ID   SYL_TRIEI               Reviewed;         929 AA.
AC   Q114V5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=Tery_1704;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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; CP000393; ABG50969.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q114V5; -.
DR   SMR; Q114V5; -.
DR   STRING; 203124.Tery_1704; -.
DR   EnsemblBacteria; ABG50969; ABG50969; Tery_1704.
DR   KEGG; ter:Tery_1704; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
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; 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; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
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..929
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009459"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           614..618
FT                   /note="'KMSKS' region"
FT   BINDING         617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   929 AA;  105715 MW;  CBEA3835F051A92A CRC64;
     MDSKYNPVSI EQKWQKNWAE QNQDQTPINN NQPKFYALSM FPYPSGNLHM GHVRNYTITD
     VIARLKRMQG YRVLHPMGWD AFGLPAENAA IDRGIPPAKW TLENIAQMKE QLRRLGFSID
     WDKEVATCTP EYYRWTQWIF LQFFQAGLAY QKESAVNWDP IDQTVLANEQ VDGEGRSWRS
     GAKVERKMLR QWFFKITDYA EQLLNDLDKL PGWPERVKLM QANWIGKSVG AYLEFPIVGM
     DQKIGVFTTR PDTVYGVSYV VLAPEHPLTA KVTTPEQQIT VETFIKEVAA ESELERTAED
     KPKRGVPTGG KAINPFNNQE VPIWIADYVL YEYGTGAVMG VPAHDVRDFQ FAKQYNLPIK
     TVIVPDDSND DHKLTEAYTD VGVMVNSGPF NGEKSTVAKK AIIELAEDEG YGKGRVQYRL
     RDWLISRQRY WGAPIPIIHC PKCGAVPVPD EDLPVKLPES VEFSGRGPSP LAKLEDWVNV
     SCPSCGTPAK RETDTMDTFI DSSWYYLRYP DATNEEQVFD SKIVNDWLPV DQYVGGIEHA
     ILHLLYSRFF TKVLRDRGLC DFDEPFQNLL TQGMVQGVTY KNPVTGKYIP FADVNPQEPK
     DPKTGDKLEV FFEKMSKSKY NGVDPMDVMA TYGADTARMF ILFKAPPEKD LEWDDADVQG
     QFRFLNRVWS MVMEFLANHS FSELKAKHHG ITQADLKDLG WSRYLITEIT KNISAFKLRN
     VVKVYPVEDV LVAIEAKFNY SETQQETKDD LQKVLTWIKS RFGGELTKAE KDVRRAVHNA
     IKEVTEDLDG DYQFNTAVSE MMKLSNALGD ASCKDSPIYA EALETLLLLL APFAPHITEE
     LWQIAGNFGS VHTHAWPKFD PEALVVDEIT LVIQIKGKTR GTIQVPAQAD KETLEKLARE
     SDIAQRHLAG KEIKKVIVVP RKLVNFVVI