ID   SYL_METBU               Reviewed;         962 AA.
AC   Q12WA2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=Mbur_1356;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(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; CP000300; ABE52274.1; -; Genomic_DNA.
DR   RefSeq; WP_011499419.1; NC_007955.1.
DR   AlphaFoldDB; Q12WA2; -.
DR   SMR; Q12WA2; -.
DR   STRING; 259564.Mbur_1356; -.
DR   GeneID; 3997572; -.
DR   KEGG; mbu:Mbur_1356; -.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OrthoDB; 23906at2157; -.
DR   Proteomes; UP000001979; 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; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR   Gene3D; 3.30.2320.20; Class I aminoacyl-tRNA synthetases (RS); 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00395; leuS_arch; 1.
DR   PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
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..962
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009371"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           631..635
FT                   /note="'KMSKS' region"
FT   BINDING         634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   962 AA;  110794 MW;  735ABD6E1D31D010 CRC64;
     MQQDYNSSNI EQKWQQKWNE SKVFEAEADD RDKYFITIPY PYLNGNLHAG HTRTFTIGDV
     VARYKRMMGN NVLYPMGFHV TGTPIVGLAE LIQNRDPETM KVYTEFHGIP VETLKGMDTP
     EKIVDYFSVE AERSMRSIGY SIDWRRKFTT TDPNYKKFIE WQFNLLYEKD LIVKGSHPVK
     WCPNDDNPVE DHDILHGEEA TIIDYTLVKF KYDGMIIPCA TLRPETVFGV TNLWINPDLE
     HVKIKVTFEG REEVWVVSKE AYRKLIFTDR EVEFIEDVDA SSLIGIKVTN PLNDAQVITL
     PASFVKGENG SGIVMSVPSH APYDYLALRD LYDKDLREYG ITEDLRELKF ISLIKVKEFG
     EFPAIEAVEQ FGVKDQDDPK AEEATKIVYR REFHGGVLKE NTGKYSGMAV SKIKDVLTRD
     LIEMGIGEVF YEFSEPVVCR CGTPCVVNMV KGQWFLNYSN PEWKDKVYRC IENMDIIPED
     LRVEFNNKVD WLKDKACARK KGLGTLLPFD NQWLIESLGD STIYMSYYII AKFIAMGIET
     EQLVPELFDH VLLKKCSLET AAERSGIDAN IIEQISSDFE YWYPVDLRSS GKDLIPNHLL
     FFLFHHVAIF DEDKWPRAIA INGFVSLEGK KMSKSKGPLL TLNDAITNYG ADISRMYILS
     SAEQMQDADW KNSGIETARK QIERFYNFSK DIIGSGIPTC NVENLKGIDK WMLSRLQQRI
     LETNEALDTI RTRNALQNAY FLLFNDIRWY QKRGGNALLC EVLDVWIRLM APFTPHICEE
     IWEAIGHTDN DLISLADYPQ YDESLVDTQA EFTEELIGGT LSDVDEIIRV TKLTPKKAIL
     YTSPEWKMET FKKALSMQKE GNLNPGILIK DLMRDPEMRS HGKEVPKFAQ KVVSDITAMN
     EEKFDTLSNF DLDEKIALEE NLEFFKNELG CSVEIYSADN AEYDPENKAR FAYPLRPAIY
     LE
//