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SYL_GEOSM
ID   SYL_GEOSM               Reviewed;         824 AA.
AC   C6E100;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=GM21_0766;
OS   Geobacter sp. (strain M21).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter; unclassified Geobacter.
OX   NCBI_TaxID=443144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M21;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lovley D.;
RT   "Complete sequence of Geobacter sp. M21.";
RL   Submitted (JUL-2009) 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; CP001661; ACT16840.1; -; Genomic_DNA.
DR   RefSeq; WP_012774457.1; NC_012918.1.
DR   AlphaFoldDB; C6E100; -.
DR   SMR; C6E100; -.
DR   STRING; 443144.GM21_0766; -.
DR   EnsemblBacteria; ACT16840; ACT16840; GM21_0766.
DR   KEGG; gem:GM21_0766; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
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; 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.
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..824
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000202220"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           581..585
FT                   /note="'KMSKS' region"
FT   BINDING         584
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   824 AA;  92698 MW;  873509B070F041FC CRC64;
     MEEKYNPSAV EEKWQGYWAE HESFKATEDP TRKKYYLLEM FPYPSGKIHM GHVRNYSIGD
     VIARFKRMQG YNVLHPMGWD AFGMPAENAA IQHKSHPAKW TYENIAYMRG QLKTLGLSYD
     WDRELATCDL DYYKWEQRIF LEMYKKGLAY KKSSAVNWCP KCETVLANEQ VEDGCCWRCD
     SPVRQKELEQ WSFRITNYAQ ELLDDTYKLT GWPERVLTMQ RNWIGRSTGC EIDFPLENGL
     GKIKVFTTRQ DTLFGATFMS LAAEHPMALD LAGDAQRAQV EAFIDKVKKT DRIKRGAEDL
     EKEGVFTGSY CVNPVTNTKM PIYLANFVLM DYGTGAVMAV PTHDQRDFEF AKKYNLPLKV
     VIQPEGETLD PAAMTEAYTA EGIMANSGRF DGMGNGDAKE AIADFLEKEG IGKKTVNFRL
     RDWGISRQRY WGNPIPVINC DLCGVVAVPE ADLPVVLPMD AEFTGEGGNP LARVDSFTTC
     TCPQCGEAAR RETDTMDTFV QSSWYFLRYC SPKFSAGPLD REKVEAWMPV DQYIGGIEHA
     VLHLLYARFF TKVLRDLGYC NVDEPFSNLL TQGMVIKDGA KMSKSKGNVV DPNALIERYG
     ADTARLFSLF AAPPEKDLDW SDQGVDGSYR FLNRVWRLVY DVLPVIGEAG AVNPDSLGAE
     AKKLRRAVHK TIKKVSEDVE ERFHFNTAIA AVMELVNAIQ AFAAKDAPEN VAVVREAVES
     VVRLLAPFVP HFAEELWSQL GHDTVLEAAG WPGYDAAAVV DEEVTVVIQV NGKLRSKLTV
     APDAKEEEVR AQALADDKIK PYLEGKDVKK VVYVPGKLVS IVVA
 
 
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