PFAM accession number:PF03449
Interpro abstract (IPR022691):

Bacterial proteins GreA and GreB are necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. Arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked DNA/RNA/ polymerase ternary complexes. Cleavage of the nascent transcript by cleavage factors, such as GreA or GreB, allows the resumption of elongation from the new 3' terminus [ (PUBMED:8431948) (PUBMED:7854424) ]. Escherichia coli GreA and GreB are sequence homologues and have homologues in every known bacterial genome [ (PUBMED:12914698) ]. GreA induces cleavage two or three nucleotides behind the terminus and can only prevent the formation of arrested complexes while greB releases longer sequences up to eighteen nucleotides in length and can rescue preexisting arrested complexes. These functional differences correlate with a distinctive structural feature, the distribution of positively charged residues on one face of the N-terminal coiled coil. Remarkably, despite close functional similarity, the prokaryotic Gre factors have no sequence or structural similarity with eukaryotic TFIIS.

GO process:regulation of DNA-templated transcription, elongation (GO:0032784)
GO function:DNA binding (GO:0003677)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry GreA_GreB_N