ID   SYL_THEVB               Reviewed;         857 AA.
AC   Q8DH61;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=tll2098;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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; BA000039; BAC09650.1; -; Genomic_DNA.
DR   RefSeq; NP_682888.1; NC_004113.1.
DR   RefSeq; WP_011057933.1; NC_004113.1.
DR   AlphaFoldDB; Q8DH61; -.
DR   SMR; Q8DH61; -.
DR   STRING; 197221.22295825; -.
DR   PRIDE; Q8DH61; -.
DR   EnsemblBacteria; BAC09650; BAC09650; BAC09650.
DR   KEGG; tel:tll2098; -.
DR   PATRIC; fig|197221.4.peg.2196; -.
DR   eggNOG; COG0495; Bacteria.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000440; 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; -; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
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; 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; PTHR43740; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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..857
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152102"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           615..619
FT                   /note="'KMSKS' region"
FT   BINDING         618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   857 AA;  97076 MW;  A28EA8AFF7FEEAC6 CRC64;
     MDDRYDPQVI EAKWQQEWAA RQLDRTDTDP QKPKFYALSM FPYPSGNLHM GHVRNYTITD
     VIARCRRMQG YRVLHPMGWD AFGLPAENAA IERGIHPRVW TQQNIGQMRQ ELQRLGLSYD
     WEREVTTCHP DYYRWTQWLF LEFFEAGLAY QKEAAVNWDP VDQTVLANEQ VDSEGRSWRS
     GALVERRLLK QWFLKITAYA EELLNDLEQL TGWPERVKLM QANWIGQSRG AYLEFPIVGS
     DEKIGVFTTR PDTVYGVTYV VLAPEHPLTL KVTTSRRRKT VEAFIASVQQ ESELERTAGD
     RPKRGVATGG KALNPFTGEE IPIWIANYVL YEYGTGAVMG VPAHDERDFQ FAKAHRLPIR
     QVIIPPDGKA STRLRAAYTE PGKLINSGQF DGMDSTAAKV AITEYATAQG WGREHVQYRL
     RDWLISRQRY WGVPIPIIHC PQCGPVPVPR SELPVLLPEE VEFTGRGPSP LAKLAAWRDV
     PCPKCGGPAQ RETDTMDTFI DSSWYYFRYA DARNSEAPFD PAAIKDWLPV DQYVGGIEHA
     ILHLLYSRFF TKVLRDRQLV HVSEPFQRLL TQGMVQGRTY KNPRTGKYVI PSRIADLNQP
     TDPDTGEALE VVYEKMSKSK YNGVAPGDVI QQYGADTARM FILFKAPPEK DLEWDDADVE
     GQFRFLNRVW RLVQTFKAKG GRLGQPLPAT LTKAEKDLRR AIHTAIKEIS EDIEGDYQLN
     TAVAELMKLS NALSSADCYT SGVYSEGIQT LLTLLAPFAP HISEELWHQL GGTDSIHRQP
     WPKADPTALV ADEITLVIQV MGKTRGAIQV PATASQAELE EAAQHSEIGQ RYLAGKTIKK
     IIVVPGKLVN FVLESSR