ID   SYL_CARHZ               Reviewed;         821 AA.
AC   Q3AF30;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=CHY_0393;
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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; CP000141; ABB15559.1; -; Genomic_DNA.
DR   RefSeq; WP_011343330.1; NC_007503.1.
DR   AlphaFoldDB; Q3AF30; -.
DR   SMR; Q3AF30; -.
DR   STRING; 246194.CHY_0393; -.
DR   KEGG; chy:CHY_0393; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   InParanoid; Q3AF30; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002706; 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; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
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; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
DR   PRINTS; PR00985; TRNASYNTHLEU.
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..821
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334741"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           583..587
FT                   /note="'KMSKS' region"
FT   BINDING         586
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   821 AA;  95008 MW;  52887B954D2593AB CRC64;
     MQERYDFKAI EAKWQKKWEE LKLYEVDDFS EKPKYYCLEM FPYPSGKLHM GHVRNYSIGD
     VVARYKRMRG YAVLHPMGWD AFGLPAENAA IKHGNVHPAD WTWDNIANMR RQLKELGISY
     DWRREIATCH PEYYRWTQWL FLQFYKKGLA YKKKAPVNWC PGCQTVLANE QVIDGECERC
     HSRVEKKELE QWFFKITAYA ERLLQDIKKL TGWPEKVKIM QENWIGRSEG AEITFKIKGH
     EETISVFTTR PDTIFGVTYM VLAPEHPLVE KISRGTQYEK DVLEFKRKMM YLSEIERTAE
     TAEKEGVFTG AYAINPFTGE EIPILLANYV LVEYGTGAVM GVPAHDQRDF LFAKKYNLPI
     KVVITPPGQE LKAEELTEAY TGEGILVNSG EFTGLANKEA IRIITQEAEK RGFGKYRVNY
     RLRDWLISRQ RYWGAPIPVL YCEKCGIVPV PEDQLPVVLP YNVEFRPTGE SPLKYVPEFL
     NATCPECGGP ATRETDTMDT FICSSWYYYR YTSPRDKQQP WSKEKVERWL PVDQYIGGVE
     HAILHLLYSR FFTKVLYDLG LVHVDEPFTN LLTQGMVLKD GAKMSKSKGN VVSPEEIVEK
     YGADTARLFI LFAAPPERDL EWSDQGVEGS FRFLNRVWRL IYQTKDRISD ELREFSAKDK
     ELNRLLHATI KKVTEDIEER FNFNTAISAI MELVNGLYQY KEGEINPGLL KEALNKLVIL
     LAPFAPHIAE ELWEALGNKQ SVHLEKWPEY DEEALITEEV EIVIQVNGKV KDRVMVPRNA
     AEDELKEIAL NTPKIKELTA DKKIIKVIIV PEKLINIVVA G
//