ID   SYL_SYNSC               Reviewed;         875 AA.
AC   Q3AJU8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 125.
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=Syncc9605_1380;
OS   Synechococcus sp. (strain CC9605).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=110662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9605;
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., Martinez M., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9605.";
RL   Submitted (JUL-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; CP000110; ABB35134.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3AJU8; -.
DR   SMR; Q3AJU8; -.
DR   STRING; 110662.Syncc9605_1380; -.
DR   KEGG; syd:Syncc9605_1380; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OrthoDB; 9810365at2; -.
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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..875
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334829"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           60..70
FT                   /note="'HIGH' region"
FT   MOTIF           634..638
FT                   /note="'KMSKS' region"
FT   BINDING         637
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   875 AA;  96528 MW;  AC3754A1958463C4 CRC64;
     MPSAGSVNAA NPAVDTSAQT GRYDPTALEQ RWQESWKADG VDTTEVGGEK PGFFALSMFP
     YPSGSLHMGH VRNYVITDVI ARVQRMLGHA VLHPMGWDAF GLPAENAAIE RNVDPGEWTD
     RNIDQMRAQL DRLGLSIDWS REQATCHSDY YRWTQWLFLE LLEGGLAYRK NATVNWDPVD
     QTVLANEQVD GDGRSWRSGA LVEQRQLNQW FLRITDYAEP LLNDLDALKG WPERVRTMQA
     NWIGRSEGAE ISFNVEGAQN QTITVFTTRP DTLAGASYVV LAPENELVDS LSSEEQKDTV
     EAFRKEVARL STIERTCDDR PKRGVPIGSH VINPLTGVVL PVWIADYVLA EYGTGAVMGV
     PAHDQRDIAF AQSNGLPIQQ VIDAEGAAEA IAAGQAWTDA GTLVNSGSFD GTASSEAKGA
     ITGHGAEQGW ARSKVTYRLR DWLISRQRYW GCPIPVIHCD NCGAVPVPRE DLPVELPRGI
     DLSGKGGSPL SQQSDWVNVA CPRCGKPAKR ETDTMDTFMC SSWYFLRFAD PHNTEKPFSK
     EAVNRWLPVK QYVGGIEHAI LHLLYARFFT KALKDRGLID INEPFERLLT QGMVQGVTYR
     NATTGKYIAP ADVADAEDPR DPNTGDKLEV LFEKMSKSKY NGVDPAAVID RYGADTARMF
     ILFKAPPEKD LEWDDADVEG QFRFLQRLWR LVEAGSARID SLEPMQRPAD LSDADSDVRR
     ALHLAIEAVS EDLSDEIQLN TAISELMKLS NAISSTGIDA LSAPVLQEAL SGLVRLLAPF
     APHLAEEFWN RLGGSGSVHR QSWPVLDPTA LVQDSVEVVI QVKGKVRGKL QVPASAGKEE
     LERLALASDV AEKWLEGAAP RRVIVVPGKL VNLVP
//