Bacterial cellulose-binding domain-like sequences in eucaryotic polypeptides

Protein Seq Data Anal. 1991 Dec;4(6):349-53.

Abstract

The catalytic domain of endoglucanase II of Trichoderma reesei and the spore germination-specific polypeptide 270-11 of Dictyostelium discoideum contain amino acid sequences which share identity with the sequences of the cellulose-binding domains of several bacterial beta-1,4-glycanases. This is the first report of the presence of such sequences in eucaryotic polypeptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cellulase / chemistry*
  • Cellulase / metabolism
  • Cellulose / chemistry
  • Cellulose / metabolism*
  • Dictyostelium / enzymology*
  • Molecular Sequence Data
  • Peptides / metabolism
  • Sequence Alignment
  • Trichoderma / enzymology*

Substances

  • Peptides
  • Cellulose
  • endoglucanase 2
  • Cellulase