ID SYLA_AQUAE Reviewed; 634 AA. AC O66680; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 141. DE RecName: Full=Leucine--tRNA ligase subunit alpha; DE EC=6.1.1.4; DE AltName: Full=Leucyl-tRNA synthetase subunit alpha; DE Short=LeuRS; GN Name=leuS; OrderedLocusNames=aq_351; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."; RL Nature 392:353-358(1998). 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 -!- SUBUNIT: Seems to consist of an alpha chain and a beta chain. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000305}. 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; AE000657; AAC06643.1; -; Genomic_DNA. DR PIR; D70331; D70331. DR RefSeq; NP_213240.1; NC_000918.1. DR RefSeq; WP_010880178.1; NC_000918.1. DR PDB; 3O0A; X-ray; 1.77 A; A/B=225-443. DR PDB; 3PZ0; X-ray; 2.40 A; A/B/C/D=228-439. DR PDB; 3PZ5; X-ray; 2.50 A; A/B=228-439. DR PDBsum; 3O0A; -. DR PDBsum; 3PZ0; -. DR PDBsum; 3PZ5; -. DR AlphaFoldDB; O66680; -. DR SMR; O66680; -. DR STRING; 224324.aq_351; -. DR EnsemblBacteria; AAC06643; AAC06643; aq_351. DR KEGG; aae:aq_351; -. DR PATRIC; fig|224324.8.peg.284; -. DR eggNOG; COG0495; Bacteria. DR HOGENOM; CLU_004427_0_1_0; -. DR InParanoid; O66680; -. DR OrthoDB; 9810365at2; -. DR BRENDA; 6.1.1.4; 396. DR EvolutionaryTrace; O66680; -. DR Proteomes; UP000000798; 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-KW. DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro. DR CDD; cd00812; LeuRS_core; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. 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; PF00133; tRNA-synt_1; 1. DR Pfam; PF13603; tRNA-synt_1_2; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR PRINTS; PR00985; TRNASYNTHLEU. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..634 FT /note="Leucine--tRNA ligase subunit alpha" FT /id="PRO_0000151962" FT MOTIF 43..51 FT /note="'HIGH' region" FT STRAND 230..237 FT /evidence="ECO:0007829|PDB:3O0A" FT HELIX 241..243 FT /evidence="ECO:0007829|PDB:3O0A" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:3O0A" FT HELIX 250..259 FT /evidence="ECO:0007829|PDB:3O0A" FT STRAND 260..269 FT /evidence="ECO:0007829|PDB:3O0A" FT HELIX 271..276 FT /evidence="ECO:0007829|PDB:3O0A" FT STRAND 279..282 FT /evidence="ECO:0007829|PDB:3O0A" FT HELIX 288..298 FT /evidence="ECO:0007829|PDB:3O0A" FT HELIX 304..315 FT /evidence="ECO:0007829|PDB:3O0A" FT HELIX 319..323 FT /evidence="ECO:0007829|PDB:3O0A" FT STRAND 330..338 FT /evidence="ECO:0007829|PDB:3O0A" FT TURN 340..342 FT /evidence="ECO:0007829|PDB:3O0A" FT STRAND 345..351 FT /evidence="ECO:0007829|PDB:3O0A" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:3PZ0" FT STRAND 361..365 FT /evidence="ECO:0007829|PDB:3O0A" FT TURN 367..369 FT /evidence="ECO:0007829|PDB:3O0A" FT HELIX 371..380 FT /evidence="ECO:0007829|PDB:3O0A" FT TURN 396..398 FT /evidence="ECO:0007829|PDB:3O0A" FT HELIX 411..413 FT /evidence="ECO:0007829|PDB:3O0A" FT HELIX 418..431 FT /evidence="ECO:0007829|PDB:3O0A" FT STRAND 434..437 FT /evidence="ECO:0007829|PDB:3O0A" SQ SEQUENCE 634 AA; 73989 MW; 0119CA3F7A018766 CRC64; MMKEFNPREI EKKWQKRWEE AGVFKAQEGK PNKFYVLEMF PYPSGRIHMG HVRNYTIGDA IARYLKMRGK NILHPMGWDA FGLPAENAAI KHGIHPAKWT YENIDYMKKQ LKILGFSYDW DREIATCDPE YYKWNQWIFL KMLERGIAYR KTAKVNWCPH DQTVLANEQV IEGKCWRCGT PIVQKEVPSW FLRITAYADR LLEDLKKLEG KWPERVIAQQ RNWIGRSEGA LIRFYVEIEE PEKFLNCVPE ELKETLLKEK RIYIDVFTTR PDTVFGATFV VLAPEHPLVP VLACIGERLG NACYSDVENF VEKMKKMSTR ERTMEEDKEG VFLGVYATNP ANGEKIPVWS ANYVLYEYGT GAIMCVPAHD QRDWEFAKKY DLPIKVVVKP EGAWDFEKGA YEGKGTLVNS DGFDGLDSET AKRKITEWLQ DRGLGEKKVS YRLRDWNISR QRYWGTPIPV VYCEKCGMVP VPEDQLPVKL PLDVKFTGQG NPLETSEEFV NTTCPKCGGK ARRETDTMDT FFDSSWYFLR FCDPKNDREP FSREKVDYWM PVDVYIGGIE HAVLHLLYAR FFQKFLKDLG LVRDDEPFEK LITQGMVLKK WVSVKKLLDY LGLSEEDEVE ELKKRLEELG ARRA //