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Protein

Glucan 1,3-beta-glucosidase 2

Gene

EXG2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei254 – 2541Proton donorBy similarity
Active sitei334 – 3341NucleophileBy similarity

GO - Molecular functioni

  1. glucan exo-1,3-beta-glucosidase activity Source: SGD

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. fungal-type cell wall organization Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciYEAST:YDR261C-MONOMER.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

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:YDR261C
ORF Names:YD9320A.12C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR261c.
SGDiS000002669. EXG2.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. fungal-type cell wall Source: SGD
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 562540Glucan 1,3-beta-glucosidase 2PRO_0000007894Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi539 – 5391N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP52911.
PaxDbiP52911.

Expressioni

Gene expression databases

GenevestigatoriP52911.

Interactioni

Protein-protein interaction databases

BioGridi32311. 19 interactions.
IntActiP52911. 1 interaction.
STRINGi4932.YDR261C.

Structurei

3D structure databases

ProteinModelPortaliP52911.
SMRiP52911. Positions 51-477.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
GeneTreeiENSGT00390000009809.
HOGENOMiHOG000114462.
InParanoidiP52911.
KOiK01210.
OMAiGARWDNT.
OrthoDBiEOG7JT75H.

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.

P52911-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLKSFFFSA FLVLCLSKFT QGVGTTEKEE SLSPLELNIL QNKFASYYAN
60 70 80 90 100
DTITVKGITI GGWLVTEPYI TPSLYRNATS LAKQQNSSSN ISIVDEFTLC
110 120 130 140 150
KTLGYNTSLT LLDNHFKTWI TEDDFEQIKT NGFNLVRIPI GYWAWKQNTD
160 170 180 190 200
KNLYIDNITF NDPYVSDGLQ LKYLNNALEW AQKYELNVWL DLHGAPGSQN
210 220 230 240 250
GFDNSGERIL YGDLGWLRLN NTKELTLAIW RDMFQTFLNK GDKSPVVGIQ
260 270 280 290 300
IVNEPLGGKI DVSDITEMYY EAFDLLKKNQ NSSDNTTFVI HDGFQGIGHW
310 320 330 340 350
NLELNPTYQN VSHHYFNLTG ANYSSQDILV DHHHYEVFTD AQLAETQFAR
360 370 380 390 400
IENIINYGDS IHKELSFHPA VVGEWSGAIT DCATWLNGVG VGARYDGSYY
410 420 430 440 450
NTTLFTTNDK PVGTCISQNS LADWTQDYRD RVRQFIEAQL ATYSSKTTGW
460 470 480 490 500
IFWNWKTEDA VEWDYLKLKE ANLFPSPFDN YTYFKADGSI EEKFSSSLSA
510 520 530 540 550
QAFPRTTSSV LSSTTTSRKS KNAAISNKLT TSQLLPIKNM SLTWKASVCA
560
LAITIAALCA SL
Length:562
Mass (Da):63,508
Last modified:October 1, 1996 - v1
Checksum:i5814509CC3D93F73
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46870 Genomic DNA. Translation: CAA86950.1.
Z70202 Genomic DNA. Translation: CAA94100.1.
Z68329 Genomic DNA. Translation: CAA92719.1.
BK006938 Genomic DNA. Translation: DAA12101.1.
PIRiS55516.
RefSeqiNP_010547.1. NM_001180569.1.

Genome annotation databases

EnsemblFungiiYDR261C; YDR261C; YDR261C.
GeneIDi851848.
KEGGisce:YDR261C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46870 Genomic DNA. Translation: CAA86950.1.
Z70202 Genomic DNA. Translation: CAA94100.1.
Z68329 Genomic DNA. Translation: CAA92719.1.
BK006938 Genomic DNA. Translation: DAA12101.1.
PIRiS55516.
RefSeqiNP_010547.1. NM_001180569.1.

3D structure databases

ProteinModelPortaliP52911.
SMRiP52911. Positions 51-477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32311. 19 interactions.
IntActiP52911. 1 interaction.
STRINGi4932.YDR261C.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Proteomic databases

MaxQBiP52911.
PaxDbiP52911.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR261C; YDR261C; YDR261C.
GeneIDi851848.
KEGGisce:YDR261C.

Organism-specific databases

CYGDiYDR261c.
SGDiS000002669. EXG2.

Phylogenomic databases

eggNOGiCOG2730.
GeneTreeiENSGT00390000009809.
HOGENOMiHOG000114462.
InParanoidiP52911.
KOiK01210.
OMAiGARWDNT.
OrthoDBiEOG7JT75H.

Enzyme and pathway databases

BioCyciYEAST:YDR261C-MONOMER.

Miscellaneous databases

NextBioi969766.

Gene expression databases

GenevestigatoriP52911.

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...

Publicationsi

« Hide 'large scale' publications
  1. "EXG2, a gene coding for a exo-1,3-B-glucanase with a GPI anchor attachment site in the carboxy terminus."
    Correa J., Vazquez de Aldana C., San Segundo P., del Rey F.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204510 / AB320.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEXG2_YEAST
AccessioniPrimary (citable) accession number: P52911
Secondary accession number(s): D6VSP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2410 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.