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Entry version 89 (11 Dec 2019)
Sequence version 1 (26 Apr 2005)
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Protein

Exo-1,4-beta-xylosidase xlnD

Gene

xlnD

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score:

Annotation score:4 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

Xylan 1,4-beta-xylosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.2 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

  • Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini. EC:3.2.1.37

<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>pH dependencei

Optimum pH is 5.1.1 Publication

Temperature dependencei

Optimum temperature is 52 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: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei307By similarity1

<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 functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00114

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH3 Glycoside Hydrolase Family 3

mycoCLAP, a database of fungal genes encoding lignocellulose-active proteins

More...
mycoCLAPi
XYL3C_EMENI

<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:
Exo-1,4-beta-xylosidase xlnD (EC:3.2.1.37)
Alternative name(s):
1,4-beta-D-xylan xylohydrolase xlnD
Beta-xylosidase A
Beta-xylosidase xlnD
Xylobiase xlnD
<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:xlnD
Synonyms:xylA
ORF Names:AN2359
<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>OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
<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 identifieri227321 [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
  • UP000000560 <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 VII
  • UP000005890 Componenti: Unassembled WGS sequence

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18Sequence analysisAdd BLAST18
<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_000039329319 – 803Exo-1,4-beta-xylosidase xlnDAdd BLAST785

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi21N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi44N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi85N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi122N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi140N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi234N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi437N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi474N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi515N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi611N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi676N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi698N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q5BAS1

<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
162425.CADANIAP00009060

<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

1803
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
Q5BAS1

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 information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000031216

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5BAS1

KEGG Orthology (KO)

More...
KOi
K15920

Identification of Orthologs from Complete Genome Data

More...
OMAi
YYTPQFL

Database of Orthologous Groups

More...
OrthoDBi
321444at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 1 hit
3.20.20.300, 1 hit
3.40.50.1700, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR026891 Fn3-like
IPR002772 Glyco_hydro_3_C
IPR036881 Glyco_hydro_3_C_sf
IPR001764 Glyco_hydro_3_N
IPR036962 Glyco_hydro_3_N_sf
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF14310 Fn3-like, 1 hit
PF00933 Glyco_hydro_3, 1 hit
PF01915 Glyco_hydro_3_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01217 Fn3_like, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445 SSF51445, 1 hit
SSF52279 SSF52279, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q5BAS1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRSLISVAVL SALPTAFSQA NTSYTDYNVE ANPDLFPLCL QHLNASFPDC
60 70 80 90 100
ASGPLSLTPV CDRSLSPKDR ATALVSLFTF DELVNNTGNT GLGVSRLGLP
110 120 130 140 150
NYQVWGEALH GVGRANFVES GNFSWATSFP MPITMMAALN KTLIHQIGTI
160 170 180 190 200
VSTQLRAFSN AGLGGVDVYS PNINTFRHPV WGRGQETPGE DAFLTSVYGY
210 220 230 240 250
EYITALQGGV DPETLKIIAT AKHYAGYDIE SWNNHSRLGN DMQITQQELS
260 270 280 290 300
EYYTPPFIVA SRDAKVRSVM CSYNAVNGVP SCANKFFLQT LLRDTFEFSE
310 320 330 340 350
DGYVSGDCGA VYNVWNPHGY ASNEAAASAD SILAGTDIDC GTSYQWHSED
360 370 380 390 400
AFEDSLVSRS DIERGVIRLY SNLVQAGYFD GEDAPYRDIT WDDVLSTDAW
410 420 430 440 450
NIAYEAAVEG IVLLKNDETL PLSKDIKSVA VIGPWANVTE ELQGNYFGPA
460 470 480 490 500
PYLISPLTGF RDSGLDVHYA LGTNLTSHST SGFEEALTAA KQADAIIFAG
510 520 530 540 550
GIDNTIEAEA MDRENITWPG NQLDLISKLS ELGKPLVVLQ MGGGQVDSSS
560 570 580 590 600
LKDNDNVNAL IWGGYPGQSG GHALADIITG KRAPAGRLVT TQYPAEYAEV
610 620 630 640 650
FPAIDMNLRP NETSGNPGQT YMWYTGTPVY EFGHGLFYTT FEESTETTDA
660 670 680 690 700
GSFNIQTVLT TPHSGYEHAQ QKTLLNFTAT VKNTGERESD YTALVYVNTT
710 720 730 740 750
AGPAPYPKKW VVGFDRLGGL EPGDSQTLTV PVTVESVART DEQGNRVLYP
760 770 780 790 800
GSYELALNNE RSVVVKFELK GEEAVILSWP EDTTSDFVSS IDGGLDRKQD

VIA
Length:803
Mass (Da):87,196
Last modified:April 26, 2005 - 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:i9EF12F7391B043B2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti14 – 15PT → A in CAA73902 (PubMed:9546179).Curated2
Sequence conflicti52S → T in CAA73902 (PubMed:9546179).Curated1
Sequence conflicti209G → A in CAA73902 (PubMed:9546179).Curated1
Sequence conflicti215L → S in CAA73902 (PubMed:9546179).Curated1
Sequence conflicti754 – 755EL → DV in CAA73902 (PubMed:9546179).Curated2

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
Y13568 Genomic DNA Translation: CAA73902.1
AACD01000039 Genomic DNA Translation: EAA64470.1
BN001307 Genomic DNA Translation: CBF86686.1

NCBI Reference Sequences

More...
RefSeqi
XP_659963.1, XM_654871.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
CBF86686; CBF86686; ANIA_02359
EAA64470; EAA64470; AN2359.2

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2875035

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ani:AN2359.2

<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
Y13568 Genomic DNA Translation: CAA73902.1
AACD01000039 Genomic DNA Translation: EAA64470.1
BN001307 Genomic DNA Translation: CBF86686.1
RefSeqiXP_659963.1, XM_654871.1

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
6Q7IX-ray1.48A/B19-803[»]
6Q7JX-ray2.14A/B20-803[»]
SMRiQ5BAS1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00009060

Protein family/group databases

CAZyiGH3 Glycoside Hydrolase Family 3
mycoCLAPiXYL3C_EMENI

Proteomic databases

PRIDEiQ5BAS1

Genome annotation databases

EnsemblFungiiCBF86686; CBF86686; ANIA_02359
EAA64470; EAA64470; AN2359.2
GeneIDi2875035
KEGGiani:AN2359.2

Phylogenomic databases

HOGENOMiHOG000031216
InParanoidiQ5BAS1
KOiK15920
OMAiYYTPQFL
OrthoDBi321444at2759

Enzyme and pathway databases

UniPathwayiUPA00114

Family and domain databases

Gene3Di2.60.40.10, 1 hit
3.20.20.300, 1 hit
3.40.50.1700, 1 hit
InterProiView protein in InterPro
IPR026891 Fn3-like
IPR002772 Glyco_hydro_3_C
IPR036881 Glyco_hydro_3_C_sf
IPR001764 Glyco_hydro_3_N
IPR036962 Glyco_hydro_3_N_sf
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
PfamiView protein in Pfam
PF14310 Fn3-like, 1 hit
PF00933 Glyco_hydro_3, 1 hit
PF01915 Glyco_hydro_3_C, 1 hit
SMARTiView protein in SMART
SM01217 Fn3_like, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
SSF52279 SSF52279, 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 nameiXYND_EMENI
<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: Q5BAS1
Secondary accession number(s): C8VNG4, O42810
<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: March 23, 2010
Last sequence update: April 26, 2005
Last modified: December 11, 2019
This is version 89 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

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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