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Entry version 148 (18 Sep 2019)
Sequence version 2 (10 Apr 2019)
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Protein

Polyprotein P1234

Gene
N/A
Organism
Venezuelan equine encephalitis virus (strain P676) (VEEV)
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

Polyprotein P1234: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.By similarity
Polyprotein P123: The early replication complex formed by the polyprotein P123 and nsP4 synthesizes the minus-strand RNAs (antigenome) (By similarity). Polyprotein P123 is a short-lived polyprotein that accumulates during early stage of infection (Probable). As soon P123 is cleaved into mature proteins, the plus-strand RNAs synthesis begins (By similarity).By similarityCurated
Polyprotein P123': The early replication complex formed by the polyprotein P123' and nsP4 synthesizes minus-strand RNAs (antigenome) (Probable). Polyprotein P123' is a short-lived polyprotein that accumulates during early stage of infection (Probable). As soon P123' is cleaved into mature proteins, the plus-strand RNAs synthesis begins (Probable).Curated
mRNA-capping enzyme nsP1: Cytoplasmic capping enzyme that catalyzes two virus-specific reactions: methyltransferase and nsP1 guanylyltransferase (PubMed:26041283). mRNA-capping is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP (Probable). NsP1 capping consists in the following reactions: GTP is first methylated into 7-methyl-GMP and then is covalently linked to nsP1 to form the m7GMp-nsP1 complex from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure (PubMed:26041283). NsP1 is also needed for the initiation of the minus-strand RNAs synthesis (By similarity). Probably serves as a membrane anchor for the replication complex composed of nsP1-nsP4 (By similarity). Nsp1 is needed for the initiation of the minus-strand RNAs synthesis (By similarity). Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell (By similarity).By similarityCurated1 Publication
Protease nsP2: Multifunctional protein whose N-terminus is part of the RNA polymerase complex and displays NTPase, RNA triphosphatase and helicase activities (By similarity). NTPase and RNA triphosphatase are involved in viral RNA capping and helicase keeps a check on the dsRNA replication intermediates (By similarity). The C-terminus harbors a protease that specifically cleaves the polyproteins and releases the mature proteins (By similarity). Required for the shutoff of minus-strand RNAs synthesis (By similarity). Inhibits host translation to ensure maximal viral gene expression and evade host immune response (By similarity).By similarity
Non-structural protein 3: Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (By similarity). Displays mono-ADP-ribosylhydrolase activity (By similarity). ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (By similarity). Binds proteins of FXR family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (By similarity). The nsp3-FXR complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of FXR family members to self-assemble and bind DNA (By similarity).By similarity
Non-structural protein 3': Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (By similarity). Displays mono-ADP-ribosylhydrolase activity (Probable). ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (Probable). Binds proteins of FXR family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (Probable). The nsp3'-FXR complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of FXR family members to self-assemble and bind DNA (Probable).By similarityCurated
RNA-directed RNA polymerase nsP4: RNA dependent RNA polymerase (By similarity). Replicates genomic and antigenomic RNA by recognizing replications specific signals. The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (By similarity). The late replication complex composed of fully processed nsP1-nsP4 is responsible for the production of genomic and subgenomic plus-strand RNAs (By similarity).By similarity

Miscellaneous

Viral replication produces dsRNA in the late phase of infection, resulting in a strong activation of host EIF2AK2/PKR, leading to almost complete phosphorylation of EIF2A (By similarity). This inactivates completely cellular translation initiation, resulting shutoff of host proteins synthesis (By similarity). However, phosphorylation of EIF2A is probably not the only mechanism responsible for the host translation shutoff (By similarity). The viral translation can still occur normally because it relies on a hairpin structure in the coding region of sgRNA and is EIF2A-, EIF2D-, EIF4G- EIF4A-independent (By similarity).By similarity
Polyprotein P1234: The genome codes for P123, but readthrough of a terminator codon UGA occurs between the codons for Gln-1879 and Arg-1881 giving rise to P1234 (By similarity). P1234 is cleaved quickly by nsP2 into P123' and nsP4 (By similarity). Further processing of p123' gives nsP1, nsP2 and nsP3' which is 6 amino acids longer than nsP3 since the cleavage site is after the readthrough (By similarity). This unusual molecular mechanism ensures that few nsP4 are produced compared to other non-structural proteins (By similarity). Mutant viruses with no alternative termination site grow significantly slower than wild-type virus (By similarity). The opal termination codon is frequently mutated to a sense codon on passage in cell culture (By similarity). The presence of the opal codon may be a requirement for viral maintenance in both vertebrate and invertebrate hosts and a selective advantage may be conferred in cell culture for the sense codon (By similarity).By similarity

