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Q0C8Z0

- EXGB_ASPTN

UniProt

Q0C8Z0 - EXGB_ASPTN

Protein

Probable glucan endo-1,6-beta-glucosidase B

Gene

exgB

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides By similarity.By similarity

    Catalytic activityi

    Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-glucans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei222 – 2221Proton donorBy similarity
    Active sitei324 – 3241NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable glucan endo-1,6-beta-glucosidase B (EC:3.2.1.75)
    Alternative name(s):
    Beta-1,6-glucanase B
    Endo-1,6-beta-D-glucanase B
    Endo-1,6-beta-glucanase B
    Gene namesi
    Name:exgB
    ORF Names:ATEG_09844
    OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
    Taxonomic identifieri341663 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000007963: Unassembled WGS sequence

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 404384Probable glucan endo-1,6-beta-glucosidase BPRO_0000394709Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ0C8Z0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000217590.
    OMAiSEHFPQG.
    OrthoDBiEOG776T0C.

    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.

    Q0C8Z0-1 [UniParc]FASTAAdd to Basket

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    MTTYQTLFLI PLAISTLVTA WLPETDKTIT SRNGTNLFAS SKGKIRGVNM    50
    GSQFVFEPWI AEKAWSSMGC KGQKSEFDCV VSLGQDAANK AFAQHWGSWI 100
    TQDDITEIQS YTLNTIRVPI GYWMKEDLVN KTSEHFPQGG FAYLEKLCGW 150
    ASDAGLYIIL DLHGAPGAQT PHNPFTGQYA STAGFYNDYQ FGRALEFLEW 200
    ITTKVHQSDS FRNVGMLEIV NEPLQNAQKV GSMRSTYYPD AFKRIRAAEQ 250
    KLNVSKSGYL HIQMMDKLWG SGDPEEYLTD KYYVAYDDHR YLKWDPKVNV 300
    SKENYISTSC SDELDSNTPT IVGEWSLSVP DDVASTPDWD MDTNKDFYKK 350
    WFAAQITAYE KQRGWVFWTW KTQLGGYRWS YKDAVAAGVV PEDIDSALNM 400
    GVCN 404
    Length:404
    Mass (Da):45,814
    Last modified:October 17, 2006 - v1
    Checksum:i57FDB335BFFF69E8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476608 Genomic DNA. Translation: EAU30035.1.
    RefSeqiXP_001218466.1. XM_001218465.1.

    Genome annotation databases

    EnsemblFungiiCADATEAT00003862; CADATEAP00003862; CADATEAG00003862.
    GeneIDi4354491.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476608 Genomic DNA. Translation: EAU30035.1 .
    RefSeqi XP_001218466.1. XM_001218465.1.

    3D structure databases

    ProteinModelPortali Q0C8Z0.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADATEAT00003862 ; CADATEAP00003862 ; CADATEAG00003862 .
    GeneIDi 4354491.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000217590.
    OMAi SEHFPQG.
    OrthoDBi EOG776T0C.

    Family and domain databases

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

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NIH 2624 / FGSC A1156.

    Entry informationi

    Entry nameiEXGB_ASPTN
    AccessioniPrimary (citable) accession number: Q0C8Z0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 43 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3