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UniProtKB - P19811 (RPOA_EAVBU)

Entry version 176 (23 Feb 2022)
Sequence version 3 (13 Apr 2004)
Previous versions | rss
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Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Equine arteritis virus (strain Bucyrus) (EAV)
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

The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.

1 Publication

Nsp1 is essential for viral subgenomic mRNA synthesis.

1 Publication

Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity.

1 Publication

The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.

1 Publication

The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.

2 Publications

Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity).

Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (PubMed:19297500).

If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity).

By similarity1 Publication

Miscellaneous

Nsp1 contains an inactivated papain-like cysteine proteinase domain due to a Lys instead of a Cys in position 73.

<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

  • 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). EC:3.4.19.12

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 sitei164For Nsp1 papain-like cysteine proteinase activity2 Publications1
Active sitei230For Nsp1 papain-like cysteine proteinase activity1 Publication1
Active sitei270For Nsp2 cysteine proteinase activity1 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 bindingi319Zinc 1Combined sources1
Active sitei332For Nsp2 cysteine proteinase activity1 Publication1
Metal bindingi349Zinc 1Combined sources1
Metal bindingi354Zinc 1Combined sources1
Metal bindingi356Zinc 1Combined sources1
Active sitei1103Charge relay system; for 3C-like serine proteinase activityPROSITE-ProRule annotation1
Active sitei1129Charge relay system; for 3C-like serine proteinase activityPROSITE-ProRule annotation1
Active sitei1184Charge relay system; for 3C-like serine proteinase activityPROSITE-ProRule annotation1
Metal bindingi2374Zinc 2PROSITE-ProRule annotationCombined sources1
Metal bindingi2377Zinc 2PROSITE-ProRule annotationCombined sources1
Metal bindingi2387Zinc 3PROSITE-ProRule annotationCombined sources1
Metal bindingi2392Zinc 2PROSITE-ProRule annotationCombined sources1
Metal bindingi2395Zinc 2PROSITE-ProRule annotationCombined sources1
Metal bindingi2399Zinc 3; via tele nitrogenPROSITE-ProRule annotationCombined sources1
Metal bindingi2402Zinc 3; via pros nitrogenPROSITE-ProRule annotationCombined sources1
Metal bindingi2403Zinc 3PROSITE-ProRule annotationCombined sources1
Metal bindingi2412Zinc 4PROSITE-ProRule annotationCombined sources1
Metal bindingi2414Zinc 4; via pros nitrogenPROSITE-ProRule annotationCombined sources1
Metal bindingi2423Zinc 4PROSITE-ProRule annotationCombined sources1
Metal bindingi2426Zinc 4PROSITE-ProRule annotationCombined sources1
<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>Sitei2429Involved in mRNA transcription process1
Active sitei2963PROSITE-ProRule annotation1
Active sitei2978PROSITE-ProRule annotation1
Active sitei3007PROSITE-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 fingeri25 – 44C4-type; atypicalAdd BLAST20
<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 bindingi2528 – 2535ATPBy 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Helicase, Hydrolase, Lyase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase
Biological processHost-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host ISG15 by virus, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Viral immunoevasion, Viral RNA replication
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.21.114, 6985
3.4.22.B50, 6985