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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

mRNA-capping enzyme nsP1: Inhibited by sinefungin.1 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>Sitei37Involved in the phosphoramide link with 7-methyl-GMPBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei1012For cysteine protease nsP2 activityPROSITE-ProRule annotation1
Active sitei1081For cysteine protease nsP2 activityPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1339ADP-ribose1 Publication1
Binding sitei1353ADP-riboseBy similarity1
Binding sitei1361ADP-riboseBy similarity1
Binding sitei1441ADP-ribose1 Publication1
Binding sitei1442ADP-ribose1 Publication1
Binding sitei1443ADP-ribose1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi1596ZincBy similarity1
Metal bindingi1598ZincBy similarity1
Metal bindingi1621ZincBy similarity1
Metal bindingi1639ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi721 – 728NTPPROSITE-ProRule annotation8

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

GO - Biological processi

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

Molecular functionHelicase, Hydrolase, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase
Biological processEukaryotic host gene expression shutoff by virus, Eukaryotic host transcription shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Inhibition of host RNA polymerase II by virus, mRNA capping, mRNA processing, Viral RNA replication
LigandATP-binding, GTP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:
Polyprotein P1234
Short name:
P1234
Alternative name(s):
Non-structural polyprotein
Cleaved into the following 7 chains:
Polyprotein P123'
Short name:
P123'
Polyprotein P123
Short name:
P123
mRNA-capping enzyme nsP1 (EC:2.1.1.-1 Publication, EC:2.7.7.-1 Publication)
Alternative name(s):
Non-structural protein 1
Protease nsP2 (EC:3.1.3.33By similarity, EC:3.4.22.-By similarity, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity)
Alternative name(s):
Non-structural protein 2
Short name:
nsP2
Non-structural protein 3' (EC:3.1.3.84By similarity)
Short name:
nsP3'
Non-structural protein 3 (EC:3.1.3.84By similarity)
Short name:
nsP3
RNA-directed RNA polymerase nsP4 (EC:2.7.7.19By similarity, EC:2.7.7.48PROSITE-ProRule annotation)
Alternative name(s):
Non-structural protein 4
Short name:
nsP4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiVenezuelan equine encephalitis virus (strain P676) (VEEV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri36385 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiVirusesRiboviriaTogaviridaeAlphavirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 hostiBos taurus (Bovine) [TaxID: 9913]
Didelphis marsupialis (Southern opossum) [TaxID: 9268]
Equus asinus (Donkey) (Equus africanus asinus) [TaxID: 9793]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Melanoconion [TaxID: 53535]
Philander opossum (Gray four-eyed opossum) [TaxID: 9272]
Proechimys [TaxID: 10162]
Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000166022 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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
  • UP000143596 Componenti: Genome
  • UP000171441 Componenti: Genome
  • UP000125491 Componenti: Genome
  • UP000110878 Componenti: Genome
  • UP000173580 Componenti: Genome
  • UP000008658 Componenti: Genome
  • UP000180662 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

Polyprotein P1234 :
Polyprotein P123' :
Polyprotein P123 :
mRNA-capping enzyme nsP1 :
Protease nsP2 :
Non-structural protein 3 :
  • Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein Curated
  • Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' form aggregates in cytoplasm (By similarity). NsP3 is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity
Non-structural protein 3' :
  • Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated
  • Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' form aggregates in cytoplasm (By similarity). NsP3' is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (Probable).By similarityCurated
RNA-directed RNA polymerase nsP4 :

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host cell projection, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003083901 – 2492Polyprotein P1234Add BLAST2492
ChainiPRO_00002287671 – 1886Polyprotein P123'Add BLAST1886
ChainiPRO_00002287681 – 1879Polyprotein P123Add BLAST1879
ChainiPRO_00000412041 – 535mRNA-capping enzyme nsP1Add BLAST535
ChainiPRO_0000041205536 – 1329Protease nsP2Add BLAST794
ChainiPRO_00002287691330 – 1886Non-structural protein 3'Add BLAST557
ChainiPRO_00000412061330 – 1879Non-structural protein 3Add BLAST550
ChainiPRO_00000412071887 – 2493RNA-directed RNA polymerase nsP4Add BLAST607

