Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 34 (18 Sep 2019)
Sequence version 1 (16 Apr 2014)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA

Gene

cpdA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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

Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. Can also hydrolyze cGMP, p-nitrophenyl phosphate (pNPP), bis-(p-nitrophenyl phosphate) (bis(pNPP)), p-nitrophenyl phenylphosphonate (pNPPP) and 2',3'-cAMP. May play a role in pathogenicity, not only by hydrolyzing cAMP, but also by altering properties of the cell wall.UniRule annotation2 Publications

<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

Enhanced by magnesium or manganese. Activity decreases in the presence of orthovanadate and phosphotyrosine.1 Publication

<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

  1. KM=5.5 mM for 3',5'-cAMP1 Publication
  2. KM=0.9 mM for bis(pNPP)1 Publication
  3. KM=0.9 mM for pNPPP1 Publication
  4. KM=1 mM for 2',3'-cAMP1 Publication
  1. Vmax=1.1 µmol/min/mg enzyme with 3',5'-cAMP as substrate1 Publication
  2. Vmax=74 µmol/min/mg enzyme with bis(pNPP) as substrate1 Publication
  3. Vmax=112.7 µmol/min/mg enzyme with pNPPP as substrate1 Publication
  4. Vmax=14.7 µmol/min/mg enzyme with 2',3'-cAMP as substrate1 Publication
  5. Vmax=0.017 µmol/min/mg enzyme with pNPP as substrate1 Publication

pH dependencei

Optimum pH is 8.5-9.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section 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 bindingi21Iron2 Publications1
Metal bindingi23Iron2 Publications1
<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 sitei23cAMPUniRule annotation1 Publication1
Metal bindingi63Iron2 Publications1
Metal bindingi63Manganese2 Publications1
Binding sitei63cAMPUniRule annotation1 Publication1
Metal bindingi97Manganese2 Publications1
Metal bindingi169Manganese2 Publications1
Metal bindingi207Manganese2 Publications1
Metal bindingi209Iron2 Publications1
Binding sitei209cAMPUniRule annotation1 Publication1

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 bindingi97 – 98cAMPUniRule annotation1 Publication2

<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
LigandcAMP, Iron, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MTBH37RV:G185E-4954-MONOMER

<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:
3',5'-cyclic adenosine monophosphate phosphodiesterase CpdAUniRule annotation (EC:3.1.4.53UniRule annotation)
Short name:
3',5'-cyclic AMP phosphodiesteraseUniRule annotation
Short name:
cAMP phosphodiesteraseUniRule annotation
<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:cpdAUniRule annotation
Synonyms:icc
Ordered Locus Names:Rv0805
<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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
<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
  • UP000001584 <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

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

More...
TubercuListi
Rv0805

<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

Cell membrane, Cell wall, Cytoplasm, Membrane, Secreted

<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_and_biotech_section">'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>Mutagenesisi21D → A: 90% decrease in bis(pNPP) hydrolysis. Does not affect cAMP hydrolysis. 1 Publication1
Mutagenesisi23H → A: 50% decrease in bis(pNPP) hydrolysis. Does not affect cAMP hydrolysis. 1 Publication1
Mutagenesisi66D → A: 25% decrease in bis(pNPP) hydrolysis. 70% decrease in cAMP hydrolysis. 1 Publication1
Mutagenesisi97N → A: Loss of bis(pNPP) and 3',5'-cAMP hydrolysis. Strong decrease in 2',3'-cAMP hydrolysis. 2 Publications1
Mutagenesisi98H → A: 40% decrease in bis(pNPP) hydrolysis. Strong decrease in 3',5'-cAMP and 2',3'-cAMP hydrolysis. 1 Publication1
Mutagenesisi140H → A: No change in activity. 2 Publications1
Mutagenesisi169H → A: 50% decrease in bis(pNPP) hydrolysis. Does not affect cAMP hydrolysis. 1 Publication1
Mutagenesisi207H → A: 75% decrease in bis(pNPP) hydrolysis. Does not affect cAMP hydrolysis. 1 Publication1
Mutagenesisi209H → A: 80% decrease in hydrolysis of 3',5'-cAMP and bis(pNPP). 40% decrease in 2',3'-cAMP hydrolysis. 1 Publication1
Mutagenesisi229Y → A: 40% decrease in bis(pNPP) hydrolysis. 80% decrease in 3',5'-cAMP and 2',3'-cAMP hydrolysis. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004133701 – 3183',5'-cyclic adenosine monophosphate phosphodiesterase CpdAAdd BLAST318

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P9WP65

<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

Homodimer.

