ID   SYL_UREP2               Reviewed;         806 AA.
AC   B1AJ10;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=UPA3_0387;
OS   Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; Ureaplasma.
OX   NCBI_TaxID=505682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA   Methe B.A., Glass J., Waites K., Shrivastava S.;
RT   "Genome sequence of Ureaplasma parvum serovar 3.";
RL   Submitted (FEB-2008) 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; CP000942; ACA33294.1; -; Genomic_DNA.
DR   RefSeq; WP_010891746.1; NC_010503.1.
DR   AlphaFoldDB; B1AJ10; -.
DR   SMR; B1AJ10; -.
DR   GeneID; 29672253; -.
DR   KEGG; upa:UPA3_0387; -.
DR   HOGENOM; CLU_004427_0_0_14; -.
DR   Proteomes; UP000002162; 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; 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; 2.
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.
FT   CHAIN           1..806
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000074849"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           580..584
FT                   /note="'KMSKS' region"
FT   BINDING         583
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   806 AA;  93299 MW;  B5F61AFE314A41A9 CRC64;
     MYNHNKIEKK WQKYWLDNKT FKFVDNPNNP KKFYVLDMFP YPSGKGLHVG HPKGYTATDV
     ISRFKRLNGY DVLHPIGWDA FGLPAEQYAL ETNNHPHTFT QQNIKIFRKQ LQMIGFDFDY
     DKEVDTTDPQ FYQWTQWIFV QLYKHNLAEI QDIDVNWCEN LGTVLSNEEV VLNDKNERVS
     ERGGHPVVRK PMKQWVLKIV DYADKLLDGL NEVEFSESLK SLQRNWIGKS IGTSVQFKIK
     DSLLTLDVFT TRIDTIYGVQ YLVVAPEHPI LKSITSEQQI NVVQSYIEQT KKISDLDRIA
     DTNKTGVFSG AYAINPINQE IIPIWVSDYV LMNFATGAVM GVPAHDERDY AFAKKYALPI
     KSVIDTKQKL PYAGDGLHIN SAMINGLNIK QSQNVLNDYL IKNHLGKKVA NYKLRNWIFS
     RQRYWGEPFP VLFDENNQIK IIEDLPVLLP NLNEFKPSKT GESPLANAQE WLYVEIDGKK
     YRRETNTMPQ WAGSSWYFLA YILKNEDGSY TPLNSEEAKK RFAKWLPVDV YIGGQEHAVL
     HLLYSRFWHR FLYDIGVVPT KEPFYKVINQ GMILGENNEK MSKSKGNVIN PDDIIASHGA
     DTLRIYEMFM GPLTASLPWN PDGLDAMRKW LDRVYRLYHN LSELEVVEDL NKLNEEIIIA
     YHTLIKNYTK AINEQAFNIA ISEMMVFVNV LYKNKVINYE LLDNFLILLS CYAPHLAEEL
     YSLNHSESVC LQKMPIYDEQ KIIAQNITIP IQINGKLKHT INVLRDTNAE ELVNLALACE
     QVKQEIGDQP IKKQIVVVNK IINFVI
//