ID A0A9W6VHJ9_9PSEU Unreviewed; 958 AA.
AC A0A9W6VHJ9;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 9.
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:GLY67507.1};
GN ORFNames=Atai01_41260 {ECO:0000313|EMBL:GLY67507.1};
OS Amycolatopsis taiwanensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=342230 {ECO:0000313|EMBL:GLY67507.1, ECO:0000313|Proteomes:UP001165136};
RN [1] {ECO:0000313|EMBL:GLY67507.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 103393 {ECO:0000313|EMBL:GLY67507.1};
RA Ichikawa N., Sato H., Tonouchi N.;
RT "Amycolatopsis taiwanensis NBRC 103393.";
RL Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP +
CC diphosphate; 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:ARBA00047469, 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:RU363039}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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:GLY67507.1}.
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DR EMBL; BSTI01000008; GLY67507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9W6VHJ9; -.
DR Proteomes; UP001165136; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 3.40.50.620:FF:000056; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000060; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000087; Leucine--tRNA ligase; 1.
DR FunFam; 3.90.740.10:FF:000017; Leucine--tRNA ligase; 1.
DR FunFam; 1.10.730.10:FF:000011; Leucine--tRNA ligase chloroplastic/mitochondrial; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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; 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; 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:UP001165136}.
FT DOMAIN 73..180
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 303..496
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 806..922
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 727..731
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT COMPBIAS 12..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 730
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 958 AA; 107777 MW; 420459F5C28BCA00 CRC64;
MSEAAAQHGA GTPSQEQGTP SDTPGHRYNA ELAGSLELRW QGYWAEHGTY NAPNPVGPFA
SDHLPADKLF VQDMFPYPSG AGLHVGHPLG FIGTDVYARY NRMIGRNVLH TMGFDAFGLP
AEQYAVQTGQ HPRKTTEENI VTYLRQIRRL GLGHDERRRI STIDPGYYKW TQWIFLRIYN
SFYDEKLGKA RPIAELEAEY AQDKRRTPDG RGWHELTRAE QQGVLDQHRL AYLAEAPVNW
CPGLGTVLSN EEVTPDGRSE RGNFPVFRRN LRQWMMRITA YADRLVDDLD RLDWPEKIKS
MQRNWIGRSR GARISFPAGA ERIEVFTTRP DTVFGATYLV LAPEHPLVDK VTTDAWASDV
DSLWTGGAAT PGEAVEAYRL AASRKSELDR QENRDKTGVF TGSYAVNPVN GKQIPIFIAD
YVLMGYGTGA IMAVPGQDQR DWDFAEKFGL DIIRTVQPSE DFDGKAFTGE GPAVNSGFLD
GMDVDEAKKA IIAWLEEHGH GAGTVQYKLR DWLFSRQRYW GEPFPIVYDA DGTAHAIPES
MLPVELPEVD DYSPKTFDPE DADAEPSPPL SRATDWVEVT LDLGDGPQRY RRDTNTMPNW
AGSCWYQLRY VDPDNAERFV DPENERYWLG PRPDEHGAND PGGVDLYVGG VEHAVLHLLY
SRFWQKVLYD LGEVSSDEPY RRLVNQGYIQ AYAYTDSRGF HVPADQVEER DGKFFYQGLE
VKQEYGKMGK SLKNVVTPDE MCATYGADTF RLYEMSMGPI DVSRPWATKD VVGAHRFLQR
LWRLVVDEQT GELRVSTADI TDEDRKQLHR TIAGVREDYA ELRFNTAGAK LIELNNHLTK
VYGSAEATPR ELVEPLVLML APLCPHISEE LWHRLGHQDS LVHGPFPAVD ERYLVEETVV
YPVQVNGKVR ARITVPADAA KDAVESAALS DAKIAAVLDG QAPRKVIVVP GRLVNLVV
//
