Q652F9 · GUN17_ORYSJ

Function

Catalytic activity

  • Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
    EC:3.2.1.4 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

149750100150200250300350400450
TypeIDPosition(s)Description
Active site77Nucleophile
Active site406
Active site458
Active site467

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Molecular Functioncellulase activity
Biological Processcell wall organization
Biological Processcellulose catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

    • GH9Glycoside Hydrolase Family 9

Names & Taxonomy

Protein names

  • Recommended name
    Endoglucanase 17
  • EC number
  • Alternative names
    • Endo-1,4-beta glucanase 17
    • OsGLU13

Gene names

    • Name
      GLU13
    • ORF names
      OsJ_020012, P0624H09.19
    • Ordered locus names
      Os06g0256900, LOC_Os06g14540

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Nipponbare
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    Q652F9
  • Secondary accessions
    • A0A0P0WUX1
    • Q0DD41

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-21
ChainPRO_000024929422-497Endoglucanase 17
Glycosylation451N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyl hydrolase 9 (cellulase E) family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    497
  • Mass (Da)
    54,384
  • Last updated
    2004-10-25 v1
  • Checksum
    7AA1465C0A72B8D3
MAAAGGAVLLLVLATATSVTGQHDYSDALHKSILFFEGQRSGRLPPDQRLRWRRDSALNDGATAGVDLTGGYYDAGDNVKFGFPMAFTATLMSWGLIDFGRSFGAHAAEAREAVRWATDYLMKATATPNTVYVQVGDAFRDHSCWERPEDMDTPRTVYKVDPSHPGSDVAAETAAALAAASIVFRDADPDYSNRLLDRAIQVFEFADKYRGPYSSSLHAAVCPCYCDYSGYKDELLWGAAWLHKASRRREYRDYIKRNEVVLGASEAINEFGWDNKHAGINVLISKEVLMGKDEYFQSFRVNADNFICTLLPGISNHPQIQYSPGGLLFKVGNSNMQHVTSLSFLLLAYSNYLSHANVRVPCGTSSASPVQLRRVAKRQVDYILGDNPLRMSYMVGYGSRYPLRIHHRGSSLPSVAAHPAQIGCKAGATYYASAAPNPNLLVGAVVGGPSNTSDAFPDARAVFQQSEPTTYINAPLLGLLAYFSAHPNLAQSDLLYD

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict331in Ref. 5; AK060686

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP005619
EMBL· GenBank· DDBJ
BAD46308.1
EMBL· GenBank· DDBJ
Genomic DNA
AP008212
EMBL· GenBank· DDBJ
BAF19232.1
EMBL· GenBank· DDBJ
Genomic DNA
AP014962
EMBL· GenBank· DDBJ
BAS97102.1
EMBL· GenBank· DDBJ
Genomic DNA
CM000143
EMBL· GenBank· DDBJ
EAZ36529.1
EMBL· GenBank· DDBJ
Genomic DNA
AK060686
EMBL· GenBank· DDBJ
-mRNA No translation available.

Genome annotation databases

Similar Proteins

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