ID   SYL_ROSCS               Reviewed;         904 AA.
AC   A7NFJ2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Rcas_0077;
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000804; ABU56214.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7NFJ2; -.
DR   SMR; A7NFJ2; -.
DR   STRING; 383372.Rcas_0077; -.
DR   PRIDE; A7NFJ2; -.
DR   EnsemblBacteria; ABU56214; ABU56214; Rcas_0077.
DR   KEGG; rca:Rcas_0077; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000263; 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; 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   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.
FT   CHAIN           1..904
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334806"
FT   MOTIF           49..59
FT                   /note="'HIGH' region"
FT   MOTIF           663..667
FT                   /note="'KMSKS' region"
FT   BINDING         666
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   904 AA;  101643 MW;  9B368CC849759718 CRC64;
     MSDTGTKRRI ERFDPAIEPK WREFWEREGI FKAGRRAGAP RRYILEMFPY PSGDLHIGHL
     KNYVIGDALT RYYVIRGYDV LHPFGWDAFG LPAENAAIKY GRHPREWTYG NIAESKKSLE
     IAGIMYDWSR EVTTCDPDYY RWNQWLFLLL YRKGLAYRAK ATVNWDPVDQ TVLANEQVDA
     EGRSWRSGAK VEKRELEQWF FRITAYAERL LNDLDKLDKW PENVKTMQRN WIGRSEGAEV
     TFLALPPGAD LHAPPPPDAE PLVVFTTRPD TLWGATFMVL APEHPLVSKL TAPERRAEVE
     AYIARARMES EIERTSATRE KTGVFLGSYA INPVNDERIP IWIADYVLMG YGAGAIMAVP
     AHDERDFAFA RQFGLPVRVV VQPPGETLDG ATMTEAWPGD GVMVNSGPIN GLPVGKGEGQ
     SVKATIAWLE ANGKGKGTVT YRLRDWLISR QRYWGTPIPM LHLPDGTIKP VPEDQLPVVL
     PEVQDYLPKG KSPLAAAESW VNTIDPETGQ PARRDTDTMD TFVDSSWYFL RFCDARNDRE
     IFSREAAHRW MPVDQYIGGV EHAILHLLYA RFITKVLYDE GLVPDDEPFR ALFTQGMVQR
     RVRTPLEVVA PGMVRFPEEL RRKLELPADA QSLDQARALL KERGYTLEEE SNGGFTAVSG
     PVTMSKSAGN GIPVGPFVRQ YGSDVARIVV LFAAPPENSM EWTDEGVAGA QRFLNRIVAL
     FSPDREEIVA ALNSGNGAAP EGEERALYRK LHETIRKVTL DTEQFRFNTA IAALMELLNE
     ASRYRSEAGR VTPVFAQTAA TFARLLSPFA PHLAEELHSW CGGTGSVYDT GWPEWDEAAL
     ALDEVEIVLQ VNGKLRGRIM APANADEQQL REWALTNPRV LSFVGDKTVR KVVVVPGKLV
     NVVV