ID G3LS55_9BRAS Unreviewed; 161 AA. AC G3LS55; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 22-FEB-2023, entry version 13. DE RecName: Full=E3 ubiquitin-protein ligase listerin {ECO:0000256|RuleBase:RU367090}; DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367090}; DE AltName: Full=RING-type E3 ubiquitin transferase listerin {ECO:0000256|RuleBase:RU367090}; DE Flags: Fragment; OS Capsella rubella. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella. OX NCBI_TaxID=81985 {ECO:0000313|EMBL:AEN83400.1}; RN [1] {ECO:0000313|EMBL:AEN83400.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cr1209_26_TS4 {ECO:0000313|EMBL:AEN83397.1}, Cr1215_17_TS1 RC {ECO:0000313|EMBL:AEN83398.1}, Cr39_1_TS1 RC {ECO:0000313|EMBL:AEN83399.1}, and Cr50_1_TS1 RC {ECO:0000313|EMBL:AEN83400.1}; RX PubMed=21856647; RA Qiu S., Zeng K., Slotte T., Wright S., Charlesworth D.; RT "Reduced efficacy of natural selection on codon usage bias in selfing RT Arabidopsis and Capsella species."; RL Genome Biol. Evol. 3:868-880(2011). CC -!- FUNCTION: E3 ubiquitin-protein ligase. Component of the ribosome CC quality control complex (RQC), a ribosome-associated complex that CC mediates ubiquitination and extraction of incompletely synthesized CC nascent chains for proteasomal degradation. CC {ECO:0000256|RuleBase:RU367090}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={ECO:0000256|RuleBase:RU367090}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|RuleBase:RU367090}. CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC). CC {ECO:0000256|RuleBase:RU367090}. CC -!- SIMILARITY: Belongs to the LTN1 family. CC {ECO:0000256|RuleBase:RU367090}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JN406164; AEN83397.1; -; Genomic_DNA. DR EMBL; JN406165; AEN83398.1; -; Genomic_DNA. DR EMBL; JN406166; AEN83399.1; -; Genomic_DNA. DR EMBL; JN406167; AEN83400.1; -; Genomic_DNA. DR AlphaFoldDB; G3LS55; -. DR UniPathway; UPA00143; -. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule. DR GO; GO:1990112; C:RQC complex; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProtKB-UniRule. DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule. DR InterPro; IPR039795; LTN1/Rkr1. DR PANTHER; PTHR12389:SF0; E3 UBIQUITIN-PROTEIN LIGASE LISTERIN; 1. DR PANTHER; PTHR12389; ZINC FINGER PROTEIN 294; 1. PE 3: Inferred from homology; KW Metal-binding {ECO:0000256|RuleBase:RU367090}; KW Transferase {ECO:0000256|RuleBase:RU367090}; KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367090}; KW Zinc {ECO:0000256|RuleBase:RU367090}; KW Zinc-finger {ECO:0000256|RuleBase:RU367090}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AEN83400.1" FT NON_TER 161 FT /evidence="ECO:0000313|EMBL:AEN83400.1" SQ SEQUENCE 161 AA; 17957 MW; 61A8E07404294BC8 CRC64; LQRHVSNEER TLLLDLFRKQ KQDPVASSVV TQLPAVQILL ARLIVIAVSY CGNDFNEDDW DFVFSNLKRL IQSAVVVMEE TSENVNDFIS GVSSVEKEND TLEGLGHIVF ISDPSISNAQ NALSAFSLLN ALVKHKSTEG EDNLKSLADE TWDPVKDRIL E //