ID   SYL_EHRCJ               Reviewed;         829 AA.
AC   Q3YSH6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
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}; OrderedLocusNames=Ecaj_0282;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jake;
RX   PubMed=16707693; DOI=10.1128/jb.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA   Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA   Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(2006).
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; CP000107; AAZ68329.1; -; Genomic_DNA.
DR   RefSeq; WP_011304407.1; NC_007354.1.
DR   AlphaFoldDB; Q3YSH6; -.
DR   SMR; Q3YSH6; -.
DR   STRING; 269484.Ecaj_0282; -.
DR   EnsemblBacteria; AAZ68329; AAZ68329; Ecaj_0282.
DR   KEGG; ecn:Ecaj_0282; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000435; 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   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
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   PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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..829
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334752"
FT   MOTIF           34..44
FT                   /note="'HIGH' region"
FT   MOTIF           591..595
FT                   /note="'KMSKS' region"
FT   BINDING         594
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   829 AA;  94858 MW;  B2A7FC52332711ED CRC64;
     MHYDFKKVEQ DIQKKWNFYT DVKKAQCYVL EMFPYPSGNI HMGHLRNYTI GDVIARYKRA
     CGINVFHPIG WDAFGLPAEN AALSYNINPQ TWTKNNIDNM RCQLKSIGLS YDWNKELATC
     DADYYKHEQA FFLDFLKCGL AYRKESLVNW DPIDQTVLAN EQVIDGKGWR SGAVVEKRKL
     SQWFLKITDF AEELLNDLKV LDKWPEKVKL MQERWIGRSE GVVVDFEILN INKTLQVFTT
     CPHTLFGASF IAVSFDHPIL QCVSDSDIIQ QINDFDKNNL ITDASSTVEK FGINSGLVVK
     HPFLCMNLPV YVVNFVLMDY ATGAVFGCPA HDQRDFEFAK KYNLQIKQVV FPEIDIDLGK
     EAYVGSGTMK NSDFLDGMTV DEAKEAMIAK LQLLGIGDKM TYYRIHDWGI SRQRYWGCPI
     PIIYCEKCGT VPVSRKDLPV TLPQDVDFTK SGNPLDNHPT WKYVKCPSCG MDAERETDTF
     DTFFESSWYF AAFCGTSSGI DKDTCNMLLP VDYYIGGIEH AVLHLLYSRF FCRALTKCGY
     FNVKEPFSSL ITQGMVCHAT YSDAQGNYLF PEEARKMMEE GQHVNVGRAE KMSKSKKNVV
     NLEYIIDKYG ADTARLFILS DTPPDRDIEW LDDGIEGASK YLSKLWRMIV SYDQINLNFN
     VEDIPEDAIK YRRCVHKIVS DITSDLEFCR LNCAVAKFRE LSNILSEMIR TSVNSDVVSE
     AICILIRVIE PFIPHIAEKL WENIGGKDML WNQMWPKADT ELLIERNVNI AVQVNGKFIR
     TLTVANNIDN DQLKSMALEM AKNKIGNSVV KNVYIIPKRA VNIVIEKLS