{"metadata":{"accession":"IPR013177","entry_id":null,"type":"domain","go_terms":null,"source_database":"interpro","member_databases":{"pfam":{"PF08213":"Mitochondrial mRNA-processing protein COX24, C-terminal"},"smart":{"SM01155":"Mitochondrial domain of unknown function (DUF1713)"}},"integrated":null,"hierarchy":{"accession":"IPR013177","name":"Ribosomal protein bS22, C-terminal","type":"Domain","children":[]},"name":{"name":"Ribosomal protein bS22, C-terminal","short":"Ribosomal_bS22_C"},"description":[{"text":"<p>This domain is found at the C-terminal of small ribosomal subunit protein bS22m (formerly known as mS38; also called COX24 in yeast). The mitochondrial protein bS22m shares sequence homology with bacterial bS22, particularly in the N-terminal region, leading to its renaming to reflect their common evolutionary origin. This domain is also found in the bacterial small ribosomal subunit protein bS22, which occupies a similar position beneath the mRNA channel and interacts with 16S rRNA helix 44 to stabilise the decoding centre [[cite:PUB00163225]]. In some proteins this domain convers the whole length of the protein.</p>","llm":false,"checked":false,"updated":false},{"text":"<p>bS22m is a component of the mitochondrial ribosome (mitoribosome), responsible for the synthesis of mitochondrial genome-encoded proteins, including essential transmembrane subunits of the mitochondrial respiratory chain. Mitoribosomes are attached to the mitochondrial inner membrane, and translation products are cotranslationally integrated into the membrane [[cite:PUB00089004], [cite:PUB00098057]]. In mammals, bS22m preferentially stimulates translation initiation of COX1, COX2, and COX3 mRNAs [[cite:PUB00163226]]. In yeast, bS22m is also involved in the splicing of the COX1 mRNA [[cite:PUB00076420]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00163225":{"PMID":37034768,"ISBN":null,"volume":null,"issue":null,"year":2023,"title":"The small mycobacterial ribosomal protein, bS22, modulates aminoglycoside accessibility to its 16S rRNA helix-44 binding site.","URL":null,"raw_pages":"2023.03.31.535098","medline_journal":"bioRxiv","ISO_journal":"bioRxiv","authors":["Majumdar S","Deep A","Sharma MR","Canestrari J","Stone M","Smith C","Koripella RK","Keshavan P","Banavali NK","Wade JT","Gray TA","Derbyshire KM","Agrawal RK."],"DOI_URL":"https://doi.org/10.1101/2023.03.31.535098"},"PUB00076420":{"PMID":16339141,"ISBN":null,"volume":"281","issue":"6","year":2006,"title":"COX24 codes for a mitochondrial protein required for processing of the COX1 transcript.","URL":null,"raw_pages":"3743-51","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Barros MH","Myers AM","Van Driesche S","Tzagoloff A."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M510778200"},"PUB00089004":{"PMID":25609543,"ISBN":null,"volume":"6","issue":null,"year":2015,"title":"Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography.","URL":null,"raw_pages":"6019","medline_journal":"Nat Commun","ISO_journal":"Nat Commun","authors":["Pfeffer S","Woellhaf MW","Herrmann JM","Forster F."],"DOI_URL":"https://doi.org/10.1038/ncomms7019"},"PUB00098057":{"PMID":28154081,"ISBN":null,"volume":"355","issue":"6324","year":2017,"title":"The structure of the yeast mitochondrial ribosome.","URL":null,"raw_pages":"528-531","medline_journal":"Science","ISO_journal":"Science","authors":["Desai N","Brown A","Amunts A","Ramakrishnan V."],"DOI_URL":null},"PUB00163226":{"PMID":30968120,"ISBN":null,"volume":"47","issue":"11","year":2019,"title":"The mitoribosome-specific protein mS38 is preferentially required for synthesis of cytochrome c oxidase subunits.","URL":null,"raw_pages":"5746-5760","medline_journal":"Nucleic Acids Res","ISO_journal":"Nucleic Acids Res","authors":["Mays JN","Camacho-Villasana Y","Garcia-Villegas R","Perez-Martinez X","Barrientos A","Fontanesi F."],"DOI_URL":"https://doi.org/10.1093/nar/gkz266"},"PUB00078824":{"PMID":17125467,"ISBN":null,"volume":"403","issue":"1","year":2007,"title":"Aurora-A kinase interacting protein 1 (AURKAIP1) promotes Aurora-A degradation through an alternative ubiquitin-independent pathway.","URL":null,"raw_pages":"119-27","medline_journal":"Biochem J","ISO_journal":"Biochem. J.","authors":["Lim SK","Gopalan G."],"DOI_URL":"http://dx.doi.org/10.1042/BJ20061272"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":43,"interactions":0,"matches":6671,"pathways":7,"proteins":6670,"proteomes":5397,"sets":0,"structural_models":{"alphafold":5136,"bfvd":0},"structures":118,"taxa":11352},"entry_annotations":{"alignment:seed":39,"alignment:full":3583},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}