Protein family/group databases

MEROPS protease database

More...MEROPSi		S32.001

<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
Alternative name(s):
ORF1ab polyprotein
Cleaved into the following 14 chains:
Nsp1 papain-like cysteine proteinase (EC:3.4.22.-2 Publications)
Short name:
PCP
Nsp2 cysteine proteinase (EC:3.4.19.12, EC:3.4.22.-)
Alternative name(s):
CP2
Short name:
CP
Non-structural protein 3
Short name:
Nsp3
3C-like serine proteinase (EC:3.4.21.-)
Short name:
3CLSP
Alternative name(s):
Nsp4
Non-structural protein 5-6-7
Short name:
Nsp5-6-7
Non-structural protein 5
Short name:
Nsp5
Non-structural protein 6
Short name:
Nsp6
Non-structural protein 7-alpha
Short name:
Nsp7-alpha
Non-structural protein 7-beta
Short name:
Nsp7-beta
Non-structural protein 8
Short name:
Nsp8
RNA-directed RNA polymerase (EC:2.7.7.48)
Short name:
Pol
Short name:
RdRp
Alternative name(s):
Nsp9
Helicase2 Publications (EC:3.6.4.121 Publication, EC:3.6.4.131 Publication)
Short name:
Hel
Alternative name(s):
Nsp10
Uridylate-specific endoribonuclease nsp11 (EC:4.6.1.-)
Alternative name(s):
Non-structural protein 11
Short name:
Nsp11
Non-structural protein 12
Short name:
Nsp12
<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>OrganismiEquine arteritis virus (strain Bucyrus) (EAV)
<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 identifieri299386 [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 lineageiViruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Nidovirales › Arnidovirineae › Arteriviridae › Equarterivirinae › Alphaarterivirus › Alphaarterivirus equid ›
<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 hostiEquidae (horses) [TaxID: 9788]
<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
  • UP000000353 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei530 – 550HelicalSequence analysisAdd BLAST21
Transmembranei551 – 571HelicalSequence analysisAdd BLAST21
Transmembranei625 – 645HelicalSequence analysisAdd BLAST21
Transmembranei829 – 849HelicalSequence analysisAdd BLAST21
Transmembranei903 – 923HelicalSequence analysisAdd BLAST21
Transmembranei935 – 955HelicalSequence analysisAdd BLAST21
Transmembranei977 – 997HelicalSequence analysisAdd BLAST21
Transmembranei1291 – 1311HelicalSequence analysisAdd BLAST21
Transmembranei1333 – 1353HelicalSequence analysisAdd BLAST21
Transmembranei1355 – 1375HelicalSequence analysisAdd BLAST21
Transmembranei1385 – 1405HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Host nucleus, 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>Mutagenesisi25C → A: Complete loss of transcription. 1 Publication1
Mutagenesisi44C → A: Complete loss of transcription. 1 Publication1
Mutagenesisi164C → G or S: Complete loss of PCP proteinase activity. 2 Publications1
Mutagenesisi219H → A, G or V: No effect. 1 Publication1
Mutagenesisi230H → A, G or V: Complete loss of PCP proteinase activity. 1 Publication1
Mutagenesisi260G → V: Complete loss of nsp1-nsp2 cleavage. 1 Publication1
Mutagenesisi270C → A, H, R or S: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi271G → W: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi291D → E or N: No effect. 1 Publication1
Mutagenesisi295D → E or N: No effect. 1 Publication1
Mutagenesisi296D → E or N: No effect. 1 Publication1
Mutagenesisi297E → D or Q: No effect. 1 Publication1
Mutagenesisi319C → A, H or P: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi332H → C, I, N or Y: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi344C → A: No effect. 1 Publication1
Mutagenesisi344C → H: Almost complete loss of CP2 activity. 1 Publication1
Mutagenesisi349C → A, H or S: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi354C → A, H or P: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi356C → A: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi356C → H: No effect. 1 Publication1
Mutagenesisi831G → P: Complete loss of nsp2-nsp3 cleavage. 1 Publication1
Mutagenesisi1064E → P: Complete loss of nsp3-nsp4 cleavage. 1 Publication1
Mutagenesisi1103H → G or R: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication1
Mutagenesisi1117D → N or T: No effect. 1 Publication1
Mutagenesisi1129D → E: Complete loss of nsp3-nsp4 and nsp5-nsp6 cleavages. 1 Publication1
Mutagenesisi1129D → K or V: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication1
Mutagenesisi1179T → G or S: Partial loss of nsp4-nsp5 cleavage. 1 Publication1
Mutagenesisi1179T → N: Increased nsp5-nsp6 cleavage. 1 Publication1
Mutagenesisi1184S → C, F, I or T: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication1
Mutagenesisi1198H → L, R or Y: Complete loss of nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication1
Mutagenesisi1268E → P: Complete loss of nsp3-nsp4 and nsp4-nsp5 cleavages. 2 Publications1
Mutagenesisi1430E → P: No effect. 1 Publication1
Mutagenesisi1677E → P: Complete loss of nsp5-nsp6 cleavage. 1 Publication1
Mutagenesisi2351D → P: No effect. 1 Publication1
Mutagenesisi2370E → P: Complete loss of nsp9-nsp10 cleavage. 1 Publication1
Mutagenesisi2429S → P: RNA can replicate efficiently but does not produce the subgenomic mRNAs required for structural protein expression. 1 Publication1
Mutagenesisi2534K → Q: Abolishes ATPase and helicase activity. 1 Publication1
Mutagenesisi2800E → P: No effect. 1 Publication1
Mutagenesisi2819D → P: No effect. 1 Publication1
Mutagenesisi2835E → D, P or Q: Almost complete loss of nsp9-nsp10 cleavage. 1 Publication1
Mutagenesisi2837Q → D or N: No effect. 1 Publication1
Mutagenesisi2837Q → E: Increased nsp9-nsp10 cleavage. 1 Publication1
Mutagenesisi2837Q → P: Almost complete loss of nsp9-nsp10 cleavage. 1 Publication1
Mutagenesisi3056E → P: Complete loss of nsp10-nsp11 cleavage. 1 Publication1

