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Protein

Glucan 1,3-beta-glucosidase 2

Gene

exg2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 sitei338 – 3381Proton donorBy similarity
Active sitei439 – 4391NucleophileBy similarity

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. fungal-type cell wall beta-glucan biosynthetic process Source: PomBase
  3. regulation of cell shape Source: PomBase
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 2 (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase 2
Gene namesi
Name:exg2
ORF Names:SPAC12B10.11
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC12B10.11.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: PomBase
  2. extracellular region Source: UniProtKB-SubCell
  3. integral component of membrane Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 47Sequence AnalysisPRO_0000007895
Signal peptidei1 – ?Sequence Analysis
Chaini48 – 570523Glucan 1,3-beta-glucosidase 2PRO_0000007896Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

BioGridi279425. 1 interaction.
STRINGi4896.SPAC12B10.11-1.

Structurei

3D structure databases

ProteinModelPortaliQ10444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ10444.
KOiK01210.
OMAiGHWAVQV.
OrthoDBiEOG7ZPNTV.
PhylomeDBiQ10444.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

Q10444-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNLLEAESS CDSKSLGVDD FTSKRCREID KKALLITILL TFFVSLCVFL
60 70 80 90 100
SIILPLIFLV IIPHAQSDRK IKDTNMETTN LGVNIIDEIF NSTQVPEWAK
110 120 130 140 150
NSLLDTNTWL DTSDFNTSFT NETFAGLYTM GIFDKYDDSV QANPNVPPLN
160 170 180 190 200
EPFPYGRLPI RGVNLGGWLS MEPFITPSFF QVKNETAYLV KDELSLHAYL
210 220 230 240 250
GENATSVIEN HYNTFVTKQT FYEIREAGLD HVRITFPYWI LYSNEITNVS
260 270 280 290 300
GIGWRYLLRS IEWAREQGLR VNLDLHAAPG NQNSWNHGGY LNQMEWLDGT
310 320 330 340 350
VKGEENSQFT LKIHERLASF FSQKRYRNVV TIYGALNEPN FFVLDEHKIT
360 370 380 390 400
DWHKQAYAVI RQSNFTGLIS LSDGFRGPGN WEDHFDPFHF PNILIDVHRY
410 420 430 440 450
IIFNDFLIGL RPKDKLNVIC KSWNEEMKLK AKLPTIIGEW SLADTDCAKF
460 470 480 490 500
LNNVGEGARW DGTFTPNGGV ASCSEKVGCR CDFANQDPEN YEDSYRKFLY
510 520 530 540 550
ALATSQIETF DKTWGWFYWN WDTENATQWS YKKSWLAGLL PRLAYSTTKD
560 570
FNCSMLDSKS FMEFDEQSEF
Length:570
Mass (Da):65,687
Last modified:September 30, 1996 - v1
Checksum:i2B6E66A35AA7E1E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA94701.1.
PIRiT37578.
RefSeqiNP_594643.1. NM_001020071.1.

Genome annotation databases

EnsemblFungiiSPAC12B10.11.1; SPAC12B10.11.1:pep; SPAC12B10.11.
GeneIDi2542987.
KEGGispo:SPAC12B10.11.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA94701.1.
PIRiT37578.
RefSeqiNP_594643.1. NM_001020071.1.

3D structure databases

ProteinModelPortaliQ10444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279425. 1 interaction.
STRINGi4896.SPAC12B10.11-1.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC12B10.11.1; SPAC12B10.11.1:pep; SPAC12B10.11.
GeneIDi2542987.
KEGGispo:SPAC12B10.11.

Organism-specific databases

PomBaseiSPAC12B10.11.

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ10444.
KOiK01210.
OMAiGHWAVQV.
OrthoDBiEOG7ZPNTV.
PhylomeDBiQ10444.

Miscellaneous databases

NextBioi20804020.

Family and domain databases

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

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiEXG2_SCHPO
AccessioniPrimary (citable) accession number: Q10444
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: September 30, 1996
Last modified: March 31, 2015
This is version 102 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

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.