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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: -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

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCell 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
Ordered Locus Names:CAALFM_C102630CA
ORF Names:CaO19.10469, CaO19.2952
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Chromosome 1

Organism-specific databases

CGDiCAL0000181572 EXG2

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; Source: COMPARTMENTS

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...) asparagineSequence analysis1
Glycosylationi29N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi63N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi104N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi187N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi193N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi254N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi285N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi288N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi318N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi451N-linked (GlcNAc...) asparagineSequence 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
SMRiQ5AIA1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiQ5AIA1
OMAiHHEYQVF
OrthoDBiEOG092C22A6

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

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
DCAPWLNGVG LGSRYEGTAP YTNDRVGSCA EFNKSPDKWS KKQKKDYRRF
410 420 430 440 450
VEMQLYEYST NSQGWIFWCW KTEGATEWDF RALVKNGIMP QPLDNYKYVK
460 470
NGTDTSSASA IASNKMTLLL AFLLVILVI
Length:479
Mass (Da):54,534
Last modified:May 10, 2017 - v2
Checksum:i49580CA741366197
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP017623 Genomic DNA Translation: AOW25944.1
RefSeqiXP_721451.2, XM_716358.2

Genome annotation databases

EnsemblFungiiAOW25944; AOW25944; CAALFM_C102630CA
GeneIDi3636816
KEGGical:CAALFM_C102630CA

Similar proteinsi

Entry informationi

Entry nameiEXG2_CANAL
AccessioniPrimary (citable) accession number: Q5AIA1
Secondary accession number(s): A0A1D8PCS8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 22, 2014
Last sequence update: May 10, 2017
Last modified: March 28, 2018
This is version 82 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome