The domain within your query sequence starts at position 480 and ends at position 503; the E-value for the LRR domain shown below is 4.9e-2.
LRRLeucine-rich repeats, outliers
|SMART accession number:||SM00370|
Click on the following links for more information.
- Evolution (species in which this domain is found)
Click on to expand nodes. To display all proteins with a LRR domain in a specific node, click on it.
This tree shows only several representative species. The complete taxonomic breakdown of all proteins with LRR domain is also avaliable.
Useful shortcuts: Expand all nodes or Collapse tree
Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
- Cellular role (predicted cellular role)
Cellular role: signalling, translation
Binding / catalysis: Protein-binding
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Radauer C, Lackner P, Breiteneder H
- The Bet v 1 fold: an ancient, versatile scaffold for binding of large,hydrophobic ligands.
- BMC Evol Biol. 2008; 8: 286-286
- Display abstract
BACKGROUND: The major birch pollen allergen, Bet v 1, is a member of theubiquitous PR-10 family of plant pathogenesis-related proteins. In recentyears, a number of diverse plant proteins with low sequence similarity toBet v 1 was identified. In addition, determination of the Bet v 1structure revealed the existence of a large superfamily of structurallyrelated proteins. In this study, we aimed to identify and classify all Betv 1-related structures from the Protein Data Bank and all Bet v 1-relatedsequences from the Uniprot database. RESULTS: Structural comparisons ofrepresentative members of already known protein families structurallyrelated to Bet v 1 with all entries of the Protein Data Bank yielded 47structures with non-identical sequences. They were classified into elevenfamilies, five of which were newly identified and not included in theStructural Classification of Proteins database release 1.71. The taxonomicdistribution of these families extracted from the Pfam protein familydatabase showed that members of the polyketide cyclase family and theactivator of Hsp90 ATPase homologue 1 family were distributed among allthree superkingdoms, while members of some bacterial families wereconfined to a small number of species. Comparison of ligand bindingactivities of Bet v 1-like superfamily members revealed that theirfunctions were related to binding and metabolism of large, hydrophobiccompounds such as lipids, hormones, and antibiotics. Phylogeneticrelationships within the Bet v 1 family, defined as the group of proteinswith significant sequence similarity to Bet v 1, were determined byaligning 264 Bet v 1-related sequences. A distance-based phylogenetic treeyielded a classification into 11 subfamilies, nine exclusively containingplant sequences and two subfamilies of bacterial proteins. Plant sequencesincluded the pathogenesis-related proteins 10, the major latexproteins/ripening-related proteins subfamily, and polyketide cyclase-likesequences. CONCLUSION: The ubiquitous distribution of Bet v 1-relatedproteins among all superkingdoms suggests that a Bet v 1-like protein wasalready present in the last universal common ancestor. During evolution,this protein diversified into numerous families with low sequencesimilarity but with a common fold that succeeded as a versatile scaffoldfor binding of bulky ligands.
- Kajava AV
- Structural diversity of leucine-rich repeat proteins.
- J Mol Biol. 1998; 277: 519-27
- Display abstract
The superfamily of leucine-rich repeat proteins can be subdivided into at least six subfamilies, characterised by different lengths and consensus sequences of the repeats. It was proposed that the repeats from different subfamilies retain a similar superhelical fold, but differ in the three-dimensional structures of individual repeats. The sequence-structure relationship of three new subfamilies was examined by molecular modelling. I provide structural models for the repeats of all subfamilies. The models enable me to explain residue conservations within each subfamily. Furthermore, the difference in the packing explains why the repeats from different subfamilies never occur simultaneously in the same protein. Finally, these studies suggest different evolutionary origins for the different subfamilies. The approach used for the prediction of the leucine-rich repeat protein structures can be applied to other proteins containing internal repeats of about 20 to 30 residue in length.