<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_00000366191 – 3175Replicase polyprotein 1abAdd BLAST3175
ChainiPRO_00000366211 – 260Nsp1 papain-like cysteine proteinaseAdd BLAST260
ChainiPRO_0000036622261 – 831Nsp2 cysteine proteinaseAdd BLAST571
ChainiPRO_0000036623832 – 1064Non-structural protein 3Add BLAST233
ChainiPRO_00000366241065 – 12683C-like serine proteinaseAdd BLAST204
ChainiPRO_00000366251269 – 1677Non-structural protein 5-6-7Add BLAST409
ChainiPRO_00004231061269 – 1430Non-structural protein 5Add BLAST162
ChainiPRO_00004231071431 – 1452Non-structural protein 6Add BLAST22
ChainiPRO_00004231081453 – 1575Non-structural protein 7-alphaAdd BLAST123
ChainiPRO_00004231091576 – 1677Non-structural protein 7-betaAdd BLAST102
ChainiPRO_00000366261678 – 2370RNA-directed RNA polymeraseAdd BLAST693
ChainiPRO_00000366271678 – 1727Non-structural protein 8Add BLAST50
ChainiPRO_00000366282371 – 2837HelicaseAdd BLAST467
ChainiPRO_00000366292838 – 3056Uridylate-specific endoribonuclease nsp11Add BLAST219
ChainiPRO_00000366303057 – 3175Non-structural protein 12Add BLAST119

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi1501N-linked (GlcNAc...) asparagine; by hostCurated1

<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. There are two alternative pathways for processing. Either nsp4-5 is cleaved, which represents the major pathway or the nsp5-6 and nsp6-7 are processed, which represents the minor pathway. The major pathway occurs when nsp2 acts as cofactor for nsp4.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei260 – 261Cleavage; by PCP2
Sitei831 – 832Cleavage; by Nsp2 cysteine proteinase2
Sitei1064 – 1065Cleavage; by 3CLSP2
Sitei1268 – 1269Cleavage; by 3CLSP; in major pathway2
Sitei1430 – 1431Cleavage; by 3CLSP; in minor pathway2
Sitei1452 – 1453Cleavage; by 3CLSP; in minor pathway2
Sitei1575 – 1576Cleavage; by 3CLSP2
Sitei1677 – 1678Cleavage; by 3CLSP2
Sitei2370 – 2371Cleavage; by 3CLSP2
Sitei2837 – 2838Cleavage; by 3CLSP2
Sitei3056 – 3057Cleavage; by 3CLSP2

Keywords - PTMi

Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P19811

<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

Nsp1 interacts with cellular transcription cofactor SND1/p100.

