The domain within your query sequence starts at position 140 and ends at position 189; the E-value for the LRRCT domain shown below is 4.49e-4.
Leucine-rich repeats (LRR, see IPR001611) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape [(PUBMED:14747988)]. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [(PUBMED:11751054)]. Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response.
LRRs are often flanked by cysteine-rich domains: an N-terminal LRR domain (IPR000372) and a C-terminal LRR domain. This entry represents the C-terminal LRR domain.
There are 43815 LRRCT domains in 36442 proteins in SMART's nrdb database.
Taxonomic distribution of proteins containing LRRCT domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with LRRCT domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing LRRCT domain in the selected taxonomic class.
A structural basis of the interactions between leucine-rich repeats and protein ligands.
The leucine-rich repeat is a recently characterized structural motif used in molecular recognition processes as diverse as signal transduction, cell adhesion, cell development, DNA repair and RNA processing. We present here the crystal structure at 2.5 A resolution of the complex between ribonuclease A and ribonuclease inhibitor, a protein built entirely of leucine-rich repeats. The unusual non-globular structure of ribonuclease inhibitor, its solvent-exposed parallel beta-sheet and the conformational flexibility of the structure are used in the interaction; they appear to be the principal reasons for the effectiveness of leucine-rich repeats as protein-binding motifs. The structure can serve as a model for the interactions of other proteins containing leucine-rich repeats with their ligands.
The leucine-rich repeat: a versatile binding motif.
Leucine-rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. All proteins containing these repeats are thought to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor protein has revealed that leucine-rich repeats correspond to beta-alpha structural units. These units are arranged so that they form a parallel beta-sheet with one surface exposed to solvent, so that the protein acquires an unusual, nonglobular shape. These two features may be responsible for the protein-binding functions of proteins containing leucine-rich repeats.
SwissProt sequences and OMIM curated human diseases associated with missense mutations within the LRRCT domain.
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with LRRCT domain which could be assigned to a KEGG orthologous group, and not all proteins containing LRRCT domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.