ID   SYL_JANSC               Reviewed;         863 AA.
AC   Q28VD4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Jann_0411;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia; unclassified Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA   Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-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; CP000264; ABD53328.1; -; Genomic_DNA.
DR   RefSeq; WP_011453537.1; NC_007802.1.
DR   AlphaFoldDB; Q28VD4; -.
DR   SMR; Q28VD4; -.
DR   STRING; 290400.Jann_0411; -.
DR   EnsemblBacteria; ABD53328; ABD53328; Jann_0411.
DR   KEGG; jan:Jann_0411; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008326; 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; 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..863
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009355"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           627..631
FT                   /note="'KMSKS' region"
FT   BINDING         630
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   863 AA;  95767 MW;  5BCB6A77FEE205FF CRC64;
     MSRYDPSMIE PKWQKAWAEA GTFTASMEGN KPKYYVLEMF PYPSGRIHIG HVRNYTMGDV
     IARHKKAMGH NVLHPMGFDA FGLAAENAAM DRGIHPKDWT YKNMDDMRDQ MRPLGFSIDW
     SRDLATCDPD YYGQQQALFI DMMEAGLIDR KNAVVNWDPV DMTVLANEQV EDGKGWRSGA
     EVERKELTQW FFKISDYSDE LLEALDGLDD WPAKVKLMQA NWIGKSRGLQ FAFGLVEPVG
     GHDRVDVYTT RPDTLLGASF VGISPDHAIA KQLESESEDI AAFCAECRKG GTTAAEVETA
     EKLGFDTGLK VRHPFDTAAQ LPVYIANFIL MDYGTGAIFG CPAHDERDLD FARKYDLPVV
     STYVPIDDEG HVLPEDGGAA YVPPKPDPVR YIRGFAGEEI QSGNDAIDAA VTFCEAEGVG
     QGVTKFRLRD WGLSRQRYWG CPIPVVHCDA CGVVPEKKEN LPIELPYDVT FDVPGNPLDR
     HPTWRNTPCP SCGAPALRET DTMDTFVDSS WYFARFTAPH ADTPTSKAEV EYWMNVDQYI
     GGIEHAILHL LYSRFFARAM HITGHLPRKA IEPFDALFTQ GMVTHAIYKT TDAKNRPVYH
     YPETVDLRDG GGYLDDGTAV EIIPSAKMSK SKNNVVDPIE IIKQYGADTA RWFVLSDSPP
     ERDVEWTASG AEAAYKHLGR VWALCDRISE AARSVSEEAQ PAAGEHDTAL LREMHKTIRD
     VTNGVDSFGF NAAIAKLYAF TNTLQKSKAS HKAQREAVMT LAQLMAPMTP HLSEDIWAHQ
     GGDGLIADAP WPVANEAMLV ESTVTLPIQI NGKRRSEVTV AKDASKEEVE KRALADDAVV
     RALDGAAPKK LIVVPGRIVN VVI