1 Publication

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

<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

13175
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P19811

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

More...SMRi		P19811

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		P19811

<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>Domaini66 – 156Peptidase C31PROSITE-ProRule annotationAdd BLAST91
Domaini157 – 260Peptidase C32PROSITE-ProRule annotationAdd BLAST104
Domaini261 – 360Peptidase C33PROSITE-ProRule annotationAdd BLAST100
Domaini1065 – 1268Peptidase S32PROSITE-ProRule annotationAdd BLAST204
Domaini1716 – 1883NiRANPROSITE-ProRule annotationAdd BLAST168
Domaini2116 – 2251RdRp catalyticPROSITE-ProRule annotationAdd BLAST136
Domaini2371 – 2438AV ZBDPROSITE-ProRule annotationAdd BLAST68
Domaini2496 – 2661(+)RNA virus helicase ATP-bindingAdd BLAST166
Domaini2662 – 2793(+)RNA virus helicase C-terminalAdd BLAST132
Domaini2840 – 2930AV-Nsp11N/CoV-Nsp15MPROSITE-ProRule annotationAdd BLAST91
Domaini2932 – 3054NendoUPROSITE-ProRule annotationAdd BLAST123

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>Regioni261 – 339OTU-likeAdd BLAST79
Regioni386 – 451DisorderedSequence analysisAdd BLAST66
Regioni530 – 645HD1Add BLAST116
Regioni829 – 997HD2Add BLAST169
Regioni1291 – 1405HD3Add BLAST115
Regioni1577 – 1614DisorderedSequence analysisAdd BLAST38

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1593 – 1614Basic and acidic residuesSequence analysisAdd BLAST22

<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.
The OTU-like region is responsible for the deubiquitinating and deISGylation activities of Nsp2.Curated

<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

Belongs to the arteriviridae polyprotein family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri25 – 44C4-type; atypicalAdd BLAST20

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Conserved Domains Database

More...CDDi		cd21410, 1B_av_Nsp10-like, 1 hit
cd21160, NendoU_av_Nsp11-like, 1 hit
cd21166, NTD_av_Nsp11-like, 1 hit
cd21405, ZBD_av_Nsp10-like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.10.10, 2 hits
3.30.1330.220, 1 hit
3.30.40.20, 1 hit
3.30.70.270, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027351, (+)RNA_virus_helicase_core_dom
IPR031932, Arteri_nsp7a
IPR038451, Arteri_nsp7a_sf
IPR008743, Arterivirus_Nsp2_C33
IPR023338, Arterivirus_NSP4_peptidase
IPR008741, AV_PCPalpha
IPR025773, AV_PCPbeta
IPR023183, Chymotrypsin-like_C
IPR043502, DNA/RNA_pol_sf
IPR022230, DUF3756
IPR029323, EAV_nsp1
IPR008760, EAV_peptidase_S32
IPR037227, EndoU-like
IPR043609, NendoU_nidovirus
IPR044863, NIRAN
IPR044348, NSP10_1B_Av
IPR027355, NSP10_Av_ZBD
IPR044320, NSP11_Av_N
IPR044314, NSP11_NendoU_Av
IPR032786, NSP2_TM_arteriviridae
IPR027417, P-loop_NTPase
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR041053, Rep_1B
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR001205, RNA-dir_pol_C
IPR007094, RNA-dir_pol_PSvirus
IPR041361, Znf-RING_13

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16749, Arteri_nsp7a, 1 hit
PF19215, CoV_NSP15_C, 1 hit
PF12581, DUF3756, 1 hit
PF14754, IFR3_antag, 1 hit
PF14755, Nsp2_AV, 1 hit
PF05412, Peptidase_C33, 1 hit
PF05579, Peptidase_S32, 1 hit
PF00680, RdRP_1, 1 hit
PF17873, Rep_1B, 1 hit
PF01443, Viral_helicase1, 1 hit
PF17977, zf-RING_13, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF142877, SSF142877, 1 hit
SSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51538, AV_CP, 1 hit
PS51961, AV_NSP11N_COV_NSP15M, 1 hit
PS51493, AV_NSP4_PRO, 1 hit
PS51539, AV_PCP_ALPHA, 1 hit
PS51540, AV_PCP_BETA, 1 hit
PS51652, AV_ZBD, 1 hit
PS51958, NENDOU, 1 hit
PS51947, NIRAN, 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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by ribosomal frameshifting. AlignAdd to basket
Isoform Replicase polyprotein 1ab (identifier: P19811-1) [UniParc]FASTAAdd to basket
Also known as: pp1ab

