ID   SYL_METM7               Reviewed;         955 AA.
AC   A6VK04;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=MmarC7_1724;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
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; CP000745; ABR66780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VK04; -.
DR   SMR; A6VK04; -.
DR   STRING; 426368.MmarC7_1724; -.
DR   KEGG; mmz:MmarC7_1724; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OrthoDB; 23906at2157; -.
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; 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   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   Pfam; PF09334; tRNA-synt_1g; 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..955
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334845"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           647..651
FT                   /note="'KMSKS' region"
FT   BINDING         650
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   955 AA;  110812 MW;  A3B04A5568BD769D CRC64;
     MDQNGVNAGN GHKSIDLIQI MDKWQKKWTE AKIFEAEHDL RDKFFITAAF PYLNGVLHAG
     HLRTFTIPET IARYQRMKNK NVLWTFGFHV TGTPILGLAN QIKERKEDII WAYNNLHNIP
     MDELIKLDTP EAIVECFSKK ATEAFKRMGF SLDWRRNFKT DDKVFSKFIE WQFYKLKEMG
     HITKGSHPVR YCPKCENPVE DHDLLHGEES TTVEYSLIKF TSEFDGKEII MPMATLRPET
     LFGVTNAWVN PNEMYVMAEV YDEIQKLDSE DVDLKYNGIW IVGKECADKL KEQDRKIEIL
     KEIKGSELLG LKIKNPVTKK EVPLFPADFV EMGIGTGCVM GVPAHAPYDY IALRDLGKIE
     EVGLIPLIEI EGYDKFPAKE IVEKLGVKDQ NDDELLEQAT SKIYKDEFHK GKLNENCGEY
     AGISVKDIKE KLTKDYLNSN IAEIMYEFSE QKVVCRCGEK CIIKTVKGQW FINYSDENWK
     KLAHECIDSM NFAPENIRQE FHNKVDWMKD KACARKKGLG TLLPFDENWI IESLSDSTIY
     MAYYTIARFI NEGLTPEQLV PELFEYVFLG NGNVEEIAKN SNISKETIEE MRKEFLYYYP
     LDWRCSAKDL IPNHLTFMIF NHVALFKKEH WPRGIEINGY VTIEGKKLSK SKGPVLPVSE
     VAENFGADVA RFYITTCAEL PQDADVKFKE MEKARDNLIK LYELAVSVME EESTQKEFSL
     IDKWLLHKTY SSIKGAETAY EEFQLRKIGL MFYELINDLR WYKRRGGENN NVLKEVVEIW
     TKLLSPVTPH LCEEIWEKLG YSGFISQEMY PEIKSELINE DLELGEEFIK SAMEDIRNIK
     GVAKINPEKM YLYTADDWKY DLLEFMNENS EKNVKAIIPL VMKEDKFKRH GKEVMKLINE
     IMKIGVKKAI AEVEILENAK TFIESEFDCE VIVNGEDVKG KKKFAIPYKP AIYME
//