIKQKLALGG SIAVKITEHS
    6960 6970 6980 6990 7000
    WNADLYKLMG HFSWWTAFVT NVNASSSEAF LIGANYLGKP KEQIDGYTMH
    7010 7020 7030 7040 7050
    ANYIFWRNTN PIQLSSYSLF DMSKFPLKLR GTAVMSLKEN QINDMIYSLL
    7060 7070
    EKGRLIIREN NRVVVSSDIL VNN
    Note: Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.
    Length:7,073
    Mass (Da):790,248
    Last modified:June 10, 2008 - 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:iE6504CAFDC36BC09
    GO
    Isoform Replicase polyprotein 1a (identifier: P0C6U8-1) [UniParc]FASTAAdd to basket
    Also known as: pp1a, ORF1a polyprotein
    The sequence of this isoform can be found in the external entry P0C6U8.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:4,382
    Mass (Da):486,373
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAP13440 differs from that shown. Reason: Erroneous gene model prediction.Curated
    The sequence AAP41036 differs from that shown. Reason: Erroneous gene model prediction.Curated
    The sequence AAP82975 differs from that shown. Reason: Erroneous gene model prediction.Curated
    The sequence AAP97881 differs from that shown. Reason: Erroneous gene model prediction.Curated
    The sequence AAQ01596 differs from that shown. Reason: Erroneous gene model prediction.Curated
    The sequence AAQ01608 differs from that shown. Reason: Erroneous gene model prediction.Curated

    <p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 21871 Da. Determined by ESI. 1 Publication
    Molecular mass is 12403 Da. Determined by ESI. 1 Publication
    Molecular mass is 14974 Da. Determined by ESI. 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 varianti82G → C in strain: Isolate GD01. 1
    Natural varianti130G → R in strain: Isolate GD01. 1
    Natural varianti138I → T in strain: Isolate SZ16. 1
    Natural varianti181A → V in strain: Isolate Shanghai LY. 1
    Natural varianti225K → Q in strain: Isolate GD01. 1
    Natural varianti249Y → C in strain: Isolate Shanghai LY. 1
    Natural varianti306V → F in strain: Isolate BJ04. 1
    Natural varianti549A → S in strain: Isolate SZ3. 1
    Natural varianti765A → T in strain: Isolate FRA and Isolate Frankfurt-1. 1
    Natural varianti852K → R in strain: Isolate SZ16. 1
    Natural varianti1004N → H in strain: Isolate BJ03. 1
    Natural varianti1021V → A in strain: Isolate SZ3 and Isolate SZ16. 1
    Natural varianti1023I → T in strain: Isolate Shanghai QXC1. 1
    Natural varianti1121I → T in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16. 1
    Natural varianti1136P → L in strain: Isolate SZ3 and Isolate SZ16. 1
    Natural varianti1257K → E in strain: Isolate Shanghai QXC1. 1
    Natural varianti1319K → R in strain: Isolate GD01. 1
    Natural varianti1329F → S in strain: Isolate GD01. 1
    Natural varianti1361T → A in strain: Isolate Shanghai QXC1. 1
    Natural varianti1385I → V in strain: Isolate Shanghai QXC1. 1
    Natural varianti1538S → T in strain: Isolate GD01. 1
    Natural varianti1563M → K in strain: Isolate BJ02. 1
    Natural varianti1663L → I in strain: Isolate SZ3 and Isolate SZ16. 1
    Natural varianti1762I → L in strain: Isolate BJ03. 1
    Natural varianti1776 – 1777QQ → PP in strain: Isolate BJ03. 2
    Natural varianti1790E → G in strain: Isolate Shanghai QXC1. 1
    Natural varianti1806G → V in strain: Isolate BJ02. 1
    Natural varianti1962L → I in strain: Isolate BJ04. 1
    Natural varianti2116L → F in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16. 1
    Natural varianti2222C → Y in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16. 1
    Natural varianti2269L → S in strain: Isolate SZ3 and Isolate SZ16. 1
    Natural varianti2326V → A in strain: Isolate Shanghai QXC1. 1
    Natural varianti2392 – 2394RNR → CNH in strain: Isolate Shanghai QXC1. 3
    Natural varianti2480L → P in strain: Isolate Shanghai QXC1. 1
    Natural varianti2552A → V in strain: Isolate Urbani and Isolate Taiwan TC2. 1
    Natural varianti2556D → N in strain: Isolate HKU-39849. 1
    Natural varianti2564S → P in strain: Isolate GD01. 1
    Natural varianti2648N → Y in strain: Isolate Shanghai QXC1. 1
    Natural varianti2708S → T in strain: Isolate HKU-39849. 1
    Natural varianti2718R → T in strain: Isolate HKU-39849. 1
    Natural varianti2746C → W in strain: Isolate SZ3 and Isolate SZ16. 1
    Natural varianti2770V → L in strain: Isolate BJ01 and Isolate BJ02. 1
    Natural varianti2944T → I in strain: Isolate SIN2500, Isolate GD01 and Isolate GZ50. 1
    Natural varianti2971V → A in strain: Isolate GD01 and Isolate SZ16. 1
    Natural varianti3020V → A in strain: Isolate Shanghai QXC1. 1
    Natural varianti3047V → A in strain: Isolate CUHK-W1, Isolate GD01, Isolate SZ3, Isolate SZ16, Isolate BJ01, Isolate BJ02, Isolate BJ03 and Isolate Shanghai QXC1. 1
    Natural varianti3072V → A in strain: Isolate CUHK-W1, Isolate SZ3, Isolate SZ16 and Isolate GD01. 1
    Natural varianti3197A → V in strain: Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04 and Isolate Shanghai QXC1. 1
    Natural varianti3429Q → P in strain: Isolate BJ02. 1
    Natural varianti3488D → E in strain: Isolate BJ04. 1
    Natural varianti3717V → A in strain: Isolate Shanghai QXC1. 1
    Natural varianti3818N → T in strain: Isolate BJ04. 1
    Natural varianti3903D → N in strain: Isolate BJ03. 1
    Natural varianti3904I → F in strain: Isolate BJ02. 1
    Natural varianti3911M → V in strain: Isolate Shanghai QXC1. 1
    Natural varianti4001K → Q in strain: Isolate Shanghai LY. 1
    Natural varianti4003T → A in strain: Isolate Shanghai LY. 1
    Natural varianti4085I → H in strain: Isolate ZJ01. 1
    Natural varianti4114V → A in strain: Isolate Shanghai QXC1. 1
    Natural varianti4202V → M in strain: Isolate Shanghai QXC1. 1
    Natural varianti4240N → H in strain: Isolate ZJ01. 1
    Natural varianti4296E → G in strain: Isolate Shanghai QXC1. 1
    Natural varianti4377 – 4378LN → FK in strain: Isolate Shanghai QXC1. 2
    Natural varianti4411V → S in strain: Isolate HKU-39849. 1
    Natural varianti4459V → I in strain: Isolate Shanghai QXC1. 1
    Natural varianti4592V → E in strain: Isolate ZJ01. 1
    Natural varianti4910Q → L in strain: Isolate ZJ01. 1
    Natural varianti5112D → G in strain: Isolate SZ3. 1
    Natural varianti5131A → G in strain: Isolate Taiwan. 1
    Natural varianti5134 – 5135CY → VL in strain: Isolate Taiwan. 2
    Natural varianti5623L → S in strain: Isolate GD01. 1
    Natural varianti5720P → S in strain: Isolate GZ50 and Isolate SIN2500. 1
    Natural varianti5744R → C in strain: Isolate ZJ01. 1
    Natural varianti5767D → E in strain: Isolate CUHK-W1, Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, Isolate SIN2500, Isolate GD01, Isolate GZ50, Isolate SZ3, Isolate SZ16 and Isolate Shanghai QXC1. 1
    Natural varianti6274T → I in strain: Isolate FRA, Isolate Frankfurt-1 Isolate SIN2677, Isolate SIN2679 and Isolate SIN2748. 1
    Natural varianti6474N → S in strain: Isolate Shanghai QXC1. 1
    Natural varianti6700M → I in strain: Isolate BJ03. 1
    Natural varianti6721C → R in strain: Isolate Shanghai QXC1. 1
    Natural varianti6729D → N in strain: Isolate GD01. 1
    Natural varianti6840M → L in strain: Isolate BJ02. 1
    Natural varianti6862Q → P in strain: Isolate BJ04. 1
    Natural varianti6877D → E in strain: Isolate GD01. 1
    Natural varianti6910R → K in strain: Isolate SZ3 and Isolate SZ16. 1
    Natural varianti6937A → P in strain: Isolate BJ03. 1
    Natural varianti6992E → D in strain: Isolate BJ04. 1
    Natural varianti7008N → K in strain: Isolate GD01. 1
    Natural varianti7024K → Q in strain: Isolate BJ04. 1