- Metabolism (metabolic pathways involving proteins which contain this domain)
Click the image to view the interactive version of the map in iPath
% proteins involved KEGG pathway ID Description 25.44 map04620 Toll-like receptor signaling pathway 10.25 map04080 Neuroactive ligand-receptor interaction 8.13 map04360 Axon guidance 6.71 map04120 Ubiquitin mediated proteolysis 6.36 map04512 ECM-receptor interaction 3.89 map04640 Hematopoietic cell lineage 3.89 map00230 Purine metabolism 3.53 map05222 Small cell lung cancer 3.53 map04110 Cell cycle 3.18 map05120 Epithelial cell signaling in Helicobacter pylori infection 3.18 map04111 Cell cycle - yeast 2.83 map04612 Antigen processing and presentation 2.47 map04510 Focal adhesion 2.47 map04350 TGF-beta signaling pathway 2.12 map00562 Inositol phosphate metabolism 2.12 map00632 Benzoate degradation via CoA ligation 2.12 map04115 p53 signaling pathway 1.77 map00380 Tryptophan metabolism 1.41 map00680 Methane metabolism 1.41 map00940 Phenylpropanoid biosynthesis 1.41 map00360 Phenylalanine metabolism 0.35 map04530 Tight junction 0.35 map04010 MAPK signaling pathway 0.35 map03320 PPAR signaling pathway 0.35 map04810 Regulation of actin cytoskeleton 0.35 map00550 Peptidoglycan biosynthesis
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 LRR domain which could be assigned to a KEGG orthologous group, and not all proteins containing LRR domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of LRR domains in PDB
PDB code Main view Title 1a4y Ribonuclease inhibitor-angiogenin complex 1d0b Internalin b leucine rich repeat domain 1dce Crystal structure of rab geranylgeranyltransferase from rat brain 1dfj Ribonuclease inhibitor complexed with ribonuclease a 1ds9 Solution structure of chlamydomonas outer arm dynein light chain 1 1fqv Insights into scf ubiquitin ligases from the structure of the skp1-skp2 complex 1fs2 Insights into scf ubiquitin ligases from the structure of the skp1-skp2 complex 1g9u Crystal structure of yopm-leucine rich effector protein from yersinia pestis 1gwb Structure of glycoprotein 1b 1h6t Internalin b: crystal structure of fused n-terminal domains. 1h6u Internalin h: crystal structure of fused n-terminal domains. 1jl5 Novel molecular architecture of yopm-a leucine-rich effector protein from yersinia pestis 1k5d Crystal structure of ran-gppnhp-ranbp1-rangap complex 1k5g Crystal structure of ran-gdp-alfx-ranbp1-rangap complex 1ltx Structure of rab escort protein-1 in complex with rab geranylgeranyl transferase and isoprenoid 1m0z Crystal structure of the von willebrand factor binding domain of glycoprotein ib alpha 1m10 Crystal structure of the complex of glycoprotein ib alpha and the von willebrand factor a1 domain 1m9l Relaxation-based refined structure of chlamydomonas outer arm dynein light chain 1 1m9s Crystal structure of internalin b (inlb), a listeria monocytogenes virulence protein containing sh3-like domains. 1o6s Internalin (listeria monocytogenes) / e-cadherin (human) recognition complex 1o6t Internalin (inla,listeria monocytogenes) - functional domain,uncomplexed 1o6v Internalin (inla,listeria monocytogenes) - functional domain, uncomplexed 1ook Crystal structure of the complex of platelet receptor gpib- alpha and human alpha-thrombin 1otm Calcium-binding mutant of the internalin b lrr domain 1otn Calcium-binding mutant of the internalin b lrr domain 1oto Calcium-binding mutant of the internalin b lrr domain 1ozn 1.5a crystal structure of the nogo receptor ligand binding domain reveals a convergent recognition scaffold mediating inhibition of myelination 1p8t Crystal structure of nogo-66 receptor 1p8v Crystal structure of the complex of platelet receptor gpib- alpha and alpha-thrombin at 2.6a 1p9a Crystal structure of n-terminal domain of human platelet receptor glycoprotein ib-alpha at 1.7 angstrom resolution 1qyy Crystal structure of n-terminal domain of human platelet receptor glycoprotein ib-alpha at 2.8 angstrom resolution 1sq0 Crystal structure of the complex of the wild-type von willebrand factor a1 domain and glycoprotein ib alpha at 2.6 angstrom resolution 1u0n The ternary von willebrand factor a1-glycoprotein ibalpha- botrocetin complex 1w8a Third lrr domain of drosophila slit 1xcd Dimeric bovine tissue-extracted decorin, crystal form 1 1xec Dimeric bovine tissue-extracted decorin, crystal form 2 1xeu Crystal structure of internalin c from listeria monocytogenes 1xku Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan 1yrg The crystal structure of rna1p: a new fold for a gtpase- activating protein 1z7x X-ray structure of