ID   SYL_WOLWR               Reviewed;         838 AA.
AC   C0R573;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=WRi_000480;
OS   Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=66084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wRi;
RX   PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA   Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA   Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA   Andersson S.G.;
RT   "The mosaic genome structure of the Wolbachia wRi strain infecting
RT   Drosophila simulans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009).
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; CP001391; ACN94915.1; -; Genomic_DNA.
DR   RefSeq; WP_012673049.1; NZ_MKIF01000170.1.
DR   AlphaFoldDB; C0R573; -.
DR   SMR; C0R573; -.
DR   STRING; 66084.WRi_000480; -.
DR   KEGG; wri:WRi_000480; -.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   Proteomes; UP000001293; 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; 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.
FT   CHAIN           1..838
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199234"
FT   MOTIF           36..46
FT                   /note="'HIGH' region"
FT   MOTIF           611..615
FT                   /note="'KMSKS' region"
FT   BINDING         614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   838 AA;  95498 MW;  59AC758234BF408D CRC64;
     MKYDFKNVER FCQDKWDFSV SKSSKQEKCY VLEMFPYPSG KIHMGHLRNY AIGDVIARYK
     RARGFEVLHP IGWDAFGLPA ENAARDNNIS PEIWTKENID NMRAQLKSIG LSYNWNRELS
     TCEPNYYTHE QKFFLDFLKH GLAYRKESWV NWDPVDQTVL ANEQVVDGKG WRSGAVVEKR
     KLSQWFLKIT DFAEDLLKCL QSLKNWPEKV KTMQERWIGK SEGATIEFEV VGLNKKLKVF
     TTYPHTLFGA SFCAVAAEHP IVQDLKNGSS VVIPVLDTGI QEIKSKREND EKIGVYTGLN
     VKHPFLDKEL PLYIANFVLM EYGEGAIFGC PAHDQRDFEF AQKYNLPIIP VISSAHLGVI
     PARDQNSYNG SQCQATQMTK EAYTGDGVMF NSEFLNGLMV SEAKEVIIKK LKEKGIGKKT
     TNYRLHDWGV SRQRYWGCPI PIIYCKDCGT VPVPEKDLPV ILPADVEFTS GGNPLDKHPT
     WKFVDCPKCG KQAERETDTF DTFFESSWYF AAFCSEDKSI DKDACNRFMP VDYYIGGIEH
     AILHLLYSRF FCRALTKCGY FDIKEPFSTL ITQGMVCHAT YKDENGKWLF LAEAKELIAR
     GTKVQVGKVE KMSKSKKNTV DPNFIIEKYG ADTARLFVLS DTPPEKDMEW SDDGVEGCSR
     YVNKLWRMVM QLKPVNMHYD NKSVTGGLLE YRKKIHKLLH GLTDDLENCR LNCVVAKFRE
     MTNLIAEIDV AAGKSLIDEG ICILIRVIEP FMPHLAESLW QEIGGQPWPK ADESLLVDDT
     VTIAVQINGK LRATIEVAIN LPQEELKKIA IDSVSSKIDQ NKVRTVYAVP NKIVNIVI
//