ID   SYL_NOCSJ               Reviewed;         848 AA.
AC   A1SHV9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Noca_1884;
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) 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}.
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DR   EMBL; CP000509; ABL81394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1SHV9; -.
DR   SMR; A1SHV9; -.
DR   STRING; 196162.Noca_1884; -.
DR   PRIDE; A1SHV9; -.
DR   EnsemblBacteria; ABL81394; ABL81394; Noca_1884.
DR   KEGG; nca:Noca_1884; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; DIDWADV; -.
DR   Proteomes; UP000000640; 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   Gene3D; 3.90.740.10; -; 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   PANTHER; PTHR43740; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 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; 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..848
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334783"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           69..79
FT                   /note="'HIGH' region"
FT   MOTIF           614..618
FT                   /note="'KMSKS' region"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   848 AA;  94337 MW;  9FBB75346A8DB865 CRC64;
     MCPEQPHDTR AERDEMSEQT QQAAQPAETA AYDVRAIQDK WLPVWERLDP FRADDSSPRE
     KKYALTMFPY PSGDLHMGHA EVTALHDVVA RYWWQRGYEV LNPMGWDSFG LPAENAAIRN
     DEHPATYTYA NIETQYESFK RYAVSFDWSR RLHTSDPEYY RWTQWLFLKF RERGLAYRKS
     SPVNWCPNDQ TVLANEQVVD GRCERCGAEV TKRELTQWYF KITDYAQELL DRLDDLEPTW
     PARVVTAQRN WIGRSEGAHV DFVVDGRDEP ITVYTTRPDT IFGTTFMVVA VDSPLAAELV
     TDAQRPAFEA YREEIRKETE IERLSTDRPK TGVDLGVTAT NPVTGTQIPV WATDYVLADY
     GTGAVMGVPG GDQRDWEFAT EMGLDIVRTT QTPEGFDGEA YHGEGPAINS PAPGADAPLD
     INGLPVDEAK RATIEFLEQQ GTGAGAVNFR LRDWLLSRQR YWGVPIPIIH CDACGEVAVP
     YDQLPLELPE LRGADLKPKG VSPLAAAEEW VNVACPECGG AATRDSDTMD TFVDSSWYFL
     RYCSPDYTEG PFDVEKAKAW MPADIYVGGV EHAVLHLLYA RFFTKVLRDM GMLEVDEPFA
     AQLNQGIVIN QGKKMSKSLG NGVSLGDQLA EFGVDAVRVT LVFAGPPEDD IDWADVSPAG
     ALRFLQRAWR LSGDVTSEAG TPAAGGDVAL RRVTARTVHD AAELIESYRF NVMVARVMEL
     VNATRKAIDG APGPADPAVR EATETVAILL SLVAPYVAEE MWERLGHEPT VARVGWPEVD
     PALLVEEQVT AVVQIQGKVR ARLEVAPDIS EADLEQLAMA DPAVVRAIDG RPVRKVIVRA
     PKLVNVVV