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B0XXF8

- EGLC_ASPFC

UniProt

B0XXF8 - EGLC_ASPFC

Protein

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

Gene

eglC

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 33 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      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

    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:AFUB_048180
    OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
    Taxonomic identifieri451804 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000001699: Unassembled WGS sequence

    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 – 427409Probable glucan endo-1,3-beta-glucosidase eglCPRO_0000395140Add
    BLAST
    Propeptidei428 – 45023Removed in mature formSequence AnalysisPRO_0000395141Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Lipidationi427 – 4271GPI-anchor amidated asparagineSequence 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

    Structurei

    3D structure databases

    ProteinModelPortaliB0XXF8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi309 – 435127Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 17 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000179527.
    OrthoDBiEOG7TBCCK.
    PhylomeDBiB0XXF8.

    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.

    B0XXF8-1 [UniParc]FASTAAdd to Basket

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    MQFTHLVALA LALATSEAAH QGFNYGNTKS DGSAKSQADF QAEFSTAKNL    50
    VGTSGFTSAR LYTMIQGGTA NTPISAIPAA ITEQTSLLLG LWASGGNFAN 100
    EIAALKAAIA QYGDDLAKLV VGISVGSEDL YRNSVDGVKA NAGIGTNPDE 150
    IVSYINEVRS TIAGTKLSGA PIGHVDTWTA WVNGSNSAVI DACDWLGFDG 200
    YPYFQNTMAN SISDAKALFD ESVAKTQAVA KGKEVWITET GWPVSGKTEN 250
    LAVANLANAK TYWDEVGCPL FGKTNTWWYI LQDADPVTPN PSFGIVGSTL 300
    STTPLFDLSC SASSSSSAAA SSTAGPSASS VIGGKASGFT TAAANSAKPT 350
    FTVGKGPGGS YNGTGFWNST SSARPSSSAI SGSSSGSAAG SSGSSGSSGS 400
    GASGASGQSS SSTGSSSAPS TSNILSNAAS GLSGSICGAV VAVCLALAAL 450
    Length:450
    Mass (Da):44,943
    Last modified:April 8, 2008 - v1
    Checksum:iF687F0613C6FA2B5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499596 Genomic DNA. Translation: EDP53632.1.

    Genome annotation databases

    EnsemblFungiiCADAFUBT00004808; CADAFUBP00004720; CADAFUBG00004808.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499596 Genomic DNA. Translation: EDP53632.1 .

    3D structure databases

    ProteinModelPortali B0XXF8.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUBT00004808 ; CADAFUBP00004720 ; CADAFUBG00004808 .

    Phylogenomic databases

    HOGENOMi HOG000179527.
    OrthoDBi EOG7TBCCK.
    PhylomeDBi B0XXF8.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CEA10 / CBS 144.89 / FGSC A1163.

    Entry informationi

    Entry nameiEGLC_ASPFC
    AccessioniPrimary (citable) accession number: B0XXF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 33 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

    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