Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9URU6

- EXG1_SCHPO

UniProt

Q9URU6 - EXG1_SCHPO

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. fungal-type cell wall beta-glucan metabolic process Source: PomBase

    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

    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.
    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

    MLSFTSVFSF FLHALLLKTA FSYVIKRNNP VFDYTSEKVR GVNIGGWLVL    50
    ENWITPQLFT QFSSMSNPPT DEWGFCEVLG ADEAASQLAA HYSSFYTESD 100
    FATIASWGVN VLRIPIGYWA FNVVDGEPYV QGQEYWLDQA LTWAEQYGLK 150
    VWIDLHGVPG SQNGFENSGK TGSIGWQQND TVTRTLDIIT YVANKYTQSQ 200
    YASVVIGIET VNEPLGYGLD MDQLKQYDLD AYNIVNPLSS SVATIIHDAY 250
    VDLSIWDYGV VSPSSYNLVM DVHRYQLYES DECSKTLDDH LSDVCSIGDS 300
    IASSPYITVT GEWSGTLADC TIFEEGVDSS TFIGPNSGDI STWTDEYKGA 350
    VRLFIETQLD QFERGAGWIY WTAKTGGPSP TWDMGLLIEY GVFPQPFTDR 400
    QYSSYCG 407
    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.
    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 1, 2014
    This is version 90 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