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Entry version 66 (16 Oct 2019)
Sequence version 1 (03 Mar 2009)
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Protein

Nonribosomal peptide synthetase asaC

Gene

asaC

Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Status
Reviewed-Annotation score:

Annotation score:3 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 transcript 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

Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspergillic acid, a hydroxamic acid-containing pyrazinone with aliphatic side chains that originates from leucine (Leu) and isoleucine (Ile) (PubMed:29674152). Aspergillic acid has antibiotic properties and was shown to be lethal to mice (PubMed:29674152). The first step in the pathway is the production of deoxyaspergillic acid via a condensation between the Ile amine and the Leu carboxylic acid, followed by a reductive release from the protein forming the dipeptide aldehyde NH2-Leu-Ile-CHO, which could undergo an intermolecular cyclization resulting in a dihydropyrazinone (PubMed:29674152). As the NRPS asaC lacks a condensation domain, it is improbable that it is responsible for condensation of Leu and Ile (PubMed:29674152). One possibility is that asaC acts on a previously condensed dipeptide and functions as a Leu-Ile reductase to yield deoxyaspergillic acid (PubMed:29674152). After asaC forms deoxyaspergillic acid, the cytochrome P450 asaD oxidizes the pyrazinone to the hydroxamic acid-containing bioactive metabolite aspergillic acid (PubMed:29674152). The hydroxylase/desaturase asaB can then convert aspergillic acid to hydroxyaspergillic acid (PubMed:29674152). Both aspergillic acid and hydroxyaspergillic acid can form complexes with iron producing ferriaspergillin analogs (PubMed:29674152).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Secondary metabolite biosynthesis

This protein is involved in Secondary metabolite biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.

<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

<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 functionLigase, Multifunctional enzyme, Oxidoreductase

<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:
Nonribosomal peptide synthetase asaC1 Publication (EC:6.3.2.-1 Publication)
Short name:
NRPS asaC1 Publication
Alternative name(s):
Aspergillic acid biosynthesis cluster protein C1 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:asaC1 Publication
ORF Names:AFLA_023020
<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>OrganismiAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
<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 identifieri332952 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
<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
  • UP000001875 <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: Unassembled WGS sequence

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:AFLA_023020

<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

Abolishes the production of ferriaspergillin and aspergillic acid (PubMed:29674152).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_00004444551 – 1021Nonribosomal peptide synthetase asaCAdd BLAST1021

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei563O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expressed during the earliest stages of maize kernel infection (PubMed:23834374).1 Publication

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
5059.CADAFLAP00001678

<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>Domaini528 – 603CarrierPROSITE-ProRule annotation1 PublicationAdd BLAST76

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>Regioni17 – 418Adenylation (A) domainSequence analysis1 PublicationAdd BLAST402
Regioni646 – 888short-chain dehydrogenase/reductase (R) domainSequence analysis1 PublicationAdd BLAST243

<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

NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module (By similarity). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (By similarity). Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme (By similarity). Occasionally, epimerase (E) domains (responsible for L- to D-amino acid conversion) are present within the NRP synthetase (By similarity). AsaC contains an amino acid adenylation domain (A), a peptidyl carrier protein (PCP) domain with a phosphopantetheine prosthetic group, and a short-chain dehydrogenase/reductase terminus (R), but it does not have an identifiable condensation (C) domain required for the formation of peptide bonds during non-ribosomal peptide synthesis (PubMed:29674152).By similarity1 Publication

<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 NRP synthase family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000216790

KEGG Orthology (KO)

More...
KOi
K23631

Identification of Orthologs from Complete Genome Data

More...
OMAi
HRTHILH

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05235 SDR_e1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 1 hit
3.40.50.12780, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010071 AA_adenyl_domain
IPR036736 ACP-like_sf
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
IPR013120 Male_sterile_NAD-bd
IPR036291 NAD(P)-bd_dom_sf
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
IPR010080 Thioester_reductase-like_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
PF07993 NAD_binding_4, 1 hit
PF00550 PP-binding, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00823 PKS_PP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336 SSF47336, 1 hit
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01733 AA-adenyl-dom, 1 hit
TIGR01746 Thioester-redct, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00455 AMP_BINDING, 1 hit
PS50075 CARRIER, 1 hit
PS00012 PHOSPHOPANTETHEINE, 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.

