ID   SYL_PARMW               Reviewed;         857 AA.
AC   Q7U6T1;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=SYNW1255;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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; BX569692; CAE07770.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7U6T1; -.
DR   SMR; Q7U6T1; -.
DR   STRING; 84588.SYNW1255; -.
DR   PRIDE; Q7U6T1; -.
DR   EnsemblBacteria; CAE07770; CAE07770; SYNW1255.
DR   KEGG; syw:SYNW1255; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001422; 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; 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.
FT   CHAIN           1..857
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152104"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           616..620
FT                   /note="'KMSKS' region"
FT   BINDING         619
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   857 AA;  95500 MW;  84F8D503B0096EC3 CRC64;
     MNSRYSPADL EQRWQTTWRS EGLDVTPEPE DGKGFYALSM FPYPSGTLHM GHVRNYVITD
     VIARVQRMRG HSVLHPMGWD AFGLPAENAA IERNVDPGDW TDRNIDQMRS QLDRLGLSID
     WDREQATCHS DYYRWTQWLF LELFDGGLAY RKNATVNWDP VDQTVLANEQ VDADGRSWRS
     GALVEQRQLN QWFLRITQYA EALLNDLDQL SGWPERVRTM QANWIGRSEG AEIQFKVSSD
     SDTTITVFTT RPDTLAGASC VVLAPDHPLV NSLTSPDQQD VVQAFQAEVA RLSALERTSD
     DAPKRGVFTG ATVLNPLNGR ALPVWIADYV LVDYGTGAVM GVPAHDQRDR RFAQSYGLAV
     QQVIEAEGAA AAIAAGEAWT DPGVLIHSGD FDGLNSIEAK ERITRHGEQQ GWAVAKVTYR
     LRDWLISRQR YWGCPIPIIH CPSCGAVPVP REDLPVVLPR GIDLSGKGGS PLEQQQDWVN
     VPCPSCGEPA KRETDTMDTF MCSSWYFLRF ADPHNTEQPF SREAVNRWLP VQQYVGGIEH
     AILHLLYSRF FTKALKDRGL IDVAEPFDRL LTQGMVQGTT YRNPSTGKYV ASADVSDPET
     PTDPTSGEPL EVLFEKMSKS KYNGVDPAAV IDRYGADTAR MFILFKAPPE KDLEWDDSDV
     EGQFRFLQRI WRLVESADSR IDSLEPEERP EPLADTDAKV RRAIHIAIDA VSEDLQDEIQ
     LNTAISELMK LTNAITSVGV AELSTSVLKE ALSTLLRLLA PFAPHLAEEL WHQLGGTSSV
     HRAGWPELDP SALVQDSVDL VIQIKGKVRG TIQVPAAADK EQLEALALAS EIAAKWLEGH
     PPRRVIVVPG KLVNLVP