ID A0A6V8Q4J2_9ACTN Unreviewed; 829 AA.
AC A0A6V8Q4J2;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 19.
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=HKBW3S34_01218 {ECO:0000313|EMBL:GFP30297.1}, HKBW3S44_00034
GN {ECO:0000313|EMBL:GFP36351.1}, HKBW3S47_01049
GN {ECO:0000313|EMBL:GFP39350.1};
OS Candidatus Hakubella thermalkaliphila.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetota incertae sedis;
OC Candidatus Hakubellales; Candidatus Hakubellaceae; Candidatus Hakubella.
OX NCBI_TaxID=2754717 {ECO:0000313|EMBL:GFP39350.1, ECO:0000313|Proteomes:UP000569018};
RN [1] {ECO:0000313|Proteomes:UP000561271, ECO:0000313|Proteomes:UP000569018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S34 {ECO:0000313|EMBL:GFP30297.1,
RC ECO:0000313|Proteomes:UP000588083}, S44 {ECO:0000313|EMBL:GFP36351.1,
RC ECO:0000313|Proteomes:UP000561271}, and S47
RC {ECO:0000313|EMBL:GFP39350.1, ECO:0000313|Proteomes:UP000569018};
RA Merino N., Kawai M., Boyd E.S., Colman D.R., McGlynn S.E., Nealson K.H.,
RA Kurokawa K., Hongoh Y.;
RT "Single-cell genomics of novel Actinobacteria with the Wood-Ljungdahl
RT pathway discovered in a serpentinizing system.";
RL Front. Microbiol. 11:0-1031(2020).
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:GFP39350.1}.
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DR EMBL; BLRZ01000055; GFP30297.1; -; Genomic_DNA.
DR EMBL; BLSC01000001; GFP36351.1; -; Genomic_DNA.
DR EMBL; BLSD01000046; GFP39350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6V8Q4J2; -.
DR Proteomes; UP000561271; Unassembled WGS sequence.
DR Proteomes; UP000569018; Unassembled WGS sequence.
DR Proteomes; UP000588083; 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; 3.10.20.590:FF:000001; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000003; Leucine--tRNA ligase; 1.
DR FunFam; 1.10.730.10:FF:000011; Leucine--tRNA ligase chloroplastic/mitochondrial; 1.
DR FunFam; 3.40.50.620:FF:000100; probable leucine--tRNA ligase, mitochondrial; 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 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:UP000588083}.
FT DOMAIN 39..182
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 219..406
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 419..619
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 668..791
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 580..584
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 829 AA; 96422 MW; 30E4C98263FC6D84 CRC64;
MGNRYDHRQI EEKWHRIWEG REEKRRRAKG RKYYLLEMFP YPSGEPHMGH VKNYVIGDVL
NRVRRRQGYD VLHPMGWDAF GLPAENAAIQ TGTHPKIWID NNIKSFKRAI KALGIQYDWD
HEVTTCDPDY YRWTQWIFLK FYENGLAVRK RAPVNWCPSC NTVLANEQIV GGRCERCSTE
VTQKELVQWF FKITDYAQRL LDDMELLRGW PERVLIMQQN WIGRSEGATV EFPLVGSDRT
TPIFTTRPDT LYGVTFFILS PEHPLVEELV KGTEYEDEVR KFQEQVRKES LVDRGAPEVE
KKGLFLGRYV VNPLNEEKVP VWVANYVLME YGTGAIMAVP AHDERDFEFA RKYDLPIRVV
IKPRDGEIDE HNLREAYLGE GVMVNSGPFS GLDSQEGKKK IVRYLEKEGI GKFDVSYRLR
DWLISRQRYW GAPIPIVYCE RCGIVPVPYD DLPVLLPMDV DFKPTGQSPL TSCQEFVETS
CPRCRGLAKR ETDTMDTFVC SSWYYLRFCS PHYIEGPFPK EDVDYWMPVD QYIGGVEHAI
LHLMYSRFFT KVFYDLGMVK FKEPFANLFT QGMIYKDGAK MSKSKGNIVS PDRIVEDYGA
DTARLMILFA GPPELDMEWS DRGVEGAYRF LNRVWRLVRD SVRSLQLLSS SEREISSERE
ISQEDVKLRR KTHQTIKKFT QDVSERFSFN TAISALMELV NDMYKYNELV SQEEQNPQVL
REATEILVQL LAPIAPHLSE ELWEQLGHKE SVHDLPWPSY DEEIARSEEI TVVIQINGKL
RDRITVPVDI SEEEMKKIAL SSQKAAKFYE GKEIKKVITV PGKLVNIVV
//
