ID   SYL_METBF               Reviewed;         966 AA.
AC   Q46AW0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=Mbar_A2048;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(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; CP000099; AAZ70982.1; -; Genomic_DNA.
DR   RefSeq; WP_011307028.1; NC_007355.1.
DR   AlphaFoldDB; Q46AW0; -.
DR   SMR; Q46AW0; -.
DR   STRING; 269797.Mbar_A2048; -.
DR   PRIDE; Q46AW0; -.
DR   EnsemblBacteria; AAZ70982; AAZ70982; Mbar_A2048.
DR   GeneID; 3625563; -.
DR   KEGG; mba:Mbar_A2048; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OMA; AWNMAFQ; -.
DR   OrthoDB; 4914at2157; -.
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.
FT   CHAIN           1..966
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009370"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           632..636
FT                   /note="'KMSKS' region"
FT   BINDING         635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   966 AA;  111095 MW;  B9AD29D5E713058E CRC64;
     MEQDYKPHEI EKKWQKKWDE SQIFQAEPDK REKFFITIPY PYLNGNLHAG HTRTFTIGDV
     VARHKRMLGY NVLYPMGFHV TGTPIVGLAE LIANRDPQTM DVYERLHGIP GDILPTLDTP
     EKIVDYFKRE SEKAMRNIGY SIDWRRKFTT TDPTYKKFIE WQYIRLGEKG LIVKGSHPVK
     WCPNDNNPVE DHDILYGEEA TIVEYTLIKF RYKDLVLPCA TLRPETTYGV TNLWVNPDVT
     YVKAKVTLDG NEEFWVVSKE AFRKLTFTDR TVEYIEDVPA KSIIGIKLTN PVTDDEVISL
     PASFVRPENG SGIVMSVPAH APFDYLALRD LYDVDLSEYG ITEDLRKIKL ISLIKVPEFG
     EFPAKEIVES MGITSQKDPK AEEATKIVYR REFHGGVLKE ITGKYEGQAV SKIKDILTRD
     FISSNTGETF YEFSEPVVCR CGTPCVVNMV KGQWFLNYSN PEWKAKVYKC LAQMRIVPEE
     YRVEFENKID WLKDKACARR KGLGTHLPFD KEWLIESLGD STIYMSYYII ARFIENGELK
     IENLTLSFFD YVLLGKGDSA AASADTGLSP ELLEEIRRHF NYWYPVDLRS SGKDLVPNHL
     LFFLFHHVAL FEEDKWPKAL AVNGFVSLEG QKMSKSKGPI LTMESAVSKY GADITRMYIL
     STAEQTQDAD WQRTGIESAR RQVDRFYSFA KGVIESGKRA DLSTELKQID RWILSRIQNY
     IRDTNSALYS IQTREAIQNS FFLLQNDVKW YQRRGGETLL YYVLDNWVRL MAPFTPHLCE
     EIWEAMGHKD PVSLAQYPLY NEGLIDDGAE LAEEMIKGTL EDVEEIIRVT KMTPQKVHLY
     TAPTWKAEAI RCACEMQLEC SLEVGNLIKK LMANPDLKRF GKEIPKFVQK IVPEFKSGSS
     DRYEILTGPD IDEQALLKES ISFLEKEIGC SVEVHSADSP AFDPEKKARF AEPLRPAIYI
     EGKKKE