Protein families and their evolution-a structural perspective
- PMID: 15954844
- DOI: 10.1146/annurev.biochem.74.082803.133029
Protein families and their evolution-a structural perspective
Abstract
We can now assign about two thirds of the sequences from completed genomes to as few as 1400 domain families for which structures are known and thus more ancient evolutionary relationships established. About 200 of these domain families are common to all kingdoms of life and account for nearly 50% of domain structure annotations in the genomes. Some of these domain families have been very extensively duplicated within a genome and combined with different domain partners giving rise to different multidomain proteins. The ways in which these domain combinations evolve tend to be specific to the organism so that less than 15% of the protein families found within a genome appear to be common to all kingdoms of life. Recent analyses of completed genomes, exploiting the structural data, have revealed the extent to which duplication of these domains and modifications of their functions can expand the functional repertoire of the organism, contributing to increasing complexity.
Similar articles
-
Domain combinations in archaeal, eubacterial and eukaryotic proteomes.J Mol Biol. 2001 Jul 6;310(2):311-25. doi: 10.1006/jmbi.2001.4776. J Mol Biol. 2001. PMID: 11428892
-
Identification and distribution of protein families in 120 completed genomes using Gene3D.Proteins. 2005 May 15;59(3):603-15. doi: 10.1002/prot.20409. Proteins. 2005. PMID: 15768405
-
The structure of the protein universe and genome evolution.Nature. 2002 Nov 14;420(6912):218-23. doi: 10.1038/nature01256. Nature. 2002. PMID: 12432406 Review.
-
Multi-domain protein families and domain pairs: comparison with known structures and a random model of domain recombination.J Struct Funct Genomics. 2003;4(2-3):67-78. doi: 10.1023/a:1026113408773. J Struct Funct Genomics. 2003. PMID: 14649290
-
Protein folds, functions and evolution.J Mol Biol. 1999 Oct 22;293(2):333-42. doi: 10.1006/jmbi.1999.3054. J Mol Biol. 1999. PMID: 10529349 Review.
Cited by
-
The Unfinished Reconstructed Nature of the Last Universal Common Ancestor.J Mol Evol. 2024 Oct;92(5):584-592. doi: 10.1007/s00239-024-10187-8. Epub 2024 Jul 18. J Mol Evol. 2024. PMID: 39026043 Free PMC article. Review.
-
Development of Allosteric Ribozymes for ATP and l-Histidine Based on the R3C Ligase Ribozyme.Life (Basel). 2024 Apr 17;14(4):520. doi: 10.3390/life14040520. Life (Basel). 2024. PMID: 38672790 Free PMC article.
-
Improving enzyme functional annotation by integrating in vitro and in silico approaches: The example of histidinol phosphate phosphatases.Protein Sci. 2024 Feb;33(2):e4899. doi: 10.1002/pro.4899. Protein Sci. 2024. PMID: 38284491 Free PMC article.
-
CropGF: a comprehensive visual platform for crop gene family mining and analysis.Database (Oxford). 2023 Jul 1;2023:baad051. doi: 10.1093/database/baad051. Database (Oxford). 2023. PMID: 37410917 Free PMC article.
-
Latent generative landscapes as maps of functional diversity in protein sequence space.Nat Commun. 2023 Apr 19;14(1):2222. doi: 10.1038/s41467-023-37958-z. Nat Commun. 2023. PMID: 37076519 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources