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Protein

Chlorophyll a-b binding protein AB80, chloroplastic

Gene

AB80

Organism
Pisum sativum (Garden pea)
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

The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.1 Publication
May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.1 Publication

<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

Note: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi61Magnesium (chlorophyll-b 1 axial ligand); via carbonyl oxygenCombined sources1 Publication1
<p>This subsection of the ‘Function’ 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 sitei83Chlorophyll-a 1; via amide nitrogenCombined sources1 Publication1
Binding sitei89Chlorophyll-a 1Combined sources1 Publication1
Metal bindingi102Magnesium (chlorophyll-a 1 axial ligand)Combined sources1 Publication1
Metal bindingi105Magnesium (chlorophyll-a 2 axial ligand)Combined sources1 Publication1
Binding sitei107Chlorophyll-b 2Combined sources1 Publication1
Binding sitei140Chlorophyll-a 3Combined sources1 Publication1
Binding sitei150Chlorophyll-a 3; via amide nitrogenCombined sources1 Publication1
Metal bindingi156Magnesium (chlorophyll-b 2 axial ligand); via carbonyl oxygenCombined sources1 Publication1
Binding sitei160Chlorophyll-b 3Combined sources1 Publication1
Binding sitei168Chlorophyll-b 4 or chlorophyll-b 5Combined sources1 Publication1
Metal bindingi176Magnesium (chlorophyll-b 3 axial ligand)Combined sources1 Publication1
Binding sitei179Chlorophyll-b 4Combined sources1 Publication1
Binding sitei185Chlorophyll-b 2; via amide nitrogenCombined sources1 Publication1
Binding sitei216Chlorophyll-a 5Combined sources1 Publication1
Metal bindingi217Magnesium (chlorophyll-a 3 axial ligand)Combined sources1 Publication1
Metal bindingi220Magnesium (chlorophyll-a 4 axial ligand)Combined sources1 Publication1
Binding sitei222Chlorophyll-a 1Combined sources1 Publication1
Metal bindingi234Magnesium (chlorophyll-a 5 axial ligand)Combined sources1 Publication1
Metal bindingi249Magnesium (chlorophyll-a 6 axial ligand)Combined sources1 Publication1
Binding sitei258Chlorophyll-a 6; via amide nitrogenCombined sources1 Publication1
Binding sitei265Chlorophyll-b 5; via carbonyl oxygenCombined sources1 Publication1

<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

Biological processPhotosynthesis
LigandChlorophyll, Chromophore, Magnesium, 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:
Chlorophyll a-b binding protein AB80, chloroplastic
Alternative name(s):
LHCII type I CAB-AB80
Short name:
LHCP
<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:AB80
<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>OrganismiPisum sativum (Garden pea)
<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 identifieri3888 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeHologaleginaIRL cladeFabeaePisum

<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 Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei103 – 123HelicalSequence analysisAdd BLAST21
Transmembranei155 – 175HelicalSequence analysisAdd BLAST21
Transmembranei223 – 243HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Chloroplast, Membrane, Photosystem I, Photosystem II, Plastid, Thylakoid

