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A1CRV0

- EXGA_ASPCL

UniProt

A1CRV0 - EXGA_ASPCL

Protein

Probable glucan 1,3-beta-glucosidase A

Gene

exgA

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
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 2 (20 Apr 2010)
      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 sitei210 – 2101Proton donorBy similarity
    Active sitei307 – 3071NucleophileBy 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:ACLA_031040
    OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
    Taxonomic identifieri344612 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006701: 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 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 415393Probable glucan 1,3-beta-glucosidase APRO_0000393527Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi290 ↔ 414By similarity
    Disulfide bondi315 ↔ 341By similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi5057.CADACLAP00002273.

    Structurei

    3D structure databases

    ProteinModelPortaliA1CRV0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000114462.
    KOiK01210.
    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.

    A1CRV0-1 [UniParc]FASTAAdd to Basket

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    MLSRLSQTAL VALSLMTVLT EAVPSRMRIQ TRDSVNYQSE IVRGVNLGGW    50
    LVLEPWITPS IFENGGGAAV DEWTLAEVLG KDKARAILSQ HWSSFITQDD 100
    FNQIAQAGMN HVRIPVGYWA VSAPDEPYVD GQLEFLDNAI SWARAAGLKV 150
    MIDLHGAPGS QNGFDNSGRK GPIAWQQGDT VARTVDAFKA LAERYLPESD 200
    VVTAIEAVNE PNIPGGVNEG QLKEYYNQVL EVVHSINPDA GVFLSDGFLA 250
    TASWNGYANG ENVVMDTHHY HMFDNTLISL DINAHVRAAC EFGNQIKGSD 300
    KPVVVGEWTG ALTDCTKHLN GKDIPTRYEG QWANSPRYGD CGNKRQGSSS 350
    GLSEQERSDT RRFIEAQLDA YEGKNGWLFW TWKTEGAPGW DMQDLLANGL 400
    FPNPPTERQY GNQCA 415
    Length:415
    Mass (Da):45,665
    Last modified:April 20, 2010 - v2
    Checksum:i86978A724C6C1B67
    GO

    Sequence cautioni

    The sequence EAW08371.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027059 Genomic DNA. Translation: EAW08371.1. Sequence problems.
    RefSeqiXP_001269797.1. XM_001269796.1.

    Genome annotation databases

    GeneIDi4700820.
    KEGGiact:ACLA_031040.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027059 Genomic DNA. Translation: EAW08371.1 . Sequence problems.
    RefSeqi XP_001269797.1. XM_001269796.1.

    3D structure databases

    ProteinModelPortali A1CRV0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5057.CADACLAP00002273.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4700820.
    KEGGi act:ACLA_031040.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000114462.
    KOi K01210.
    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: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

    Entry informationi

    Entry nameiEXGA_ASPCL
    AccessioniPrimary (citable) accession number: A1CRV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 47 of the entry and version 2 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