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Entry version 44 (11 Dec 2019)
Sequence version 1 (13 Jun 2012)
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Protein

Galactose oxidase

Gene

GAOA

Organism
Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)
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>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides (By similarity).By similarity

<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

Cu2+By similarityNote: Binds 1 Cu2+ ion per subunit.By similarity

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 bindingi313CopperBy similarity1
<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 sitei536Proton acceptorBy similarity1
Metal bindingi536CopperBy similarity1
Metal bindingi537CopperBy similarity1
Metal bindingi622CopperBy 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

<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 functionOxidoreductase
LigandCopper, Metal-binding

<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:
Galactose oxidase (EC:1.1.3.9)
Short name:
GAO
Short name:
GO
Short name:
GOase
<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:GAOA
ORF Names:FGRRES_11032, FGSG_11032
<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>OrganismiGibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus) (Fusarium graminearum)
<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 identifieri229533 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium
<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
  • UP000070720 <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 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:FGRAMPH1_01G21069

<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 – 24By similarityAdd BLAST24
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000041837025 – 41By similarityAdd BLAST17
<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_000041837142 – 680Galactose oxidaseAdd BLAST639

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi59 ↔ 68PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki269 ↔ 3133'-(S-cysteinyl)-tyrosine (Cys-Tyr)By similarity
Disulfide bondi556 ↔ 559PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Galactose oxidase contains a protein-derived free radical cofactor (By similarity). In the active state, Tyr-313, which is cross-linked to Cys-269 via a thioether bond, is oxidized to a radical and acts with Cu2+ as a two-electron acceptor in the oxidation reaction. The cross-link is believed to modulate the redox potential of the tyrosyl radical, which is further stabilized by a stacking interaction with Trp-331 in the active site. The post-translational formation of the cross-link is closely linked to the propeptide cleavage event, and both are copper-dependent, autocatalytic processes. The propeptide may act as an intramolecular chaperone, facilitating thioester bond formation and copper binding by positioning of active-site residues, including copper ligands (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Thioether bond

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
I1S2N3

<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

Monomer.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
5518.FGSG_11032P0

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

3D structure databases

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

More...
SMRi
I1S2N3

Database of comparative protein structure models

More...
ModBasei
Search...

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

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>Domaini42 – 189F5/8 type CPROSITE-ProRule annotationAdd BLAST148
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati223 – 268Kelch 1Add BLAST46
Repeati279 – 321Kelch 2Add BLAST43
Repeati323 – 372Kelch 3Add BLAST50
Repeati436 – 490Kelch 4Add BLAST55
Repeati492 – 544Kelch 5Add BLAST53

Keywords - Domaini

Kelch repeat, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IJM5 Eukaryota
ENOG410XSZ3 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
I1S2N3

KEGG Orthology (KO)

More...
KOi
K04618

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02851 E_set_GO_C, 1 hit
cd00057 FA58C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.130.10.80, 1 hit
2.60.120.260, 1 hit
2.60.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000421 FA58C
IPR011043 Gal_Oxase/kelch_b-propeller
IPR037293 Gal_Oxidase_central_sf
IPR008979 Galactose-bd-like_sf
IPR015202 GO-like_E_set
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR006652 Kelch_1

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF09118 DUF1929, 1 hit
PF00754 F5_F8_type_C, 1 hit
PF01344 Kelch_1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00231 FA58C, 1 hit
SM00612 Kelch, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49785 SSF49785, 1 hit
SSF50965 SSF50965, 1 hit
SSF81296 SSF81296, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50022 FA58C_3, 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.

