ID SYL_VIBVU Reviewed; 857 AA. AC Q8DFE2; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 130. DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049}; DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049}; DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049}; DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049}; GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; GN OrderedLocusNames=VV1_0272; OS Vibrio vulnificus (strain CMCP6). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=216895; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CMCP6; RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.; RT "Complete genome sequence of Vibrio vulnificus CMCP6."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl- CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA- CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00049}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00049}. 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; AE016795; AAO08806.1; -; Genomic_DNA. DR RefSeq; WP_011078381.1; NC_004459.3. DR AlphaFoldDB; Q8DFE2; -. DR SMR; Q8DFE2; -. DR KEGG; vvu:VV1_0272; -. DR HOGENOM; CLU_004427_0_0_6; -. DR Proteomes; UP000002275; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1. DR CDD; cd00812; LeuRS_core; 1. DR Gene3D; 2.20.28.290; -; 1. DR Gene3D; 3.10.20.590; -; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1. DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002302; Leu-tRNA-ligase. DR InterPro; IPR025709; Leu_tRNA-synth_edit. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR NCBIfam; TIGR00396; leuS_bact; 1. DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 2. DR Pfam; PF13603; tRNA-synt_1_2; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR PRINTS; PR00985; TRNASYNTHLEU. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..857 FT /note="Leucine--tRNA ligase" FT /id="PRO_0000152115" FT MOTIF 42..52 FT /note="'HIGH' region" FT MOTIF 617..621 FT /note="'KMSKS' region" FT BINDING 620 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" SQ SEQUENCE 857 AA; 96677 MW; DD9EAFE51BA20E77 CRC64; MQEQYNPQDI EQKVQQHWDN NKTFVVTEDP TKEKFYCLSM FPYPSGRLHM GHVRNYTIGD VVSRFQRLQG KNVMQPIGWD AFGLPAENAA VKNNTAPAPW TYENIEYMKN QLKLLGFGYD WNREFATCTP EYYRWEQEFF TKLYEKGLVY KKTSSVNWCP NDQTVLANEQ VEDGCCWRCD TPVEQKEIPQ WFIKITEYAQ ELLDDLDKLE GWPEMVKTMQ RNWIGRSEGV ELKFEVKGQQ DLEVYTTRPD TLMGVTYVGI AAGHPLAKIA AENNPELAAF IEECKNTKVA EAELATMEKK GMATGLTAIH PLNGREVPVY VANFVLMDYG TGAVMAVPAH DQRDFEFATK YGLDIIPVIK PIDGSELDIS EAAYTEKGVL FDSGEFDGLE FQAAFDAIAA KLEAEGKGTK TVNFRLRDWG VSRQRYWGAP IPMVTTEDGQ VHPVPADQLP VILPEDVVMD GVTSPIKADK EWAKTTFNGE PALRETDTFD TFMESSWYYA RYCSPQADDI LDPEKANYWL PVDQYIGGIE HACMHLLYSR FFHKLLRDAG YVTSDEPFKQ LLCQGMVLAD AFYYTNDKGG KEWVSPTEVK VERDGKGRIT SAVDNEGRNV EHSGMIKMSK SKNNGIDPQE MVDKYGADTV RLFMMFASPA DMTLEWQESG VEGANRFLKR VWKLVNEHTS KGAAEAVDAA ALSGDQKALR RDVHKTIAKV TDDVARRQTF NTAIAAVMEL MNKLAKAPQE SAQDRAILDE ALKAVVAMLY PITPHICFEM WTALGQQDID NASWPTYDEQ ALVEDEKLIV VQVNGKVRGK ITVAADATKE QVEEIGLNEE NVSKHLDGVT IRKVIYVPGK LLSIVAN //