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Entry version 28 (16 Oct 2019)
Sequence version 1 (16 Apr 2014)
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Protein

Dephospho-CoA kinase

Gene

coaE

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

Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (PubMed:19876400, PubMed:21264299). Can also use dATP, with lower efficiency, but cannot use GTP, dGTP or CTP (PubMed:19876400).2 Publications

Miscellaneous

Was identified as a high-confidence drug target.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 <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

Inhibited by CTP (PubMed:19876400, PubMed:21731728). CTP strongly binds the enzyme at a site overlapping that of the leading substrate, dephosphocoenzyme A. Binding of CTP probably prevents interaction with dephosphocoenzyme A and oligomeric transformation to the active form, which limits the catalytic efficiency of the enzyme (PubMed:21731728).2 Publications

<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

kcat is 1.76 min(-1).1 Publication
  1. KM=34.9 µM for dephospho-CoA1 Publication
  2. KM=56.8 µM for ATP1 Publication
  3. KM=320 µM for dATP1 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: coenzyme A biosynthesis

    This protein is involved in step 5 of the subpathway that synthesizes CoA from (R)-pantothenate.UniRule annotation1 Publication
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Type III pantothenate kinase (coaX), Pantothenate kinase (coaA)
    2. Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
    3. Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
    4. Phosphopantetheine adenylyltransferase (coaD)
    5. Dephospho-CoA kinase (coaE)
    This subpathway is part of the pathway coenzyme A biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes CoA from (R)-pantothenate, the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.

    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 bindingi11 – 16ATPUniRule annotation6

    <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 processCoenzyme A biosynthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MTBH37RV:G185E-5820-MONOMER

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

    More...
    UniPathwayi
    UPA00241;UER00356

    <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:
    Dephospho-CoA kinaseUniRule annotation (EC:2.7.1.24UniRule annotation2 Publications)
    Alternative name(s):
    Dephosphocoenzyme A kinase1 PublicationUniRule 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:coaE1 PublicationUniRule annotation
    Ordered Locus Names:Rv1631
    ORF Names:MTCY01B2.23
    <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
    Rv1631

    <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 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>Mutagenesisi8G → A: Does not change either the Km or the kcat of the reaction considerably. 1 Publication1
    Mutagenesisi14K → A: Shows a 50% increase in the Km for ATP and a 19% reduction in kcat. 1 Publication1
    Mutagenesisi32D → A: Does not affect Km for ATP, but shows a 15-fold increase in the Km for dephospho-CoA. Decrease in kcat and strong decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi32D → E: Decreases Km for both ATP and dephospho-CoA. Has minimal effect on kcat. 1 Publication1
    Mutagenesisi32D → N: Does not affect Km for ATP, but shows a 2.5-fold increase in the Km for dephospho-CoA. 1 Publication1
    Mutagenesisi114L → A: Increases Km for both ATP and dephospho-CoA, but increases the enzymatic turnover. 1 Publication1
    Mutagenesisi140R → A: Loss of activity. 1 Publication1
    Mutagenesisi140R → K: Almost loss of activity. Shows very poor binding to ATP. 1 Publication1
    Mutagenesisi235C → S: Does not affect oligomerization. 1 Publication1
    Mutagenesisi368C → S: Does not affect oligomerization. 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_00001729641 – 407Dephospho-CoA kinaseAdd BLAST407

    Proteomic databases

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

    More...
    PaxDbi
    P9WPA3

    <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

    Forms monomers and homotrimers. The monomer is the active form and the trimeric form is inactive. Shift from inactive homotrimer to active monomer is induced in the presence of dephosphocoenzyme A. A dynamic equilibrium between the trimeric and monomeric forms regulates the effective concentration of active enzyme.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv1631

    <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
    P9WPA3

    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>Domaini3 – 204DPCKUniRule annotationAdd BLAST202

    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>Regioni211 – 407UPF0157CuratedAdd BLAST197