I1S2N3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKHFLSLALC FSSINAVAVT VPHKSGGTGS PEGSLQFLSL RASAPIGSAI
60 70 80 90 100
SRNNWAVTCD SAQSGNECNK AIDGNKDTFW HTFYGANGDP KPPHTYTIDM
110 120 130 140 150
KTTQNVNGLS MLPRQDGNQN GWIGRHEVYL SSDGTNWGSP VASGSWFADS
160 170 180 190 200
TTKYSNFETR PARYVRLVAV TEANGQPWTS IAEINVFQAS SYTAPQPGLG
210 220 230 240 250
RWGPTIDLPI VPAAAAIEPT SGRVLMWSSY RNDAFGGSPG GITLTSSWDP
260 270 280 290 300
STGIVSDRTV TVTKHDMFCP GISMDGNGQI VVTGGNDAKK TSLYDSSSDS
310 320 330 340 350
WIPGPDMQVA RGYQSSATMS DGRVFTIGGS WSGGVFEKNG EVYSPSSKTW
360 370 380 390 400
TSLPNAKVNP MLTADKQGLY RSDNHAWLFG WKKGSVFQAG PSTAMNWYYT
410 420 430 440 450
SGSGDVKSAG KRQSNRGVAP DAMCGNAVMY DAVKGKILTF GGSPDYQDSD
460 470 480 490 500
ATTNAHIITL GEPGTSPNTV FASNGLYFAR TFHTSVVLPD GSTFITGGQR
510 520 530 540 550
RGIPFEDSTP VFTPEIYVPE QDTFYKQNPN SIVRVYHSIS LLLPDGRVFN
560 570 580 590 600
GGGGLCGDCT TNHFDAQIFT PNYLYNSNGN LATRPKITRT STQSVKVGGR
610 620 630 640 650
ITISTDSSIT KASLIRYGTA THTVNTDQRR IPLTLTNNGG NSYSFQVPSD
660 670 680
SGVALPGYWM LFVMNSAGVP SVASTIRVTQ
Length:680
Mass (Da):72,791
Last modified:June 13, 2012 - 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:i7883D8F9637E8FE9
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
DS231670 Genomic DNA Translation: ESU17707.1
HG970334 Genomic DNA Translation: CEF87161.1

NCBI Reference Sequences

More...
RefSeqi
XP_011325329.1, XM_011327027.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
ESU17707; ESU17707; FGSG_11032

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
23557903

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
fgr:FGSG_11032

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS231670 Genomic DNA Translation: ESU17707.1
HG970334 Genomic DNA Translation: CEF87161.1
RefSeqiXP_011325329.1, XM_011327027.1

3D structure databases

SMRiI1S2N3
ModBaseiSearch...

Protein-protein interaction databases

STRINGi5518.FGSG_11032P0

Proteomic databases

PRIDEiI1S2N3

Genome annotation databases

EnsemblFungiiESU17707; ESU17707; FGSG_11032
GeneIDi23557903
KEGGifgr:FGSG_11032

Organism-specific databases

EuPathDBiFungiDB:FGRAMPH1_01G21069

Phylogenomic databases

eggNOGiENOG410IJM5 Eukaryota
ENOG410XSZ3 LUCA
InParanoidiI1S2N3
KOiK04618

Family and domain databases

CDDicd02851 E_set_GO_C, 1 hit
cd00057 FA58C, 1 hit
Gene3Di2.130.10.80, 1 hit
2.60.120.260, 1 hit
2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR000421 FA58C
IPR011043 Gal_Oxase/kelch_b-propeller
IPR037293 Gal_Oxidase_central_sf
IPR008979 Galactose-bd-like_sf
IPR015202 GO-like_E_set
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR006652 Kelch_1
PfamiView protein in Pfam
PF09118 DUF1929, 1 hit
PF00754 F5_F8_type_C, 1 hit
PF01344 Kelch_1, 1 hit
SMARTiView protein in SMART
SM00231 FA58C, 1 hit
SM00612 Kelch, 3 hits
SUPFAMiSSF49785 SSF49785, 1 hit
SSF50965 SSF50965, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS50022 FA58C_3, 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 nameiGAOA_GIBZE
<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: I1S2N3
Secondary accession number(s): A0A098DZ82
, A0A0E0SL48, O43098, Q01745, Q4HVH6, V6RUL9
<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: July 11, 2012
Last sequence update: June 13, 2012
Last modified: December 11, 2019
This is version 44 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

Reference proteome
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