ID A0A1J1EPS2_THETH Unreviewed; 878 AA. AC A0A1J1EPS2; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 14-DEC-2022, entry version 30. DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049}; DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049}; DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049}; DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049}; GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049, GN ECO:0000313|EMBL:BAW01681.1}; GN ORFNames=TTMY_1289 {ECO:0000313|EMBL:BAW01681.1}; OS Thermus thermophilus. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=274 {ECO:0000313|EMBL:BAW01681.1, ECO:0000313|Proteomes:UP000217909}; RN [1] {ECO:0000313|EMBL:BAW01681.1, ECO:0000313|Proteomes:UP000217909} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TMY {ECO:0000313|EMBL:BAW01681.1, RC ECO:0000313|Proteomes:UP000217909}; RA Fujino Y., Doi K.; RT "Complete genome sequence of Thermus thermophilus TMY."; RL Submitted (NOV-2016) 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:0000256|ARBA:ARBA00001372, ECO:0000256|HAMAP- CC Rule:MF_00049}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049, CC ECO:0000256|RuleBase:RU363035}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; AP017920; BAW01681.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1J1EPS2; -. DR SMR; A0A1J1EPS2; -. DR EnsemblBacteria; BAW01681; BAW01681; TTMY_1289. DR Proteomes; UP000217909; Chromosome. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.620; -; 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; IPR023356; Leu-tRNA-synth_dom3. DR InterPro; IPR025709; Leu_tRNA-synth_edit. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. 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 PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF14795; Leucyl-specific; 1. DR Pfam; PF00133; tRNA-synt_1; 2. DR Pfam; PF13603; tRNA-synt_1_2; 1. DR PRINTS; PR00985; TRNASYNTHLEU. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1. DR TIGRFAMs; TIGR00396; leuS_bact; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00049}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00049}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00049}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00049}; Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 12..171 FT /note="tRNA-synt_1" FT /evidence="ECO:0000259|Pfam:PF00133" FT DOMAIN 221..406 FT /note="tRNA-synt_1_2" FT /evidence="ECO:0000259|Pfam:PF13603" FT DOMAIN 419..579 FT /note="tRNA-synt_1" FT /evidence="ECO:0000259|Pfam:PF00133" FT DOMAIN 580..635 FT /note="Leucyl-specific" FT /evidence="ECO:0000259|Pfam:PF14795" FT DOMAIN 718..842 FT /note="Anticodon_1" FT /evidence="ECO:0000259|Pfam:PF08264" FT MOTIF 42..52 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049" FT BINDING 640 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049" SQ SEQUENCE 878 AA; 101135 MW; 414BED3C66927A61 CRC64; MEKYNPHAIE AKWQRFWEEK GFMKAKDLPG GRGKQYVLVM FPYPSGDLHM GHLKNYTMGD VLARFRRMQG YEVLHPMGWD AFGLPAENAA LKFGVHPKDW TYANIRQAKE SLRLMGILYD WDREVTTCEP EYYRWNQWIF LKMWEKGLAY RAKGLVNWCP KCQTVLANEQ VVEGRCWRHE DTPVEKRELE QWYLRITAYA ERLLKDLEGL DWPEKVKAMQ RAWIGRSEGA EILFPVEGKE VKIPVFTTRP DTLFGATFLV LAPEHPLTLE LAAPERREEV LAYVEAAKRK TEIERQAEGR EKTGVFLGAY ALNPATGERV PIWTADYVLY GYGTGAIMAV PAHDQRDYEF ARKFGLPIKK VIERPEDPLP EPLERAYEEP GIMVNSGPFD GTPSEEGKKR VIAWLEEKGL GKGRVTYRLR DWLISRQRYW GTPIPMVHCE ACGVVPVPEE ELPVLLPDLK DVEDIRPKGK SPLEAHPEFY ETTCPRCGGP AKRDTDTMDT FFDSSWYYLR YTDPHNDRLP FDPEKANAWM PVDQYIGGVE HAVLHLLYSR FFTKFLHDLG MVKVEEPFQG LFTQGMVLAW TDFGPVEVEG EVVRLPEPTR IRLEIPESAL SLEDVRKMGA ELRPHEDGTL HLWKPAVMSK SKGNGVMVGP FVKEQGADIA RITILFAAPP ENEMVWTEEG VQGAWRFLNR IYRRVAEDRE ALLATSEVFQ AEALEGKDRE LYGKLHETLK KVTEDLEALR FNTAIAALME FLNALYEYRK DRPVTPVYRT ALRYYLQMLF PFAPHLAEEL WHWFWPDSLF QAGWPELDEK ALEKDVVEVA VQVNGRVRGT IRIPKDAPLE VARAEALKVR NVQAHLEGKE VVKEIYVPGK ILNLVVRG //