ID   SYL_SYNE7               Reviewed;         865 AA.
AC   Q31LW9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=Synpcc7942_1920;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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; CP000100; ABB57950.1; -; Genomic_DNA.
DR   RefSeq; WP_011378240.1; NC_007604.1.
DR   AlphaFoldDB; Q31LW9; -.
DR   SMR; Q31LW9; -.
DR   STRING; 1140.Synpcc7942_1920; -.
DR   PRIDE; Q31LW9; -.
DR   EnsemblBacteria; ABB57950; ABB57950; Synpcc7942_1920.
DR   KEGG; syf:Synpcc7942_1920; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1920-MON; -.
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..865
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009457"
FT   MOTIF           58..68
FT                   /note="'HIGH' region"
FT   MOTIF           629..633
FT                   /note="'KMSKS' region"
FT   BINDING         632
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   865 AA;  97336 MW;  A7AF0B63AC9D72E1 CRC64;
     MQNGANSRSQ EYQGVSVDSR YDPQAIETKW QQSWAAAQLD RTPEADDRPK FYALSMFPYP
     SGNLHMGHVR NYTITDAIAR VKRRQGFRVL HPMGWDAFGL PAENAAIDRG VQPADWTYQN
     VAQMREQLKQ LGLSYDWDRE VTTCSPDYYR WTQWLFLQFF EAGLAYQKEA TVNWDPIDQT
     VLANEQVDSE GRSWRSGAKV ERRQLKQWFL KITDYAEELL QDLDQLTGWP ERVRLMQANW
     IGKSTGAYLE FPIVNSSDRV KVFTTRPDTV YGVSYVVLAP EHPLVTQVTT PEQQTAVAAF
     AAEVSQTSEL ERTAEDRPKR GVPTGGFVTN PFTGQAVPIW IADYVLVEYG TGAVMGVPAH
     DSRDFAFAQR YGLPVQPVIQ PTEGAIAEPW PAPFTEAGVM VNSGQFDGLS STEAKAKIIA
     FAEEQGWGQA HVQYRLRDWL ISRQRYWGCP IPIVHCPDCG PVAAADLPVQ LPDSVQFSGR
     GPSPLAQLED WVTTTCPSCG KPARRETDTM DTFMCSSWYY LRYSDASNPE IAFTKDKVND
     WLPVDQYVGG IEHAILHLLY SRFFTKVLRD RGLLSFDEPF KRLLTQGMVQ GLTYKNPKTG
     KYVPSDRISD PSQPVDPDTG DRLEVFFEKM SKSKYNGVDP ARVLDRYGAD TARMFILFKA
     PPEKDLEWDD ADVEGQFRFL NRVWRLVQTA SQVEATTAAD DKAEKDLRRA VHTAIQAVTE
     DLEEDYQLNT AIAELMKLTN ALNDAPMPGS PAYLEGVQTL VLLLAPFAPH IAEELWQQLG
     GERSVHLEGW PVLDESALIV DEIPLVIQIM GKTRGTITVP ASADRDQLQQ LAENSEIAQR
     WLDGQTIRKV IVVPGKLVNF VIASP