Rnh70p YGR276C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27549999
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Rnh70p YGR276C

Summary

Rnh70p YGR276C is a protein[1].

Key Facts

  • Rnh70p YGR276C's instance of is recorded as protein[2].
  • Rnh70p YGR276C's subclass of is recorded as protein[3].
  • Rnh70p YGR276C's UniProt protein ID is recorded as P53331[4].
  • Rnh70p YGR276C's part of is recorded as Ribonuclease H superfamily[5].
  • Rnh70p YGR276C's part of is recorded as Ribonuclease H-like superfamily[6].
  • Rnh70p YGR276C's part of is recorded as Exonuclease, RNase T/DNA polymerase III family[7].
  • Rnh70p YGR276C's part of is recorded as RNA exonuclease 1-like, exonuclease domain, protein family[8].
  • Rnh70p YGR276C's has part is recorded as Exonuclease, RNase T/DNA polymerase III[9].
  • Rnh70p YGR276C's has part is recorded as RNA exonuclease 1-like, exonuclease domain[10].
  • Rnh70p YGR276C's RefSeq protein ID is recorded as NP_011792[11].
  • Rnh70p YGR276C's molecular function is recorded as 3'-5'-exoribonuclease activity[12].
  • Rnh70p YGR276C's molecular function is recorded as exonuclease activity[13].
  • Rnh70p YGR276C's molecular function is recorded as nucleic acid binding[14].
  • Rnh70p YGR276C's molecular function is recorded as nuclease activity[15].
  • Rnh70p YGR276C's molecular function is recorded as RNA binding[16].
  • Rnh70p YGR276C's molecular function is recorded as 3'-5' exonuclease activity[17].
  • Rnh70p YGR276C's molecular function is recorded as hydrolase activity[18].
  • Rnh70p YGR276C's molecular function is recorded as protein binding[19].
  • Rnh70p YGR276C's molecular function is recorded as exonuclease activity[20].
  • Rnh70p YGR276C's cell component is recorded as nucleus[21].
  • Rnh70p YGR276C's cell component is recorded as nucleus[22].
  • Rnh70p YGR276C's biological process is recorded as generation of mature 3'-end of 5S rRNA generated by RNA polymerase III[23].
  • Rnh70p YGR276C's biological process is recorded as ribosome biogenesis[24].
  • Rnh70p YGR276C's biological process is recorded as exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)[25].
  • Rnh70p YGR276C's biological process is recorded as tRNA processing[26].

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [2] . Q905695. Retrieved . wikidata.org.
  2. [3] . Q20641742. Retrieved . wikidata.org.
  3. [4] . Q905695. Retrieved . wikidata.org.
  4. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] . wikidata.org.
  7. [8] . wikidata.org.
  8. [9] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . Q20641742. Retrieved . wikidata.org.
  11. [12] . Three conserved members of the RNase D family have unique and overlapping functions in the processing of 5S, 5.8S, U4, U5, RNase MRP and RNase P RNAs in yeast. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domains. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . An inter-species protein-protein interaction network across vast evolutionary distance. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . Three conserved members of the RNase D family have unique and overlapping functions in the processing of 5S, 5.8S, U4, U5, RNase MRP and RNase P RNAs in yeast. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Three conserved members of the RNase D family have unique and overlapping functions in the processing of 5S, 5.8S, U4, U5, RNase MRP and RNase P RNAs in yeast. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] . Wikidata. wikidata.org.

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Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Rnh70p YGR276C. Retrieved May 3, 2026, from https://4ort.xyz/entity/rnh70p-ygr276c
MLA “Rnh70p YGR276C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/rnh70p-ygr276c.
BibTeX @misc{4ortxyz_rnh70p-ygr276c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Rnh70p YGR276C}}, year = {2026}, url = {https://4ort.xyz/entity/rnh70p-ygr276c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Rnh70p YGR276C — https://4ort.xyz/entity/rnh70p-ygr276c (retrieved 2026-05-03)

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