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><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
MATFSATGFG GSFVRDWSLD LPDACEHGAG LCCEVDGSTL CAECFRGCEG 
        60         70         80         90        100
MEQCPGLFMG LLKLASPVPV GHKFLIGWYR AAKVTGRYNF LELLQHPAFA 
       110        120        130        140        150
QLRVVDARLA IEEASVFIST DHASAKRFPG ARFALTPVYA NAWVVSPAAN 
       160        170        180        190        200
SLIVTTDQEQ DGFCWLKLLP PDRREAGLRL YYNHYREQRT GWLSKTGLRL 
       210        220        230        240        250
WLGDLGLGIN ASSGGLKFHI MRGSPQRAWH ITTRSCKLKS YYVCDISEAD 
       260        270        280        290        300
WSCLPAGNYG GYNPPGDGAC GYRCLAFMNG ATVVSAGCSS DLWCDDELAY 
       310        320        330        340        350
RVFQLSPTFT VTIPGGRVCP NAKYAMICDK QHWRVKRAKG VGLCLDESCF 
       360        370        380        390        400
RGICNCQRMS GPPPAPVSAA VLDHILEAAT FGNVRVVTPE GQPRPVPAPR 
       410        420        430        440        450
VRPSANSSGD VKDPAPVPPV PKPRTKLATP NPTQAPIPAP RTRLQGASTQ 
       460        470        480        490        500
EPLASAGVAS DSAPKWRVAK TVYSSAERFR TELVQRARSV GDVLVQALPL 
       510        520        530        540        550
KTPAVQRYTM TLKMMRSRFS WHCDVWYPLA VIACLLPIWP SLALLLSFAI 
       560        570        580        590        600
GLIPSVGNNV VLTALLVSSA NYVASMDHQC EGAACLALLE EEHYYRAVRW 
       610        620        630        640        650
RPITGALSLV LNLLGQVGYV ARSTFDAAYV PCTVFDLCSF AILYLCRNRC 
       660        670        680        690        700
WRCFGRCVRV GPATHVLGST GQRVSKLALI DLCDHFSKPT IDVVGMATGW 
       710        720        730        740        750
SGCYTGTAAM ERQCASTVDP HSFDQKKAGA TVYLTPPVNS GSALQCLNVM 
       760        770        780        790        800
WKRPIGSTVL GEQTGAVVTA VKSISFSPPC CVSTTLPTRP GVTVVDHALY 
       810        820        830        840        850
NRLTASGVDP ALLRVGQGDF LKLNPGFRLI GGWIYGICYF VLVVVSTFTC 
       860        870        880        890        900
LPIKCGIGTR DPFCRRVFSV PVTKTQEHCH AGMCASAEGI SLDSLGLTQL 
       910        920        930        940        950
QSYWIAAVTS GLVILLVCHR LAISALDLLT LASPLVLLVF PWASVGLLLA 
       960        970        980        990       1000
CSLAGAAVKI QLLATLFVNL FFPQATLVTM GYWACVAALA VYSLMGLRVK 
      1010       1020       1030       1040       1050
VNVPMCVTPA HFLLLARSAG QSREQMLRVS AAAPTNSLLG VARDCYVTGT 
      1060       1070       1080       1090       1100
TRLYIPKEGG MVFEGLFRSP KARGNVGFVA GSSYGTGSVW TRNNEVVVLT 
