ID SYL_ARTS2 Reviewed; 843 AA.
AC A0JX57;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
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=Arth_2247;
OS Arthrobacter sp. (strain FB24).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=290399;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB24;
RX PubMed=24501649; DOI=10.4056/sigs.4438185;
RA Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL Stand. Genomic Sci. 9:106-116(2013).
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; CP000454; ABK03627.1; -; Genomic_DNA.
DR RefSeq; WP_011692091.1; NC_008541.1.
DR AlphaFoldDB; A0JX57; -.
DR SMR; A0JX57; -.
DR STRING; 290399.Arth_2247; -.
DR KEGG; art:Arth_2247; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000000754; 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; cd00812; LeuRS_core; 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; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; 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..843
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334729"
FT MOTIF 61..71
FT /note="'HIGH' region"
FT MOTIF 606..610
FT /note="'KMSKS' region"
FT BINDING 609
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 843 AA; 92600 MW; 9C5CE6DF8B5BFEB1 CRC64;
MSVQPETETG TAAVATEGPE EGTYSFAAME AKWPQVWEDL KVFTPVDDGS RERRYVLDMF
PYPSGDLHMG HAEAFAMGDV VARYLRQKGY DVLHPIGWDS FGLPAENAAI KRNAHPSEWT
YANIDTQAAS FKRYAISADW SRRLHTSDPE YYRWTQWLFK RFYERGLAYR KDSPVNWCPK
DQTVLANEQV VNGACERCGT AVTKKSLNQW YFKITDYADR LLDDMDELRG HWPERVLAMQ
KNWIGRSEGA HVNFVIEAAG DKPAKDVTVF TTRPDTLYGA TFFVVAADAP MAVELVTDEH
AAALDAYREQ VKALSEIERQ STEREKTGVF TGRYAVNPLN GEKLPVWAAD YVLADYGTGA
IMAVPAHDQR DLDFARTFDL PVRAVLDTGE DDPAVTGKAT AGEGTLINSG VLDGLPKAEA
IPTAIDMLEK QGTGEKFVNF RLRDWLLSRQ RFWGTPIPII HCPACGEVPV PDDQLPVTLP
ADLRGEDLSP KGTSPLAAAE AWVNVECPNC HGPAKRDTDT MDTFVDSSWY FLRFVSPQYT
EGPFDPKKIN DWMPVGQYVG GVEHAILHLL YARFFTKVIH DLGMIDADEP FSALLNQGQV
LNGGKAMSKS LGNGVDLGEQ LDKYGVDAVR LTMIFASPPE DDVDWADVSP SGSAKFLARA
WRLAQDVSSA PGADAAQGDR ALRSVTHRTI ADAAALLDSN KFNVVVAKLM ELVNATRKTI
DAASGAGGAD PAVREAAEAV AVILSLFAPY TAEDMWNVLG HPASVANAGW PSHDEALLVQ
DTVTAVVQVQ GKVRDRLEVS PEIGEDELRE LALASENVQR ALDGRGIRTV IVRAPKLVNI
VPA
//
