ID SYL_METMP Reviewed; 955 AA.
AC Q6LZD2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 115.
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=MMP0697;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX950229; CAF30253.1; -; Genomic_DNA.
DR RefSeq; WP_011170641.1; NC_005791.1.
DR AlphaFoldDB; Q6LZD2; -.
DR SMR; Q6LZD2; -.
DR STRING; 267377.MMP0697; -.
DR EnsemblBacteria; CAF30253; CAF30253; MMP0697.
DR GeneID; 2761186; -.
DR KEGG; mmp:MMP0697; -.
DR PATRIC; fig|267377.15.peg.714; -.
DR eggNOG; arCOG00809; Archaea.
DR HOGENOM; CLU_004174_0_0_2; -.
DR OrthoDB; 23906at2157; -.
DR Proteomes; UP000000590; 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; 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; Reference proteome.
FT CHAIN 1..955
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152134"
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; 110690 MW; E0C03FBAA1C7E93F CRC64;
MDQKEVIGET GHKSVDLIKI MDKWQKKWTE AKIFEAEHDS RDKFFITAAF PYLNGVLHAG
HLRTFTIPET IARYQRMKNK NVLWTFGFHV TGTPILGLAN QIKERKEDII WAYNNLHNIP
MDELLKLNTP EAIVECFSKK ATEAFKRMGF SLDWRRNFKT DDKVFSKFIE WQFYKLKEMG
HITKGSHPVR YCPKCENPVE DHDLLHGEES TTVEYSLIKF TSKFDGKEII MPMATLRPET
VFGVTNAWVN PNEIYVMAEV HDEIQKLDSE DVDLKYNGIW IIGKECADKL KEQDRKIEIL
KEIKGSELLG LKIKNPVTKK EVPLLPADFV EMGIGTGCVM SVPAHAPYDY VALRDLGKVE
EVGLIPLIEI EGYDKYPAKE IVEKLGIKDQ NDEELLEQAT SKIYKDEFHK GKLNENCGEY
TGISVKDIKE KLTKDYINSN IAEIMYEFSE QKVVCRCGEK CIIKTVKGQW FINYSDENWK
KLAHECIDNM NFAPEGIRQE FHNKVDWMKD KACARKRGLG TILPFDENWI IESLSDSTIY
MAYYTIARFI NEGLTPEQLI PELFDYVYLG NGNAEEIAKN SKIQAETIEE MRKEFLYYYP
LDWRCSAKDL IPNHLTFMIF NHVALFGREH WPRGIEINGY VTIEGKKLSK SKGPVLPVSE
VAENFGADVA RFYITTCAEL PQDADVKFKE MEKARDNLIK LYDLAVSVME EESAEKELSL
IDKWLLHKTY SSINSAETAY EEFQLRKIGL MFYELINDLR WYKRRGGENN SVLKEVVEIW
TKLLSPVTPH LCEEIWEKLG YAGFISQEMY PVSKPELINE DLELGEEFIK SAMEDIRNIK
GVAKINPEKM YLYTADDWKY DLLEFMNENA EKNVKALIPM VMKEDKFKRH GKEVMKLINE
IMKIGVKKAI AEVEILENAK TFIESEFDCK VIVNGEDVKG KKKFAIPYKP AIYME
//