      1110       1120       1130       1140       1150
ASHVVGRANM ATLKIGDAML TLTFKKNGDF AEAVTTQSEL PGNWPQLHFA 
      1160       1170       1180       1190       1200
QPTTGPASWC TATGDEEGLL SGEVCLAWTT SGDSGSAVVQ GDAVVGVHTG 
      1210       1220       1230       1240       1250
SNTSGVAYVT TPSGKLLGAD TVTLSSLSKH FTGPLTSIPK DIPDNIIADV 
      1260       1270       1280       1290       1300
DAVPRSLAML IDGLSNRESS LSGPQLLLIA CFMWSYLNQP AYLPYVLGFF 
      1310       1320       1330       1340       1350
AANFFLPKSV GRPVVTGLLW LCCLFTPLSM RLCLFHLVCA TVTGNVISLW 
      1360       1370       1380       1390       1400
FYITAAGTSY LSEMWFGGYP TMLFVPRFLV YQFPGWAIGT VLAVCSITML 
      1410       1420       1430       1440       1450
AAALGHTLLL DVFSASGRFD RTFMMKYFLE GGVKESVTAS VTRAYGKPIT 
      1460       1470       1480       1490       1500
QESLTATLAA LTDDDFQFLS DVLDCRAVRS AMNLRAALTS FQVAQYRNIL 
      1510       1520       1530       1540       1550
NASLQVDRDA ARSRRLMAKL ADFAVEQEVT AGDRVVVIDG LDRMAHFKDD 
      1560       1570       1580       1590       1600
LVLVPLTTKV VGGSRCTICD VVKEEANDTP VKPMPSRRRR KGLPKGAQLE 
      1610       1620       1630       1640       1650
WDRHQEEKRN AGDDDFAVSN DYVKRVPKYW DPSDTRGTTV KIAGTTYQKV 
      1660       1670       1680       1690       1700
VDYSGNVHYV EHQEDLLDYV LGKGSYEGLD QDKVLDLTNM LKVDPTELSS 
      1710       1720       1730       1740       1750
KDKAKARQLA HLLLDLANPV EAVNQLNLRA PHIFPGDVGR RTFADSKDKG 
      1760       1770       1780       1790       1800
FVALHSRTMF LAARDFLFNI KFVCDEEFTK TPKDTLLGYV RACPGYWFIF 
      1810       1820       1830       1840       1850
RRTHRSLIDA YWDSMECVYA LPTISDFDVS PGDVAVTGER WDFESPGGGR 
      1860       1870       1880       1890       1900
AKRLTADLVH AFQGFHGASY SYDDKVAAAV SGDPYRSDGV LYNTRWGNIP 
      1910       1920       1930       1940       1950
YSVPTNALEA TACYRAGCEA VTDGTNVIAT IGPFPEQQPI PDIPKSVLDN 
      1960       1970       1980       1990       2000
CADISCDAFI APAAETALCG DLEKYNLSTQ GFVLPSVFSM VRAYLKEEIG 
      2010       2020       2030       2040       2050
DAPPLYLPST VPSKNSQAGI NGAEFPTKSL QSYCLIDDMV SQSMKSNLQT 
      2060       2070       2080       2090       2100
ATMATCKRQY CSKYKIRSIL GTNNYIGLGL RACLSGVTAA FQKAGKDGSP 
      2110       2120       2130       2140       2150
IYLGKSKFDP IPAPDKYCLE TDLESCDRST PALVRWFATN LIFELAGQPE 
      2160       2170       2180       2190       2200
LVHSYVLNCC HDLVVAGSVA FTKRGGLSSG DPITSISNTI YSLVLYTQHM 
