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Any macromolecular complex composed of two or more polypeptide subunits, which may or may not be identical. Protein complexes may have other associated non-protein prosthetic groups, such as nucleotides, metal ions or other small molecules. A pentameric complex related to replication factor C, which loads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) onto DNA and has roles in telomere length regulation and other aspects of genome stability. In Saccharomyces the subunits are known as Elg1p, Rfc2p, Rfc3p, Rfc4p, and Rfc5p. A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which the constituent parts function together. A constituent part of an intracellular organelle, an organized structure of distinctive morphology and function, occurring within the cell. Includes constituent parts of the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton but excludes the plasma membrane. Any constituent part of a chromosome, a structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.

View Gene Ontology (GO) Term

GO TERM SUMMARY

Name: Elg1 RFC-like complex
Acc: GO:0031391
Aspect: Cellular Component
Desc: A pentameric complex related to replication factor C, which loads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) onto DNA and has roles in telomere length regulation and other aspects of genome stability. In Saccharomyces the subunits are known as Elg1p, Rfc2p, Rfc3p, Rfc4p, and Rfc5p.
Synonyms:
  • Elg1-RLC
  • RFC (Elg1)
  • Elg1-RFC
Proteins in PDR annotated with:
   This term: 14 [Search]
   Term or descendants: 14 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0031391 - Elg1 RFC-like complex (interactive image map)

YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle