SYL_STRAW
ID SYL_STRAW Reviewed; 962 AA.
AC Q82C66;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=SAV_5488;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC73200.1; -; Genomic_DNA.
DR RefSeq; WP_010986890.1; NZ_JZJK01000066.1.
DR AlphaFoldDB; Q82C66; -.
DR SMR; Q82C66; -.
DR STRING; 227882.SAV_5488; -.
DR EnsemblBacteria; BAC73200; BAC73200; SAVERM_5488.
DR KEGG; sma:SAVERM_5488; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000428; 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; 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; 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..962
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152092"
FT REGION 559..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 68..79
FT /note="'HIGH' region"
FT MOTIF 733..737
FT /note="'KMSKS' region"
FT COMPBIAS 566..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 736
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 962 AA; 106570 MW; 5EB57AE371334BF8 CRC64;
MSETNPAAAS EVAAPHRYTA AVAAEIEARW QDFWDAEGTY EAPNPTGDLA GGPALVAKPK
KFVMDMFPYP SGAGLHVGHP LGYIATDVFA RFQRMTGHNV LHTLGFDAFG LPAEQYAVQT
GTHPRVSTEA NIENMKVQLR RLGLGHDKRR SFATIDPDYY KWTQWIFLQI FNSWYDEEAN
KARPIAELVA QFESGERAVP RADGATRAWR ELTAAERADV LGEYRLAYAS EAPVNWSPGL
GTVLANEEVT ADGRSERGNF PVFKAKLRQW NMRITAYADR LLDDLDALDW PEAIKLQQRN
WIGRSEGARV DFPIDGEAVT VFTTRPDTLF GATYMVLAPE HPLVEKFTPA AWPEGTHDVW
TGGHATPAEA VAAYRAQAAS KSDVERQAEA KDKTGVFTGA YATNPVSGEQ VPVFIADYVL
MGYGTGAIMA VPAHDTRDFA FARAFELSMR CVVEPSDDRG TDPSTWDDAF ASYDAKIVNS
SSGEISLDGL GVVEAKARIT EWLERKGLGE GTVNFRLRDW LFSRQRYWGE PFPIVYDEDG
IAHALPESML PLELPEVEDY SPRTFDPDDA NTSPETPLSR NEDWVNVTLD LGDGRGPQKY
RRETNTMPNW AGSCWYELRY LDPHNDQKLV DPAIEQYWMG PREGQPTGGV DLYVGGAEHA
VLHLLYARFW SKVLFDLGHI SSAEPFHKLF NQGMIQAYVY RDSRGIAVPA AEVEERDGAY
YYQGEKVSRL LGKMGKSLKN AVTPDEICAE YGADTLRLYE MAMGPLDVSR PWDTRAVVGQ
FRLLQRLWRN VVDEATGEVT VVDAEPDEET LRALHKAIDG VRQDLEGMRF NTAIAKVTEL
NNQLTKAGGP VPRTVAESLV LLVAPLAPHI AEELWRKLGH NDSVVHQDFP VADPAYVVDE
AVTCVVQIKG KVKARLEVSP AISEEELEKV ALADEKVVAA LGGAGIRKVI VRAPKLVNIV
TA