      2210       2220       2230       2240       2250
LLCGLEGYFP EIAEKYLDGS LELRDMFKYV RVYIYSDDVV LTTPNQHYAA 
      2260       2270       2280       2290       2300
SFDRWVPHLQ ALLGFKVDPK KTVNTSSPSF LGCRFKQVDG KCYLASLQDR 
      2310       2320       2330       2340       2350
VTRSLLYHIG AKNPSEYYEA AVSIFKDSII CCDEDWWTDL HRRISGAART 
      2360       2370       2380       2390       2400
DGVEFPTIEM LTSFRTKQYE SAVCTVCGAA PVAKSACGGW FCGNCVPYHA 
      2410       2420       2430       2440       2450
GHCHTTSLFA NCGHDIMYRS TYCTMCEGSP KQMVPKVPHP ILDHLLCHID 
      2460       2470       2480       2490       2500
YGSKEELTLV VADGRTTSPP GRYKVGHKVV AVVADVGGNI VFGCGPGSHI 
      2510       2520       2530       2540       2550
AVPLQDTLKG VVVNKALKNA AASEYVEGPP GSGKTFHLVK DVLAVVGSAT 
      2560       2570       2580       2590       2600
LVVPTHASML DCINKLKQAG ADPYFVVPKY TVLDFPRPGS GNITVRLPQV 
      2610       2620       2630       2640       2650
GTSEGETFVD EVAYFSPVDL ARILTQGRVK GYGDLNQLGC VGPASVPRNL 
      2660       2670       2680       2690       2700
WLRHFVSLEP LRVCHRFGAA VCDLIKGIYP YYEPAPHTTK VVFVPNPDFE 
      2710       2720       2730       2740       2750
KGVVITAYHK DRGLGHRTID SIQGCTFPVV TLRLPTPQSL TRPRAVVAVT 
      2760       2770       2780       2790       2800
RASQELYIYD PFDQLSGLLK FTKEAEAQDL IHGPPTACHL GQEIDLWSNE 
      2810       2820       2830       2840       2850
GLEYYKEVNL LYTHVPIKDG VIHSYPNCGP ACGWEKQSNK ISCLPRVAQN 
      2860       2870       2880       2890       2900
LGYHYSPDLP GFCPIPKELA EHWPVVSNDR YPNCLQITLQ QVCELSKPCS 
      2910       2920       2930       2940       2950
AGYMVGQSVF VQTPGVTSYW LTEWVDGKAR ALPDSLFSSG RFETNSRAFL 
      2960       2970       2980       2990       3000
DEAEEKFAAA HPHACLGEIN KSTVGGSHFI FSQYLPPLLP ADAVALVGAS 
      3010       3020       3030       3040       3050
LAGKAAKAAC SVVDVYAPSF EPYLHPETLS RVYKIMIDFK PCRLMVWRNA 
      3060       3070       3080       3090       3100
TFYVQEGVDA VTSALAAVSK LIKVPANEPV SFHVASGYRT NALVAPQAKI 
      3110       3120       3130       3140       3150
SIGAYAAEWA LSTEPPPAGY AIVRRYIVKR LLSSTEVFLC RRGVVSSTSV 
      3160       3170 
QTICALEGCK PLFNFLQIGS VIGPV
Note: Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.
Length:3,175
Mass (Da):345,384
Last modified:April 13, 2004 - v3
<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:iCB536C1F5091045C
GO
Isoform Replicase polyprotein 1a (identifier: P19811-2) [UniParc]FASTAAdd to basket
Also known as: pp1a, ORF1a polyprotein

