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Entry version 121 (02 Jun 2021)
Sequence version 1 (01 Nov 1996)
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Protein

5'-deoxyadenosine deaminase

Gene

dadD

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
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

Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated (PubMed:24375099).

Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions (PubMed:25917907).

May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens (PubMed:24375099).

1 Publication1 Publication

Miscellaneous

SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine (PubMed:25917907). 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent (PubMed:24375099).2 Publications

<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

<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

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

<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 120000 sec(-1) for 5'-deoxyadenosine deamination. kcat is 160 sec(-1) for S-methyl-5'-thioadenosine deamination. kcat is 1300 sec(-1) for S-adenosyl-L-homocysteine deamination. kcat is 110 sec(-1) for adenosine deamination (at pH 9 and 60 degrees Celsius).1 Publication
  1. KM=0.014 mM for 5'-deoxyadenosine (at pH 9 and 60 degrees Celsius)1 Publication
  2. KM=0.11 mM for S-methyl-5'-thioadenosine (at pH 9 and 60 degrees Celsius)1 Publication
  3. KM=1.1 mM for S-adenosyl-L-homocysteine (at pH 9 and 60 degrees Celsius)1 Publication
  4. KM=0.15 mM for adenosine (at pH 9 and 60 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 9.0.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: S-adenosyl-L-methionine biosynthesis

    This protein is involved in the pathway S-adenosyl-L-methionine biosynthesis, which is part of Amino-acid biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway S-adenosyl-L-methionine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi55Zinc; via tele nitrogenUniRule annotation1
    Metal bindingi57Zinc; via tele nitrogenUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei84SubstrateUniRule annotation1
    Binding sitei176SubstrateUniRule annotation1
    Metal bindingi203Zinc; via tele nitrogenUniRule annotation1
    Binding sitei206SubstrateUniRule annotation1
    Metal bindingi292ZincUniRule annotation1
    Binding sitei292SubstrateUniRule 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 functionHydrolase
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MJAN243232:G1GKE-1669-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.5.4.28, 3260
    3.5.4.31, 3260
    3.5.4.4, 3260
    3.5.4.41, 3260

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00315

    <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:
    5'-deoxyadenosine deaminase1 PublicationUniRule annotation (EC:3.5.4.41UniRule annotation1 Publication)
    Short name:
    5'-dA deaminase1 PublicationUniRule annotation
    Alternative name(s):
    5'-methylthioadenosine deaminase1 Publication (EC:3.5.4.311 Publication)
    Short name:
    MTA deaminase1 Publication
    Adenosine deaminase1 Publication (EC:3.5.4.41 Publication)
    S-adenosylhomocysteine deaminase2 Publications (EC:3.5.4.282 Publications)
    Short name:
    SAH deaminase2 Publications
    <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:dadD1 PublicationUniRule annotation
    Ordered Locus Names:MJ1541
    <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>OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
    <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 identifieri243232 [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 lineageiArchaeaEuryarchaeotaMethanomada groupMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
    <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
    • UP000000805 <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: Chromosome

    <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>Mutagenesisi136Y → R: Lowers temperature stability by 10 degrees Celsius and decreases activity by 364-fold with 5'-deoxyadenosine as substrate. Lowers temperature stability by 35 degrees Celsius and decreases activity by 100000-fold with 5'-deoxyadenosine as substrate; when associated with R-150. 1 Publication1
    Mutagenesisi150E → R: Lowers temperature stability by 10 degrees Celsius and decreases activity by 571-fold with 5'-deoxyadenosine as substrate. Lowers temperature stability by 35 degrees Celsius and decreases activity by 100000-fold with 5'-deoxyadenosine as substrate; when associated with R-136. 1 Publication1
    Mutagenesisi294C → S: No effect on temperature stability. 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_00001223111 – 4205'-deoxyadenosine deaminaseAdd BLAST420

    <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

    Homotetramer.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    243232.MJ_1541

