Domains within Clostridium acetobutylicum ATCC 824 protein Q97LM0_CLOAB (Q97LM0)

Beta-mannanase ManB-like enzyme, contains ChW-repeats

Alternative representations: 1 /

Protein length531 aa
Source databaseUniProt
Identifiers Q97LM0_CLOAB, Q97LM0

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

This domain architecture was probably invented with the emergence of Clostridium acetobutylicum

Predicted functional partners

Q97LM0_CLOAB is shown as CA_C0538 in the network

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The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for CA_C0538

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 272562.CA_C0538 in eggNOG.

OGTaxonomic classDescription
717G5All organisms (root)alpha-glucosidase [EC:3.2.1.20],glucan 1,4-alpha-glucosidase [EC:3.2.1.3],poly(beta-D-mannuronate) lyase [EC:4.2.2.3]
LCOG4124All organisms (root)mannan endo-1,4-beta-mannosidase [EC:3.2.1.78],pectate disaccharide-lyase [EC:4.2.2.9],endoglucanase [EC:3.2.1.4]
COG5492Bacteria (superkingdom)alpha-glucosidase [EC:3.2.1.20],glucan 1,4-alpha-glucosidase [EC:3.2.1.3],poly(beta-D-mannuronate) lyase [EC:4.2.2.3]
COG4124Bacteria (superkingdom)mannan endo-1,4-beta-mannosidase [EC:3.2.1.78],pectate disaccharide-lyase [EC:4.2.2.9],endoglucanase [EC:3.2.1.4]

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: