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Q0CR35

- EXGA_ASPTN

UniProt

Q0CR35 - EXGA_ASPTN

Protein

Probable glucan 1,3-beta-glucosidase A

Gene

exgA

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 47 (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. It could also function biosynthetically as a transglycosylase By similarity.By similarity

    Catalytic activityi

    Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

    Cofactori

    Manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei209 – 2091Proton donorBy similarity
    Active sitei308 – 3081NucleophileBy similarity

    GO - Molecular functioni

    1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    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

    Keywords - Ligandi

    Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable glucan 1,3-beta-glucosidase A (EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase 1
    Exo-1,3-beta-glucanase A
    Gene namesi
    Name:exgA
    Synonyms:exg1
    ORF Names:ATEG_03849
    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 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 416395Probable glucan 1,3-beta-glucosidase APRO_0000393531Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi290 ↔ 415By similarity
    Disulfide bondi316 ↔ 341By similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi33178.CADATEAP00008924.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0CR35.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000114462.
    OMAiIINEPNT.
    OrthoDBiEOG7JT75H.

    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.

    Q0CR35-1 [UniParc]FASTAAdd to Basket

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    MLYNLSKAVL ALSVLAASAD AAGIRLEKRA STFDYETEMV RGVCLGGWLV    50
    LEPWLSPGLF DAAPDGAVDE WTYTEILGQD EAKARLIGHW DTFITEQDFF 100
    DIAAAGMNHV RIPIGYWAVE ALPGDPYVDG QLEYLDRAIE WAGAAGLKVI 150
    VDLHGAPGSQ NGFDNSGRKG AIQWGQGDTL GQTVNAFRKL AERYVPSSDV 200
    VTAIEAVNEP FIPGGVNEDQ LKEYYQQAYD IVTQMSPDVD LVFSDGFINP 250
    TPWNGFISDS GNIVMDNHHY EVFDINLLRM SVDDHVRSVC DFGRTQLAPA 300
    TKPVVVGEWT GAMTDCARYL NGRGVGARYD GAMGGESVGD CGPFIQGSVS 350
    DLSPDDQKNM RRFIEAQLDA WEMKSGWLFW NWKTEQGAPG WDMKDLLDNG 400
    VFPFPLESRK YPGQCG 416
    Length:416
    Mass (Da):45,747
    Last modified:October 17, 2006 - v1
    Checksum:i24F9987F9D3BA259
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476598 Genomic DNA. Translation: EAU35651.1.
    RefSeqiXP_001213027.1. XM_001213027.1.

    Genome annotation databases

    EnsemblFungiiCADATEAT00008924; CADATEAP00008924; CADATEAG00008924.
    GeneIDi4318487.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH476598 Genomic DNA. Translation: EAU35651.1 .
    RefSeqi XP_001213027.1. XM_001213027.1.

    3D structure databases

    ProteinModelPortali Q0CR35.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 33178.CADATEAP00008924.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADATEAT00008924 ; CADATEAP00008924 ; CADATEAG00008924 .
    GeneIDi 4318487.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000114462.
    OMAi IINEPNT.
    OrthoDBi EOG7JT75H.

    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 nameiEXGA_ASPTN
    AccessioniPrimary (citable) accession number: Q0CR35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 47 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