The sequence of this isoform differs from the canonical sequence as follows:
     1728-3175: Missing.

Note: Produced by conventional translation.Curated
Show »
Length:1,727
Mass (Da):186,992
Checksum:iFB0DB046FA0C74F6
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0328871728 – 3175Missing in isoform Replicase polyprotein 1a. CuratedAdd BLAST1448

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
X53459 Genomic RNA Translation: CAC42774.2
X53459 Genomic RNA Translation: CAC42775.2
X52277 Genomic RNA Translation: CAA36520.1

Protein sequence database of the Protein Information Resource

More...PIRi		A39925, RRWVEV

NCBI Reference Sequences

More...RefSeqi		NP_127506.1, NC_002532.2
NP_127507.1, NC_002532.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		921339

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		vg:921339

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
X53459 Genomic RNA Translation: CAC42774.2
X53459 Genomic RNA Translation: CAC42775.2
X52277 Genomic RNA Translation: CAA36520.1
PIRiA39925, RRWVEV
RefSeqiNP_127506.1, NC_002532.2
NP_127507.1, NC_002532.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MBMX-ray2.00A/B/C/D1071-1268[»]
2L8KNMR-A1454-1575[»]
4IUMX-ray1.45A261-392[»]
4N0NX-ray2.00A2371-2772[»]
4N0OX-ray2.65A/C/E/G2371-2772[»]
5F17X-ray3.20A/B/C/D/E/F2838-3056[»]
5HBZX-ray3.10A/B/C/D/E/F2838-3056[»]
5HC1X-ray3.10A/B/C/D2838-3056[»]
BMRBiP19811
SMRiP19811
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiS32.001

Proteomic databases

PRIDEiP19811

Genome annotation databases

GeneIDi921339
KEGGivg:921339

Enzyme and pathway databases

BRENDAi3.4.21.114, 6985
3.4.22.B50, 6985

Miscellaneous databases

EvolutionaryTraceiP19811

Family and domain databases

CDDicd21410, 1B_av_Nsp10-like, 1 hit
cd21160, NendoU_av_Nsp11-like, 1 hit
cd21166, NTD_av_Nsp11-like, 1 hit
cd21405, ZBD_av_Nsp10-like, 1 hit
Gene3Di2.40.10.10, 2 hits
3.30.1330.220, 1 hit
3.30.40.20, 1 hit
3.30.70.270, 1 hit
InterProiView protein in InterPro
IPR027351, (+)RNA_virus_helicase_core_dom
IPR031932, Arteri_nsp7a
IPR038451, Arteri_nsp7a_sf
IPR008743, Arterivirus_Nsp2_C33
IPR023338, Arterivirus_NSP4_peptidase
IPR008741, AV_PCPalpha
IPR025773, AV_PCPbeta
IPR023183, Chymotrypsin-like_C
IPR043502, DNA/RNA_pol_sf
IPR022230, DUF3756
IPR029323, EAV_nsp1
IPR008760, EAV_peptidase_S32
IPR037227, EndoU-like
IPR043609, NendoU_nidovirus
IPR044863, NIRAN
IPR044348, NSP10_1B_Av
IPR027355, NSP10_Av_ZBD
IPR044320, NSP11_Av_N
IPR044314, NSP11_NendoU_Av
IPR032786, NSP2_TM_arteriviridae
IPR027417, P-loop_NTPase
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR041053, Rep_1B
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR001205, RNA-dir_pol_C
IPR007094, RNA-dir_pol_PSvirus
IPR041361, Znf-RING_13
PfamiView protein in Pfam
PF16749, Arteri_nsp7a, 1 hit
PF19215, CoV_NSP15_C, 1 hit
PF12581, DUF3756, 1 hit
PF14754, IFR3_antag, 1 hit
PF14755, Nsp2_AV, 1 hit
PF05412, Peptidase_C33, 1 hit
PF05579, Peptidase_S32, 1 hit
PF00680, RdRP_1, 1 hit
PF17873, Rep_1B, 1 hit
PF01443, Viral_helicase1, 1 hit
PF17977, zf-RING_13, 1 hit
SUPFAMiSSF142877, SSF142877, 1 hit
SSF50494, SSF50494, 1 hit
SSF52540, SSF52540, 1 hit
SSF56672, SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS51538, AV_CP, 1 hit
PS51961, AV_NSP11N_COV_NSP15M, 1 hit
PS51493, AV_NSP4_PRO, 1 hit
PS51539, AV_PCP_ALPHA, 1 hit
PS51540, AV_PCP_BETA, 1 hit
PS51652, AV_ZBD, 1 hit
PS51958, NENDOU, 1 hit
PS51947, NIRAN, 1 hit
PS51657, PSRV_HELICASE, 1 hit
PS50507, RDRP_SSRNA_POS, 1 hit

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 nameiRPOA_EAVBU
<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: P19811
Secondary accession number(s): Q88625, Q8QZQ5, Q91DM2
<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: February 1, 1991
Last sequence update: April 13, 2004
Last modified: February 23, 2022
This is version 176 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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