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Database: UniProt
Entry: L8TJP8_9MICC
LinkDB: L8TJP8_9MICC
Original site: L8TJP8_9MICC 
ID   L8TJP8_9MICC            Unreviewed;       840 AA.
AC   L8TJP8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049,
GN   ECO:0000313|EMBL:ELT43508.1};
GN   ORFNames=G205_17954 {ECO:0000313|EMBL:ELT43508.1};
OS   Arthrobacter nitrophenolicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT43508.1, ECO:0000313|Proteomes:UP000011189};
RN   [1] {ECO:0000313|Proteomes:UP000011189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJCon {ECO:0000313|Proteomes:UP000011189};
RX   PubMed=23516196; DOI=10.1128/genomeA.00058-13;
RA   Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.;
RT   "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT   Arthrobacter sp. Strain SJCon.";
RL   Genome Announc. 1:e0005813-e0005813(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:0000256|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC         Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC       ECO:0000256|RuleBase:RU363035}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELT43508.1}.
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DR   EMBL; AOFD01000047; ELT43508.1; -; Genomic_DNA.
DR   RefSeq; WP_009358812.1; NZ_AOFD01000047.1.
DR   AlphaFoldDB; L8TJP8; -.
DR   SMR; L8TJP8; -.
DR   PATRIC; fig|683150.5.peg.3523; -.
DR   Proteomes; UP000011189; Unassembled WGS sequence.
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; 3.10.20.590; -; 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 {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00049};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00049}; Reference proteome {ECO:0000313|Proteomes:UP000011189}.
FT   DOMAIN          59..200
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          240..425
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          441..644
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          678..801
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           60..70
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   MOTIF           605..609
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         608
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   840 AA;  92439 MW;  6D7766646F02E28C CRC64;
     MGVQPETETG AAVAAEAPEE GTYSFTAMEA KWPQVWEDLK VFTPVDDGSR ERRYVLDMFP
     YPSGDLHMGH AEAFAMGDVV ARYLRQQGYD VLHPIGWDSF GLPAENAAIK RNAHPSEWTY
     ANIDTQAASF KRYAISADWS RRLHTSDPEY YRWTQWLFKR FYERGLAYRK NSPVNWCPKD
     QTVLANEQVV NGACERCGTT VTKKSLNQWY FKITDYADRL LDDMEQLRGH WPERVLAMQK
     NWIGRSEGAH VNFVIEADGG KPAKEVTVFT TRPDTLYGAT FFVVAADAPL AVELVTEEHA
     AALDEYREQV KALSEIERQS TEREKTGVFT GRYAINPLNG EKLPVWAADY VLADYGTGAI
     MAVPAHDQRD LDFARTFDLP VRAVLDTGEE DPAVSGTATA GEGTLINSGE LDGLPKSEAI
     PAAIAILERQ GTGEKFVNFR LRDWLLSRQR FWGTPIPIIH CPSCGEVPVP DEQLPVTLPA
     DLRGEDLAPK GTSPLAAAEA WVNVECPSCH GPAKRDTDTM DTFVDSSWYF LRFVSPHYTE
     GPFDPQKIND WMPVGQYVGG VEHAILHLLY ARFFTKVIND LGMIEANEPF SALLNQGQVL
     NGGKAMSKSL GNGVDLGEQL DKYGVDAVRL TMIFASPPED DVDWADVSPS GSAKFLARAW
     RLAQDVASAP GTDFSTGDRA LRSVTHRTIA DAAELLDANK FNVVVAKLME LVNATRKAID
     SGAGGADPAV REAAEAVAVI LSLFAPYTAE DMWNVLGHPA SVANAGWPVH DPALLVQATV
     TAVVQVQGKV RDRLEVSPDV SEDELRELAL ASENVQRAMD GRGIRTVIVR APKLVNIVPA
//
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