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Transcription elongation factor, N-terminal
This domain adopts a long alpha-hairpin structure. [1]. 7854424. Crystal structure of the GreA transcript cleavage factor from Escherichia coli. Stebbins CE, Borukhov S, Orlova M, Polyakov A, Goldfarb A, Darst SA;. Nature. 1995;373:636-640. (from Pfam)
GreA/GreB family elongation factor
This domain has an FKBP-like fold. [1]. 7854424. Crystal structure of the GreA transcript cleavage factor from Escherichia coli. Stebbins CE, Borukhov S, Orlova M, Polyakov A, Goldfarb A, Darst SA;. Nature. 1995;373:636-640. (from Pfam)
transcription elongation factor GreB
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 ternary complexes
transcription elongation factor GreB induces cleavage of the nascent transcript to allow the resumption of elongation from the new 3' terminus; releases sequences of up to 9 nucleotides in length
The GreA and GreB transcription elongation factors enable to continuation of RNA transcription past template-encoded arresting sites. Among the Proteobacteria, distinct clades of GreA and GreB are found. GreB differs functionally in that it releases larger oligonucleotides. This HMM describes proteobacterial GreB.
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