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UniProtKB - P23776 (EXG1_YEAST)

Entry version 174 (08 May 2019)
Sequence version 1 (01 Nov 1991)
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Protein

Glucan 1,3-beta-glucosidase I/II

Gene

EXG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme hydrolyzes both 1,3-beta- and 1,6-beta-linkages and even has beta-glucosidase activity. It could also function biosynthetically as a transglycosylase.

Miscellaneous

Present with 4280 molecules/cell in log phase SD medium.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

  • Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose. EC:3.2.1.58

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 sitei232Proton donorBy similarity1
Active sitei334NucleophileBy 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

  • glucan exo-1,3-beta-glucosidase activity Source: SGD
Complete GO annotation on QuickGO ...

GO - Biological processi

  • cellular glucan metabolic process Source: SGD
  • fungal-type cell wall organization Source: SGD
  • glucan catabolic process Source: GO_Central
Complete GO annotation on QuickGO ...

<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 processCell wall biogenesis/degradation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		YEAST:YLR300W-MONOMER

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		GH5 Glycoside Hydrolase Family 5

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

More...mycoCLAPi		EXG5A_YEAST

<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:
Glucan 1,3-beta-glucosidase I/II (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase I/II
Soluble cell wall protein 6
<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:EXG1
Synonyms:BGL1, SCW6
Ordered Locus Names:YLR300W
ORF Names:L8003.3
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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
  • UP000002311 <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 XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YLR300W

Saccharomyces Genome Database

More...SGDi		S000004291 EXG1

<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

Cell wall, 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 – 19Sequence analysisAdd BLAST19
<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_000000789220 – 404 PublicationsAdd BLAST21
<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_000000789341 – 448Glucan 1,3-beta-glucosidase I/IIAdd BLAST408

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>Glycosylationi165N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi325N-linked (GlcNAc...) asparagine1 Publication1

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P23776

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

More...PaxDbi		P23776

PRoteomics IDEntifications database

More...PRIDEi		P23776

2D gel databases

2-DE database at Universidad Complutense de Madrid

More...COMPLUYEAST-2DPAGEi		P23776

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P23776

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P23776

<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

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		31564, 109 interactors

Database of interacting proteins

More...DIPi		DIP-6384N

Protein interaction database and analysis system

More...IntActi		P23776, 3 interactors

STRING: functional protein association networks

More...STRINGi		4932.YLR300W

<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

1448
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		P23776

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P23776

<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 5 (cellulase A) family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

Ensembl GeneTree

More...GeneTreei		ENSGT00940000176313

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000114462

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P23776

KEGG Orthology (KO)

More...KOi		K01210

Identification of Orthologs from Complete Genome Data

More...OMAi		IRFPYGT

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001547 Glyco_hydro_5
IPR018087 Glyco_hydro_5_CS
IPR017853 Glycoside_hydrolase_SF

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00150 Cellulase, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51445 SSF51445, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00659 GLYCOSYL_HYDROL_F5, 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.

P23776-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLSLKTLLCT LLTVSSVLAT PVPARDPSSI QFVHEENKKR YYDYDHGSLG 
        60         70         80         90        100
EPIRGVNIGG WLLLEPYITP SLFEAFRTND DNDEGIPVDE YHFCQYLGKD 
       110        120        130        140        150
LAKSRLQSHW STFYQEQDFA NIASQGFNLV RIPIGYWAFQ TLDDDPYVSG 
       160        170        180        190        200
LQESYLDQAI GWARNNSLKV WVDLHGAAGS QNGFDNSGLR DSYKFLEDSN 
       210        220        230        240        250
LAVTTNVLNY ILKKYSAEEY LDTVIGIELI NEPLGPVLDM DKMKNDYLAP 
       260        270        280        290        300
AYEYLRNNIK SDQVIIIHDA FQPYNYWDDF MTENDGYWGV TIDHHHYQVF 
       310        320        330        340        350
ASDQLERSID EHIKVACEWG TGVLNESHWT VCGEFAAALT DCTKWLNSVG 
       360        370        380        390        400
FGARYDGSWV NGDQTSSYIG SCANNDDIAY WSDERKENTR RYVEAQLDAF 
       410        420        430        440 
EMRGGWIIWC YKTESSLEWD AQRLMFNGLF PQPLTDRKYP NQCGTISN
Length:448
Mass (Da):51,311
Last modified:November 1, 1991 - 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:iF0AD512E410375BD
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 conflicti41Y → Q AA sequence (PubMed:9748433).Curated1
Sequence conflicti46H → G AA sequence (PubMed:9748433).Curated1
Sequence conflicti77R → H AA sequence (PubMed:2125957).Curated1

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
M34341 Genomic DNA Translation: AAA34599.1
U17243 Genomic DNA Translation: AAB67345.1
AY693069 Genomic DNA Translation: AAT93088.1
BK006945 Genomic DNA Translation: DAA09610.1

Protein sequence database of the Protein Information Resource

More...PIRi		JN0118

NCBI Reference Sequences

More...RefSeqi		NP_013403.1, NM_001182188.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YLR300W_mRNA; YLR300W_mRNA; YLR300W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		851007

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YLR300W

<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
M34341 Genomic DNA Translation: AAA34599.1
U17243 Genomic DNA Translation: AAB67345.1
AY693069 Genomic DNA Translation: AAT93088.1
BK006945 Genomic DNA Translation: DAA09610.1
PIRiJN0118
RefSeqiNP_013403.1, NM_001182188.1

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
1H4PX-ray1.75A/B41-448[»]
SMRiP23776
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31564, 109 interactors
DIPiDIP-6384N
IntActiP23776, 3 interactors
STRINGi4932.YLR300W

Protein family/group databases

CAZyiGH5 Glycoside Hydrolase Family 5
mycoCLAPiEXG5A_YEAST

PTM databases

iPTMnetiP23776

2D gel databases

COMPLUYEAST-2DPAGEiP23776

Proteomic databases

MaxQBiP23776
PaxDbiP23776
PRIDEiP23776

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR300W_mRNA; YLR300W_mRNA; YLR300W
GeneIDi851007
KEGGisce:YLR300W

Organism-specific databases

EuPathDBiFungiDB:YLR300W
SGDiS000004291 EXG1

Phylogenomic databases

GeneTreeiENSGT00940000176313
HOGENOMiHOG000114462
InParanoidiP23776
KOiK01210
OMAiIRFPYGT

Enzyme and pathway databases

BioCyciYEAST:YLR300W-MONOMER

Miscellaneous databases

EvolutionaryTraceiP23776
PMAP-CutDBiP23776

Protein Ontology

More...PROi		PR:P23776

Family and domain databases

InterProiView protein in InterPro
IPR001547 Glyco_hydro_5
IPR018087 Glyco_hydro_5_CS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00150 Cellulase, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00659 GLYCOSYL_HYDROL_F5, 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 nameiEXG1_YEAST
<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: P23776
Secondary accession number(s): D6VYU4, Q9UR92
<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: November 1, 1991
Last sequence update: November 1, 1991
Last modified: May 8, 2019
This is version 174 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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