SUPERFAMILY 1.75 HMM library and genome assignments server

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Glycosyl hydrolases family 6, cellulases superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Alpha and beta proteins (a/b) [ 51349] (147)
Fold:   7-stranded beta/alpha barrel [ 51988] (3)
Superfamily:   Glycosyl hydrolases family 6, cellulases [ 51989]
Families:   Glycosyl hydrolases family 6, cellulases [ 51990] (3)


Superfamily statistics
Genomes (263) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 538 4,053 14
Proteins 532 4,018 14


Functional annotation
General category Metabolism
Detailed category Polysaccharide metabolism and transport

Document:
Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Glycosidases, i.e. enzymes hydrolyzing O- and S-gl0Moderately InformativeDirect
Enzyme Commission (EC)Cellulose 1,4-beta-cellobiosidase (non-reducing en9.368e-16Highly InformativeDirect
Enzyme Commission (EC)Cellulase0.00001349Highly InformativeDirect

Document: EC annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Hydrolases0Least InformativeDirect
Enzyme Commission (EC)Glycosylases0Moderately InformativeDirect
Enzyme Commission (EC)Cellulase0.00004206Highly InformativeDirect

Document: EC annotation of SCOP domains

InterPro annotation
Cross references IPR001524 SSF51989 Protein matches
Abstract

Glycoside hydrolase family 6 comprises enzymes with several known activities; endoglucanase ; cellobiohydrolase . These enzymes were formerly known as cellulase family B.

The 3D structure of the enzymatic core of cellobiohydrolase II (CBHII) from the fungus Trichoderma reesei reveals an alpha-beta protein with a fold similar to the ubiquitous barrel topology first seen in triose phosphate isomerase [PubMed2377893]. The active site of CBHII is located at the C-terminal end of a parallel beta barrel, in an enclosed tunnel through which the cellulose threads. Two aspartic acid residues, located in the centre of the tunnel are the probable catalytic residues [PubMed2377893].


InterPro database


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Enzyme Commission (EC) ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 13 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a Glycosyl hydrolases family 6, cellulases domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 13 hidden Markov models representing the Glycosyl hydrolases family 6, cellulases superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Enzyme Commission (EC) · Internal database links ]