human ribonuclease inhibitor complexed with ribonuclease i 1ziw Human toll-like receptor 3 extracellular domain structure 2a0z The molecular structure of toll-like receptor 3 ligand binding domain 2ass Crystal structure of the skp1-skp2-cks1 complex 2ast Crystal structure of skp1-skp2-cks1 in complex with a p27 peptide 2bex Crystal structure of placental ribonuclease inhibitor in complex with human eosinophil derived neurotoxin at 2a resolution 2bnh Porcine ribonuclease inhibitor 2ca6 Miras structure determination from hemihedrally twinned crystals 2ft3 Crystal structure of the biglycan dimer core protein 2id5 Crystal structure of the lingo-1 ectodomain 2o6q Structural diversity of the hagfish variable lymphocyte receptors a29 2o6r Structural diversity of the hagfish variable lymphocyte receptors b61 2o6s Structural diversity of the hagfish variable lymphocyte receptors b59 2omt Crystal structure of inla g194s+s/hec1 complex 2omu Crystal structure of inla g194s+s y369s/hec1 complex 2omv Crystal structure of inla s192n y369s/hec1 complex 2omw Crystal structure of inla s192n y369s/mec1 complex 2omx Crystal structure of inla s192n g194s+s/hec1 complex 2omy Crystal structure of inla s192n/hec1 complex 2omz Crystal structure of inla y369a/hec1 complex 2p1m Tir1-ask1 complex structure 2p1n Mechanism of auxin perception by the tir1 ubiqutin ligase 2p1o Mechanism of auxin perception by the tir1 ubiquitin ligase 2p1p Mechanism of auxin perception by the tir1 ubiquitin ligase 2p1q Mechanism of auxin perception by the tir1 ubiquitin ligase 2q4g Ensemble refinement of the protein crystal structure of human ribonuclease inhibitor complexed with ribonuclease i 2r9u Crystal structure of lamprey variable lymphocyte receptor ectodomain 2uzx Structure of the human receptor tyrosine kinase met in complex with the listeria monocytogenes invasion protein inlb: crystal form i 2uzy Structure of the human receptor tyrosine kinase met in complex with the listeria monocytogenes invasion protein inlb: low resolution, crystal form ii 2v70 Third lrr domain of human slit2 2v9s Second lrr domain of human slit2 2v9t Complex between the second lrr domain of slit2 and the first ig domain from robo1 2wfh The human slit 2 dimerization domain d4 2wqu Internalin domain of listeria monocytogenes inlb: triclinic crystal form 2wqv Internalin domain of listeria monocytogenes inlb: rhombohedral crystal form 2wqw Double-disulfide cross-linked crystal dimer of the listeria monocytogenes inlb internalin domain 2wqx Inlb321_4r: s199r, d200r, g206r, a227r, c242a mutant of the listeria monocytogenes inlb internalin domain 2z62 Crystal structure of the tv3 hybrid of human tlr4 and hagfish vlrb.61 2z63 Crystal structure of the tv8 hybrid of human tlr4 and hagfish vlrb.61 2z64 Crystal structure of mouse tlr4 and mouse md-2 complex 2z65 Crystal structure of the human tlr4 tv3 hybrid-md-2- eritoran complex 2z66 Crystal structure of the vt3 hybrid of human tlr4 and hagfish vlrb.61 2z7x Crystal structure of the tlr1-tlr2 heterodimer induced by binding of a tri-acylated lipopeptide 2z80 Crystal structure of the tlr1-tlr2 heterodimer induced by binding of a tri-acylated lipopeptide 2z81 Crystal structure of the tlr1-tlr2 heterodimer induced by binding of a tri-acylated lipopeptide 2z82 Crystal structure of the tlr1-tlr2 heterodimer induced by binding of a tri-acylated lipopeptide 3a79 Crystal structure of tlr2-tlr6-pam2csk4 complex 3a7b Crystal structure of tlr2-streptococcus pneumoniae lipoteichoic acid complex 3a7c Crystal structure of tlr2-pe-dtpa complex 3c6n Small molecule agonists and antagonists of f-box protein- substrate interactions in auxin perception and signaling 3c6o Small molecule agonists and antagonists of f-box protein- substrate interactions in auxin perception and signaling 3c6p Small molecule agonists and antagonists of f-box protein- substrate interactions in auxin perception and signaling 3cig Crystal structure of mouse tlr3 ectodomain 3ciy Mouse toll-like receptor 3 ectodomain complexed with double- stranded rna 3cvr Crystal structure of the full length ipah3 3e6j Crystal structure of variable lymphocyte receptor (vlr) rbc36 in complex with h-trisaccharide 3fxi Crystal structure of the human tlr4-human md-2-e.coli lps ra complex 3g06 The salmonella virulence effector ssph2 functions as a novel e3 ligase 3g39 Structure of a lamprey variable lymphocyte receptor 3g3a Structure of a lamprey variable lymphocyte receptor in complex with a protein antigen 3g3b Structure of a lamprey variable lymphocyte receptor mutant in complex with a protein antigen