ID   SYL_SYNR3               Reviewed;         864 AA.
AC   A5GT82;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=SynRCC307_1188;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-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; CT978603; CAK28091.1; -; Genomic_DNA.
DR   RefSeq; WP_011935605.1; NC_009482.1.
DR   AlphaFoldDB; A5GT82; -.
DR   SMR; A5GT82; -.
DR   STRING; 316278.SynRCC307_1188; -.
DR   PRIDE; A5GT82; -.
DR   EnsemblBacteria; CAK28091; CAK28091; SynRCC307_1188.
DR   KEGG; syr:SynRCC307_1188; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001115; 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   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; 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..864
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334831"
FT   REGION          298..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           622..626
FT                   /note="'KMSKS' region"
FT   BINDING         625
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   864 AA;  96134 MW;  2BEF084AA3D038F1 CRC64;
     MASSESRYSP TSLEPKWQQR WQEMGLDQTP EPSAERAENF YALSMFPYPS GNLHMGHVRN
     YVITDVIARL MRLKGKRVLH PMGWDAFGLP AENAAIERGV DPADWTDRNI AQMREQLQRL
     GLSIDWSREV ATCHSDYYRW TQWLFLQFLN ADLAYRKEAT VNWDPIDQTV LANEQVDADG
     RSWRSGALAE KRKLRQWFLK ITAVADELLD DLEQLKGWPE RVRTMQANWI GRSSGATLRF
     AIEADGKQAI EVFTTRPDTV FGVSYVVLAP EHDLVDQLTS ADQRQAVEAF RQSLQSISEQ
     DRVADDRPKR GVATGGTVQH PFTGQAVPVW IADYVLPDYG TGAVMGVPAH DSRDFAFAKQ
     YDLPITTVVV EPGQAPDSGE PSEAFTGLGE LVGSADFDGL QGEEAKTAII QAAEQRGVGA
     AKITFRLRDW LISRQRYWGC PIPVIHCDDC GVVPVPESDL PVELPRDVDL SGSGGSPLER
     ATEWKQVRCP KCGKPATRET DTMDTFMCSS WYYLRYTDAN NDSAAFTNAS IDAWMPVDQY
     VGGVEHAILH LLYSRFFTKV LQQRNLVSCS EPFQKLLTQG MVQGVTYRNP KTRKYIAPSA
     VSDPNQPTDP DDGEALEVFF EKMSKSKYNG VDPGAVVDRY GADTARMFIL FKAPPEKDLE
     WDDADVEGQF RFLQRIWRLC DGAKASGLQL QSPLPLPAEL TPAETDLRRA VHTAIEAVSD
     DLQGDELQFN TAVSELMKLS NAMAGQLEAV STAVAQEAVR SLLLLLAPFA PHLADELWEQ
     LQGSGSIHQQ RWPEVDASAL VRDTITVVLQ VKGKVRGNLE VPAAISKDEL EQVALASDVA
     QKWLEGNAPK RVIVVPGKLV NLVP