SYL_RUEST
ID SYL_RUEST Reviewed; 857 AA.
AC Q1GKN8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=TM1040_0045;
OS Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX NCBI_TaxID=292414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040;
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., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA Richardson P.;
RT "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL Submitted (MAY-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; CP000377; ABF62778.1; -; Genomic_DNA.
DR RefSeq; WP_011537416.1; NC_008044.1.
DR AlphaFoldDB; Q1GKN8; -.
DR SMR; Q1GKN8; -.
DR STRING; 292414.TM1040_0045; -.
DR EnsemblBacteria; ABF62778; ABF62778; TM1040_0045.
DR KEGG; sit:TM1040_0045; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000636; 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; 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; 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; Reference proteome.
FT CHAIN 1..857
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009433"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT MOTIF 628..632
FT /note="'KMSKS' region"
FT BINDING 631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 857 AA; 95857 MW; 67FE4D9302BC6DA8 CRC64;
MSRYEASDIE ARWQKAWEEA AIFQAKEDHS KPKYYVLEMF PYPSGKLHMG HVRNYTMGDV
IARYKLSTGH NVLHPMGFDA FGMPAENAAM ASGGHPKDWT YSNIDTMVEQ MKPLGLSLDW
SRMFATCDPE YYGQQQALFL DFLEKGLVYR KNAVVNWDPV DMTVLANEQV ENGRGWRSGA
LVERRELTQW FFKISDYSDE LLEALDGLEN WPAKVRLMQE NWIGKSRGLQ FSFERTDGEE
AIEVYTTRPD TLMGASFVGI SPDHPIAKKL EAESQEVADF VAECRKGGTT EEAIETAEKL
GYDTGLRVKH PLDPNWELPV WIANFILMDY GTGAIFACPA HDQRDFEFAT KYNLPIIPVL
EPVEGAGELT EAYVPTKAEK VRYVRGFAGD ELQTGEEGVN TAVDKAEAEG WGQGVTKFRL
RDWGLSRQRY WGCPIPVVHC PDCGVVPEKK ENLPIALPYD EDGKAIDFSV PGNPLDRHPS
WRNCACPNCG KPAQRETDTM DTFVDSSWYF ARFTAPRAET PTDLDAANYW MNVDQYIGGI
EHAILHLLYS RFFARAMQIC GHLPESAKEP FDALFTQGMV THAIYENAER KDDNGRAIYH
YPSEVEERDG GVFVKETGER IKVIPSAKMS KSKNNVVDPL AIISTYGADT ARWFVLSDSP
PERDVEWTAS GAEAAYKHLN RVWNLCDRIG EMDPDAKGEG DEELLREMHK AIRDVTLGVE
SFGFNAAIAK LYGFTNTLSK SKASAAVQKQ AIKTLAQLMS PMTPHLAEDI WAHQGGEGLI
ANAAWPVADE SMLVEDSVTL PIQVNGKRRG EITVAKDLDK AEVEKLALAH EAVQRVLEGA
APKKVIVVPG RIVNVVA