Posfai, J., Bhagwat, A. S., Roberts, R. J. (December 1988) Sequence Motifs Specific for Cytosine Methyltransferases. Gene, 74 (1). pp. 262-266. ISSN 0378-1119
Abstract
Using a new alignment method, the sequences of 13 m5C methyltransferases (MTases) have been examined. Five extremely well-conserved blocks of sequence have been detected and have been used as fixed points for the alignment of the 13 sequences. Following this initial alignment, five further blocks of similarity have been identified to give a total of ten recognizable blocks of sequence homology that are all arranged in a common order. The structures of these MTases consist of a variable-length N-terminal arm followed by eight well-conserved blocks each separated by small variable-length regions. A large variable-length segment of 90 to 270 amino acids (aa) then follows. After this are two blocks, and a variable-length C-terminal segment completes the sequence. Within the final alignment, 20 aa in the protein sequences, and 86 nucleotides in the nucleotide sequences are invariant. The strongest conservation is found in proximity to a suspected functional site that contains the dipeptide proline-cysteine. Consensus patterns can be defined for the five best conserved blocks and, when used as search motifs, are able to clearly distinguish between the m5C MTases and all other identified proteins in the PIR database. This suggests they may be of use in identifying putative MTases among protein sequences of unknown function.
| Item Type: | Paper |
|---|---|
| Subjects: | bioinformatics > genomics and proteomics > alignment > sequence alignment bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase |
| CSHL Authors: | |
| Communities: | CSHL labs > Roberts lab |
| Depositing User: | Gail Sherman |
| Date: | 25 December 1988 |
| Date Deposited: | 26 Sep 2017 18:39 |
| Last Modified: | 26 Sep 2017 18:39 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/35196 |
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