B8N0E8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSIFSSISSL GLEACYRHHV RTSPNATAVV DGDQSMTYRE LETRVNDLAS
60 70 80 90 100
ILGRENIEEE EPIGILVPMG IAHVVAQAAV LRLGGSCVPM DLSFPDQRIN
110 120 130 140 150
DLLRALKTRI VLTVESEKAR FAEFQTILVD SKYANLHQNG YHEDTIPAVE
160 170 180 190 200
TGRNHRTHIL HTSGTTGLPK PVEIMSKGIT RMAFNTQCVE FKSTDRVAQI
210 220 230 240 250
SAPSFDAALF EIWTTLARGA AIVLLPKNVV IDPVALHDSL RKYRITSILV
260 270 280 290 300
TTALLNHVVS AIPNAFEDLD YVLTGGEAAN PSVMQVILEN GPPKKLVHAY
310 320 330 340 350
GPTECTIITT YHLTTLEEVR RGQTPIGRPL DNTTVYILDD NLQPVKEGIV
360 370 380 390 400
GELYIGGDAV ARGYLGRPEA NAKSFLEVSH LSKDGSPVRI YRSGDLVRML
410 420 430 440 450
DTGAIEFVAR ADNMVKIRGF RIEPAEIEGA LLKSEMVQGT VVLPVHRPGK
460 470 480 490 500
ETYIVAFVIP KHDGAFSLEQ LDEYLRRRLP AYMMPRLEAV ASLPLTVHGK
510 520 530 540 550
IDRVAVMKKH MEETKRAEQQ VLISSNVKDA GDSVTWLRTL WTSVLGISNI
560 570 580 590 600
DNEASFFHLG GSSLQAAALL VHIRRRFGLT LTMQQIYDSP TLLGLASVID
610 620 630 640 650
AGHAKSKVDH SRLGIFIADS QLAKDIPVLS KEAPDWRSPS EGKVFLTGAT
660 670 680 690 700
GFLGTYFLRE LIDRPDVRSV KCLVRASDAH SARKRLLGAL DKYGLGWADN
710 720 730 740 750
LDKVTAIAGD LGKDLFGLSE TEFHELALWT SVIFHVGAHV NYVQPYEKHR
760 770 780 790 800
NTNVYGTLNC IKLATTGRTK ALHYTSTAAV TGPVSHFTGA DKIPEDVDLG
810 820 830 840 850
EFQGWLPYDI GYTQSKWVSE QLIHSMIAKG LPAIVFRPGF IMGDSLRGKG
860 870 880 890 900
NCDDFMCRVF IGSIKLGYRP ILPNQSKIMI PVDFITTALL HITSNPYNFG
910 920 930 940 950
RTFHLVPQTP EEDTDIETSW NMLKELGYDL KAVEYKDWLE ILSKDKDLLT
960 970 980 990 1000
NPLLPMLPVL QEPVRKHLTR WELYEDMATY DVTNTRRSLA DRGKLKSGIG
1010 1020
LEDLRRHVED WVARGLVPSR N
Length:1,021
Mass (Da):113,315
Last modified:March 3, 2009 - 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:iB55B484101FD24C7
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
EQ963473 Genomic DNA Translation: EED55031.1

NCBI Reference Sequences

More...
RefSeqi
XP_002373813.1, XM_002373772.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
EED55031; EED55031; AFLA_023020

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7917700

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
afv:AFLA_023020

<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
EQ963473 Genomic DNA Translation: EED55031.1
RefSeqiXP_002373813.1, XM_002373772.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi5059.CADAFLAP00001678

Genome annotation databases

EnsemblFungiiEED55031; EED55031; AFLA_023020
GeneIDi7917700
KEGGiafv:AFLA_023020

Organism-specific databases

EuPathDBiFungiDB:AFLA_023020

Phylogenomic databases

HOGENOMiHOG000216790
KOiK23631
OMAiHRTHILH

Family and domain databases

CDDicd05235 SDR_e1, 1 hit
Gene3Di1.10.1200.10, 1 hit
3.40.50.12780, 1 hit
InterProiView protein in InterPro
IPR010071 AA_adenyl_domain
IPR036736 ACP-like_sf
IPR025110 AMP-bd_C
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
IPR013120 Male_sterile_NAD-bd
IPR036291 NAD(P)-bd_dom_sf
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
IPR010080 Thioester_reductase-like_dom
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
PF07993 NAD_binding_4, 1 hit
PF00550 PP-binding, 1 hit
SMARTiView protein in SMART
SM00823 PKS_PP, 1 hit
SUPFAMiSSF47336 SSF47336, 1 hit
SSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01733 AA-adenyl-dom, 1 hit
TIGR01746 Thioester-redct, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit
PS50075 CARRIER, 1 hit
PS00012 PHOSPHOPANTETHEINE, 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 nameiASAC_ASPFN
<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: B8N0E8
<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 20, 2018
Last sequence update: March 3, 2009
Last modified: October 16, 2019
This is version 66 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 programFungal 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

Complete proteome, Reference proteome

Documents

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