ID   SYL_META3               Reviewed;         969 AA.
AC   A6UTK3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Maeo_0233;
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL   Submitted (JUN-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}.
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DR   EMBL; CP000743; ABR55825.1; -; Genomic_DNA.
DR   RefSeq; WP_011972957.1; NC_009635.1.
DR   AlphaFoldDB; A6UTK3; -.
DR   SMR; A6UTK3; -.
DR   STRING; 419665.Maeo_0233; -.
DR   EnsemblBacteria; ABR55825; ABR55825; Maeo_0233.
DR   GeneID; 5326548; -.
DR   KEGG; mae:Maeo_0233; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OMA; AWNMAFQ; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000001106; 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; -; 1.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_00049_A; Leu_tRNA_synth_A; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR020791; Leu-tRNA-lgase_arc.
DR   InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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; PTHR45794; PTHR45794; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00395; leuS_arch; 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..969
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334843"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           658..662
FT                   /note="'KMSKS' region"
FT   BINDING         661
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   969 AA;  112812 MW;  BEF958BA8BD0A60F CRC64;
     MSVDFVKIAE KWQKRWEEDK IFENPSKLKY TEQEKKDKFF ITAAFPYLNG VLHAGHLRTF
     TIPEITARYQ RMNNKTVLWT FGFHVSGTPI IGLAELLKKQ APETIWAYNK LHNIPMGELQ
     TLTTPENIVN YFSKKATESF KKMGFALDWR RNFKTDDETF KKFVEWQFLK LKEKNLIVKG
     SHPVRYCPSC DNPVEDHDLL KGEEATLQEY ILLKFKTKLN IEIDGEDKEY ECIIPMATLR
     PETIYGVVNA WINPNDTYHI IKVYDEVQSQ EEGSDEISLK YNGIWIVSKE ASDKLKNQDR
     TVELIKEIKG EELVGKIVIN PVNNKEVPLY PADFVSSEMG TGCVMSVPAH APKDFVALRD
     YYSSINKELT DDELISLIKI DGYGKYPAKE IVEKMGITNQ KDEKLEDATH TIYKQEFHKG
     ILNENCGEYE GIAVRDIKDK LASDFINNNM AETLQEFSIP EVVCRCGEKC IVKTVKGQWF
     ITYSDLEWKK KAHNWVDKMN FVPETIRMDF HNKIDWMKDK ACARKKGLGT RFPFDKDWVI
     ESLSDSTLYM AYYTVAKTIN TNNILPEQLI PELFDYVYYG KGDINEISNN TKIPVELINE
     MRNEFEYYYP LDWRCSAKDL VPNHLTFMIF NHVALFDDEK YYPKGIVVNG YVTIEGKKLS
     KSKGPVLPIE EVATNYGPDV GRFYITTCAE LPHDADVKFK EMEHARDNLI RFYELATELK
     DTEKTITELS TIDKWLLHKV HSDLKIINES YNEFQLRKIG TLFYGLTHNL KWYKRRGGNN
     NQLLKYVVEI WTKVLAPITP HLCEEIWEMF GYNKNNNYIS NETFPQLDNS YINENCELGE
     EFIKNTMDDI RNIINIANIA PKTIYLYTAD DWKFEVLKIM MENKGAPVNK MMPLIMKNAE
     LRRYGKEIPK LINEIVKNGI SNPIDEENIL NDAKQFLENE FQCKIIVNGE DIGNKKRFAI
     PNKVAIYIE