{"metadata":{"accession":"PF04002","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR025657","hierarchy":null,"name":{"name":"RadC-like JAB domain","short":"RadC"},"description":[{"text":"<p>A family of proteins present widely across the bacteria. This family was named initially with reference to the E. coli radC102 mutation which suggested that RadC was involved in repair of DNA lesions [[cite:PUB00009802]]. However the relevant mutation has subsequently been shown to be in recG, where radC is in fact an allele of recG [[cite:PUB00044698]]. In addition, a personal communication from Claverys, J-P, et al, indicates a total failure of all attempts to characterise a radiation-related function for RadC in Streptococcus pneumoniae, suggesting that it is not involved in repair of DNA lesions, in recombination during transformation, in gene conversion, nor in mismatch repair. Computational analysis, however, provides a possible function. The RadC-like family belong to the JAB superfamily  of metalloproteins [[cite:PUB00057473]]. The domain shows fusions to an N-terminal  Helix-hairpin-Helix (HhH) domain in most instances. Other domain combinations include fusions to the anti-restriction module ArdC, the DinG/RAD3-like superfamily II helicases and the DNAG-like primase. In some bacteria, closely related DinG/Rad3- like superfamily II helicases are fused to a 3'-5' exonuclease in the  same position as the RadC-like JAB domain. These conserved domain associations lead to the hypothesis that the RadC-like JAB domains  might function as a nuclease [[cite:PUB00057473]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00057473":{"PMID":21890906,"ISBN":null,"volume":"39","issue":"22","year":2011,"title":"Evolution of the deaminase fold and multiple origins of eukaryotic editing and mutagenic nucleic acid deaminases from bacterial toxin systems.","URL":null,"raw_pages":"9473-97","medline_journal":"Nucleic Acids Res","ISO_journal":"Nucleic Acids Res.","authors":["Iyer LM","Zhang D","Rogozin IB","Aravind L."],"DOI_URL":"http://dx.doi.org/10.1093/nar/gkr691"},"PUB00009802":{"PMID":10224240,"ISBN":null,"volume":"152","issue":"1","year":1999,"title":"Tandem repeat recombination induced by replication fork defects in Escherichia coli requires a novel factor, RadC.","URL":null,"raw_pages":"5-13","medline_journal":"Genetics","ISO_journal":"Genetics","authors":["Saveson CJ","Lovett ST."],"DOI_URL":"http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=10224240&action=stream&blobtype=pdf"},"PUB00044698":{"PMID":11053371,"ISBN":null,"volume":"182","issue":"22","year":2000,"title":"radC102 of Escherichia coli is an allele of recG.","URL":null,"raw_pages":"6287-91","medline_journal":"J Bacteriol","ISO_journal":"J. Bacteriol.","authors":["Lombardo MJ","Rosenberg SM."],"DOI_URL":"http://dx.doi.org/10.1128/JB.182.22.6287-6291.2000"}},"set_info":{"accession":"CL0366","name":"JAB"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":69,"interactions":0,"matches":19208,"pathways":0,"proteins":19203,"proteomes":13115,"sets":1,"structural_models":{"alphafold":12619},"structures":1,"taxa":19503},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":535,"alignment:full":9593},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}