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Protein

Glucan 1,3-beta-glucosidase 2

Gene

EXG2

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. EXG2 is not heavily involved in the exoglucanase function of the adhesion process.1 Publication

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 sitei227Proton donorBy similarity1
Active sitei306NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan 1,3-beta-glucosidase 2 (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase 2
Gene namesi
Name:EXG2
ORF Names:CaO19.10469, CaO19.2952
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0000181572. EXG2.

Subcellular locationi

GO - Cellular componenti

  • anchored component of plasma membrane Source: CGD
  • extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000042485522 – 456Glucan 1,3-beta-glucosidase 2Add BLAST435
PropeptideiPRO_0000424856457 – 479Removed in mature formSequence analysisAdd BLAST23

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi25N-linked (GlcNAc...)Sequence analysis1
Glycosylationi29N-linked (GlcNAc...)Sequence analysis1
Glycosylationi63N-linked (GlcNAc...)Sequence analysis1
Glycosylationi104N-linked (GlcNAc...)Sequence analysis1
Glycosylationi187N-linked (GlcNAc...)Sequence analysis1
Glycosylationi193N-linked (GlcNAc...)Sequence analysis1
Glycosylationi254N-linked (GlcNAc...)Sequence analysis1
Glycosylationi285N-linked (GlcNAc...)Sequence analysis1
Glycosylationi288N-linked (GlcNAc...)Sequence analysis1
Glycosylationi318N-linked (GlcNAc...)Sequence analysis1
Glycosylationi451N-linked (GlcNAc...)Sequence analysis1
Lipidationi456GPI-anchor amidated serineSequence analysis1

Post-translational modificationi

Predicted to be a substrate for cleavage by KEX2.

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PRIDEiQ5AIA1.

Expressioni

Inductioni

Induced during cell wall regeneration and repressed by HAP43.2 Publications

Structurei

3D structure databases

ProteinModelPortaliQ5AIA1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiQ5AIA1.
KOiK01210.
OrthoDBiEOG092C22A6.

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.

Q5AIA1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLFLIHLMA LCCMFVAEVA CEQFNSTSNS SSAQSSLIDF QYKGVSIGGW
60 70 80 90 100
LVLEPYITPS LFNATLSSGE TWTDLPVDEY HFCEKLGAKE AEKRLTDHWE
110 120 130 140 150
SMYNETDFKQ IKEAGLNMVR IPIGYWSFEK LEGDPYVSGA QDYLDKAIEW
160 170 180 190 200
SHANDLKVMI DLHGAPNTQN GFDNSGLRNL GYPGWQNKTE YVNHTYKVLQ
210 220 230 240 250
QMFQKYGTGK YASDYKNTII GIEVLNEPLN PNMDKLKEFY IESYNDGREI
260 270 280 290 300
QVINNTIFFQ EAFQPIGYWD SFLEKGEIKV TETSNGTNHT TTKKADFKNI
310 320 330 340 350
IIDHHHYEVF TESQVASNVS THLENIKNYA SAIGKEKAKA IVGEWSAALT
360 370 380 390 400
DCAPWLNGIG LGSRYEGTAP YTNDRVGSCA EFNKSPDKWS KKQKKDYRRF
410 420 430 440 450
VEMQLYEYST NSQGWIFWCW KTEGATEWDF RALVKNGIMP QPLDNYKYVK
460 470
NGTDTSSASA IASNKMTLLL AFLLVILVI
Length:479
Mass (Da):54,548
Last modified:April 26, 2005 - v1
Checksum:i44C813A741367E97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000017 Genomic DNA. Translation: EAL02371.1.
AACQ01000015 Genomic DNA. Translation: EAL02652.1.
RefSeqiXP_721179.1. XM_716086.1.
XP_721451.1. XM_716358.1.

Genome annotation databases

EnsemblFungiiEAL02371; EAL02371; CaO19.10469.
EAL02652; EAL02652; CaO19.2952.
GeneIDi3636816.
3637086.
KEGGical:CaO19.10469.
cal:CaO19.2952.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000017 Genomic DNA. Translation: EAL02371.1.
AACQ01000015 Genomic DNA. Translation: EAL02652.1.
RefSeqiXP_721179.1. XM_716086.1.
XP_721451.1. XM_716358.1.

3D structure databases

ProteinModelPortaliQ5AIA1.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ5AIA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAL02371; EAL02371; CaO19.10469.
EAL02652; EAL02652; CaO19.2952.
GeneIDi3636816.
3637086.
KEGGical:CaO19.10469.
cal:CaO19.2952.

Organism-specific databases

CGDiCAL0000181572. EXG2.

Phylogenomic databases

InParanoidiQ5AIA1.
KOiK01210.
OrthoDBiEOG092C22A6.

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 nameiEXG2_CANAL
AccessioniPrimary (citable) accession number: Q5AIA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 22, 2014
Last sequence update: April 26, 2005
Last modified: November 2, 2016
This is version 73 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. Candida albicans
    Candida albicans: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  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.