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi419S-palmitoyl cysteine; by hostBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Polyprotein P1234: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123' and nsP4, which associate to form the early replication complex (By similarity). At the same time, P1234 is also cut at the nsP1/nsP2 site early in infection but with lower efficiency (By similarity). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123' and P1234 and allowing the formation of the late replication complex (By similarity). NsP3'/nsP4 site is not cleaved anymore and P34 is produced rather than nsP4 (By similarity).By similarity
Polyprotein P123: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P123 is cleaved at the nsP1/nsP2 site with low efficiency (By similarity). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123 and allowing the formation of the late replication complex (By similarity).By similarity
Polyprotein P123': Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P123' is cleaved at the nsP1/nsP2 site with low efficiency (By similarity). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123' and allowing the formation of the late replication complex (By similarity).By similarity
mRNA-capping enzyme nsP1: Palmitoylated by host palmitoyltransferases ZDHHC2 and ZDHHC19.By similarity
Non-structural protein 3: Phosphorylated by host on serines and threonines.By similarity
Non-structural protein 3': Phosphorylated by host on serines and threonines.By similarity
RNA-directed RNA polymerase nsP4: ubiquitinated; targets the protein for rapid degradation via the ubiquitin system (By similarity). Nsp4 is present in extremely low quantities due to low frequency of translation through the amber stop-codon and the degradation by the ubiquitin pathway (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei535 – 536Cleavage; by protease nsP2By similarity2
Sitei1329 – 1330Cleavage; by protease nsP2By similarity2
Sitei1886 – 1887Cleavage; by protease nsP2By similarity2

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P36328

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

mRNA-capping enzyme nsP1:

Interacts with non-structural protein 3 (By similarity). Non-structural protein 3:

Interacts with mRNA-capping enzyme nsP1 (By similarity). mRNA-capping enzyme nsP1:

Interacts with RNA-directed RNA polymerase nsP4 (By similarity). RNA-directed RNA polymerase nsP4:

Interacts with mRNA-capping enzyme nsP1 (By similarity). RNA-directed RNA polymerase nsP4:

Interacts with protease nsP2 (By similarity). Protease nsP2:

Interacts with RNA-directed RNA polymerase nsP4 (By similarity). mRNA-capping enzyme nsP1:

Interacts with protease nsP2 (By similarity). Protease nsP2:

Interacts with mRNA-capping enzyme nsP1 (By similarity). RNA-directed RNA polymerase nsP4 interacts with itself (By similarity). mRNA-capping enzyme nsP1 interacts with itself (By similarity). Protease nsP2:

Interacts with KPNA1/karyopherin-alpha1; this interaction probably allows the active transport of protease nsP2 into the host nucleus (By similarity). Non-structural protein 3:

Interacts with host DDX1 (By similarity). Non-structural protein 3:

Interacts with host DDX3 (By similarity). Non-structural protein 3:

Interacts (via C-terminus) with host FXR1; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-FXR1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (By similarity). Non-structural protein 3:

Interacts (via C-terminus) with host FXR2; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-FXR2 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (By similarity). Non-structural protein 3:

Interacts (via C-terminus) with host FMR1; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-FMR1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (By similarity).

By similarity

<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

12493
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

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SMRi
P36328

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P36328

<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_and_domains_section">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>Domaini28 – 259Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST232
Domaini690 – 841(+)RNA virus helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST152
Domaini842 – 990(+)RNA virus helicase C-terminalPROSITE-ProRule annotationAdd BLAST149
Domaini1003 – 1322Peptidase C9PROSITE-ProRule annotationAdd BLAST320
Domaini1330 – 1489MacroPROSITE-ProRule annotation1 PublicationAdd BLAST160
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati1818 – 18391By similarityAdd BLAST22
Repeati1852 – 18732By similarityAdd BLAST22
Domaini2250 – 2365RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

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>Regioni244 – 263NsP1 membrane-bindingBy similarityAdd BLAST20
Regioni1004 – 1023Nucleolus localization signalBy similarityAdd BLAST20
Regioni1818 – 18732 X 21 AA approximate repeats, binding to host FXR family membersBy similarityAdd BLAST56

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1056 – 1065Nuclear export signalBy similarity10
Motifi1179 – 1183Nuclear localization signalBy similarity5

