ID SYL_SALRD Reviewed; 863 AA.
AC Q2S415;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 121.
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=SRU_0933;
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31;
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC46207.1; -; Genomic_DNA.
DR RefSeq; WP_011403694.1; NC_007677.1.
DR RefSeq; YP_445066.1; NC_007677.1.
DR AlphaFoldDB; Q2S415; -.
DR SMR; Q2S415; -.
DR STRING; 309807.SRU_0933; -.
DR EnsemblBacteria; ABC46207; ABC46207; SRU_0933.
DR KEGG; sru:SRU_0933; -.
DR PATRIC; fig|309807.25.peg.967; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000008674; 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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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 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.
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_1000009423"
FT MOTIF 42..53
FT /note="'HIGH' region"
FT MOTIF 635..639
FT /note="'KMSKS' region"
FT BINDING 638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 863 AA; 98948 MW; DE2DC62AD14854EA CRC64;
MAYPFHDIET KWQQYWEEHQ TFRTPDEVPD DQEEFYVLDM FPYPSGSGLH VGHPEGYTAT
DIVARYKRKQ GFNVLHPMGW DAFGLPAEQY ALKTNTHPRE TTEKNIAQFK RQLKRLGFSY
DWQREINTTD PDYYKWTQWI FLQLYEKGLA YQSEEPVWWC EELGTVLANE EVIDGKSERG
GYPCERVPMR QWVLKITEYA DRLLEGLEDL DWPESTKEMQ RNWIGRSEGA NVYFDLVGAD
DALEVYTTRP DTLFGATYMV LAPEHELLDE ITTDEHREDV DEYCRQALRK SERKRQQQGD
KTGVFTGGYA VNPVNGEEIP IWVADYVLVS YGTGAIMAVP AHDERDHAFA NKYDLPIREV
VEGGDIDEEA YTGDGPHVHS ANEAVSLNGL RNEEAKEAIT EWLDEEEKGE RTVNYQLQDW
LFSRQRYWGE PFPIVFTEDG EDKPVPEEEL PVTLPDLDVF EPSGTPEGPL ATIEDWRETT
DPETGEPAQR ETNTMPQWAG SCWYYLRFID PDNDEQLVDP EKEEYWMPVD LYVGGSEHAV
LHLLYARFWH KVLYDAGVVS TKEPFQTLVH QGMILGETEY TAYRDDAGEF VSAEQVDDDA
DLTPVPVDDG DVKKDGDVFV LADRPAVRVD ARSHKMSKSR GNVINPDDVV DEYGADTLRL
YEMFMGPLEQ DKPWSTDDME GVHRFLNRIW RLVVDADSGG LAVSDEEPDR EQLRTLHRTI
KTVTEDIEAR DFNTAIAAMM EFVNAANKWD ALPRQVATPF VLLLSPFAPH LAEELWARLG
HDQSLAYADW PAYDDELIRR EVVEMPVQVD GTVRATIEVA ADAEEADVLA TAKEAENVAR
HLDDEDLQRE IYVPGQIVNF VTG
//
