ID   SYL_WOLTR               Reviewed;         865 AA.
AC   Q5GS31;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 132.
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=Wbm0605;
OS   Wolbachia sp. subsp. Brugia malayi (strain TRS).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=292805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRS;
RX   PubMed=15780005; DOI=10.1371/journal.pbio.0030121;
RA   Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N.,
RA   Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J.,
RA   Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S.,
RA   Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D.,
RA   Koonin E., Slatko B.;
RT   "The Wolbachia genome of Brugia malayi: endosymbiont evolution within a
RT   human pathogenic nematode.";
RL   PLoS Biol. 3:599-614(2005).
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; AE017321; AAW71193.1; -; Genomic_DNA.
DR   RefSeq; WP_011256803.1; NC_006833.1.
DR   AlphaFoldDB; Q5GS31; -.
DR   SMR; Q5GS31; -.
DR   STRING; 292805.Wbm0605; -.
DR   KEGG; wbm:Wbm0605; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   Proteomes; UP000000534; 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; 3.40.50.620; HUPs; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; 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; 2.
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..865
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009464"
FT   MOTIF           36..46
FT                   /note="'HIGH' region"
FT   MOTIF           608..612
FT                   /note="'KMSKS' region"
FT   BINDING         611
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   865 AA;  98820 MW;  CACA7BBB8CECF813 CRC64;
     MKYDFKNVEK FYQDRWDFSI GKNNEQGKCY VLEMFPYPSG KIHMGHLRNY VIGDVIARYK
     RACGFEVLHP IGWDAFGLPA ENAARDNNVN PAAWTKENID NMRAQLKSIG LSYNWERELS
     TCEADYYKHE QKFFLDFLKQ GLVYRKKSWV NWDPIDQTVL ANEQVVDGKG WRSGAIVEKR
     ELSQWFLKIT DFAEDLLECL QGLENWPEKV KMMQDRWIGK SEGVTIEFKI VGLNKKLKVF
     TTCPHTLFGA SFCAVAIEHP IVQDLMSKEI QDLISSIKIQ GKNNEKVGIY TGLNVKHPFL
     DKELPLYVAN FVLMEYREGA IFGCPAHDQR DFEFAQEYDL PIIPVISSAR LGIIPACDQG
     SYTGSQCQAT RMADGLNEEY TNNSIMFNSE FLNGLTVSEA RKVIVEKLEE KGIGKKTINY
     RLHDWGVSRQ RYWGCPIPVI YCKNCGTVPV PEEDLPVTLP TDVDFTSGGN PLDKHPTWKF
     VNCPKCKEQA ERETDTFDTF FESSWYFAAF CSENKSIDKN ACNRFMPVDY YIGGIEHAIL
     HLLYSRFFCR ALTKCGYFNV KEPFSTLITQ GMVCHVTYKD KNGKWLFPEE AKRLITQGAK
     IQVGKVEKMS KSKKNTVDPN FIIEKYGADT ARLFVLSDTP PEKDMEWSND GVEGCSRYIN
     KLWRMVMQFK PVVILNQSPV KQVADTEIQK EDMLSHAGMI PDKNVTGKFL GYRKKIHKLL
     HGLTDDLENC RLNCVVAKFR EMTNLIAEID VKTGKSLINE GICILIRVVE PFIPHLAESL
     WREIGGEGML YLQPWPKAAK SLLIDDVVTV AVQINGKLRA TIEVAINLHQ EELKQIAINS
     VSNRVDQSKV RAVYAVSNKI VNIVT
//