<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>Mutagenesisi102E → A: Decreases binding to chlorophyll-b. 2 Publications1
Mutagenesisi102E → Q: Causes a strong decrease in LHCII complex stability; when associated with L-105. 2 Publications1
Mutagenesisi105H → A: Decreases binding to chlorophyll-a. 2 Publications1
Mutagenesisi105H → F: Decreases binding to chlorophyll, more chlorophyll-a than chlorophyll-b is lost. Causes a strong decrease in LHCII complex stability. 2 Publications1
Mutagenesisi105H → L: Decreases binding to chlorophyll, more chlorophyll-a than chlorophyll-b is lost. Causes a strong decrease in LHCII complex stability. Complex stability is reduced further; when associated with Q-102. 2 Publications1
Mutagenesisi114 – 115LG → VF: Decreases binding to chlorophyll-b. 1 Publication2
Mutagenesisi168Q → A: Decreases binding to chlorophyll-b. 2 Publications1
Mutagenesisi168Q → E or S: Decreases binding to chlorophyll, more chlorophyll-b than chlorophyll-a is lost. Causes a strong decrease in LHCII complex stability. 2 Publications1
Mutagenesisi176E → A: Decreases binding to chlorophyll-b. 1 Publication1
Mutagenesisi217E → A: Decreases binding to chlorophyll-a. 1 Publication1
Mutagenesisi220N → A: Decreases binding to chlorophyll-a and possibly chlorophyll-b. 1 Publication1
Mutagenesisi234Q → E or S: Decreases binding to chlorophyll. Causes a moderate decrease in LHCII complex stability. 2 Publications1
Mutagenesisi234Q → L: Decreases binding to chlorophyll-a. 2 Publications1
Mutagenesisi249H → A: Decreases binding to chlorophyll-a. 2 Publications1
Mutagenesisi249H → F or L: Decreases binding to chlorophyll-a and chlorophyll-b. Causes a minor decrease in LHCII complex stability. 2 Publications1

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 37ChloroplastCuratedAdd BLAST37
<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_000000368038 – 269Chlorophyll a-b binding protein AB80, chloroplasticAdd BLAST232

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei38N2-acetylarginineBy similarity1

<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

Photoregulated by reversible phosphorylation of its threonine residues.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P07371

<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

The LHC complex consists of chlorophyll a-b binding proteins.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
CAOO222657EBI-2353186,EBI-780656From Arabidopsis thaliana.

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-40897N

Protein interaction database and analysis system

More...
IntActi
P07371, 3 interactors

<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

1269
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P07371

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

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SMRi
P07371

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P07371

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

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

The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.

<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

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.3460.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001344 Chloro_AB-bd_pln
IPR022796 Chloroa_b-bind
IPR023329 Chlorophyll_a/b-bd_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR21649 PTHR21649, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00504 Chloroa_b-bind, 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>.<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.

P07371-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAASSSSSMA LSSPTLAGKQ LKLNPSSQEL GAARFTMRKS ATTKKVASSG
60 70 80 90 100
SPWYGPDRVK YLGPFSGESP SYLTGEFPGD YGWDTAGLSA DPETFSKNRE
110 120 130 140 150
LEVIHSRWAM LGALGCVFPE LLSRNGVKFG EAVWFKAGSQ IFSEGGLDYL
160 170 180 190 200
GNPSLVHAQS ILAIWATQVI LMGAVEGYRI AGGPLGEVVD PLYPGGSFDP
210 220 230 240 250
LGLADDPEAF AELKVKELKN GRLAMFSMFG FFVQAIVTGK GPLENLADHL
260
ADPVNNNAWS YATNFVPGK
Length:269
Mass (Da):28,654
Last modified:April 1, 1988 - 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:iD2BD6A9EFC4BAF77
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
K02067 Genomic DNA Translation: AAA33651.1
M64619 Genomic DNA Translation: AAA63413.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A26780 CDPM80

<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
K02067 Genomic DNA Translation: AAA33651.1
M64619 Genomic DNA Translation: AAA63413.1
PIRiA26780 CDPM80

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VCRX-ray9.50A38-269[»]
2BHWX-ray2.50A/B/C38-269[»]
ProteinModelPortaliP07371
SMRiP07371
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-40897N
IntActiP07371, 3 interactors

Proteomic databases

PRIDEiP07371

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP07371

Family and domain databases

Gene3Di1.10.3460.10, 1 hit
InterProiView protein in InterPro
IPR001344 Chloro_AB-bd_pln
IPR022796 Chloroa_b-bind
IPR023329 Chlorophyll_a/b-bd_dom_sf
PANTHERiPTHR21649 PTHR21649, 1 hit
PfamiView protein in Pfam
PF00504 Chloroa_b-bind, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiCB22_PEA
<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: P07371
Secondary accession number(s): P35389, Q53X02
<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 1, 1988
Last sequence update: April 1, 1988
Last modified: September 12, 2018
This is version 107 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 programPlant 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, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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