Histidine kinase/HSP90-like ATPase superfamily
IPR036890
Definition
This domain superfamily is found in several ATP-binding proteins, including: DNA mismatch repair protein MutL, Chaperone protein HtpG, DNA gyrase subunit B, Anti-sigma F factor, histidine kinase PMID:15157101, topoisomerases PMID:15105144, heat shock protein HSP90 [[cite:PMID:15292259], [cite:PMID:14718169], [cite:PMID:15217611]], phytochrome-like ATPases and DNA mismatch repair proteins. The fold of this domain consists of two layers, α/β, which contains an 8-stranded mixed β-sheet. DNA mismatch repair protein MutL is an essential component of the methyl-directed mismatch repair (MMR) system, which corrects replication errors and maintains genomic integrity. MutL functions in the Dam-dependent MMR pathway, where the methylation status of GATC sequences is used to distinguish the parental strand from the newly synthesised strand containing the replication error. MutL acts as a molecular matchmaker, facilitating the ATP-dependent assembly of stable complexes between DNA-binding proteins involved in the repair process without itself remaining part of the final effector complex. Following mismatch recognition by MutS, MutL is recruited to the site of damage, where it coordinates downstream repair events, including activation of the endonuclease MutH and recruitment of the UvrD helicase and exonucleases required for excision of the error-containing strand. The ATPase activity of MutL, mediated by its N-terminal GHKL domain, is essential for these functions, driving the conformational changes necessary for proper coordination of the repair machinery [[cite:PMID:32652606], [cite:PMID:10199405]].
32 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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