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Sequence motifs specific for cytosine methyltransferases

Using a new alignment method, the sequences of 13 m 5 C 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... Full description

Journal Title: Gene 1988, Vol.74(1), pp.261-265
Main Author: Posfai, Janos
Other Authors: Bhagwat, Ashok S , Roberts, Richard J
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0378-1119 ; E-ISSN: 1879-0038 ; DOI: 10.1016/0378-1119(88)90299-5
Link: https://www.sciencedirect.com/science/article/pii/0378111988902995
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recordid: elsevier_sdoi_10_1016_0378_1119_88_90299_5
title: Sequence motifs specific for cytosine methyltransferases
format: Article
creator:
  • Posfai, Janos
  • Bhagwat, Ashok S
  • Roberts, Richard J
subjects:
  • Restriction-Modification Systems
  • Sequence Alignment
  • Sequence Database
  • Engineering
  • Biology
  • Anatomy & Physiology
ispartof: Gene, 1988, Vol.74(1), pp.261-265
description: Using a new alignment method, the sequences of 13 m 5 C 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 wellconserved 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 m 5 C 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.
language: eng
source:
identifier: ISSN: 0378-1119 ; E-ISSN: 1879-0038 ; DOI: 10.1016/0378-1119(88)90299-5
fulltext: fulltext
issn:
  • 0378-1119
  • 03781119
  • 1879-0038
  • 18790038
url: Link


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titleSequence motifs specific for cytosine methyltransferases
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subjectRestriction-Modification Systems ; Sequence Alignment ; Sequence Database ; Engineering ; Biology ; Anatomy & Physiology
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descriptionUsing a new alignment method, the sequences of 13 m 5 C 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 wellconserved 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 m 5 C 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.
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