http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID260083

Outgoing Links

Predicate Object
abstract Cohesin domain, interaction parter of dockerin. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. Cohesin modules are phylogenetically distributed into three groups: type I cohesin-dockerin interactions mediate assembly of a range of dockerin-borne enzymes to the complex, while type-II interactions mediate attachment of the cellulosome complex to the bacterial cell wall. Recently discovered type-III cohesins, such as found in the anchoring scaffoldin ScaE, appears to contribute to increased stability of the elaborate cellulosome complex. While the presence of cohesin and dockerin domains in a genome can be indicative of cellulolytic activity, cohesin domains may occur in a wider range of domain architectures, biological systems, and taxonomic lineages.
title cohesin_like
isDiscussedBy http://rdf.ncbi.nlm.nih.gov/pubchem/reference/22063917
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18053578
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21366419
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13345217
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13815728
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5831544
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/29369964
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/360610
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/29482470
type http://purl.obolibrary.org/obo/SO_0000417

Incoming Links

Predicate Subject
has component http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ0TR53
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ8XL08

Total number of triples: 14.