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SWIM, a novel Zn-chelating domain present in bacteria, archaea and eukaryotes.
- Source :
-
Trends in biochemical sciences [Trends Biochem Sci] 2002 Aug; Vol. 27 (8), pp. 384-6. - Publication Year :
- 2002
-
Abstract
- A previously undetected domain with a CxCx(n)CxH pattern of predicted zinc-chelating residues was identified in a variety of prokaryotic and eukaryotic proteins. These include bacterial ATPases of the SWI2/SNF2 family, plant MuDR transposases and transposase-derived Far1 nuclear proteins, and vertebrate MEK kinase-1. This domain was designated SWIM after SWI2/SNF2 and MuDR, and is predicted to have DNA-binding and protein-protein interaction functions in different contexts.
- Subjects :
- Amino Acid Sequence
Animals
Archaeal Proteins chemistry
Bacterial Proteins chemistry
Binding Sites
Cyclin-Dependent Kinase Inhibitor Proteins
DNA metabolism
Eukaryotic Cells chemistry
Fungal Proteins chemistry
Fungal Proteins metabolism
Molecular Sequence Data
Plant Proteins chemistry
Plant Proteins metabolism
Protein Serine-Threonine Kinases chemistry
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Transposases chemistry
Transposases metabolism
Vertebrates
Archaeal Proteins metabolism
Bacterial Proteins metabolism
Cell Cycle Proteins
DNA-Binding Proteins metabolism
MAP Kinase Kinase Kinase 1
Nuclear Proteins
Protein Serine-Threonine Kinases metabolism
Repressor Proteins
Saccharomyces cerevisiae Proteins
Transcription Factors metabolism
Zinc metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0968-0004
- Volume :
- 27
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Trends in biochemical sciences
- Publication Type :
- Academic Journal
- Accession number :
- 12151216
- Full Text :
- https://doi.org/10.1016/s0968-0004(02)02140-0