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Entry version 118 (13 Nov 2019)
Sequence version 2 (25 Oct 2002)
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Protein

Ribose-phosphate pyrophosphokinase

Gene

prs

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

Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). It can also use dATP as diphosphoryl donor.UniRule annotation1 Publication

Miscellaneous

M.jannaschii PRPP synthase is more compact than the PRPP synthase in the B. subtilis subunit. This is mainly due to truncations of eight residues at the N terminus, 14 residues at the C terminus and to a seven-residue shorter loop.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 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

Mg2+UniRule annotation1 PublicationNote: Binds 2 Mg2+ ions per subunit (PubMed:28031352). Mn2+ is also accepted, but the activity is less than 15% of that obtained with Mg2+, when assayed at pH 9.5 (PubMed:16288921).1 PublicationUniRule annotation1 Publication

<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

Activated by inorganic phosphate, with a maximal activity at 190 mM. Above this concentration inorganic phosphate progressively inhibits the kinase. Completely inhibited by ADP, and partially inhibited by alpha,beta-methylene ATP (mATP). Lack of allosteric regulation.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=2.6 mM for ATP (at pH 9 and 85 degrees Celsius)1 Publication
  2. KM=2.8 mM for ribose 5-phosphate (at pH 9 and 85 degrees Celsius)1 Publication
  1. Vmax=2.2 mmol/min/mg enzyme (at pH 9 and 85 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 9.5. The activity declines strongly above pH 10.1 Publication

Temperature dependencei

Optimum temperature is 85 degrees Celsius. 70% of maximal activity at 72 and 95 degrees Celsius.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: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I).UniRule annotation1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-phosphate pyrophosphokinase (prs)
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

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 bindingi125Magnesium 1UniRule annotation1
Metal bindingi163Magnesium 2UniRule annotation1
<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 sitei186UniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei188Ribose-5-phosphateUniRule annotation1
Binding sitei212Ribose-5-phosphateUniRule annotationCombined sources1 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 bindingi34 – 36ATPUniRule annotationCombined sources1 Publication3
Nucleotide bindingi92 – 93ATPUniRule annotationCombined sources1 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 functionKinase, Transferase
Biological processNucleotide biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.6.1 3260

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

More...
UniPathwayi
UPA00087;UER00172

<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:
Ribose-phosphate pyrophosphokinase1 PublicationUniRule annotation (EC:2.7.6.1UniRule annotation1 Publication)
Short name:
RPPK1 PublicationUniRule annotation
Alternative name(s):
5-phospho-D-ribosyl alpha-1-diphosphateUniRule annotation
Phosphoribosyl diphosphate synthase1 PublicationUniRule annotation
Phosphoribosyl pyrophosphate synthase1 PublicationUniRule annotation
Short name:
P-Rib-PP synthaseUniRule annotation
Short name:
PRPP synthase1 PublicationUniRule annotation
Short name:
PRPPaseUniRule 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:prs1 PublicationUniRule annotation
Ordered Locus Names:MJ1366
<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>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_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 identifieri243232 [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 lineageiArchaeaEuryarchaeotaMethanomada groupMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
<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
  • UP000000805 <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 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_00001412381 – 284Ribose-phosphate pyrophosphokinaseAdd BLAST284

<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
243232.MJ_1366

<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

1284
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
Q58761

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
Q58761

<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

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>Regioni216 – 220Ribose-5-phosphate bindingUniRule annotationCombined sources1 Publication5

<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 ribose-phosphate pyrophosphokinase family. Class III (archaeal) subfamily.1 PublicationUniRule annotation1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
arCOG00067 Archaea
COG0462 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q58761

KEGG Orthology (KO)

More...
KOi
K00948

Identification of Orthologs from Complete Genome Data

More...
OMAi
FGWARQD

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q58761

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06223 PRTases_typeI, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.2020, 2 hits

HAMAP database of protein families

More...
HAMAPi
MF_00583_A RibP_PPkinase_A, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029099 Pribosyltran_N
IPR000836 PRibTrfase_dom
IPR029057 PRTase-like
IPR005946 Rib-P_diPkinase
IPR037514 Rib-P_diPkinase_arc

The PANTHER Classification System

More...
PANTHERi
PTHR10210 PTHR10210, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00156 Pribosyltran, 1 hit
PF13793 Pribosyltran_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53271 SSF53271, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01251 ribP_PPkin, 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.

Q58761-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIVVSGSQSQ NLAFKVAKLL NTKLTRVEYK RFPDNEIYVR IVDEINDDEA
60 70 80 90 100
VIINTQKNQN DAIVETILLC DALRDEGVKK ITLVAPYLAY ARQDKKFNPG
110 120 130 140 150
EAISIRALAK IYSNIVDKLI TINPHETHIK DFFTIPFIYG DAVPKLAEYV
160 170 180 190 200
KDKLNDPIVL APDKGALEFA KTASKILNAE YDYLEKTRLS PTEIQIAPKT
210 220 230 240 250
LDAKDRDVFI VDDIISTGGT MATAVKLLKE QGAKKIIAAC VHPVLIGDAL
260 270 280
NKLYSAGVEE VVGTDTYLSE VSKVSVAEVI VDLL
Length:284
Mass (Da):31,395
Last modified:October 25, 2002 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9EAE9805785B1127
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB99374 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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: AAB99374.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...
PIRi
E64470

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAB99374; AAB99374; MJ_1366

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mja:MJ_1366

<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: AAB99374.1 Different initiation.
PIRiE64470

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
1U9YX-ray2.65A/B/C/D1-284[»]
1U9ZX-ray2.80A/B/C/D1-284[»]
SMRiQ58761
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_1366

Genome annotation databases

EnsemblBacteriaiAAB99374; AAB99374; MJ_1366
KEGGimja:MJ_1366

Phylogenomic databases

eggNOGiarCOG00067 Archaea
COG0462 LUCA
InParanoidiQ58761
KOiK00948
OMAiFGWARQD
PhylomeDBiQ58761

Enzyme and pathway databases

UniPathwayiUPA00087;UER00172
BRENDAi2.7.6.1 3260

Miscellaneous databases

EvolutionaryTraceiQ58761

Family and domain databases

CDDicd06223 PRTases_typeI, 1 hit
Gene3Di3.40.50.2020, 2 hits
HAMAPiMF_00583_A RibP_PPkinase_A, 1 hit
InterProiView protein in InterPro
IPR029099 Pribosyltran_N
IPR000836 PRibTrfase_dom
IPR029057 PRTase-like
IPR005946 Rib-P_diPkinase
IPR037514 Rib-P_diPkinase_arc
PANTHERiPTHR10210 PTHR10210, 1 hit
PfamiView protein in Pfam
PF00156 Pribosyltran, 1 hit
PF13793 Pribosyltran_N, 1 hit
SUPFAMiSSF53271 SSF53271, 2 hits
TIGRFAMsiTIGR01251 ribP_PPkin, 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 nameiKPRS_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: Q58761
<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: October 25, 2002
Last sequence update: October 25, 2002
Last modified: November 13, 2019
This is version 118 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation 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. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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