<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

Protease nsP2: The N-terminus exhibits NTPase and RNA triphosphatase activities and is proposed to have helicase activity, whereas the C-terminus possesses protease activity (By similarity). Contains a nuclear localization signal and a nuclear export signal, these two motifs are probably involved in the shuttling between the cytoplasm and the nucleus of nsP2 (By similarity).By similarity
Non-structural protein 3': In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (By similarity). The central part has a zinc-binding function (By similarity). The C-terminus contains two approximate repeats necessary and sufficient for formation of the nsP3'/FXR complex (By similarity).By similarity
Non-structural protein 3: In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (By similarity). The central part has a zinc-binding function (By similarity). The C-terminus contains two approximate repeats necessary and sufficient for formation of the nsP3/FXR complex (By similarity).By similarity

Keywords - Domaini

Repeat

Phylogenomic databases

Database of Orthologous Groups

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OrthoDBi
VOG09000048

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR027351 (+)RNA_virus_helicase_core_dom
IPR002588 Alphavirus-like_MT_dom
IPR002620 Alphavirus_nsp2pro
IPR002589 Macro_dom
IPR027417 P-loop_NTPase
IPR007094 RNA-dir_pol_PSvirus
IPR001788 Tymovirus_RNA-dep_RNA_pol

Pfam protein domain database

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Pfami
View protein in Pfam
PF01661 Macro, 1 hit
PF01707 Peptidase_C9, 1 hit
PF00978 RdRP_2, 1 hit
PF01443 Viral_helicase1, 1 hit
PF01660 Vmethyltransf, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00506 A1pp, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51743 ALPHAVIRUS_MT, 1 hit
PS51154 MACRO, 1 hit
PS51520 NSP2PRO, 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_length">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P36328-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEKVHVDIEE DSPFLRALQR SFPQFEVEAK QVTDNDHANA RAFSHLASKL
60 70 80 90 100
IETEVDPSDT ILDIGSAPAR RMYSKHKYHC ICPMRCAEDP DRLYKYATKL
110 120 130 140 150
KKNCKEITDK ELDKKMKELA AVMSDPDLET ETMCLHDDES CRYEGQVAVY
160 170 180 190 200
QDVYAVDGPT SLYHQANKGV RVAYWIGFDT TPFMFKNLAG AYPSYSTNWA
210 220 230 240 250
DETVLTARNI GLCSSDVMER SRRGMSILRK KYLKPSNNVL FSVGSTIYHE
260 270 280 290 300
KRDLLRSWHL PSVFHLRGKQ NYTCRCETIV SCDGYVVKRI AISPGLYGKP
310 320 330 340 350
SGYAATMHRE GFLCCKVTDT LNGERVSFPV CTYVPATLCD QMTGILATDV
360 370 380 390 400
SADDAQKLLV GLNQRIVVNG RTQRNTNTMK NYLLPVVAQA FARWAKEYKE
410 420 430 440 450
DQEDERPLGL RDRQLVMGCC WAFRRHKITS IYKRPDTQTI IKVNSDFHSF
460 470 480 490 500
VLPRIGSNTL EIGLRTRIRK MLEEHKEPSP LITAEDIQEA KCAADEAKEV
510 520 530 540 550
REAEELRAAL PPLAADFEEP TLEADVDLML QEAGAGSVET PRGLIKVTSY
560 570 580 590 600
AGEDKIGSYA VLSPQAVLKS EKLSCIHPLA EQVIVITHSG RKGRYAVEPY
610 620 630 640 650
HGKVVVPEGH AIPVQDFQAL SESATIVYNE REFVNRYLHH IATHGGALNT
660 670 680 690 700
