02031nas a2200253   4500008004100000245009200041210006900133300000800202490000600210520096700216653008801183653004501271653013401316653003101450653007301481100001801554700001401572700001501586700001901601700001301620700002401633700001401657856010601671       2008                        eng d00aPrediction of enzyme function by combining sequence similarity and protein interactions0 aPrediction of enzyme function by combining sequence similarity a  a2490 v93 aBACKGROUND: A number of studies have used protein interaction data alone for protein function prediction. Here, we introduce a computational approach for annotation of enzymes, based on the observation that similar protein sequences are more likely to perform the same function if they share similar interacting partners. RESULTS: The method has been tested against the PSI-BLAST program using a set of 3,890 protein sequences from which interaction data was available. For protein sequences that align with at least 40% sequence identity to a known enzyme, the specificity of our method in predicting the first three EC digits increased from 80% to 90% at 80% coverage when compared to PSI-BLAST. CONCLUSION: Our method can also be used in proteins for which homologous sequences with known interacting partners can be detected. Thus, our method could increase 10% the specificity of genome-wide enzyme predictions based on sequence matching by PSI-BLAST alone.10aAmino Acid *Software Structure-Activity Relationship Substrate Specificity/genetics10aAmino Acid Sequence/physiology Databases10aAutomated Predictive Value of Tests Protein Interaction Mapping Proteins/analysis/metabolism Sequence Alignment Sequence Analysis10aProtein *Sequence Homology10aProtein Enzymes/analysis/*metabolism Fuzzy Logic Pattern Recognition1 aEspadaler, J.1 aEswar, N.1 aQuerol, E.1 aAviles, F., X.1 aSali, A.1 aMarti-Renom, M., A.1 aOliva, B.  uhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1850556201778nas a2200205   4500008004100000245007500041210006900116300001300185490000800198520097700206653011101183653003901294653004101333100002001374700001401394700002401408700001701432700001701449856010601466       2007                        eng d00aProtein translocation into peroxisomes by ring-shaped import receptors0 aProtein translocation into peroxisomes by ringshaped import rece  a4795-8020 v5813 aFolded and functional proteins destined for translocation from the cytosol into the peroxisomal matrix are recognized by two different peroxisomal import receptors, Pex5p and Pex7p. Both cargo-loaded receptors dock on the same translocon components, followed by cargo release and receptor recycling, as part of the complete translocation process. Recent structural and functional evidence on the Pex5p receptor has provided insight on the molecular requirements of specific cargo recognition, while the remaining processes still remain largely elusive. Comparison of experimental structures of Pex5p and a structural model of Pex7p reveal that both receptors are built by ring-like arrangements with cargo binding sites, central to the respective structures. Although, molecular insight into the complete peroxisomal translocon still remains to be determined, emerging data allow to deduce common molecular principles that may hold for other translocation systems as well.10aAmino Acid Sequence Binding Sites Humans Molecular Sequence Data Peroxisomes/*metabolism Protein Structure10aCytoplasmic and Nuclear/*chemistry10aTertiary Protein Transport Receptors1 aStanley, W., A.1 aFodor, K.1 aMarti-Renom, M., A.1 aSchliebs, W.1 aWilmanns, M.  uhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17884042