PROSITE documentation PDOC51784Exonuclease I (ExoI) SH3-like and C-terminal domains profiles
In bacteria, exonuclease I (ExoI) is a monomeric processive 3'-5' exonuclease that degrades single-stranded DNA. The enzyme has been implicated as primarily being involved in repairing frameshift mutations. ExoI consists of three domains: an N-terminal nuclease domain with homology to the proofreading domain of E. coli DNA polymereae I and other DnaQ superfamily enzymes, a central domain with a portion that resembles an SH3 domain fold and a C-terminal α-helical domain. While a typical SH3-like domain consists of five or six antiparallel β-strands that form a compact β-sandwich, the β-sandwich of the SH3-like domain in ExoI is surrounded by α-helices, resulting in a substantially elaborated fold (see <PDB:1FXX>) [1,2,3].
The profile we developed covers the entire ExoI SH3-like and C-terminal domains.
Last update:December 2015 / First entry.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Breyer W.A. Matthews B.W. |
| Title | Structure of Escherichia coli exonuclease I suggests how processivity is achieved. | |
| Source | Nat. Struct. Biol. 7:1125-1128(2000). | |
| PubMed ID | 11101894 | |
| DOI | 10.1038/81978 |
| 2 | Authors | Busam R.D. |
| Title | Structure of Escherichia coli exonuclease I in complex with thymidine 5'-monophosphate. | |
| Source | Acta Crystallogr. D 64:206-210(2008). | |
| PubMed ID | 18219121 | |
| DOI | 10.1107/S090744490706012X |
| 3 | Authors | Korada S.K.C. Johns T.D. Smith C.E. Jones N.D. McCabe K.A. Bell C.E. |
| Title | Crystal structures of Escherichia coli exonuclease I in complex with single-stranded DNA provide insights into the mechanism of processive digestion. | |
| Source | Nucleic Acids Res. 41:5887-5897(2013). | |
| PubMed ID | 23609540 | |
| DOI | 10.1093/nar/gkt278 |
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