ID   SYL_SYNS9               Reviewed;         884 AA.
AC   Q3AXV7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=Syncc9902_1106;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
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; CP000097; ABB26070.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3AXV7; -.
DR   SMR; Q3AXV7; -.
DR   STRING; 316279.Syncc9902_1106; -.
DR   EnsemblBacteria; ABB26070; ABB26070; Syncc9902_1106.
DR   KEGG; sye:Syncc9902_1106; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000002712; 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; 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; Reference proteome.
FT   CHAIN           1..884
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334830"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           69..79
FT                   /note="'HIGH' region"
FT   MOTIF           643..647
FT                   /note="'KMSKS' region"
FT   COMPBIAS        15..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         646
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   884 AA;  97885 MW;  09C2423CAC7AAB09 CRC64;
     MYGTIAAKPH AGPVNAASSS ASANNSPQEN RYDPSALEQR WRARWKDQGL DTTETESSKP
     GFFALSMFPY PSGSLHMGHV RNYVITDVIA RVQRMRGDSV LHPMGWDAFG LPAENAAIER
     NIDPGEWTDR NIDQMRNQLD RLGLSIDWDR EQATCHSDYY RWTQWLFLEL LEGGLAYRKN
     ATVNWDPVDQ TVLANEQVDA DGRSWRSGAL VEQRQLNQWF LRITDYAEAL LNDLDKLKGW
     PERVRTMQAN WIGRSEGAEI TFQVTGSSQQ SITVFTTRPD TLSGASYVVL APEHQLVDGL
     TTEEHLASVD QFRKQVARLS TIERTSDERP KQGVATGACV TNPLTGEQLP VWIADYVLAD
     YGTGAVMGVP AHDQRDIQFA KANALPIRQV IDAEGAKEAI DAGKAWTEAG TLINSGVFDG
     QPSNQGKGSI TSHGETAGWA TSKVTYRLRD WLISRQRYWG CPIPVIHCPT CGVVPVPRDD
     LPVELPRGID LSGKGGSPLS QQSDWVNVSC PCCGGAAKRE TDTMDTFMCS SWYFLRFADP
     HNTDQPFSKE AVRRWLPVKQ YVGGIEHAIL HLLYSRFFTK ALRDRGLIDI DEPFERLLTQ
     GMVQAITYRN PITGKYIATA DVSDPNDPLD PTTGDKLEVL FEKMSKSKYN GVDPAAVIDR
     YGADTARMFI LFKAPPEKDL EWDDADVEGQ FRFLQRLWRL VENASSTLTD LNSTGCPADL
     TDQEADVRRA LHLAIDAVSD DLNGEIQLNT AISELMKLSN TITSSGPDRL RPPILQEALS
     GLIRLLAPFA PHIAEEFWSR LGGDGSVHQQ SWPSVDPSAL IQDTISIVIQ VKGKVRGSIQ
     APADADKATL ESMALSSDVA NKWLEGATPK RVIVVPGKLV NLVP