ID SYL_TRIEI Reviewed; 929 AA. AC Q114V5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 27-MAR-2024, entry version 108. 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=Tery_1704; OS Trichodesmium erythraeum (strain IMS101). OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae; OC Oscillatoriales; Microcoleaceae; Trichodesmium. OX NCBI_TaxID=203124; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMS101; RX PubMed=25831533; DOI=10.1073/pnas.1422332112; RA Walworth N., Pfreundt U., Nelson W.C., Mincer T., Heidelberg J.F., Fu F., RA Waterbury J.B., Glavina del Rio T., Goodwin L., Kyrpides N.C., Land M.L., RA Woyke T., Hutchins D.A., Hess W.R., Webb E.A.; RT "Trichodesmium genome maintains abundant, widespread noncoding DNA in situ, RT despite oligotrophic lifestyle."; RL Proc. Natl. Acad. Sci. U.S.A. 112:4251-4256(2015). 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; CP000393; ABG50969.1; -; Genomic_DNA. DR AlphaFoldDB; Q114V5; -. DR SMR; Q114V5; -. DR STRING; 203124.Tery_1704; -. DR KEGG; ter:Tery_1704; -. DR eggNOG; COG0495; Bacteria. DR HOGENOM; CLU_004427_0_0_3; -. DR OrthoDB; 9810365at2; -. 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; 3.10.20.590; -; 1. DR Gene3D; 3.40.50.620; HUPs; 2. 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..929 FT /note="Leucine--tRNA ligase" FT /id="PRO_1000009459" FT MOTIF 42..52 FT /note="'HIGH' region" FT MOTIF 614..618 FT /note="'KMSKS' region" FT BINDING 617 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" SQ SEQUENCE 929 AA; 105715 MW; CBEA3835F051A92A CRC64; MDSKYNPVSI EQKWQKNWAE QNQDQTPINN NQPKFYALSM FPYPSGNLHM GHVRNYTITD VIARLKRMQG YRVLHPMGWD AFGLPAENAA IDRGIPPAKW TLENIAQMKE QLRRLGFSID WDKEVATCTP EYYRWTQWIF LQFFQAGLAY QKESAVNWDP IDQTVLANEQ VDGEGRSWRS GAKVERKMLR QWFFKITDYA EQLLNDLDKL PGWPERVKLM QANWIGKSVG AYLEFPIVGM DQKIGVFTTR PDTVYGVSYV VLAPEHPLTA KVTTPEQQIT VETFIKEVAA ESELERTAED KPKRGVPTGG KAINPFNNQE VPIWIADYVL YEYGTGAVMG VPAHDVRDFQ FAKQYNLPIK TVIVPDDSND DHKLTEAYTD VGVMVNSGPF NGEKSTVAKK AIIELAEDEG YGKGRVQYRL RDWLISRQRY WGAPIPIIHC PKCGAVPVPD EDLPVKLPES VEFSGRGPSP LAKLEDWVNV SCPSCGTPAK RETDTMDTFI DSSWYYLRYP DATNEEQVFD SKIVNDWLPV DQYVGGIEHA ILHLLYSRFF TKVLRDRGLC DFDEPFQNLL TQGMVQGVTY KNPVTGKYIP FADVNPQEPK DPKTGDKLEV FFEKMSKSKY NGVDPMDVMA TYGADTARMF ILFKAPPEKD LEWDDADVQG QFRFLNRVWS MVMEFLANHS FSELKAKHHG ITQADLKDLG WSRYLITEIT KNISAFKLRN VVKVYPVEDV LVAIEAKFNY SETQQETKDD LQKVLTWIKS RFGGELTKAE KDVRRAVHNA IKEVTEDLDG DYQFNTAVSE MMKLSNALGD ASCKDSPIYA EALETLLLLL APFAPHITEE LWQIAGNFGS VHTHAWPKFD PEALVVDEIT LVIQIKGKTR GTIQVPAQAD KETLEKLARE SDIAQRHLAG KEIKKVIVVP RKLVNFVVI //