InterPro : IPR006641

Name  YqgF/RNase H-like domain Short Name  YqgF/RNaseH-like_dom
Type  Domain Description  The YqgF domain family is described as RNase H-like and typified by the Escherichia coli protein YqgF [].YqgF domain-containing proteins are predicted to be ribonucleases or resolvases based on homology to RuvC Holliday junction resolvases.The group of proteins containing this domain are found primarily in the low-GC Gram-positive bacteria Holliday junction resolvases (HJRs) and in eukaryote orthologs. The RuvC HJRs are conspicuously absent in the low-GC Gram-positive bacterial lineage, with the exception of Ureaplasma urealyticum(, []). Furthermore, loss of function ruvC mutants of Escherichia colishow a residual HJR activity that cannot be ascribed to the prophage-encoded RusA resolvase []. This suggests that the YqgF family proteins could be alternative HJRs whose function partially overlaps with that of RuvC [].The functions of eukaryotic proteins having this domain are less well described. In Saccharomyces cerevisiae(Baker's yeast) Spt6p and its orthologues, the catalytic residues are substituted indicating that they lack the enzymatic function of resolvases []. Spt6p has been implicated in transcription initiation []and in maintaining normal chromatin structure during transcription elongation [].Horizontal gene transfer, lineage-specific gene loss and gene family expansion, and non-orthologous gene displacement seem to have been major forces in the evolution of HJRs and related nucleases. The diversity of HJRs and related nucleases in bacteria and archaea contrasts with their near absence in eukaryotes. The few detected eukaryotic representatives of the endonuclease fold and the RNase H fold have probably been acquired from bacteria via horizontal gene transfer. The identity of the principal HJR(s) involved in recombination in eukaryotes remains uncertain; this function could be performed by topoisomerase IB or by a novel, so far undetected, class of enzymes. Likely HJRs and related nucleases were identified in the genomes of numerous bacterial and eukaryotic DNA viruses. Gene flow between viral and cellular genomes has probably played a major role in the evolution of this class of enzymes.The YqgF domain is also found in Tex proteins, where maintains the core structural elements and aligns especially well with RuvC nucleases, although Tex does not appear to possess nuclease activity []. Tex (toxin expression) is a highly conserved bacterial protein involved in expression of critical toxin genes [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

1 Child Features

Id Name Short Name Type
IPR028231 Transcription elongation factor Spt6, YqgF domain Spt6_YqgF Domain

0 Contains

3 Found In

Id Name Short Name Type
IPR012337 Ribonuclease H-like domain RNaseH-like_dom Domain
IPR017072 Transcription elongation factor Spt6 TF_Spt6 Family
IPR005227 Resolvase, holliday junction-type, YqgF-like Resolv_Hlld_junc_YqgF-like Family

1 Parent Features

Id Name Short Name Type
IPR012337 Ribonuclease H-like domain RNaseH-like_dom Domain

5 Publications

First Author Title Year Journal Volume Pages
Aravind L SURVEY AND SUMMARY: holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories. 2000 Nucleic Acids Res 28 3417-32
Mahdi AA Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82. 1996 J Mol Biol 257 561-73
Kaplan CD Transcription elongation factors repress transcription initiation from cryptic sites. 2003 Science 301 1096-9
Fuchs TM A new gene locus of Bordetella pertussis defines a novel family of prokaryotic transcriptional accessory proteins. 1996 J Bacteriol 178 4445-52
Johnson SJ Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa. 2008 J Mol Biol 377 1460-73



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)