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Protein

Glucan 1,3-beta-glucosidase 1

Gene

exg1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei213Proton donorBy similarity1
Active sitei312NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

  • fungal-type cell wall beta-glucan metabolic process Source: PomBase
  • fungal-type cell wall disassembly involved in conjugation with cellular fusion Source: PomBase
  • glucan catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan 1,3-beta-glucosidase 1 (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase
Gene namesi
Name:exg1
ORF Names:SPBC1105.05
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1105.05.
PomBaseiSPBC1105.05. exg1.

Subcellular locationi

GO - Cellular componenti

  • actin fusion focus Source: PomBase
  • barrier septum Source: PomBase
  • cell surface Source: GO_Central
  • extracellular region Source: PomBase
  • fungal-type cell wall Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000000788723 – 407Glucan 1,3-beta-glucosidase 1Add BLAST385

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi295 ↔ 406By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

MaxQBiQ9URU6.
PRIDEiQ9URU6.

Interactioni

Protein-protein interaction databases

BioGridi276537. 19 interactors.

Structurei

3D structure databases

ProteinModelPortaliQ9URU6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000114462.
InParanoidiQ9URU6.
KOiK01210.
OMAiMDVHRYQ.
OrthoDBiEOG092C22A6.
PhylomeDBiQ9URU6.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9URU6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSFTSVFSF FLHALLLKTA FSYVIKRNNP VFDYTSEKVR GVNIGGWLVL
60 70 80 90 100
ENWITPQLFT QFSSMSNPPT DEWGFCEVLG ADEAASQLAA HYSSFYTESD
110 120 130 140 150
FATIASWGVN VLRIPIGYWA FNVVDGEPYV QGQEYWLDQA LTWAEQYGLK
160 170 180 190 200
VWIDLHGVPG SQNGFENSGK TGSIGWQQND TVTRTLDIIT YVANKYTQSQ
210 220 230 240 250
YASVVIGIET VNEPLGYGLD MDQLKQYDLD AYNIVNPLSS SVATIIHDAY
260 270 280 290 300
VDLSIWDYGV VSPSSYNLVM DVHRYQLYES DECSKTLDDH LSDVCSIGDS
310 320 330 340 350
IASSPYITVT GEWSGTLADC TIFEEGVDSS TFIGPNSGDI STWTDEYKGA
360 370 380 390 400
VRLFIETQLD QFERGAGWIY WTAKTGGPSP TWDMGLLIEY GVFPQPFTDR

QYSSYCG
Length:407
Mass (Da):45,506
Last modified:May 1, 2000 - v1
Checksum:i4F2C717A4C65ECF9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti178Q → E in BAA13789 (PubMed:9501991).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB50968.1.
D89127 mRNA. Translation: BAA13789.1.
PIRiT39282.
T42370.
RefSeqiNP_596461.1. NM_001022380.2.

Genome annotation databases

EnsemblFungiiSPBC1105.05.1; SPBC1105.05.1:pep; SPBC1105.05.
GeneIDi2539993.
KEGGispo:SPBC1105.05.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB50968.1.
D89127 mRNA. Translation: BAA13789.1.
PIRiT39282.
T42370.
RefSeqiNP_596461.1. NM_001022380.2.

3D structure databases

ProteinModelPortaliQ9URU6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276537. 19 interactors.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Proteomic databases

MaxQBiQ9URU6.
PRIDEiQ9URU6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1105.05.1; SPBC1105.05.1:pep; SPBC1105.05.
GeneIDi2539993.
KEGGispo:SPBC1105.05.

Organism-specific databases

EuPathDBiFungiDB:SPBC1105.05.
PomBaseiSPBC1105.05. exg1.

Phylogenomic databases

HOGENOMiHOG000114462.
InParanoidiQ9URU6.
KOiK01210.
OMAiMDVHRYQ.
OrthoDBiEOG092C22A6.
PhylomeDBiQ9URU6.

Miscellaneous databases

PROiQ9URU6.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEXG1_SCHPO
AccessioniPrimary (citable) accession number: Q9URU6
Secondary accession number(s): P78778
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 2000
Last modified: October 5, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.