RNA polymerase, RBP11-like subunit
IPR036603
Definition
RNA polymerase (RNAP) II, which is responsible for all mRNA synthesis in eukaryotes, consists of 12 subunits. Subunits Rpb3 and Rpb11 form a heterodimer that is functionally analogous to the archaeal RNAP D/L heterodimer, and the prokaryotic RNAP alpha subunit homodimer. In each case, they play a key role in RNAP assembly by forming a platform on which the catalytic subunits (eukaryotic Rpb1/Rpb2, and prokaryotic beta/beta') can interact PMID:11453250. These different subunits share regions of homology. Rpb11 contains a domain (Rpb11-like domain) that is required for dimerisation, and binds to a homologous region on Rpb3. The Rpb11-like domain in Rpb11 and archaeal L subunits is contiguous, whereas in Rpb3, archaeal D, and prokaryotic alpha subunits ([interpro:IPR011263]), the Rpb11-like domain is interrupted by an insert domain ([interpro:IPR011262]). In the prokaryotic RNAP alpha subunit, the Rpb11-like domain and the insert domain form two subregions of the N-terminal domain. The structure of the Rpb11-like domain consists of a two-layer α/β fold consisting of β(2)-α-β(2)-α. Rpb3 and Rpb11 in yeast RNAP [[cite:PMID:11313498], [cite:PMID:12191485], [cite:PMID:16537912]] have been shown to share a high degree of sequence and structural similarity to the alpha subunit of bacterial RNAP [[cite:PMID:9657722], [cite:PMID:12000971]].
6 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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