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Q0C7P6

- EGLC_ASPTN

UniProt

Q0C7P6 - EGLC_ASPTN

Protein

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

Gene

eglC

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 36 (01 Oct 2014)
      Sequence version 1 (17 Oct 2006)
      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:ATEG_10288
    OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
    Taxonomic identifieri341663 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000007963: 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 – 463445Probable glucan endo-1,3-beta-glucosidase eglCPRO_0000395147Add
    BLAST
    Propeptidei464 – 48623Removed in mature formSequence AnalysisPRO_0000395148Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
    Lipidationi463 – 4631GPI-anchor amidated glycineSequence 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

    ProteinModelPortaliQ0C7P6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi310 – 457148Ser-richAdd
    BLAST
    Compositional biasi333 – 40270Gly-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 17 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5309.
    OMAiTNTWWYI.
    OrthoDBiEOG7TBCCK.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR000490. Glyco_hydro_17.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00332. Glyco_hydro_17. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q0C7P6-1 [UniParc]FASTAAdd to Basket

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    MQLTQLLALA LSLATSEAAY KGFNYGDKKP DGSSKYQADF ASEFETAQNL    50
    VGAPGFTSAR LYTMIQAGTA NDPISAIPAA IAQNTSLLLG LWASGNNMNN 100
    ELTALKAAIS QYGEDLSKLV VGISVGSEDL YRNSVLGQKV NAGVGVDPHV 150
    LASYIEEVRS TISGTPLSGA PLGHVDTWND WVNGSNAAVI DAVDWVGFDG 200
    YPYFQNTMAN SIDDAKALFN EAVAKTKSAA GNKEVWITET GWPVSGKTEN 250
    LAVASIPNAK RFWDEVGCPL FDNTNTWWYT LQDAFGASVP NPSFGIVGST 300
    LTTQPLFDLS CSKSNTTSSS AIASPTSTAA AAGGVAGGST GSASGSSTGT 350
    GSSSGSGSNS NTGAASGAVG AADRETSGTS GSANTNGTSG SGSGSNSTSG 400
    HGSNVTVPTR PTSVSNVSPS KSSSALFTGA ATSMGASPSS VGNVGPSKSS 450
    GAASPSSTTM FTGAATSVSA PVVHVVLLAL MMVIAA 486
    Length:486
    Mass (Da):48,753
    Last modified:October 17, 2006 - v1
    Checksum:iF168A8CD88AF0DD4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476610 Genomic DNA. Translation: EAU29285.1.
    RefSeqiXP_001218636.1. XM_001218635.1.

    Genome annotation databases

    EnsemblFungiiCADATEAT00003164; CADATEAP00003164; CADATEAG00003164.
    GeneIDi4354731.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476610 Genomic DNA. Translation: EAU29285.1 .
    RefSeqi XP_001218636.1. XM_001218635.1.

    3D structure databases

    ProteinModelPortali Q0C7P6.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADATEAT00003164 ; CADATEAP00003164 ; CADATEAG00003164 .
    GeneIDi 4354731.

    Phylogenomic databases

    eggNOGi COG5309.
    OMAi TNTWWYI.
    OrthoDBi EOG7TBCCK.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR000490. Glyco_hydro_17.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00332. Glyco_hydro_17. 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 nameiEGLC_ASPTN
    AccessioniPrimary (citable) accession number: Q0C7P6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 36 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