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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 GreA
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. GreA differs functionally in that it releases smaller oligonucleotides. Because members of the family outside the Proteobacteria resemble GreA more closely than GreB, the GreB clade (TIGR01461) forms a plausible outgroup and the remainder of the GreA/B family, included in this model, is designated GreA. In the Chlamydias and some spirochetes, the region described by this HMM is found as the C-terminal region of a much larger protein.
transcription elongation factor GreA induces cleavage of the nascent transcript to allow the resumption of elongation from the new 3' terminus; releases sequences of 2 to 3 nucleotides
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