    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
    AY278741 Genomic RNA Translation: AAP13442.1
    AY278741 Genomic RNA Translation: AAP13440.1 Sequence problems.
    AY274119 Genomic RNA Translation: AAP41036.1 Sequence problems.
    AY278554 Genomic RNA Translation: AAP13566.1
    AY282752 Genomic RNA Translation: AAP30711.1
    AY304495 Genomic RNA No translation available.
    AY304486 Genomic RNA No translation available.
    AY304488 Genomic RNA No translation available.
    AY278491 Genomic RNA No translation available.
    AY283794 Genomic RNA No translation available.
    AY283795 Genomic RNA No translation available.
    AY283796 Genomic RNA No translation available.
    AY283797 Genomic RNA No translation available.
    AY283798 Genomic RNA No translation available.
    AY286320 Genomic RNA Translation: AAP49011.4
    AY278488 Genomic RNA Translation: AAP30028.1
    AY278489 Genomic RNA Translation: AAP51225.1
    AY278490 Genomic RNA No translation available.
    AY279354 Genomic RNA No translation available.
    AY291451 Genomic RNA Translation: AAP37015.1
    AY310120 Genomic RNA Translation: AAP50483.1
    AY291315 Genomic RNA Translation: AAP33696.1
    AY323977 Genomic RNA Translation: AAP72973.2
    AY321118 Genomic RNA No translation available.
    AY338174 Genomic RNA Translation: AAQ01594.1
    AY338174 Genomic RNA Translation: AAQ01596.1 Sequence problems.
    AY338175 Genomic RNA Translation: AAQ01606.1
    AY338175 Genomic RNA Translation: AAQ01608.1 Sequence problems.
    AY348314 Genomic RNA Translation: AAP97879.1
    AY348314 Genomic RNA Translation: AAP97881.1 Sequence problems.
    AP006557 Genomic RNA Translation: BAC81346.1
    AP006558 Genomic RNA Translation: BAC81360.1
    AP006559 Genomic RNA Translation: BAC81374.1
    AP006560 Genomic RNA Translation: BAC81388.1
    AP006561 Genomic RNA Translation: BAC81402.1
    AY427439 Genomic RNA Translation: AAQ94058.1
    AY322205 Genomic RNA Translation: AAP82966.1
    AY322206 Genomic RNA Translation: AAP82975.1 Sequence problems.
    AY322207 Genomic RNA Translation: AAP82967.1
    AY463059 Genomic RNA Translation: AAP82978.2
    AY269391 Genomic RNA Translation: AAP04003.1
    AY268049 Genomic RNA Translation: AAP04587.1

    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