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Q9URU6

- EXG1_SCHPO

UniProt

Q9URU6 - EXG1_SCHPO

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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: 3 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei213 – 2131Proton donorBy similarity
Active sitei312 – 3121NucleophileBy similarity

GO - Molecular functioni

  1. glucan endo-1,6-beta-glucosidase activity Source: PomBase

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. fungal-type cell wall beta-glucan metabolic process 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 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
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC1105.05.

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. barrier septum Source: PomBase
  2. extracellular region Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 407385Glucan 1,3-beta-glucosidase 1PRO_0000007887Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi295 ↔ 406By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

MaxQBiQ9URU6.

Interactioni

Protein-protein interaction databases

BioGridi276537. 20 interactions.
STRINGi4896.SPBC1105.05-1.

Structurei

3D structure databases

ProteinModelPortaliQ9URU6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ9URU6.
KOiK01210.
OMAiIINEPNT.
OrthoDBiEOG7JT75H.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781Q → E in BAA13789. (PubMed:9501991)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CU329671 Genomic DNA. Translation: CAB50968.1 .
D89127 mRNA. Translation: BAA13789.1 .
PIRi T39282.
T42370.
RefSeqi NP_596461.1. NM_001022380.2.

3D structure databases

ProteinModelPortali Q9URU6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 276537. 20 interactions.
STRINGi 4896.SPBC1105.05-1.

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

Proteomic databases

MaxQBi Q9URU6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC1105.05.1 ; SPBC1105.05.1:pep ; SPBC1105.05 .
GeneIDi 2539993.
KEGGi spo:SPBC1105.05.

Organism-specific databases

PomBasei SPBC1105.05.

Phylogenomic databases

eggNOGi COG2730.
HOGENOMi HOG000114462.
InParanoidi Q9URU6.
KOi K01210.
OMAi IINEPNT.
OrthoDBi EOG7JT75H.
PhylomeDBi Q9URU6.

Miscellaneous databases

NextBioi 20801136.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00150. Cellulase. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-407.
    Strain: PR745.

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 29, 2014
This is version 91 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