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Entry version 103 (11 Dec 2019)
Sequence version 1 (21 Dec 2004)
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Protein

Polyamine aminopropyltransferase

Gene

speE

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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

Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to agmatine to yield N1-aminopropylagmatine. An efficient aminopropyltransferase activity has been also observed with norspermidine which produces thermine, and spermidine which produces spermine and thermospermine. The aminopropyl activity with homospermidine, mitsubishine, thermine, 1,3-diaminopropane, putrescine (1,4-diaminobutane), spermine and caldopentamine are very low. The reaction involves a nucleophilic attack on the C-3 methylene of the propylamine moiety adjacent to the positively charged sulfur of decarboxy-AdoMet.2 Publications

Miscellaneous

In T.thermophilus, the biosynthetic pathways of spermidine operates via N1-aminopropylagmatine without the production of putrescine.1 Publication

<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 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

Kcat is 0.73 sec(-1) for aminopropyl transferase activity with S-adenosylmethioninamine as substrate (at pH 9 and 37 degrees Celsius). Kcat is 0.65 sec(-1) for aminopropyl transferase activity with spermidine as substrate (at pH 9 and 37 degrees Celsius). Kcat is 0.53 sec(-1) for aminopropyl transferase activity with norspermidine as substrate (at pH 9 and 37 degrees Celsius). Kcat is 0.37 sec(-1) for aminopropyl transferase activity with agmatine as substrate (at pH 9 and 37 degrees Celsius). Kcat is 0.29 sec(-1) for aminopropyl transferase activity with mitsubishine as substrate (at pH 9 and 37 degrees Celsius).1 Publication
  1. KM=0.57 µM for norspermidine (at pH 9 and 37 degrees Celsius)1 Publication
  2. KM=0.77 µM for agmatine (at pH 9 and 37 degrees Celsius)1 Publication
  3. KM=1.64 µM for S-adenosylmethioninamine (at pH 9 and 37 degrees Celsius)1 Publication
  4. KM=1.73 µM for spermidine (at pH 9 and 37 degrees Celsius)1 Publication
  5. KM=38.3 µM for mitsubishine (at pH 9 and 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 8.5 at 60 degrees Celsius.1 Publication

    Temperature dependencei

    Optimum temperature is above 80 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei9PolyamineUniRule annotation1
    Binding sitei33S-adenosylmethioninamineUniRule annotation1
    Binding sitei64PolyamineUniRule annotation1
    Binding sitei88PolyamineUniRule annotation1
    Binding sitei108S-adenosylmethioninamine1 Publication1
    <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 sitei158Proton acceptorUniRule annotation1
    Binding sitei168S-adenosylmethioninamine; via carbonyl oxygenUniRule annotation1

    <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 functionTransferase
    Biological processPolyamine biosynthesis

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-16736
    TTHE300852:G1GKC-842-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.5.1.104 2305

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q5SK28

    <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:
    Polyamine aminopropyltransferase1 PublicationUniRule annotation
    Alternative name(s):
    Agmatine aminopropyltransferase1 Publication (EC:2.5.1.1041 Publication)
    N1-aminopropylagmatine synthase1 Publication
    Norspermidine aminopropyltransferase1 Publication (EC:2.5.1.1261 Publication)
    Spermidine aminopropyltransferase1 Publication (EC:2.5.1.791 Publication)
    Spermine synthase1 Publication (EC:2.5.1.221 Publication)
    Thermine synthase1 Publication
    Thermospermine synthase1 Publication
    Triamine/agmatine aminopropyltransferase1 Publication
    Short name:
    TAAPT1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:speEUniRule annotation
    Ordered Locus Names:TTHA0824
    <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>OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    <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 identifieri300852 [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 lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    <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
    • UP000000532 <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: Chromosome

    <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

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking both speB and speE genes show defective growth at 70 degrees Celsius and significantly defective growth at 78 degrees Celsius. They accumulate agmatine and N1-aminopropylagmatine.1 Publication

    <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_10000120281 – 314Polyamine aminopropyltransferaseAdd BLAST314

    <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

    Homotetramer.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    300852.55772206

