ID   SYL_RUTMC               Reviewed;         816 AA.
AC   A1AV52;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; OrderedLocusNames=Rmag_0005;
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Ruthia.
OX   NCBI_TaxID=413404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(2007).
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}.
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DR   EMBL; CP000488; ABL01809.1; -; Genomic_DNA.
DR   RefSeq; WP_011737435.1; NC_008610.1.
DR   AlphaFoldDB; A1AV52; -.
DR   SMR; A1AV52; -.
DR   STRING; 413404.Rmag_0005; -.
DR   EnsemblBacteria; ABL01809; ABL01809; Rmag_0005.
DR   KEGG; rma:Rmag_0005; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002587; 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: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; 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; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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; Reference proteome.
FT   CHAIN           1..816
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009420"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           574..578
FT                   /note="'KMSKS' region"
FT   BINDING         577
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   816 AA;  93408 MW;  B464A5B928F544BF CRC64;
     MNSEYNAQKI EAQAQKYWQE NKSFEVSEDT SKEKYYCLSM FPYPSGSLHM GHVRNYSIGD
     VISRYQKMQG KNVMQPIGWD GFGLPAENAA LENKVSPAKW TYENIDYMRD QLSKLGFGYD
     WSREIATCHQ KYYRWEQWLF IKLFEKDLVY KKNAIVNWDP VDQTVLANEQ VIDGRGWRSN
     ALIEKKKISQ WFMRITNYAD ELIYGLDKLD GWPDAVKTMQ KNWIGKSVGL EVDFPRHNAD
     SIKVYTTRPD TLMGVTYLVI SSEHPIALEA GKNNPQVQAF IDECKTIQIT KETMKTIDKK
     GIDLGVKCIH PITSDDVPIW IANFVLIGYG TGAVMSVPAH DKRDYEFAKK YGIAIKKVIN
     ENISIDKNAM TDKGVLFNSG EFNGLNFDQA FNEIAKTLTD KNLGRKKTNY RLQDWGISRQ
     RYWGCPIPII NCQNCGIVVV PEADLPVVLP EVMSFDSVGS LIKKMPEFYQ TTCPKCGKMA
     QQETDTLDTF FESSWYFARY TCKDNNDKML DKRANYWLAN GGVDQYIGGI EHAILHLLYA
     RFFNKLLRDE GFIKNDEPFK NLLTQGMVLK DGAKMSKSKG NTVDPAQMIE KYGADTVRLF
     ILFAAPPTQN LEWSDSGLEG VHRFINKVYR LIMDFIQDHK SHAIGTLNNF DKAQKDIRLK
     THQTLSKITD NMSRRYLFNT VIAALMKLCN TLSKFNDTSK TSMAIRQESI HILLKTLSPI
     APHLCHYLWK KLGNIKAIIN EPWPNVDKSA LVQDKMQIIV QVNGKLRTKL MFSTDVDNAQ
     IEAQTLANEN ITKFTKGKII VKVIIVPNKL VNIVVK