ID A0A0Q5B3J4_9MICO Unreviewed; 860 AA.
AC A0A0Q5B3J4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=ASF46_07015 {ECO:0000313|EMBL:KQQ10749.1};
OS Rathayibacter sp. Leaf296.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1736327 {ECO:0000313|EMBL:KQQ10749.1, ECO:0000313|Proteomes:UP000050868};
RN [1] {ECO:0000313|EMBL:KQQ10749.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ10749.1,
RC ECO:0000313|Proteomes:UP000050868};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ10749.1, ECO:0000313|Proteomes:UP000050868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf296 {ECO:0000313|EMBL:KQQ10749.1,
RC ECO:0000313|Proteomes:UP000050868};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQQ10749.1}.
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DR EMBL; LMNR01000001; KQQ10749.1; -; Genomic_DNA.
DR RefSeq; WP_056866915.1; NZ_LMNR01000001.1.
DR AlphaFoldDB; A0A0Q5B3J4; -.
DR STRING; 1736327.ASF46_07015; -.
DR Proteomes; UP000050868; 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; 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:UP000050868}.
FT DOMAIN 26..224
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 236..446
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 460..661
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 696..819
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 55..65
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 623..627
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 860 AA; 96482 MW; 33FEAB2F3830DBA4 CRC64;
MADETSQQTG ANDEDRYDFR ALQEKWLPIW EETRPFSTDL PDDKRPRKYV LDMFPYPSGD
LHMGHAEAYA LGDVIARYWR QQGFNVLHPI GWDSFGLPAE NAAIKRGLNP RTWTYDNIEQ
QKRSMKRYAA SFDWDRVIHT SDPDYYKWNQ WLFLKMYEKG LAYRKDSWVN WDPVDQTVLA
NEQVLADGTS ERSGAVVVKK KLTQWYFKIT DYADRLLDDL NQLEGSWPSK VIAMQRNWIG
RSIGADVEFE IEGRDERVTV FTTRPDTLYG ATFMVVAPDS DLATELVEGS EPELRDAFRS
YLEKVQKSSE IERLTADRPK TGVFLGRYAI NPVNGERLPI WAADYVLSDY GHGAVMAVPA
HDQRDLDFAR AFDLPVRVVV DTSAPVTGAI PVIPEDPEEL AALEARYSAD PAITGEALTG
DGRLMNSGPL DGLSKRTAIE RVIKLLEERG RGRSAKNYRL RDWLISRQRY WGTPIPIIHG
ENGELIPVPE DQLPVVLPPT EGLDLQPKGS SPLGAAEDWV NVPNPVDGSP ARRDPDTMDT
FVDSSWYFLR FLSPNDDTQA FDPKLAEKWA PVDQYVGGVT HAILHLLYAR FITKVLFDLG
YVSFTEPFTA LLNQGMVQMD GAAMSKSKGN IVRLSEQLDE YGVDAVRLTM AFAGPPEDDI
DWADVSPSGS AKFLARAWRL AKDVTSKPDI EWKNGDAALR RQTHRFLSES PSLIEAFKFN
VVVARLMELV NATRKTIDSG AGGGDAAVRE AAEVIAMALN LFAPYTAEDM WSRLGYQGPV
AHVVWRKADP TLLVEEKVTA ILQVDGKVRD RLEVSPKISS DELEEKARAT AGVARALQGR
EVVKAIVRAP RLVNLVTKAV
//
