SYL_THEFY
ID SYL_THEFY Reviewed; 830 AA.
AC Q47MY0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=Tfu_2156;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ56189.1; -; Genomic_DNA.
DR RefSeq; WP_011292579.1; NC_007333.1.
DR AlphaFoldDB; Q47MY0; -.
DR SMR; Q47MY0; -.
DR STRING; 269800.Tfu_2156; -.
DR EnsemblBacteria; AAZ56189; AAZ56189; Tfu_2156.
DR KEGG; tfu:Tfu_2156; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OMA; DIDWADV; -.
DR OrthoDB; 32262at2; -.
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 Gene3D; 3.90.740.10; -; 1.
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; 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 PANTHER; PTHR43740; PTHR43740; 2.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 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.
FT CHAIN 1..830
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334834"
FT REGION 379..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT MOTIF 593..597
FT /note="'KMSKS' region"
FT BINDING 596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 830 AA; 92640 MW; 1A44B3A2BAE1EACE CRC64;
MTAVSGDQTT SGSYDVRALQ EKWQARWAKE NPFTASEDPA DPRPRRYVLD MFPYPSGDLH
MGHAEAFAIG DVIARYHFAR GENVLHPIGW DSFGLPAENA AIKHNFHPAE WTYTNIETQA
ESFRRYAISL DWSRRLHTSD PEYYRWNQWF FLRFFERGLA YRKDGLVNWC PKDQTVLANE
QVIQGKCERC GTEVERRALN QWYFKITDYA QRLLDDMEQL EGKWPERVLT MQRNWIGRSE
GADVQFTIEG REEPVTVFTT RPDTLYGATF FVVAPDSPLA DELCAPEQRE AFEAYRTQVS
KLSDIERQST EREKTGVFLG RYAINPVNGE RIPVWAADYV LADYGHGAIM AVPAHDQRDL
DFARKFNLPV RVVVDTGEPD PAETGIATPG EGTLINSGPL NGLSKSEAIP RIIEILTERG
TGKAAVNYRL RDWLVSRQRF WGTPIPIIHC PECGEVPVPD EELPVRLPDL RGAALAPKGV
SPLAAATDWV NVSCPRCGGP AKRDTDTMDT FVDSSWYFLR YCSPNLDTAP FDQEKVAKWG
PIDQYVGGVE HAILHLLYSR FFTKVLYDMG MVPFTEPFVR LLNQGQVINQ GKAMSKSLGN
GVDLGQEIDR YGVDAVRLTM VFAGPPEEDI DWADVSPGAS VKFLNRAYRV MAEAAAASAP
GVDPATGDLA LRRMTHQTLA KVTEAVEAQR FNVAIARIME LVTAARRAID SGPGAADPAV
REAAEVIAIT LGLFAPYVAE EGWEMLGHTG SVSVGTWREP DPALLVQESV TCVVQVASKV
RDKLQVSPDI SAEELERLAL ASEKVQNHIA GREIRRIVVR EPKLVNIVVA