ID   SYL_CERS4               Reviewed;         847 AA.
AC   Q3IZL4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 119.
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=RHOS4_24520; ORFNames=RSP_0840;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC
RC   12203 / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-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; CP000143; ABA80020.1; -; Genomic_DNA.
DR   RefSeq; WP_011338533.1; NZ_CP030271.1.
DR   RefSeq; YP_353921.1; NC_007493.2.
DR   AlphaFoldDB; Q3IZL4; -.
DR   SMR; Q3IZL4; -.
DR   STRING; 272943.RSP_0840; -.
DR   EnsemblBacteria; ABA80020; ABA80020; RSP_0840.
DR   KEGG; rsp:RSP_0840; -.
DR   PATRIC; fig|272943.9.peg.2803; -.
DR   eggNOG; COG0495; Bacteria.
DR   OrthoDB; 9810365at2; -.
DR   PhylomeDB; Q3IZL4; -.
DR   Proteomes; UP000002703; Chromosome 1.
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; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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; Reference proteome.
FT   CHAIN           1..847
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009414"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   847 AA;  94033 MW;  E52C27363BB7CAC6 CRC64;
     MSRYDPAATE SRWQAAWDAA GVFTARHDPA RPKYYVLEMF PYPSGRIHMG HVRNYTMGDV
     VARQKAAAGF SVLHPMGWDA FGMPAENAAM ERGGHPKDWT YGNIADMRAQ MKPLGLSIDW
     SREFATCDPE YYGQQQAMFI DMMEAGLVYR KNAVVNWDPV DMTVLANEQV IDGKGWRSGA
     PVVRRELTQW FFRISDYAGE LLEALDTLKD WPEKVRLMQA NWIGQSRGLQ FAFSMAGAPE
     GFDRLEVYTT RPDTLMGASF AAISPDHPLA RHLERHDPEV AEFVAECRRV GTSEEALEKA
     EKKGFDTGLR VRHPFDAAWE LPVYIANFIL MDYGTGAIFG CPAHDQRDFE FATKYGLPIR
     PVFLPEGCEE TALAEAFVPM KSERVHYIRG FAGAEVQTGE EGVAAAIAFC ESQGVGRGVT
     NYRLRDWGIS RQRYWGCPIP VIHCETCGVV PEAKENLPVR LPDDVSFDVP GNPLDRHPTW
     RDCTCPKCGA KARRETDTMD TFVDSSWYYA RFTAPRAATP TDAEEADYWM NVDQYIGGIE
     HAILHLLYSR FFARAMQKTG HLPAKAIEPF NALFTQGMVT HEIYLTRDAA GRPVYHLPED
     VTDGKLADGT PVEIIPSAKM SKSKKNVVDP MNIIRQFGAD TARWFVMSDS PPERDVEWTA
     SGAEAASKHL HRVWRLADEI SRADGEANAE DGALDKATAR AIAEVTQGVE GFAFNKAIAK
     LYEFTNTLSR SGAGAEAKKR AMRTMAQLMS PMVPHLAEEV WAMLGGEGLV AQAAWPKADP
     ALLIDDTVTL PIQVNGKRRG EITVPKEMAA SEVEKLVLAD EAVQRALGGA APKKLIVVPG
     RIVNVVI
//