Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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LamGL LamG-like jellyroll fold domain

SMART accession number:	SM00560
Description:
Interpro abstract (IPR006558):	The LamG-like jellyroll fold domain is associated with proteins of largely unknown function found in the metazoa and bacteria, but not in other organisms. The purpose of this fold is unknown.
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 139 LamGL domains in 67 proteins in SMART's nrdb database.

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 LamGL domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with LamGL domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Homo sapiens, Mus musculus, Rattus norvegicus, Takifugu rubripes

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Beckmann G, Hanke J, Bork P, Reich JG
  • Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins.
  • J Mol Biol. 1998; 275: 725-30
  • Display abstract

  • Using a new method for construction and database searches of sequence consensus strings, we have identified a new superfamily of protein modules comprising laminin G, thrombospondin N and the pentraxin families. The conserved patterns correspond mainly to hydrophobic core residues located in central beta strands of the known three-dimensional structures of two pentraxins, the human C-reactive protein and the serum amyloid P-component. Thus, we predict a similar jellyroll fold for all members of this superfamily. In addition, the conservation of two exposed aspartate residues in the majority of superfamily members suggests hitherto unrecognised functional sites.

• 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 20.00 map00511 N-Glycan degradation 20.00 map00600 Sphingolipid metabolism 20.00 map01032 Glycan structures - degradation 10.00 map00604 Glycosphingolipid biosynthesis - ganglioseries 10.00 map00531 Glycosaminoglycan degradation 10.00 map00561 Glycerolipid metabolism 10.00 map00052 Galactose metabolism 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 LamGL domain which could be assigned to a KEGG orthologous group, and not all proteins containing LamGL domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

• Links (links to other resources describing this domain)

• INTERPRO	IPR006558

Send comments to Ivica Letunic