    <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

    1314
    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
    Q5SK28

    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
    Q5SK28

    <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>Domaini4 – 241PABSUniRule annotationAdd BLAST238

    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>Regioni53 – 54Polyamine bindingUniRule annotation2
    Regioni140 – 141S-adenosylmethioninamine binding1 Publication2

    <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 spermidine/spermine synthase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CCX Bacteria
    COG0421 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000256146

    KEGG Orthology (KO)

    More...
    KOi
    K00797

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    SDMWPGQ

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q5SK28

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.30.140.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00198 Spermidine_synth, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR030374 PABS
    IPR030373 PABS_CS
    IPR029063 SAM-dependent_MTases
    IPR001045 Spermi_synthase
    IPR035246 Spermidine_synt_N
    IPR037163 Spermidine_synt_N_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF17284 Spermine_synt_N, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53335 SSF53335, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01330 PABS_1, 1 hit
    PS51006 PABS_2, 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.

    Q5SK28-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MDYGMYFFEH VTPYETLVRR MERVIASGKT PFQDYFLFES KGFGKVLILD
    60 70 80 90 100
    KDVQSTERDE YIYHETLVHP AMLTHPEPKR VLIVGGGEGA TLREVLKHPT
    110 120 130 140 150
    VEKAVMVDID GELVEVAKRH MPEWHQGAFD DPRAVLVIDD ARAYLERTEE
    160 170 180 190 200
    RYDVVIIDLT DPVGEDNPAR LLYTVEFYRL VKAHLNPGGV MGMQAGMILL
    210 220 230 240 250
    THHRVHPVVH RTVREAFRYV RSYKNHIPGF FLNFGFLLAS DAFDPAAFSE
    260 270 280 290 300
    GVIEARIRER NLALRHLTAP YLEAMFVLPK DLLEALEKET MVSTDQNPFY
    310
    VTPEGEARQA PYKG
    Length:314
    Mass (Da):36,006
    Last modified:December 21, 2004 - 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:i4B6E438CFE60552A
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AP008226 Genomic DNA Translation: BAD70647.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011172918.1, NC_006461.1
    YP_144090.1, NC_006461.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAD70647; BAD70647; BAD70647

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    3168303

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ttj:TTHA0824

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|300852.9.peg.818

    <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
    AP008226 Genomic DNA Translation: BAD70647.1
    RefSeqiWP_011172918.1, NC_006461.1
    YP_144090.1, NC_006461.1

    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
    1UIRX-ray2.00A/B1-314[»]
    3ANXX-ray2.50A/B1-314[»]
    SMRiQ5SK28
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi300852.55772206

    Genome annotation databases

    EnsemblBacteriaiBAD70647; BAD70647; BAD70647
    GeneIDi3168303
    KEGGittj:TTHA0824
    PATRICifig|300852.9.peg.818

    Phylogenomic databases

    eggNOGiENOG4105CCX Bacteria
    COG0421 LUCA
    HOGENOMiHOG000256146
    KOiK00797
    OMAiSDMWPGQ
    PhylomeDBiQ5SK28

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16736
    TTHE300852:G1GKC-842-MONOMER
    BRENDAi2.5.1.104 2305
    SABIO-RKiQ5SK28

    Miscellaneous databases

    EvolutionaryTraceiQ5SK28

    Family and domain databases

    Gene3Di2.30.140.10, 1 hit
    HAMAPiMF_00198 Spermidine_synth, 1 hit
    InterProiView protein in InterPro
    IPR030374 PABS
    IPR030373 PABS_CS
    IPR029063 SAM-dependent_MTases
    IPR001045 Spermi_synthase
    IPR035246 Spermidine_synt_N
    IPR037163 Spermidine_synt_N_sf
    PfamiView protein in Pfam
    PF17284 Spermine_synt_N, 1 hit
    SUPFAMiSSF53335 SSF53335, 1 hit
    PROSITEiView protein in PROSITE
    PS01330 PABS_1, 1 hit
    PS51006 PABS_2, 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 nameiSPEE_THET8
    <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: Q5SK28
    Secondary accession number(s): P83816
    <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: January 15, 2008
    Last sequence update: December 21, 2004
    Last modified: December 11, 2019
    This is version 103 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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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