ID   SYL_NOCFA               Reviewed;         950 AA.
AC   Q5YN65;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 123.
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=NFA_55240;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD60376.1; -; Genomic_DNA.
DR   RefSeq; WP_011212058.1; NC_006361.1.
DR   AlphaFoldDB; Q5YN65; -.
DR   SMR; Q5YN65; -.
DR   STRING; 247156.NFA_55240; -.
DR   GeneID; 61136093; -.
DR   KEGG; nfa:NFA_55240; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000006820; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   Gene3D; 3.40.50.620; HUPs; 3.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; 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; Reference proteome.
FT   CHAIN           1..950
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152056"
FT   MOTIF           66..77
FT                   /note="'HIGH' region"
FT   MOTIF           721..725
FT                   /note="'KMSKS' region"
FT   BINDING         724
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   950 AA;  105624 MW;  2F6FF32904598B35 CRC64;
     MQDTRATESD VPEHRYNAAL AGRIERRWQQ RWLERGTFHA PNPTGPLAGP TATLPADKLF
     VQDMFPYPSG AGLHVGHPLG YIATDVFARY HRMRGRNVLH ALGYDAFGLP AEQYAVQTGA
     HPRDTTESNI ATMQRQLDRL GLGHDRRRSF ATTDPEYYRW TQWIFLQIYN AWYDLELNRA
     RPISELEEQF ASGARPAPDG KDWASMSQAE RAAVIDSYRL VYQTDSMVNW CPGLGTVLSN
     EEVTAEGRSE RGNFPVFRKR LWQWMMRITA YADRLVDDLD LLDWPENVKA MQRNWIGRSR
     GAQVRFDSPA GQIEVFTTRP DTLFGATYVV LAPEHDLVDA LAAAQWPADT DPRWTGGAAT
     PAEAVAQYRK SIAAKSDLER QENKEKTGVF LGVHAVNPVN GARVPIFIAD YVLSGYGTGA
     IMAVPGHDQR DWEFATAFGL PIVEVISGGD ITAAAHTGEG ELVNSDYLNG LSVEEAKATV
     IGRLEADGHG TGTIQYKLRD WLFARQRYWG EPFPIVYDED GAPHALPESM LPVRLPELDD
     FAPVTFDPDD ADSEPSPPLA KATDWVHVEL DLGDGPKKYR RDTNVMPNWA GSSWYQLRYA
     DPTNADAFCA KENEQYWLGP RTAEHGPDDP GGVDLYVGGV EHAVLHLLYA RFWQKVLFDL
     GYVSSSEPYR RLFNQGYIQA FAYTDPRGAY VPAAEVVERD GAFFWTDATG TEIEVSQEYG
     KIGKSLKNAI SPDEVCDQFG ADTFRFYEMS MGPLDTSRPW STKDVVGAHR FLQRVWRLVV
     DEETGASRVT EDAPTDETLR FLHRTIAGVD EDFAALRDNT AGAKLIELTN HLTKSYPSGT
     PRAAVEPLVL MLAPLAPHVA EELWERLGHS ESLAHGPFPV ADPAWLVEET VEYPIQVNGK
     VRSRIQVPAD ADNAAIEAAA LADEKIAALL AGATPRKLIV VPGRLVNIVA
//