Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.
Several types of domain occur in beta-1, 4-glycanases. The best characterized of these are the catalytic domains and the cellulose-binding domains. The domains may be joined by linker sequences rich in proline or hydroxyamino acids or both. Some of the enzymes contain repeated sequences up to 150 amino acids in length. The enzymes can be grouped into families on the basis of sequence similarities between the catalytic domains. There are sequence similarities between the cellulose-binding domains, of which two types have been identified, and also between some domains of unknown function. The beta-1, 4-glycanases appear to have arisen by the shuffling of a relatively small number of progenitor sequences.
Gilkes
N R
NR
Department of Microbiology, University of British Columbia, Vancouver, Canada.
Henrissat
B
B
Kilburn
D G
DG
Miller
R C
RC
Warren
R A
RA
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics; D001665:Binding Sites; D002480:Cellulase / Q000145:classification / Q000235:genetics*; D043364:Endo-1,4-beta Xylanases; D005656:Fungal Proteins / Q000235:genetics; D006026:Glycoside Hydrolases / Q000145:classification / Q000235:genetics*; D008969:Molecular Sequence Data; D011487:Protein Conformation
D001426:Bacterial Proteins; D005656:Fungal Proteins; D006026:Glycoside Hydrolases; D002480:Cellulase; D043364:Endo-1,4-beta Xylanases