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Q0CEU4

- EGLD_ASPTN

UniProt

Q0CEU4 - EGLD_ASPTN

Protein

Probable endo-beta-1,4-glucanase D

Gene

eglD

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 25 (01 Oct 2014)
      Sequence version 1 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates By similarity.By similarity

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei164 – 1641Proton donorBy similarity
    Active sitei210 – 2101NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. cellulose binding Source: InterPro

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable endo-beta-1,4-glucanase D (EC:3.2.1.4)
    Short name:
    Endoglucanase D
    Alternative name(s):
    Carboxymethylcellulase D
    Cellulase D
    Gene namesi
    Name:eglD
    ORF Names:ATEG_07790
    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 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 360341Probable endo-beta-1,4-glucanase DPRO_0000394066Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi330 ↔ 347By similarity
    Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi341 ↔ 357By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ0CEU4.
    SMRiQ0CEU4. Positions 324-358.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini322 – 35837CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 234215CatalyticAdd
    BLAST
    Regioni235 – 30369Ser/Thr-rich linkerAdd
    BLAST

    Domaini

    Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 61 family.Curated
    Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG120437.
    HOGENOMiHOG000158937.
    OMAiGYIDSPP.
    OrthoDBiEOG7KM64H.

    Family and domain databases

    InterProiIPR000254. Cellulose-bd_dom_fun.
    IPR005103. Glyco_hydro_61.
    [Graphical view]
    PfamiPF00734. CBM_1. 1 hit.
    PF03443. Glyco_hydro_61. 1 hit.
    [Graphical view]
    ProDomiPD001821. CBD_fun. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00236. fCBD. 1 hit.
    [Graphical view]
    SUPFAMiSSF57180. SSF57180. 1 hit.
    PROSITEiPS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q0CEU4-1 [UniParc]FASTAAdd to Basket

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    MKTSFGLLAL AAAAKLVNAH ATVFAVWIND EDQGLGNTAD GYIRSPPNNS    50
    PVTDVTSKDM TCNVNGATAA AKTLDVKAGD KITFEWHHNS RDASDDIIAS 100
    SHLGPVMVYM APTEKGSAGS GWVKIAEDGY SNGKWAVDTL IANRGKHSIT 150
    VPDVPAGEYL FRPEIIALHE GNREGGAQLY MECVQVKVTS DGSKTLPEGV 200
    SIPGTYTATD PGILFDIYNS FDSYPIPGPA VWDGSSSGSS SGSSKTTAAA 250
    PAATSAASAS STKAPATTAA PVQTESAKPA TSTTQAAAPT TLVTSAKPTA 300
    TATAGAGDSG SGSCSATAPA TGVVKMYAQC GGMNYSGSTT CESGLTCKQW 350
    NPYYHQCVKA 360
    Length:360
    Mass (Da):36,795
    Last modified:October 17, 2006 - v1
    Checksum:i0BABA36D957D8F7D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476604 Genomic DNA. Translation: EAU32052.1.
    RefSeqiXP_001216411.1. XM_001216411.1.

    Genome annotation databases

    EnsemblFungiiCADATEAT00003463; CADATEAP00003463; CADATEAG00003463.
    GeneIDi4322940.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476604 Genomic DNA. Translation: EAU32052.1 .
    RefSeqi XP_001216411.1. XM_001216411.1.

    3D structure databases

    ProteinModelPortali Q0CEU4.
    SMRi Q0CEU4. Positions 324-358.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADATEAT00003463 ; CADATEAP00003463 ; CADATEAG00003463 .
    GeneIDi 4322940.

    Phylogenomic databases

    eggNOGi NOG120437.
    HOGENOMi HOG000158937.
    OMAi GYIDSPP.
    OrthoDBi EOG7KM64H.

    Family and domain databases

    InterProi IPR000254. Cellulose-bd_dom_fun.
    IPR005103. Glyco_hydro_61.
    [Graphical view ]
    Pfami PF00734. CBM_1. 1 hit.
    PF03443. Glyco_hydro_61. 1 hit.
    [Graphical view ]
    ProDomi PD001821. CBD_fun. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00236. fCBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57180. SSF57180. 1 hit.
    PROSITEi PS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiEGLD_ASPTN
    AccessioniPrimary (citable) accession number: Q0CEU4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 25 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