ID A0A7Y6M1P5_9ACTN Unreviewed; 828 AA.
AC A0A7Y6M1P5;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
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 ORFNames=HTZ77_04305 {ECO:0000313|EMBL:NUW30646.1};
OS Nonomuraea montanisoli.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=2741721 {ECO:0000313|EMBL:NUW30646.1, ECO:0000313|Proteomes:UP000586042};
RN [1] {ECO:0000313|EMBL:NUW30646.1, ECO:0000313|Proteomes:UP000586042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMC257 {ECO:0000313|EMBL:NUW30646.1,
RC ECO:0000313|Proteomes:UP000586042};
RA Chanama M.;
RT "Nonomuraea sp. SMC257, a novel actinomycete isolated from soil.";
RL Submitted (JUN-2020) 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: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:NUW30646.1}.
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DR EMBL; JABWGN010000002; NUW30646.1; -; Genomic_DNA.
DR RefSeq; WP_175588115.1; NZ_JABWGN010000002.1.
DR AlphaFoldDB; A0A7Y6M1P5; -.
DR Proteomes; UP000586042; 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 CDD; cd00812; LeuRS_core; 1.
DR FunFam; 1.10.730.10:FF:000002; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000003; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000056; Leucine--tRNA ligase; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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; 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; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 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:UP000586042}.
FT DOMAIN 23..222
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 234..417
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 431..632
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 669..792
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 54..64
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 594..598
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 828 AA; 92375 MW; E51F36D7633F7B25 CRC64;
MGPSRGRRTF AVSEYDPQAL QAKWQQRWEE LDPFRAGEDA ADARERRYML DMFPYPSGDL
HMGHGEVFAI GDVVARYWFQ RGYNVLHPIG WDSFGLPAEN AAIKRNAHPA EWTYANIETQ
ATSFRRYGIS FDWSRRLHTS DPEYYRWNQW LFNRFFERGL AYRKGGLVNW CPNDQTVLAN
EQVVAGKCER CGADVVRREL TQWYFKITDY AERLLKDMEQ LEGGWPERVL TMQRNWIGRS
EGADVLFEIE GREEPVHVYT TRPDTLFGAT FFVVAVDAAL ADEIVTDDRR EEFEAYRAEV
AKLSDIERLS TDKEKTGVFL GRHAINPVNG ERIPVWAADY VLSDYGHGAI MAVPAHDQRD
LDFALKFGLP VKVVVHTGLA DPGETGEATP GEGSLVNSGP LDGLSKAEAI AKIIDILRTQ
GRGEASVNFR LRDWLLSRQR FWGTPIPIIH CLDCGEVPVP DDQLPVTLPD LRGEALAPKG
VSPLASATDW VNVECPKCGG RAMRDTDTMD TFVDSSWYYL RYCSPDYTDG PFDVEQVRKW
GPIDQYVGGV EHAVLHLLYS RFFTKVLHDM GMVDFTEPFL RLLNQGQVIN GGKAMSKSLG
NGVDLGQQID EYGVDAVRLT MVFAGPPEDD IDWADVSPAA SQKFLARAFR VMDDVAGEPG
VSFEAGDLEL RKFTHRTIDE VTKLVESHRF NVAVARLMEL TSAARKAIDS GPGAADPAVR
EAAEALAVML SLVAPYTAEE GWERLGHTGS TVALAGWPVA EPALLVQDSV TCVVQVAGKV
RDRLEVSPSI SEDELRGLAL GSDKVRAYLD GEPRKVIVRA PKLVNIVP
//