    <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 UPF0157 domain is involved in the proper folding of the full length enzyme.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

    In the N-terminal section; belongs to the CoaE family.Curated
    In the C-terminal section; belongs to the UPF0157 (GrpB) family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108ZQD Bacteria
    COG0237 LUCA
    COG2320 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K00859

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    IRVDGWP

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00376 Dephospho_CoA_kinase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001977 Depp_CoAkinase
    IPR007344 GrpB/CoaE
    IPR027417 P-loop_NTPase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01121 CoaE, 1 hit
    PF04229 GrpB, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52540 SSF52540, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00152 TIGR00152, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51219 DPCK, 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.

    P9WPA3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLRIGLTGGI GAGKSLLSTT FSQCGGIVVD GDVLAREVVQ PGTEGLASLV
    60 70 80 90 100
    DAFGRDILLA DGALDRQALA AKAFRDDESR GVLNGIVHPL VARRRSEIIA
    110 120 130 140 150
    AVSGDAVVVE DIPLLVESGM APLFPLVVVV HADVELRVRR LVEQRGMAEA
    160 170 180 190 200
    DARARIAAQA SDQQRRAVAD VWLDNSGSPE DLVRRARDVW NTRVQPFAHN
    210 220 230 240 250
    LAQRQIARAP ARLVPADPSW PDQARRIVNR LKIACGHKAL RVDHIGSTAV
    260 270 280 290 300
    SGFPDFLAKD VIDIQVTVES LDVADELAEP LLAAGYPRLE HITQDTEKTD
    310 320 330 340 350
    ARSTVGRYDH TDSAALWHKR VHASADPGRP TNVHLRVHGW PNQQFALLFV
    360 370 380 390 400
    DWLAANPGAR EDYLTVKCDA DRRADGELAR YVTAKEPWFL DAYQRAWEWA

    DAVHWRP
    Length:407
    Mass (Da):44,669
    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:i166F7A3052943DD7
    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: CCP44395.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    E70559

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_216147.1, NC_000962.3
    WP_003408069.1, NZ_NVQJ01000016.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CCP44395; CCP44395; Rv1631

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    885165

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv1631
    mtv:RVBD_1631

    <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: CCP44395.1
    PIRiE70559
    RefSeqiNP_216147.1, NC_000962.3
    WP_003408069.1, NZ_NVQJ01000016.1

    3D structure databases

    SMRiP9WPA3
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv1631

    Proteomic databases

    PaxDbiP9WPA3

    Genome annotation databases

    EnsemblBacteriaiCCP44395; CCP44395; Rv1631
    GeneIDi885165
    KEGGimtu:Rv1631
    mtv:RVBD_1631

    Organism-specific databases

    TubercuListiRv1631

    Phylogenomic databases

    eggNOGiENOG4108ZQD Bacteria
    COG0237 LUCA
    COG2320 LUCA
    KOiK00859
    OMAiIRVDGWP

    Enzyme and pathway databases

    UniPathwayiUPA00241;UER00356
    BioCyciMTBH37RV:G185E-5820-MONOMER

    Family and domain databases

    HAMAPiMF_00376 Dephospho_CoA_kinase, 1 hit
    InterProiView protein in InterPro
    IPR001977 Depp_CoAkinase
    IPR007344 GrpB/CoaE
    IPR027417 P-loop_NTPase
    PfamiView protein in Pfam
    PF01121 CoaE, 1 hit
    PF04229 GrpB, 1 hit
    SUPFAMiSSF52540 SSF52540, 1 hit
    TIGRFAMsiTIGR00152 TIGR00152, 1 hit
    PROSITEiView protein in PROSITE
    PS51219 DPCK, 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 nameiCOAE_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: P9WPA3
    Secondary accession number(s): L0T8U1, O06148, P63826
    <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: October 16, 2019
    This is version 28 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

    Complete proteome, Reference proteome

    Documents

    1. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries
    2. SIMILARITY comments
      Index of protein domains and families
    3. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    4. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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