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A2QH21

- EGLC_ASPNC

UniProt

A2QH21 - EGLC_ASPNC

Protein

Probable glucan endo-1,3-beta-glucosidase eglC

Gene

eglC

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 41 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      Previous versions | rss
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    Functioni

    Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase By similarity.By similarity

    Catalytic activityi

    Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei128 – 1281NucleophileBy similarity
    Active sitei239 – 2391Proton donorBy similarity

    GO - Molecular functioni

    1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH17. Glycoside Hydrolase Family 17.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable glucan endo-1,3-beta-glucosidase eglC (EC:3.2.1.39)
    Alternative name(s):
    Endo-1,3-beta-glucanase eglC
    Laminarinase eglC
    Gene namesi
    Name:eglC
    ORF Names:An03g05290
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 6R

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity. Secretedcell wall By similarity
    Note: Covalently-linked GPI-modified cell wall protein.By similarity

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. cell wall Source: UniProtKB-SubCell
    3. extracellular region Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell wall, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 430412Probable glucan endo-1,3-beta-glucosidase eglCPRO_5000219799Add
    BLAST
    Propeptidei431 – 46030Removed in mature formSequence AnalysisPRO_0000395144Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi312 – 3121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
    Lipidationi430 – 4301GPI-anchor amidated serineSequence Analysis

    Post-translational modificationi

    The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer By similarity.By similarity

    Keywords - PTMi

    Glycoprotein, GPI-anchor, Lipoprotein

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi309 – 445137Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 17 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5309.
    HOGENOMiHOG000179527.
    OrthoDBiEOG7TBCCK.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    A2QH21-1 [UniParc]FASTAAdd to Basket

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    MQLAQLAAFA MTLATSEAAY QGFNYGNKFS DESSKFQADF EAEFKAAKNL    50
    VGTSGFTSAR LYTMIQAYST SDVIEAIPAA IAQDTSLLLG LWASGGGMDN 100
    EITALKTAIS QYGEELGKLV VGISVGSEDL YRNSVEGAEA DAGVGVNPDE 150
    LVEYIKEVRS VIAGTALADV SIGHVDTWDS WTNSSNSAVV EAVDWLGFDG 200
    YPFFQSSMAN SIDNAKTLFE ESVAKTKAVA GDKEVWITET GWPVSGDSQG 250
    DAVASIANAK TFWDEVGCPL FGNVNTWWYI LQDASPTTPN PSFGIVGSTL 300
    STTPLFDLSC KNSTTSSSSA VVSAAASSAA GSKAVGSSQA SSGAAAWATS 350
    ASGSAKPTFT VGRPGVNGTV FGNGTYPLRP SGSASARPSA GAISSGSGSS 400
    SSGSGSSGST GTSATSGQSS SSGSSAAAGS SSPAAFSGAS TLSGSLFGAV 450
    VAVFMTLAAL 460
    Length:460
    Mass (Da):46,347
    Last modified:June 15, 2010 - v2
    Checksum:iF7B5114CE78833B2
    GO

    Sequence cautioni

    The sequence CAK49181.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270057 Genomic DNA. Translation: CAK49181.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270057 Genomic DNA. Translation: CAK49181.1 . Different initiation.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH17. Glycoside Hydrolase Family 17.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG5309.
    HOGENOMi HOG000179527.
    OrthoDBi EOG7TBCCK.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
      Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
      , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
      Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CBS 513.88 / FGSC A1513.

    Entry informationi

    Entry nameiEGLC_ASPNC
    AccessioniPrimary (citable) accession number: A2QH21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 41 of the entry and version 2 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3