Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Evidence for an evolutionary relationship among type-II restriction endonucleases.

Gene - 4 Jul 1995

Jeltsch A, Kröger M, Pingoud A

Abstract excerpt

Type-II restriction-modification (R-M) systems comprise two enzymes, a DNA methyltransferase (MTase) and a restriction endonuclease (ENase), each of which specifically interact with the same 4-8 bp sequence. All type-II MTases share several amino acid (aa) sequence motifs, which makes an evolutionary relatedness among these enzymes probable. The type-II ENases, in contrast, except for some homologous...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Base Composition
Share to Biological Evolution

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genotype

Share to Phenotype

Share to Phylogeny

Share to Sequence Homology, Amino Acid

Share to Substrate Specificity

Source

Identifiers

PMID: 7628720
DOI: 10.1016/0378-1119(95)00181-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evidence for an evolutionary relationship among type-II restriction endonucleases.PMID 7628720Read ↗

Diversity of DNA methyltransferases that recognize asymmetric target sequences.Semantic proximity Read ↗

Molecular evolution of DNA-(cytosine-N4) methyltransferases: evidence for their polyphyletic origin.Semantic proximity Read ↗

DsaV methyltransferase and its isoschizomers contain a conserved segment that is similar to the segment in Hhai methyltransferase that is in contact with DNA bases.Semantic proximity Read ↗

Novel m4C modification in type I restriction-modification systems.Semantic proximity Read ↗

EcoBLMcrX, a classical modification-dependent restriction enzyme in Escherichia coli B: Characterization in vivo and in vitro with a new approach to cleavage site determination.Semantic proximity Read ↗

Individual- and population-based diversity in restriction-modification systems.Semantic proximity Read ↗

The BsaHI restriction-modification system: cloning, sequencing and analysis of conserved motifs.Semantic proximity Read ↗

Mutations that confer de novo activity upon a maintenance methyltransferase.Semantic proximity Read ↗

Mva1269I: a monomeric type IIS restriction endonuclease from Micrococcus varians with two EcoRI- and FokI-like catalytic domains.Semantic proximity Read ↗

MnlI--The member of H-N-H subtype of Type IIS restriction endonucleases.Semantic proximity Read ↗

EcoKI with an amino acid substitution in any one of seven DEAD-box motifs has impaired ATPase and endonuclease activities.Semantic proximity Read ↗

Genotyping of DNA using sequence-specific methyltransferases followed by immunochemical detection.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.