ID   SYL_METM5               Reviewed;         955 AA.
AC   A4FYA3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=MmarC5_0879;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-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; CP000609; ABO35187.1; -; Genomic_DNA.
DR   RefSeq; WP_011868641.1; NC_009135.1.
DR   AlphaFoldDB; A4FYA3; -.
DR   SMR; A4FYA3; -.
DR   STRING; 402880.MmarC5_0879; -.
DR   GeneID; 4929284; -.
DR   KEGG; mmq:MmarC5_0879; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OrthoDB; 23906at2157; -.
DR   Proteomes; UP000000253; 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..955
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334844"
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;  110927 MW;  FF89DC413B300682 CRC64;
     MDQNGVNEGT GHKSVDLIQI MDKWQKKWTE AKIFEAEHDL RDKFFITAAF PYLNGVLHAG
     HLRTFTIPET IARYQRMKNK NVLWTFGFHV TGTPILGLAN QIKDRKEDII WAYNNLHNIP
     MDELLKLKTP EAIVECFSKK ATEAFKRMGF SLDWRRNFKT DDKVFSKFIE WQFYKLKEMG
     HITKGSHPVR YCPKCENPVE DHDLLHGEES TTVEYSLIKF TSEFDGKEII MPMATLRPET
     LFGVTNAWVN PNEIYVMAKV HDEIQKLDGE DVELKYNGIW IVGKECADKL KEQDRKIEIL
     KEIKGNELLG LKIKNPVTKK EVPLLPADFV EMGIGTGWVM SVPAHAPYDY VALRDLGKIE
     EVGLIPLIEI EGYDKYPAKE IVEKLGVKDQ NDDELLEQAT SKIYKDEFHK GKLNENCGEY
     AGISVKDIKE KLTKDYLNSN IAEIMYEFSE QKVVCRCGEK CIIKTVKGQW FINYSDENWK
     KLAHECIDNM NFAPENIRQE FHNKVDWMKD KACARKKGLG TILPFDENWI IESLSDSTIY
     MAYYTIARFI NEGLTPEQLI PELFEYVYLG NGNVEEITKN SNISKETIEE MRKEFLYYYP
     LDWRCSAKDL IPNHLTFMIF NHVALFGREH WPRGIEINGY VTIEGKKLSK SKGPVLPVSE
     VAENFGADVA RFYITTCAEL PQDADVKFKE MEKARDNLIK LYELAVSVME EEKTEKELSL
     IDKWLLHKTY SSINGAETAY EEFQLRKIGL MFYELINDLR WYKRRGGENN NVLKEVVEIW
     TKLLSPVTPH LCEEIWEKLG YAGFISQELY PEIKLEMVNE DLELGEEFIK SAMEDIRNIN
     GVAKINPEKM YLYTADDWKY DLLEFMNENS EKNVKALIPM VMKEDKFKRH GKEVMKLINE
     IMKIGVKKAI AEVEILENAK TFIESEFDCE VIVNGEDVKG KKKFAIPYKP AIYME
//