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Database: UniProt
Entry: SYL_METSB
LinkDB: SYL_METSB
Original site: SYL_METSB 
ID   SYL_METSB               Reviewed;         876 AA.
AC   B8EQP4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 84.
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=Msil_0336;
OS   Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS   13906 / BL2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Methylocella.
OX   NCBI_TaxID=395965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2;
RX   PubMed=20472789; DOI=10.1128/jb.00506-10;
RA   Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA   Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT   "Complete genome sequence of the aerobic facultative methanotroph
RT   Methylocella silvestris BL2.";
RL   J. Bacteriol. 192:3840-3841(2010).
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; CP001280; ACK49315.1; -; Genomic_DNA.
DR   RefSeq; WP_012589385.1; NC_011666.1.
DR   AlphaFoldDB; B8EQP4; -.
DR   SMR; B8EQP4; -.
DR   STRING; 395965.Msil_0336; -.
DR   KEGG; msl:Msil_0336; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002257; 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; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 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.
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..876
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199214"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           630..634
FT                   /note="'KMSKS' region"
FT   BINDING         633
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   876 AA;  97986 MW;  D68C834EEF4747A5 CRC64;
     MDFERYNARE TEPKWRDKWE RSATFKTDND DPRPKYYVLE MFPYPSGRIH MGHVRNYTMG
     DVIARYKRAR GFSVLHPMGW DAFGMPAENA AMQNKSHPAA WTYANIEAMR AQLKSMGLSL
     DWSREIATCD PAYYRHQQKM FLDFLAAGLV DRKKSKVNWD PVDHTVLANE QVIDGRGWRS
     GALVEQRELT QWFFKITDYA EDLLRSLDGL TRWPEKVRLM QANWIGRSEG LLVRFALEPT
     LSAPATEIEV YTTRPDTLFG AKFLAIAADH PIAADCAKAD PALAAFIAEC RLRGTSVAAI
     ETAEKKGVDT GLRVRHPFDE NWLLPVYVAN FVLMDYGTGA IFGCPAHDQR DLDFANAYGL
     GATPVILPPD ADPKTFVIAD KAYDGDGLLF HSRFLDGMTV EAAQEEVARR LEEHPLGNRP
     QAKRQVNFRL RDWGISRQRY WGCPIPIIHC PEHGAVPVPA KDLPVELPPD VSFDEPGNPL
     DRHPTWKHVN CPICAAPSLR ETDTMDTFVD SSWYFARFTQ PWMEDAPTDP SAIAKWLPVD
     QYIGGVEHAI LHLLYARFFT RAMQATGHAG EIREPFAGLF TQGMVVHETY RSEAGDWMFP
     ADVRIEIGPA GRRAFDLASG AEVSIGGIEK MSKSKRNTVD PDEIIGTFGA DTARWFVLSD
     SPPERDVIWT EEGVQGAAKF VQRLWRLIGE LIFLSGADGA PKPQSISPQA AAIRRAAHQS
     LIRLEEDLDR LRFNRAVAQA HDLANKLGAA VGDIDSVEIA PDLRFAFREA AEILTLMIAP
     MMPHLAEECW ARLGHKGLAA EAPWPQADHS LVVEETIDLP VQVNGKKRGD LIIDRAAGRE
     AIEAAALALE PVKRALEGRP VKKIIIVPQR IVNVVA
//
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