ID   SYL_METVS               Reviewed;         952 AA.
AC   A6USJ5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Mevan_1575;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
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; CP000742; ABR55467.1; -; Genomic_DNA.
DR   RefSeq; WP_012066381.1; NC_009634.1.
DR   AlphaFoldDB; A6USJ5; -.
DR   SMR; A6USJ5; -.
DR   STRING; 406327.Mevan_1575; -.
DR   EnsemblBacteria; ABR55467; ABR55467; Mevan_1575.
DR   GeneID; 5325458; -.
DR   KEGG; mvn:Mevan_1575; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OMA; AWNMAFQ; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000001107; 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   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..952
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334846"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           644..648
FT                   /note="'KMSKS' region"
FT   BINDING         647
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   952 AA;  111051 MW;  13D20D32E0B8A923 CRC64;
     MVENMETSFK SIDLIQIMDK WQRKWDESKI FETKHDNREK FFISAAFPYL NGVLHAGHLR
     TFTIPETIAR YQRMKNKNVL WTFGFHVTGT PILGLANQIK EKKEDIIWAY TNLHNIPMDE
     LLKLDTPEAI VECFSKKATD AFKKMGFSLD WRRNFKTDDK VFSKFIEWQF YKLKDLGLIK
     KGSHPVRYCP KCENPVEDHD LLHGEESTTV EYNLIKFTST FDEKDVIIPM ATLRPETVFG
     VTNAWVNPDE IYVLAEVYDE IQKLDSEDVD LKYNGLWIVG KECADKLKEQ DKNIKILKEF
     KGSELIGLKI KNPVTNLKVP IFPAEFVEMN IGTGCVMSVP AHAPYDYVAL RDLEKVEEVG
     LISLIEIEGY GKYPAKEIVE KMNIKNQKDE ALLEEATSKI YKDEFHKGKL NENCPEYKGT
     SVKDIKEKLI KDYMNFGISE IMYEFSEPKV VCRCGEKCII KTVKGQWFIT YSDENWKRLA
     HECIDSMEFA PENLRHEFHN KIDWMKDKAC ARRKGLGTKL PFDTNWMIES LSDSTIYMAY
     YTIARFINAG INENQLTSEL FEYVFSGNGN LAEISNVSEV SIEIIEEMRK EFLYFYPLDW
     RCSAKDLIPN HLSFMIFNHV ALFKKEHWPR GIEINGYVTI EGKKLSKSKG PVLPVLEVSE
     TFGADVARFY ITTCAELPQD ADVKFKEMEK ARDNLIKLYE LAVLVTKEGI IEKELSIIDK
     WLLHKTHSSI NFAEKAYEEF HLRKIGLMFY ELINDLRWYK RRGGDNNGVL KEVVEIWTKL
     LSPVTPHLCE EIWELLGHNG FISKEIFPNV KIEYINEELE LGEEFIRFTM EDIRNIKNVA
     KINPEKMYLY TADDWKYELL EFMNKNSEKN VKELIPIVMK EERFKRHGKD VMKLINDLMK
     VGVKKAIAEV EILENAKTFI EKEFECNVII GGEDFNGKKK FAIPYKPAIY ME