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P23044

- GUN_ROBSP

UniProt

P23044 - GUN_ROBSP

Protein

Endoglucanase 1

Gene

eg 1

Organism
Robillarda sp. (strain Y-20)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 2 (20 Feb 2007)
      Previous versions | rss
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    Functioni

    Active towards carboxymethyl cellulose.

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei176 – 1761Proton donorBy similarity
    Active sitei284 – 2841NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    UniPathwayiUPA00696.

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.
    mycoCLAPiEGL5A_ROBSP.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase 1 (EC:3.2.1.4)
    Alternative name(s):
    Carboxymethyl-cellulase I
    Short name:
    CMCase I
    Endo-1,4-beta-glucanase
    Endoglucanase I
    Gene namesi
    Name:eg 1
    OrganismiRobillarda sp. (strain Y-20)
    Taxonomic identifieri72589 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotamitosporic AscomycotaRobillarda

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Chaini18 – 385368Endoglucanase 1PRO_0000184049Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliP23044.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23044-1 [UniParc]FASTAAdd to Basket

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    MKLVFSALAS LLSGASATIY YAGVAESSGE FGVWSATQTP GTGLPGRFGV    50
    DYAFISEAAV DVHVDQNHLN LFRVAFLLER MCPPATGLGA AFNETHFDYF 100
    KEAVDYITVT KGAYAILDPH NYMRYNDPSY QPFSGSVIGN TSDSTAATTE 150
    QFGEFWGELA SRFNDNERVI FGLMNEPHDM ATSLVLANNQ AAIDAIRAAN 200
    ASNLIIMPGN SWTGGHSWTE GSDPSSALLN QFKDPLNNTA IDIHEYLDYD 250
    FSGGHLECVS DPETNLAALT AWLKENNLKA FITEFGGSNS TSCQEMLPDL 300
    INYMADNAEY IGWTAWAAGP FWGPNSPCCT NSTQLGSLEP GSTAVDGSPG 350
    LYDTVWLPVI QPLVPTELQW SGPASISGGE LTSRA 385
    Length:385
    Mass (Da):41,428
    Last modified:February 20, 2007 - v2
    Checksum:i149604D42369AD33
    GO

    Sequence cautioni

    The sequence described in 1 Publication differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 282SS → GN AA sequence (PubMed:2277031)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB030819 Genomic DNA. Translation: BAA90480.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB030819 Genomic DNA. Translation: BAA90480.1 .

    3D structure databases

    ProteinModelPortali P23044.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.
    mycoCLAPi EGL5A_ROBSP.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00696 .

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Endoglucanase gene from cellulolytic fungi, Robillarda sp. Y-20."
      Kashiwagi Y.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning and sequencing of the endo-cellulase cDNA from Robillarda sp. Y-20."
      Yoshigi N., Taniguchi H., Sasaki T.
      J. Biochem. 108:388-392(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-385, PROTEIN SEQUENCE OF 18-35.

    Entry informationi

    Entry nameiGUN_ROBSP
    AccessioniPrimary (citable) accession number: P23044
    Secondary accession number(s): Q9P981
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 73 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

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3