3 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv0805

<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

1318
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
P9WP65

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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 general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal domain is used to better adjust the substrates into the active sites and to facilitate subcellular localization of the protein.1 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 cAMP phosphodiesterase class-III family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG41070EG Bacteria
COG1409 LUCA

KEGG Orthology (KO)

More...
KOi
K03651

Identification of Orthologs from Complete Genome Data

More...
OMAi
CAWLDQH

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WP65

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07402 MPP_GpdQ, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.21.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00905 cAMP_phosphodiest_CpdA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR026575 cAMP_Pdiest_CpdA
IPR029052 Metallo-depent_PP-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00149 Metallophos, 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.

P9WP65-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHRLRAAEHP RPDYVLLHIS DTHLIGGDRR LYGAVDADDR LGELLEQLNQ
60 70 80 90 100
SGLRPDAIVF TGDLADKGEP AAYRKLRGLV EPFAAQLGAE LVWVMGNHDD
110 120 130 140 150
RAELRKFLLD EAPSMAPLDR VCMIDGLRII VLDTSVPGHH HGEIRASQLG
160 170 180 190 200
WLAEELATPA PDGTILALHH PPIPSVLDMA VTVELRDQAA LGRVLRGTDV
210 220 230 240 250
RAILAGHLHY STNATFVGIP VSVASATCYT QDLTVAAGGT RGRDGAQGCN
260 270 280 290 300
LVHVYPDTVV HSVIPLGGGE TVGTFVSPGQ ARRKIAESGI FIEPSRRDSL
310
FKHPPMVLTS SAPRSPVD
Length:318
Mass (Da):34,233
Last modified:April 16, 2014 - 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:i7C1B683C5E375B3F
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
AL123456 Genomic DNA Translation: CCP43553.1

Protein sequence database of the Protein Information Resource

More...
PIRi
F70536

NCBI Reference Sequences

More...
RefSeqi
NP_215320.1, NC_000962.3
WP_003404120.1, NZ_NVQJ01000064.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CCP43553; CCP43553; Rv0805

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
885326

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv0805
mtv:RVBD_0805

<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
AL123456 Genomic DNA Translation: CCP43553.1
PIRiF70536
RefSeqiNP_215320.1, NC_000962.3
WP_003404120.1, NZ_NVQJ01000064.1

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
2HY1X-ray1.93A3-278[»]
2HYOX-ray2.25A3-278[»]
2HYPX-ray2.05A3-278[»]
3IB7X-ray1.60A2-318[»]
3IB8X-ray1.80A2-318[»]
SMRiP9WP65
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0805

Proteomic databases

PaxDbiP9WP65

Genome annotation databases

EnsemblBacteriaiCCP43553; CCP43553; Rv0805
GeneIDi885326
KEGGimtu:Rv0805
mtv:RVBD_0805

Organism-specific databases

TubercuListiRv0805

Phylogenomic databases

eggNOGiENOG41070EG Bacteria
COG1409 LUCA
KOiK03651
OMAiCAWLDQH
PhylomeDBiP9WP65

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-4954-MONOMER

Family and domain databases

CDDicd07402 MPP_GpdQ, 1 hit
Gene3Di3.60.21.10, 1 hit
HAMAPiMF_00905 cAMP_phosphodiest_CpdA, 1 hit
InterProiView protein in InterPro
IPR004843 Calcineurin-like_PHP_ApaH
IPR026575 cAMP_Pdiest_CpdA
IPR029052 Metallo-depent_PP-like
PfamiView protein in Pfam
PF00149 Metallophos, 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 nameiCPDA_MYCTU
<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: P9WP65
Secondary accession number(s): L0T7J7, O06629, Q7D993
<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: April 16, 2014
Last sequence update: April 16, 2014
Last modified: September 18, 2019
This is version 34 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, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again