ID   SYL_MYCPU               Reviewed;         807 AA.
AC   Q98RB6;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 124.
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=MYPU_0930;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC   Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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; AL445563; CAC13266.1; -; Genomic_DNA.
DR   PIR; E90523; E90523.
DR   RefSeq; WP_010924897.1; NC_002771.1.
DR   AlphaFoldDB; Q98RB6; -.
DR   SMR; Q98RB6; -.
DR   STRING; 272635.gene:17576673; -.
DR   KEGG; mpu:MYPU_0930; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_14; -.
DR   BioCyc; MPUL272635:G1GT6-91-MONOMER; -.
DR   Proteomes; UP000000528; 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   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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   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; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..807
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152051"
FT   MOTIF           38..49
FT                   /note="'HIGH' region"
FT   MOTIF           579..583
FT                   /note="'KMSKS' region"
FT   BINDING         582
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   807 AA;  93884 MW;  C888CC0524A9A3A1 CRC64;
     MYNHKEIEKK WQKIWDQSKA FKTGNKSDKK YYVLDMFPYP SGSGLHVGHP EGYTATDIIA
     RFKRLKGFDV LHPMGWDAFG LPAEQYAIST GNNPNEFTQK NIATFKKQIK SLGLSYDFDK
     EVNTTDPKFY EQTQWIFKEL YKKGLAVLAD IDVNWCEELG TVLANEEVLI DKDGNKVSER
     GSFPVVKKKM RQWVLKITNY ADKLLEGLED LDWENSLKLL QKNWIGKSTG TKVKFALELL
     DESIEVFTTR IETIFGATFL TISPEHPLVE KIVTSENKEK VKDFIKEFEK LDDRQKADKN
     EKNGIFTGSY AINPFNQKKI PIWIGDFVLL SYGTGAIMSV PAHDKRDYEF ANKYGLEIKQ
     VIVSKENVEL PYLESGHLIN SSEFNGLSSK EAIEKLNQYV EKNNLGQVET FYKLRDWIFS
     RQRYWGEPFP VAFDDENNVY LIDGLVELPF MENIKPSKNG QSPLFNNKKW LYFEKDGKKL
     TRETNTMPQW AGSNWYYLAY ILKNADGSYE KLDSEEAKKR FKKWLPVDLY IGGQEHAVLH
     LLYSRFWHRF LYDIGVVPTK EPFQKVVNQG MILGTDGQKM SKSRGNIINP SEIVDELGAD
     TLRVYEMFMG PLTDDKDWQV ESIKGIRKWL ERVYRLFEMF FDGQKTIEKS NEDHLILSQY
     NKLIKEIENE VELLKFNTAI SKLMVFVNLL YKVEKIPSWE ILKNFALILS LFAPHIAEEL
     LEKMNQKQVK DQIWPTYDPT YLESNLTKYV IQINGKVRAI VDFELDKTQE EVLAKAMQIE
     KIKTLLENKN IIKVIFVANK VLNLIVK
//