Families of Type III Restriction Endonucleases Based on Sequence Similarity of the Catalytic Domain

Abstract Restriction endonucleases are well known because of their use in genetic engineering. However, many groups of these enzymes that are not suitable for practical use have been studied much worse. Type III restriction endonucleases are among the least studied major groups of these enzymes. In particular, such endonucleases are poorly represented in protein domain databases, which can be explained by the large size of these proteins and their complex domain organization, including regions of unidentified spatial structure and highly variable sequence. In this work we used predicted structures of Type III restriction endonucleases to detect the catalytic domains that perform hydrolysis of DNA. As a result, seven families of such domains were identified and described with HMM profiles. The obtained profiles were used to classify all known Type III restriction endonucleases, correct their annotations, and search for new representatives in complete prokaryotic genomes.

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Publication Details

Journal
Molecular Biology
Published
2026-07-27
DOI
https://doi.org/10.1134/s0026893326700044
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
0.00
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article

Families of Type III Restriction Endonucleases Based on Sequence Similarity of the Catalytic Domain

I. S. Rusinov, A. S. Karyagina, A. V. Alexeevski, S. A. Spirin
Molecular Biology
Bacterial Genetics and Biotechnology
article

Families of Type III Restriction Endonucleases Based on Sequence Similarity of the Catalytic Domain

I. S. Rusinov, A. S. Karyagina, A. V. Alexeevski, S. A. Spirin
article en

Abstract

Abstract Restriction endonucleases are well known because of their use in genetic engineering. However, many groups of these enzymes that are not suitable for practical use have been studied much worse. Type III restriction endonucleases are among the least studied major groups of these enzymes. In particular, such endonucleases are poorly represented in protein domain databases, which can be explained by the large size of these proteins and their complex domain organization, including regions of unidentified spatial structure and highly variable sequence. In this work we used predicted structures of Type III restriction endonucleases to detect the catalytic domains that perform hydrolysis of DNA. As a result, seven families of such domains were identified and described with HMM profiles. The obtained profiles were used to classify all known Type III restriction endonucleases, correct their annotations, and search for new representatives in complete prokaryotic genomes.

Molecular BiologyVol. 60(4)
National Research University Higher School of Economics (RU), Lomonosov Moscow State University (RU), Kurchatov Institute (RU), Ministry of Health of the Russian Federation (RU), All-Russian Scientific Research Institute of Food Biotechnology (RU)
Openalex Percentile: Top 9%
Bacterial Genetics and Biotechnology
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