DEEYYKTVKP SEHDGEYLYD IDRKQCVKKE LVTGLGLTGE LVDPPFHEFA
710 720 730 740 750
YESLRTRPAA PYQVPTIGVY GVPGSGKSGI IKSAVTKKDL VVSAKKENCA
760 770 780 790 800
EIIRDVKKMK GLDVNARTVD SVLLNGCKHP VETLYIDEAF ACHAGTLRAL
810 820 830 840 850
IAIIRPKKAV LCGDPKQCGF FNMMCLKVHF NHEICTQVFH KSISRRCTKS
860 870 880 890 900
VTSVVSTLFY DKRMRTTNPK ETKIVIDTTG STKPKQDDLI LTCFRGWVKQ
910 920 930 940 950
LQIDYKGNEI MTAAASQGLT RKGVYAVRYK VNENPLYAPT SEHVNVLLTR
960 970 980 990 1000
TEDRIVWKTL AGDPWIKILT AKYPGNFTAT IEEWQAEHDA IMRHILERPD
1010 1020 1030 1040 1050
PTDVFQNKAN VCWAKALVPV LKTAGIDMTT EQWNTVDYFE TDKAHSAEIV
1060 1070 1080 1090 1100
LNQLCVRFFG LDLDSGLFSA PTVPLSIRNN HWDNSPSPNM YGLNKEVVRQ
1110 1120 1130 1140 1150
LSRRYPQLPR AVATGRVYDM NTGTLRNYDP RINLVPVNRR LPHALVLHHN
1160 1170 1180 1190 1200
EHPQSDFSSF VSKLKGRTVL VVGEKLSVPG KKVDWLSDQP EATFRARLDL
1210 1220 1230 1240 1250
GIPGDVPKYD IVFINVRTPY KYHHYQQCED HAIKLSMLTK KACLHLNPGG
1260 1270 1280 1290 1300
TCVSIGYGYA DRASESIIGA IARQFKFSRV CKPKSSHEET EVLFVFIGYD
1310 1320 1330 1340 1350
RKARTHNPYK LSSTLTNIYT GSRLHEAGCA PSYHVVRGDI ATATEGVIIN
1360 1370 1380 1390 1400
AANSKGQPGG GVCGALYKKF PESFDLQPIE VGKARLVKGA AKHIIHAVGP
1410 1420 1430 1440 1450
NFNKVSEVEG DKQLAEAYES IAKIVNDNNY KSVAIPLLST GIFSGNKDRL
1460 1470 1480 1490 1500
TQSLNHLLTA LDTTDADVAI YCRDKKWEMT LKEAVARREA VEEICISDDS
1510 1520 1530 1540 1550
SVTEPDAELV RVHPKSSLAG RKGYSTSDGK TFSYLEGTKF HQAAKDIAEI
1560 1570 1580 1590 1600
NAMWPVATEA NEQVCMYILG ESMSSIRSKC PVEESEASTP PSTLPCLCIH
1610 1620 1630 1640 1650
AMTPERVQRL KASRPEQITV CSSFPLPKYR ITGVQKIQCS QPILFSPKVP
1660 1670 1680 1690 1700
AYIHPRKYLV ETPPVEETPE SPAENQSTEG TPEQPALVNV DATRTRMPEP
1710 1720 1730 1740 1750
IIIEEEEEDS ISLLSDGPTH QVLQVEADIH GSPSVSSSSW SIPHASDFDV
1760 1770 1780 1790 1800
DSLSILDTLD GASVTSGAVS AETNSYFARS MEFRARPVPA PRTVFRNPPH
1810 1820 1830 1840 1850
PAPRTRTPPL AHSRASSRTS LVSTPPGVNR VITREELEAL TPSRAPSRSA
1860 1870 1880 1890 1900
SRTSLVSNPP GVNRVITREE FEAFVAQQQX RFDAGAYIFS SDTGQGHLQQ
1910 1920 1930 1940 1950
KSVRQTVLSE VVLERTELEI SYAPRLDQEK EELLRKKLQL NPTPANRSRY
1960 1970 1980 1990 2000
QSRRVENMKA ITARRILQGL GHYLKAEGKV ECYRTLHPVP LYSSSVNRAF
2010 2020 2030 2040 2050
SSPKVAVEAC NAMLKENFPT VASYCIIPEY DAYLDMVDGA SCCLDTASFC
2060 2070 2080 2090 2100
PAKLRSFPKK HSYLEPTIRS AVPSAIQNTL QNVLAAATKR NCNVTQMREL
2110 2120 2130 2140 2150
PVLDSAAFNV ECFKKYACNN EYWETFKENP IRLTEENVVN YITKLKGPKA
2160 2170 2180 2190 2200
AALFAKTHNL NMLQDIPMDR FVMDLKRDVK VTPGTKHTEE RPKVQVIQAA
2210 2220 2230 2240 2250
DPLATADLCG IHRELVRRLN AVLLPNIHTL FDMSAEDFDA IIAEHFQPGD
2260 2270 2280 2290 2300
CVLETDIASF DKSEDDAMAL TALMILEDLG VDAELLTLIE AAFGEISSIH
2310 2320 2330 2340 2350
LPTKTKFKFG AMMKSGMFLT LFVNTVINIV IASRVLRERL TGSPCAAFIG
2360 2370 2380 2390 2400
DDNIVKGVKS DKLMADRCAT WLNMEVKIID AVVGEKAPYF CGGFILCDSV
2410 2420 2430 2440 2450
TGTACRVADP LKRLFKLGKP LAVDDEHDDD RRRALHEEST RWNRVGILPE
2460 2470 2480 2490
LCKAVESRYE TVGTSIIVMA MTTLASSVKS FSYLRGAPIT LYG
Length:2,493
Mass (Da):277,950
Last modified:April 10, 2019 - v2
<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:i0B7E85A996197E63
GO

