{"metadata":{"accession":"PF03690","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR003226","hierarchy":null,"name":{"name":"Uncharacterised protein family (UPF0160)","short":"MYG1_exonuc"},"description":[{"text":"<p>This entry includes MYG1 exonuclease from human and its orthologues. MYG1 is a 3'-5' exonuclease which cleaves in situ on specific transcripts in both nucleus and mitochondrion. It is involved in regulating spatially segregated organellar RNA processing, acting as a coordinator of nucleo-mitochondrial crosstalk [[cite:PUB00155300]]. In nucleolus, processes pre-ribosomal RNA involved in ribosome assembly and alters cytoplasmic translation. In mitochondrial matrix, it processes 3'-termini of the mito-ribosomal and messenger RNAs and controls translation of mitochondrial proteins [[cite:PUB00155300]]. Overexpression of MYG1 has been associated with the autoimmune disorder vitiligo, suggesting that MYG1 may play some role in human innate immunity [[cite:PUB00155301]]. Studies in yeast suggested a potential antiviral function of MYG1 [[cite:PUB00155302]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00155300":{"PMID":31081026,"ISBN":null,"volume":"47","issue":"11","year":2019,"title":"Myg1 exonuclease couples the nuclear and mitochondrial translational programs through RNA processing.","URL":null,"raw_pages":"5852-5866","medline_journal":"Nucleic Acids Res","ISO_journal":"Nucleic Acids Res","authors":["Grover R","Burse SA","Shankrit S","Aggarwal A","Kirty K","Narta K","Srivastav R","Ray AK","Malik G","Vats A","Motiani RK","Thukral L","Roy SS","Bhattacharya S","Sharma R","Natarajan K","Mukerji M","Pandey R","Gokhale RS","Natarajan VT."],"DOI_URL":"https://doi.org/10.1093/nar/gkz371"},"PUB00155301":{"PMID":23706493,"ISBN":null,"volume":"71","issue":"3","year":2013,"title":"Correlation of increased MYG1 expression and its promoter polymorphism with disease progression and higher susceptibility in vitiligo patients.","URL":null,"raw_pages":"195-202","medline_journal":"J Dermatol Sci","ISO_journal":"J Dermatol Sci","authors":["Dwivedi M","Laddha NC","Begum R."],"DOI_URL":"https://doi.org/10.1016/j.jdermsci.2013.04.026"},"PUB00155302":{"PMID":36888656,"ISBN":null,"volume":"120","issue":"11","year":2023,"title":"Diverse yeast antiviral systems prevent lethal pathogenesis caused by the L-A mycovirus.","URL":null,"raw_pages":"e2208695120","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc Natl Acad Sci U S A","authors":["Chau S","Gao J","Diao AJ","Cao SB","Azhieh A","Davidson AR","Meneghini MD."],"DOI_URL":"https://doi.org/10.1073/pnas.2208695120"}},"set_info":{"accession":"CL0137","name":"HAD"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":89,"interactions":0,"matches":5764,"pathways":0,"proteins":5549,"proteomes":4320,"sets":1,"structural_models":{"alphafold":4529},"structures":21,"taxa":10390},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":167,"alignment:full":4159},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"24an","name":"Crystal structure of nuclease MYG1 bound to Mn2+ and AMP"}}}