ID   SYL_DEIGD               Reviewed;         819 AA.
AC   Q1J0W5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=Dgeo_0567;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-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; CP000359; ABF44869.1; -; Genomic_DNA.
DR   RefSeq; WP_011529711.1; NC_008025.1.
DR   AlphaFoldDB; Q1J0W5; -.
DR   SMR; Q1J0W5; -.
DR   STRING; 319795.Dgeo_0567; -.
DR   PRIDE; Q1J0W5; -.
DR   EnsemblBacteria; ABF44869; ABF44869; Dgeo_0567.
DR   KEGG; dge:Dgeo_0567; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002431; 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; 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; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..819
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334748"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           586..590
FT                   /note="'KMSKS' region"
FT   BINDING         589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   819 AA;  92337 MW;  833A11110FC061E9 CRC64;
     MTKPEIREPR AERYNPHAIE PKWQARWEQE GLYTFHEDPS KTKHYALTMF PYPSGNLHIG
     HWYANVAPDA HARWMRMRGY NVFFPMGFDA FGLPAENAAI KHGLNPATWT SSNIEHMLGQ
     FKRMGTMIDW SRSLATCDPE YYRWNQWFFT EFFRRGLAYK KDGLVNWCPK DQTVLANEQV
     VDGRCERCGT PVERRNLSQW YLKITDYAEE LLDFRDTDMP ERVRAMQTNW IGKSVGAEIT
     FDTPAGPETV FTTRPDTLMG ATFLVLAPEH PKVPALTTPE QAEAVRAYVE AAGRKTDVER
     QQELGEKTGV FTGSYATHPV TGHQIPIWVA DYVLMTYGTG SIMAVPAHDE RDFDFARKFG
     LEIREVIRPE GGEPLDTTQA PYVGEGVIVN SGEFDGLPGG KASIAPIIAR LEALGVAKPK
     TTYRLRDWLV SRQRYWGTPI PIVYCPDHGA QPVPADQLPV KLPENVEFMP TGQSPLKLDR
     EWMRATCPVC GGPAERDTDT MDTFVDSSWY MYRYLSPHDD QHPFDPAHAN LLPVDLYTGG
     IEHAILHLLY SRFWTKVMRD MGLTVQNEPF ARLRNQGIIL GEDGEKMSKS RGNVVDPDDL
     VREYGADTVR TYLMFIAPWE LGGPWDPSGI NGPAKWLSRV WALYFDEKAA GPEEKIGEAD
     LRYAVHSTLK KVGADYERMS FNTIIAALME LTNTLVKAKR SPVFGTPAWE EALDIFNRML
     APVAPHIAEE IWRERGGTES VHLQAWPAVD EAAATRDTVT IGVQVSGKIR GEVQISKTAT
     AEEALAAARA HPDVAKFTEG KQTIKEIYVP GRIINIVVK