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 varianti875V → E in strain: 3908, 6119, 254934, PMCHo5 and V198. 1
Natural varianti968I → T in strain: 3908, 6119, 254934, PMCHo5 and V198. 1
Natural varianti1390 – 1391AA → VT in strain: 3908, 6119, 254934, PMCHo5 and V198. 2
Natural varianti1767 – 1769GAV → EAA in strain: PMCHo5 and V198. 3
Natural varianti1767G → E in strain: 3908, 6119 and 254934. 1
Natural varianti1809P → S in strain: V198. 1
Natural varianti2094V → I in strain: 254934. 1
Natural varianti2207D → Y in strain: 3908, 6119, 254934, PMCHo5 and V198. 1
Natural varianti2423V → A in strain: V198. 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
L04653 Genomic RNA Translation: AAC19318.1 Sequence problems.
L04653 Genomic RNA Translation: AAC19320.1
U55347 Genomic RNA Translation: AAM28637.1
AF375051 Genomic RNA Translation: AAK66989.1
U55350 Genomic RNA Translation: AAM28638.1
AY986475 Genomic RNA Translation: AAY16369.1
AY973944 Genomic RNA Translation: AAY16003.1
U55345 Genomic RNA Translation: AAM28636.1
U55342 Genomic RNA Translation: AAL61965.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A44213

NCBI Reference Sequences

More...
RefSeqi
NP_040822.1, NC_001449.1
NP_040823.1, NC_001449.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2652923
2652925

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:2652923

Keywords - Coding sequence diversityi

RNA suppression of termination

<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
L04653 Genomic RNA Translation: AAC19318.1 Sequence problems.
L04653 Genomic RNA Translation: AAC19320.1
U55347 Genomic RNA Translation: AAM28637.1
AF375051 Genomic RNA Translation: AAK66989.1
U55350 Genomic RNA Translation: AAM28638.1
AY986475 Genomic RNA Translation: AAY16369.1
AY973944 Genomic RNA Translation: AAY16003.1
U55345 Genomic RNA Translation: AAM28636.1
U55342 Genomic RNA Translation: AAL61965.1
PIRiA44213
RefSeqiNP_040822.1, NC_001449.1
NP_040823.1, NC_001449.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GQEX-ray2.30A/B1330-1489[»]
3GQOX-ray2.60A/B/C/D1330-1489[»]
5ISNNMR-A1330-1489[»]
5MQXNMR-A1330-1489[»]
SMRiP36328
ModBaseiSearch...

Proteomic databases

PRIDEiP36328

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2652923
2652925
KEGGivg:2652923

Phylogenomic databases

OrthoDBiVOG09000048

Miscellaneous databases

EvolutionaryTraceiP36328

Family and domain databases

InterProiView protein in InterPro
IPR027351 (+)RNA_virus_helicase_core_dom
IPR002588 Alphavirus-like_MT_dom
IPR002620 Alphavirus_nsp2pro
IPR002589 Macro_dom
IPR027417 P-loop_NTPase
IPR007094 RNA-dir_pol_PSvirus
IPR001788 Tymovirus_RNA-dep_RNA_pol
PfamiView protein in Pfam
PF01661 Macro, 1 hit
PF01707 Peptidase_C9, 1 hit
PF00978 RdRP_2, 1 hit
PF01443 Viral_helicase1, 1 hit
PF01660 Vmethyltransf, 1 hit
SMARTiView protein in SMART
SM00506 A1pp, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51743 ALPHAVIRUS_MT, 1 hit
PS51154 MACRO, 1 hit
PS51520 NSP2PRO, 1 hit
PS51657 PSRV_HELICASE, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLN_EEVVP
<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: P36328
Secondary accession number(s): Q52QW0
, Q8JJT2, Q8QKW7, Q8UYL4, Q911J8, Q91KW9
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: April 10, 2019
Last modified: September 18, 2019
This is version 148 of the entry and version 2 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, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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