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

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

    More...
    SMRi
    Q58936

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <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 metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    arCOG00695, Archaea

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_012358_2_1_2

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q58936

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    ASYFATN

    Database of Orthologous Groups

    More...
    OrthoDBi
    40873at2157

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q58936

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.30.40.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01281, MTA_SAH_deamin, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006680, Amidohydro-rel
    IPR023512, Deaminase_MtaD/DadD
    IPR011059, Metal-dep_hydrolase_composite
    IPR032466, Metal_Hydrolase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01979, Amidohydro_1, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51338, SSF51338, 1 hit
    SSF51556, SSF51556, 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>Sequencei

    <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.

    Q58936-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MILIKNVFVN GKRQDILIEG NKIKKIGEVK KEEIENAEII DGKNKIAIPG
    60 70 80 90 100
    LINTHTHIPM TLFRGVADDL PLMEWLNNYI WPMEAKLNEE IVYWGTLLGC
    110 120 130 140 150
    IEMIRSGTTT FNDMYFFLEG IAKAVDESGM RAVLAYGMID LFDEERRERE
    160 170 180 190 200
    LKNAEKYINY INSLNNSRIM PALGPHAPYT CSKELLMEVN NLAKKYNVPI
    210 220 230 240 250
    HIHLNETLDE IKMVKEKTGM EPFIYLNSFG FFDDVRAIAA HCVHLTDEEI
    260 270 280 290 300
    KIMKQKNINV SHNPISNLKL ASGVAPIPKL LAEGINVTLG TDGCGSNNNL
    310 320 330 340 350
    NLFEEIKVSA ILHKGVNLNP TVVKAEEAFN FATKNGAKAL NIKAGEIREG
    360 370 380 390 400
    YLADIVLINL DKPYLYPKEN IMSHLVYAFN GFVDDVIIDG NIVMRDGEIL
    410 420
    TVDEEKVYEK AEEMYEILRS
    Length:420
    Mass (Da):47,468
    Last modified:November 1, 1996 - 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:i2458E0E14AF91731
    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
    L77117 Genomic DNA Translation: AAB99560.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    D64492

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_010871065.1, NC_000909.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAB99560; AAB99560; MJ_1541

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1452449

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mja:MJ_1541

    <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
    L77117 Genomic DNA Translation: AAB99560.1
    PIRiD64492
    RefSeqiWP_010871065.1, NC_000909.1

    3D structure databases

    SMRiQ58936
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi243232.MJ_1541

    Genome annotation databases

    EnsemblBacteriaiAAB99560; AAB99560; MJ_1541
    GeneIDi1452449
    KEGGimja:MJ_1541

    Phylogenomic databases

    eggNOGiarCOG00695, Archaea
    HOGENOMiCLU_012358_2_1_2
    InParanoidiQ58936
    OMAiASYFATN
    OrthoDBi40873at2157
    PhylomeDBiQ58936

    Enzyme and pathway databases

    UniPathwayiUPA00315
    BioCyciMJAN243232:G1GKE-1669-MONOMER
    BRENDAi3.5.4.28, 3260
    3.5.4.31, 3260
    3.5.4.4, 3260
    3.5.4.41, 3260

    Family and domain databases

    Gene3Di2.30.40.10, 1 hit
    HAMAPiMF_01281, MTA_SAH_deamin, 1 hit
    InterProiView protein in InterPro
    IPR006680, Amidohydro-rel
    IPR023512, Deaminase_MtaD/DadD
    IPR011059, Metal-dep_hydrolase_composite
    IPR032466, Metal_Hydrolase
    PfamiView protein in Pfam
    PF01979, Amidohydro_1, 1 hit
    SUPFAMiSSF51338, SSF51338, 1 hit
    SSF51556, SSF51556, 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 nameiDADD_METJA
    <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: Q58936
    <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: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: June 2, 2021
    This is version 121 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

    Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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